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Conserved domains on  [gi|581121380|gb|EVL37060|]
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cytochrome aa3 quinol oxidase, subunit II [Staphylococcus aureus M0853]

Protein Classification

similar to quinol oxidase subunit( domain architecture ID 11492500)

protein similar to quinol oxidase subunit

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
QOXA TIGR01432
cytochrome aa3 quinol oxidase, subunit II; This enzyme catalyzes the oxidation of quinol with ...
 18-230 1.67e-146

cytochrome aa3 quinol oxidase, subunit II; This enzyme catalyzes the oxidation of quinol with the concomitant reduction of molecular oxygen to water. This acts as the terminal electron acceptor in the respiratory chain. This subunit contains two transmembrane helices and a large external domain responsible for the binding and oxidation of quinol. QuoX is (presently) only found in gram positive bacteria of the Bacillus/Staphylococcus group. Like CyoA, the ubiquinol oxidase found in proteobacteria, the residues responsible for the ligation of Cu(a) and cytochrome c (found in the related cyt. c oxidases) are absent. Unlike CyoA, QoxA is in complex with a subunit I which contains cytochromes a similar to the cyt. c oxidases (as opposed to cytochromes b). [Energy metabolism, Electron transport]


:

Pssm-ID: 273621 [Multi-domain]  Cd Length: 226  Bit Score: 413.15  E-value: 1.67e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581121380   18 SGCSNIEIFNAKGPVASSQKFLILYSIVFMLVICFVVLGMFAIFIYKYSYNKN--AESGKMHHNAIIETIWFVIPIIIVA 95
Cdd:TIGR01432  10 SGCSNIEVLNPKGPVASSQSDLILYSIVFMLVIVFVVFVLFTIFLVKYRYRKDngAYSPKMHGNAILETIWTVIPIIIVI 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581121380   96 ALAIPTVKTLYDYEKPPKS--EKDPMVVYAVSAGYKWFFAYPDEHIETVNTLTIPKDRPVVFKLQAMDTMTSFWIPQLGG 173
Cdd:TIGR01432  90 ALAIPTVKTIYDYEKAPKStkEKDPMVVYATSADWKWFFSYPDEHIETVNYLNIPKDRPVLFKLQSADTMTSFWIPQLGG 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 581121380  174 QKYAMTGMTMNWTLEASQTGTFRGRNSNFNGEGFSRQTFKVNAVSQKDYDKWVKEVK 230
Cdd:TIGR01432 170 QKYAMTGMTMNWYLQADEVGTYRGRNANFNGEGFADQTFDVNAVSEKDFDKWVKETK 226
 
Name Accession Description Interval E-value
QOXA TIGR01432
cytochrome aa3 quinol oxidase, subunit II; This enzyme catalyzes the oxidation of quinol with ...
 18-230 1.67e-146

cytochrome aa3 quinol oxidase, subunit II; This enzyme catalyzes the oxidation of quinol with the concomitant reduction of molecular oxygen to water. This acts as the terminal electron acceptor in the respiratory chain. This subunit contains two transmembrane helices and a large external domain responsible for the binding and oxidation of quinol. QuoX is (presently) only found in gram positive bacteria of the Bacillus/Staphylococcus group. Like CyoA, the ubiquinol oxidase found in proteobacteria, the residues responsible for the ligation of Cu(a) and cytochrome c (found in the related cyt. c oxidases) are absent. Unlike CyoA, QoxA is in complex with a subunit I which contains cytochromes a similar to the cyt. c oxidases (as opposed to cytochromes b). [Energy metabolism, Electron transport]


Pssm-ID: 273621 [Multi-domain]  Cd Length: 226  Bit Score: 413.15  E-value: 1.67e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581121380   18 SGCSNIEIFNAKGPVASSQKFLILYSIVFMLVICFVVLGMFAIFIYKYSYNKN--AESGKMHHNAIIETIWFVIPIIIVA 95
Cdd:TIGR01432  10 SGCSNIEVLNPKGPVASSQSDLILYSIVFMLVIVFVVFVLFTIFLVKYRYRKDngAYSPKMHGNAILETIWTVIPIIIVI 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581121380   96 ALAIPTVKTLYDYEKPPKS--EKDPMVVYAVSAGYKWFFAYPDEHIETVNTLTIPKDRPVVFKLQAMDTMTSFWIPQLGG 173
Cdd:TIGR01432  90 ALAIPTVKTIYDYEKAPKStkEKDPMVVYATSADWKWFFSYPDEHIETVNYLNIPKDRPVLFKLQSADTMTSFWIPQLGG 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 581121380  174 QKYAMTGMTMNWTLEASQTGTFRGRNSNFNGEGFSRQTFKVNAVSQKDYDKWVKEVK 230
Cdd:TIGR01432 170 QKYAMTGMTMNWYLQADEVGTYRGRNANFNGEGFADQTFDVNAVSEKDFDKWVKETK 226
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
25-234 1.85e-81

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 248.20  E-value: 1.85e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581121380  25 IFNAKGPVASSQKFLILYSIVFMLVICFVVLGMFAIFIYKYSYNKNAESGK-MHHNAIIETIWFVIPIIIVAALAIPTVK 103
Cdd:COG1622   21 LPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIRYRRRKGDADPAqFHHNTKLEIVWTVIPIIIVIVLAVPTLR 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581121380 104 TLYDYEKPPKsekDPMVVYAVSAGYKWFFAYPDEHIETVNTLTIPKDRPVVFKLQAMDTMTSFWIPQLGGQKYAMTGMTM 183
Cdd:COG1622  101 VLHALDDAPE---DPLTVEVTGYQWKWLFRYPDQGIATVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVT 177

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 581121380 184 NWTLEASQTGTFRGRNSNFNGEGFSRQTFKVNAVSQKDYDKWVKEVKGKKT 234
Cdd:COG1622  178 ELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQKASAA 228
PRK10525 PRK10525
cytochrome o ubiquinol oxidase subunit II; Provisional
 18-251 1.30e-49

cytochrome o ubiquinol oxidase subunit II; Provisional


Pssm-ID: 182518 [Multi-domain]  Cd Length: 315  Bit Score: 168.82  E-value: 1.30e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581121380  18 SGCsNIEIFNAKGPVASSQKFLILYSIVFMLVICFVVLGMFAIFIYKY-SYNKNAE-SGKMHHNAIIETIWFVIPIIIVA 95
Cdd:PRK10525  23 SGC-NSALLDPKGQIGLEQRSLILTAFGLMLIVVIPAILMAVGFAWKYrASNKDAKySPNWSHSNKVEAVVWTVPILIII 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581121380  96 ALAIPTVKTLYDYE--KPPKSEKDPMVVYAVSAGYKWFFAYPDEHIETVNTLTIPKDRPVVFKLQAMDTMTSFWIPQLGG 173
Cdd:PRK10525 102 FLAVLTWKTTHALEpsKPLAHDEKPITIEVVSMDWKWFFIYPEQGIATVNEIAFPANVPVYFKVTSNSVMNSFFIPRLGS 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581121380 174 QKYAMTGMTMNWTLEASQTGTFRGRNSNFNGEGFSRQTFKVNAV-SQKDYDKWVKEVK-GKKTL-DQDTFDKQLLPSTPN 250
Cdd:PRK10525 182 QIYAMAGMQTRLHLIANEPGTYDGISASYSGPGFSGMKFKAIATpDRAEFDQWVAKAKqSPNTMnDMAAFEKLAAPSEYN 261


                 .
gi 581121380 251 K 251
Cdd:PRK10525 262 P 262
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 119-217 1.50e-49

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: 161.56  E-value: 1.50e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581121380 119 MVVYAVSAGYKWFFAYPDEHIETVNTLTIPKDRPVVFKLQAMDTMTSFWIPQLGGQKYAMTGMTMNWTLEASQTGTFRGR 198
Cdd:cd04212    1 LEIQVVSLDWKWLFIYPEQGIATVNELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGL 80

                         90
                 ....*....|....*....
gi 581121380 199 NSNFNGEGFSRQTFKVNAV 217
Cdd:cd04212   81 SANYSGEGFSDMKFKVLAV 99
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 28-103 5.70e-08

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: 50.02  E-value: 5.70e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 581121380   28 AKGPVASSQKFLILYSIVFMLVICFVVLGMFAIFIYKYSYNKNAESGK-MHHNAIIETIWFVIPIIIVAALAIPTVK 103
Cdd:pfam02790  12 AASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRFNRRKNPITARyTTHGQTIEIIWTIIPAVILILIALPSFK 88
 
Name Accession Description Interval E-value
QOXA TIGR01432
cytochrome aa3 quinol oxidase, subunit II; This enzyme catalyzes the oxidation of quinol with ...
 18-230 1.67e-146

cytochrome aa3 quinol oxidase, subunit II; This enzyme catalyzes the oxidation of quinol with the concomitant reduction of molecular oxygen to water. This acts as the terminal electron acceptor in the respiratory chain. This subunit contains two transmembrane helices and a large external domain responsible for the binding and oxidation of quinol. QuoX is (presently) only found in gram positive bacteria of the Bacillus/Staphylococcus group. Like CyoA, the ubiquinol oxidase found in proteobacteria, the residues responsible for the ligation of Cu(a) and cytochrome c (found in the related cyt. c oxidases) are absent. Unlike CyoA, QoxA is in complex with a subunit I which contains cytochromes a similar to the cyt. c oxidases (as opposed to cytochromes b). [Energy metabolism, Electron transport]


Pssm-ID: 273621 [Multi-domain]  Cd Length: 226  Bit Score: 413.15  E-value: 1.67e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581121380   18 SGCSNIEIFNAKGPVASSQKFLILYSIVFMLVICFVVLGMFAIFIYKYSYNKN--AESGKMHHNAIIETIWFVIPIIIVA 95
Cdd:TIGR01432  10 SGCSNIEVLNPKGPVASSQSDLILYSIVFMLVIVFVVFVLFTIFLVKYRYRKDngAYSPKMHGNAILETIWTVIPIIIVI 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581121380   96 ALAIPTVKTLYDYEKPPKS--EKDPMVVYAVSAGYKWFFAYPDEHIETVNTLTIPKDRPVVFKLQAMDTMTSFWIPQLGG 173
Cdd:TIGR01432  90 ALAIPTVKTIYDYEKAPKStkEKDPMVVYATSADWKWFFSYPDEHIETVNYLNIPKDRPVLFKLQSADTMTSFWIPQLGG 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 581121380  174 QKYAMTGMTMNWTLEASQTGTFRGRNSNFNGEGFSRQTFKVNAVSQKDYDKWVKEVK 230
Cdd:TIGR01432 170 QKYAMTGMTMNWYLQADEVGTYRGRNANFNGEGFADQTFDVNAVSEKDFDKWVKETK 226
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
25-234 1.85e-81

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 248.20  E-value: 1.85e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581121380  25 IFNAKGPVASSQKFLILYSIVFMLVICFVVLGMFAIFIYKYSYNKNAESGK-MHHNAIIETIWFVIPIIIVAALAIPTVK 103
Cdd:COG1622   21 LPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIRYRRRKGDADPAqFHHNTKLEIVWTVIPIIIVIVLAVPTLR 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581121380 104 TLYDYEKPPKsekDPMVVYAVSAGYKWFFAYPDEHIETVNTLTIPKDRPVVFKLQAMDTMTSFWIPQLGGQKYAMTGMTM 183
Cdd:COG1622  101 VLHALDDAPE---DPLTVEVTGYQWKWLFRYPDQGIATVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVT 177

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 581121380 184 NWTLEASQTGTFRGRNSNFNGEGFSRQTFKVNAVSQKDYDKWVKEVKGKKT 234
Cdd:COG1622  178 ELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQKASAA 228
CyoA TIGR01433
cytochrome o ubiquinol oxidase subunit II; This enzyme catalyzes the oxidation of ubiquinol ...
 18-230 1.36e-54

cytochrome o ubiquinol oxidase subunit II; This enzyme catalyzes the oxidation of ubiquinol with the concomitant reduction of molecular oxygen to water. This acts as the terminal electron acceptor in the respiratory chain. Subunit II is responsible for binding and oxidation of the ubiquinone substrate. This sequence is closely related to QoxA, which oxidizes quinol in gram positive bacteria but which is in complex with subunits which utilize cytochromes a in the reduction of molecular oxygen. Slightly more distantly related is subunit II of cytochrome c oxidase which uses cyt. c as the oxidant. [Energy metabolism, Electron transport]


Pssm-ID: 213620 [Multi-domain]  Cd Length: 226  Bit Score: 179.25  E-value: 1.36e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581121380   18 SGCsNIEIFNAKGPVASSQKFLILYSIVFMLVICFVVLGMFAIFIYKY-SYNKNAE-SGKMHHNAIIETIWFVIPIIIVA 95
Cdd:TIGR01433  11 SGC-NLVLLDPKGQIGLEERSLILTAFGLMLLVVIPVILMTLFFAWKYrATNKDADySPNWHHSTKIEIVVWTIPILIII 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581121380   96 ALAIPTVKTLY--DYEKPPKSEKDPMVVYAVSAGYKWFFAYPDEHIETVNTLTIPKDRPVVFKLQAMDTMTSFWIPQLGG 173
Cdd:TIGR01433  90 FLGVLTWITTHklDPYRPLASDVKPITIEVVALDWKWLFIYPEQGIATVNEIAFPVNTPINFKITSNSVMNSFFIPQLGS 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 581121380  174 QKYAMTGMTMNWTLEASQTGTFRGRNSNFNGEGFSRQTFKVNAVSQKDYDKWVKEVK 230
Cdd:TIGR01433 170 QIYAMAGMQTKLHLIANEPGVYDGISANYSGPGFSGMKFKAIATDRAAFDQWVAKAK 226
PRK10525 PRK10525
cytochrome o ubiquinol oxidase subunit II; Provisional
 18-251 1.30e-49

cytochrome o ubiquinol oxidase subunit II; Provisional


Pssm-ID: 182518 [Multi-domain]  Cd Length: 315  Bit Score: 168.82  E-value: 1.30e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581121380  18 SGCsNIEIFNAKGPVASSQKFLILYSIVFMLVICFVVLGMFAIFIYKY-SYNKNAE-SGKMHHNAIIETIWFVIPIIIVA 95
Cdd:PRK10525  23 SGC-NSALLDPKGQIGLEQRSLILTAFGLMLIVVIPAILMAVGFAWKYrASNKDAKySPNWSHSNKVEAVVWTVPILIII 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581121380  96 ALAIPTVKTLYDYE--KPPKSEKDPMVVYAVSAGYKWFFAYPDEHIETVNTLTIPKDRPVVFKLQAMDTMTSFWIPQLGG 173
Cdd:PRK10525 102 FLAVLTWKTTHALEpsKPLAHDEKPITIEVVSMDWKWFFIYPEQGIATVNEIAFPANVPVYFKVTSNSVMNSFFIPRLGS 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581121380 174 QKYAMTGMTMNWTLEASQTGTFRGRNSNFNGEGFSRQTFKVNAV-SQKDYDKWVKEVK-GKKTL-DQDTFDKQLLPSTPN 250
Cdd:PRK10525 182 QIYAMAGMQTRLHLIANEPGTYDGISASYSGPGFSGMKFKAIATpDRAEFDQWVAKAKqSPNTMnDMAAFEKLAAPSEYN 261


                 .
gi 581121380 251 K 251
Cdd:PRK10525 262 P 262
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 119-217 1.50e-49

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: 161.56  E-value: 1.50e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581121380 119 MVVYAVSAGYKWFFAYPDEHIETVNTLTIPKDRPVVFKLQAMDTMTSFWIPQLGGQKYAMTGMTMNWTLEASQTGTFRGR 198
Cdd:cd04212    1 LEIQVVSLDWKWLFIYPEQGIATVNELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGL 80

                         90
                 ....*....|....*....
gi 581121380 199 NSNFNGEGFSRQTFKVNAV 217
Cdd:cd04212   81 SANYSGEGFSDMKFKVLAV 99
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 28-226 1.47e-42

cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions. [Energy metabolism, Electron transport]


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 147.14  E-value: 1.47e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581121380   28 AKGPVASSQKFLILYSIVFMLVICFVVLGMFAIFIYKY-SYNKNAESGKMHHNAIIETIWFVIPIIIVAALAIPTVKTLY 106
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVWKFrRKGDEEKPSQIHGNRRLEYVWTVIPLIIVVGLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581121380  107 DYEKPPksEKDPMVVYAVSAGYKWFFAYPDEHIETVNTLTIPKDRPVVFKLQAMDTMTSFWIPQLGGQKYAMTGMTMNWT 186
Cdd:TIGR02866  81 YLERPI--PKDALKVKVTGYQWWWDFEYPESGFTTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALW 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 581121380  187 LEASQTGTFRGRNSNFNGEGFSRQTFKVNAVSQKDYDKWV 226
Cdd:TIGR02866 159 FNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYV 198
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 118-217 3.93e-21

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: 86.90  E-value: 3.93e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581121380 118 PMVVYAVSAGYKWFFAYPDEH---IETVNTLTIPKDRPVVFKLQAMDTMTSFWIPQLGGQKYAMTGMTMNWTLEASQTGT 194
Cdd:cd04213    1 ALTIEVTGHQWWWEFRYPDEPgrgIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDMIPGRTNRLWLQADEPGV 80

                         90       100
                 ....*....|....*....|...
gi 581121380 195 FRGRNSNFNGEGFSRQTFKVNAV 217
Cdd:cd04213   81 YRGQCAEFCGASHALMRFKVIAL 103
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 128-226 6.72e-21

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


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 86.69  E-value: 6.72e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581121380 128 YKWFFAYPDEHIETVNTLTIPKDRPVVFKLQAMDTMTSFWIPQLGGQKYAMTGMTMNWTLEASQTGTFRGRNSNFNGEGF 207
Cdd:cd13914   10 WGWEFSYPEANVTTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAFPGQYNTIKTEATEEGEYQLYCAEYCGAGH 89

                         90
                 ....*....|....*....
gi 581121380 208 SRQTFKVNAVSQKDYDKWV 226
Cdd:cd13914   90 SQMLSTVTVVSQDEYQQWL 108
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 119-214 6.50e-19

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: 80.80  E-value: 6.50e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581121380 119 MVVYAVSAGYKWFFAYPDehIETVNTLTIPKDRPVVFKLQAMDTMTSFWIPQLGGQKYAMTGMTMNWTLEASQTGTFRGR 198
Cdd:cd13842    1 LTVYVTGVQWSWTFIYPN--VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDAVPGYTSELWFVADKPGTYTII 78

                         90
                 ....*....|....*.
gi 581121380 199 NSNFNGEGFSRQTFKV 214
Cdd:cd13842   79 CAEYCGLGHSYMLGKV 94
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 92-226 1.79e-16

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: 75.18  E-value: 1.79e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581121380  92 IIVAALAIPTV-KTLYDYEKPPKSEKDPMVVYAVSAGYKWFFAYPDEhIETVNTLTIPKDRPVVFKLQAMDTMTSFWIPQ 170
Cdd:cd13918    5 IIVISLIVWTYgMLLYVEDPPDEADEDALEVEVEGFQFGWQFEYPNG-VTTGNTLRVPADTPIALRVTSTDVFHTFGIPE 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 581121380 171 LGGQKYAMTGMTMNWTLEASQTGTFRGRNSNFNGEGFSRQTFKVNAVSQKDYDKWV 226
Cdd:cd13918   84 LRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAWY 139
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 118-217 5.73e-15

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: 69.98  E-value: 5.73e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581121380 118 PMVVYAVSAGYKWFFAYPDEHI-------ETVNTLTIPKDRPVVFKLQAMDTMTSFWIPQLGGQKYAMTGMTMNWTLEAS 190
Cdd:cd13919    1 ALVVEVTAQQWAWTFRYPGGDGklgtdddVTSPELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDAVPGRTTRLWFTPT 80

                         90       100
                 ....*....|....*....|....*..
gi 581121380 191 QTGTFRGRNSNFNGEGFSRQTFKVNAV 217
Cdd:cd13919   81 REGEYEVRCAELCGLGHYRMRATVKVV 107
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 42-226 1.16e-12

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 66.54  E-value: 1.16e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581121380  42 YSIVFMLVICFVVLGMFAIFIYKYSYNKNAESGKMhhnaiIETIWFVIPIIIVAALAIPTVKTLYDYEKPPKSEkdpMVV 121
Cdd:MTH00168  26 HALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQM-----IEFVWTIIPAFILISLALPSLRLLYLMDEIDKPD---LTI 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581121380 122 YAVsaGYKWFFAY---------------PDEHI--------ETVNTLTIPKDRPVVFKLQAMDTMTSFWIPQLGGQKYAM 178
Cdd:MTH00168  98 KAV--GHQWYWSYeytdyndlefdsymvPTQDLspgqfrllEVDNRLVLPMDSKIRVLVTSADVLHSWTLPSLGLKMDAV 175

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 581121380 179 TGMTMNWTLEASQTGTFRGRNSNFNGEGFSRQTFKVNAVSQKDYDKWV 226
Cdd:MTH00168 176 PGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWV 223
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 44-226 1.24e-11

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 63.72  E-value: 1.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581121380  44 IVFMLVICFVVLGMFAIFIYKYSYNKNAESGKmhhnaiIETIWFVIPIIIVAALAIPTVKTLYDYEKPPKSEkdpMVVYA 123
Cdd:MTH00008  29 LILTLVLTVVGYAMTSLMFNKLSNRYILEAQQ------IETIWTILPALILLFLAFPSLRLLYLMDEVSNPS---ITLKT 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581121380 124 VsaGYKWFFAY---------------PDEH--------IETVNTLTIPKDRPVVFKLQAMDTMTSFWIPQLGGQKYAMTG 180
Cdd:MTH00008 100 I--GHQWYWSYeysdfsnlefdsymlPTSDlspgqfrlLEVDNRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPG 177

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 581121380 181 MTMNWTLEASQTGTFRGRNSNFNGEGFSRQTFKVNAVSQKDYDKWV 226
Cdd:MTH00008 178 RLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWV 223
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 44-227 1.50e-09

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 57.84  E-value: 1.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581121380  44 IVFMLVICFVVLGMFAIfiykysynkNAESGKMHH-----NAIIETIWFVIPIIIVAALAIPTVKTLYDYEKppksEKDP 118
Cdd:MTH00023  36 IMFLLIIIITVVLWLIV---------EALNGKFYDrflvdGTFLEIVWTIIPAVILVFIALPSLKLLYLMDE----VVSP 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581121380 119 -MVVYAVSAGYKWFFAYPDEHIETV-----------------------NTLTIPKDRPVVFKLQAMDTMTSFWIPQLGGQ 174
Cdd:MTH00023 103 aLTIKAIGHQWYWSYEYSDYEGETLefdsymvptsdlnsgdfrllevdNRLVVPINTHVRILVTGADVLHSFAVPSLGLK 182

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 581121380 175 KYAMTGMTMNWTLEASQTGTFRGRNSNFNGEGFSRQTFKVNAVSQKDYDKWVK 227
Cdd:MTH00023 183 IDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLL 235
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 38-228 4.83e-09

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 55.88  E-value: 4.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581121380  38 FLIL---YSIVFMLVICFVVLG-MFAIFIYKYSynknaeSGKMHHNAIIETIWFVIPIIIVAALAIPTVKTLYDYEKPpk 113
Cdd:MTH00139  19 QLIFfhdHAMVILIMILSFVGYiSLSLMSNKFT------SRSLLESQEVETIWTVLPAFILLFLALPSLRLLYLMDEV-- 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581121380 114 seKDPMVVYAVsAGYKWFFAY---------------PDEH--------IETVNTLTIPKDRPVVFKLQAMDTMTSFWIPQ 170
Cdd:MTH00139  91 --SDPYLTFKA-VGHQWYWSYeysdfknlsfdsymiPTEDlssgefrlLEVDNRLVLPYKSNIRALITAADVLHSWTVPS 167

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 581121380 171 LGGQKYAMTGMTMNWTLEASQTGTFRGRNSNFNGEGFSRQTFKVNAVSQKDYDKWVKE 228
Cdd:MTH00139 168 LGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILE 225
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 42-229 5.82e-09

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 55.86  E-value: 5.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581121380  42 YSIVFMLVICFVVLgmFAIFIYKYSYNKNAesgKMHHNAIIETIWFVIPIIIVAALAIPTVKTLYDYEKPPksekDPMV- 120
Cdd:MTH00038  26 YALIILTLITILVF--YGLASLLFSSPTNR---FFLEGQELETIWTIVPAFILIFIALPSLQLLYLMDEVN----NPFLt 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581121380 121 VYAVSAGYKWFFAYPDEH---------------------IETVNTLTIPKDRPVVFKLQAMDTMTSFWIPQLGGQKYAMT 179
Cdd:MTH00038  97 IKAIGHQWYWSYEYTDYNdlefdsymvptsdlstglprlLEVDNRLVLPYQTPIRVLVSSADVLHSWAVPSLGVKMDAVP 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 581121380 180 GMTMNWTLEASQTGTFRGRNSNFNGEGFSRQTFKVNAVSQKDYDKWVKEV 229
Cdd:MTH00038 177 GRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNF 226
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 37-226 1.34e-08

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 55.03  E-value: 1.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581121380  37 KFLILYSIVFMLVICFVVLGMFAIFIYKYSYNKNAESgkmhhnaIIETIWFVIPIIIVAALAIPTVKTLYDYEKPPKSEK 116
Cdd:MTH00027  54 QILFILTIIVGVVLWLIIRILLGNNYYSYYWNKLDGS-------LIEVIWTLIPAFILILIAFPSLRLLYIMDECGFSAN 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581121380 117 DPMVVyavsAGYKWFFAYPDEH-------------------------IETVNTLTIPKDRPVVFKLQAMDTMTSFWIPQL 171
Cdd:MTH00027 127 ITIKV----TGHQWYWSYSYEDygekniefdsymiptadlefgdlrlLEVDNRLILPVDTNVRVLITAADVLHSWTVPSL 202

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 581121380 172 GGQKYAMTGMTMNWTLEASQTGTFRGRNSNFNGEGFSRQTFKVNAVSQKDYDKWV 226
Cdd:MTH00027 203 AVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWI 257
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 45-233 2.38e-08

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 54.02  E-value: 2.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581121380  45 VFMLVICFVVLGMFAIFIYKYSYNKNAESGkmhhnaIIETIWFVIPIIIVAALAIPTVKTLYDYEKPpkseKDPMV-VYA 123
Cdd:MTH00051  32 ILTIIITTVLWLIIRALTTKYYHKYLFEGT------LIEIIWTLIPAAILIFIAFPSLKLLYLMDEV----IDPALtIKA 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581121380 124 VSAGYKWFFAYPDEHIETV-----------------------NTLTIPKDRPVVFKLQAMDTMTSFWIPQLGGQKYAMTG 180
Cdd:MTH00051 102 IGHQWYWSYEYSDYGTDTIefdsymiptsdlnsgdlrllevdNRLIVPIQTQVRVLVTAADVLHSFAVPSLSVKIDAVPG 181

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 581121380 181 MTMNWTLEASQTGTFRGRNSNFNGEGFSRQTFKVNAVSQKDYDKWVKEVKGKK 233
Cdd:MTH00051 182 RLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQSEEI 234
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 44-225 5.43e-08

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 52.97  E-value: 5.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581121380  44 IVFM---LVICFVVLGMFAIFIYKYSYNKNAesgkmhhnaiIETIWFVIPIIIVAALAIPTVKTLYDYEKPpkseKDP-M 119
Cdd:MTH00185  30 IVFListLVLYIIVAMVTTKLTNKYILDSQE----------IEIVWTILPAIILIMIALPSLRILYLMDEI----NDPhL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581121380 120 VVYAVSAGYKWFFAYPDEH---------------------IETVNTLTIPKDRPVVFKLQAMDTMTSFWIPQLGGQKYAM 178
Cdd:MTH00185  96 TIKAMGHQWYWSYEYTDYEqlefdsymtptqdltpgqfrlLETDHRMVVPMESPIRVLITAEDVLHSWTVPALGVKMDAV 175

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 581121380 179 TGMTMNWTLEASQTGTFRGRNSNFNGEGFSRQTFKVNAVSQKDYDKW 225
Cdd:MTH00185 176 PGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 28-103 5.70e-08

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: 50.02  E-value: 5.70e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 581121380   28 AKGPVASSQKFLILYSIVFMLVICFVVLGMFAIFIYKYSYNKNAESGK-MHHNAIIETIWFVIPIIIVAALAIPTVK 103
Cdd:pfam02790  12 AASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRFNRRKNPITARyTTHGQTIEIIWTIIPAVILILIALPSFK 88
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 119-196 1.12e-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: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 49.16  E-value: 1.12e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 581121380 119 MVVYAVSAGYKWFFAYPDEHiETVNTLTIPKDRPVVFKLQAMDTMTSFWIPQLGGQKYAMTGMTMNWTLEASQTGTFR 196
Cdd:cd13915    2 LEIQVTGRQWMWEFTYPNGK-REINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDVVPGRYTYLWFEATKPGEYD 78
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 44-200 1.33e-07

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 51.93  E-value: 1.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581121380  44 IVFMLVICFVVLgmfaIFIYKYSYNKNAESGKMHHNAIiETIWFVIPIIIVAALAIPTVKTLYDYEKPP-KSEKDPMVVy 122
Cdd:MTH00080  30 LFGEFVLAFVVF----LFLYLISNNFYFKSKKIEYQFG-ELLCSVFPVLILLMQMVPSLSLLYYYGLMNlDSNLTVKVT- 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581121380 123 avsaGYKWFFAY--PD---------------------EHIETVNTLTIPKDRPVVFKLQAMDTMTSFWIPQLGGQKYAMT 179
Cdd:MTH00080 104 ----GHQWYWSYefSDipglefdsymksldqlrlgepRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMS 179

                        170       180
                 ....*....|....*....|.
gi 581121380 180 GMTMNWTLEASQTGTFRGRNS 200
Cdd:MTH00080 180 GILSTLCYSFPMPGVFYGQCS 200
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 82-228 3.48e-07

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 50.55  E-value: 3.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581121380  82 IETIWFVIPIIIVAALAIPTVKTLYDYEKPpkseKDP-MVVYAVsaGYKWFFAY---------------PDEH------- 138
Cdd:MTH00076  61 IEMVWTIMPAIILIVIALPSLRILYLMDEI----NDPhLTVKAI--GHQWYWSYeytdyedlsfdsymiPTQDltpgqfr 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581121380 139 -IETVNTLTIPKDRPVVFKLQAMDTMTSFWIPQLGGQKYAMTGMTMNWTLEASQTGTFRGRNSNFNGEGFSRQTFKVNAV 217
Cdd:MTH00076 135 lLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEAT 214

                        170
                 ....*....|.
gi 581121380 218 SQKDYDKWVKE 228
Cdd:MTH00076 215 PLNNFLNWSSS 225
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 82-225 9.20e-07

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 49.33  E-value: 9.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581121380  82 IETIWFVIPIIIVAALAIPTVKTLYDYEKPpkseKDP-MVVYAVSAGYKWFFAYPDEH---------------------I 139
Cdd:MTH00129  61 IEIIWTVLPAVILILIALPSLRILYLMDEI----NDPhLTIKAMGHQWYWSYEYTDYEdlgfdsymiptqdltpgqfrlL 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581121380 140 ETVNTLTIPKDRPVVFKLQAMDTMTSFWIPQLGGQKYAMTGMTMNWTLEASQTGTFRGRNSNFNGEGFSRQTFKVNAVSQ 219
Cdd:MTH00129 137 EADHRMVVPVESPIRVLVSAEDVLHSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPL 216


                 ....*.
gi 581121380 220 KDYDKW 225
Cdd:MTH00129 217 EHFENW 222
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 139-225 1.29e-05

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: 44.10  E-value: 1.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581121380 139 IETVNTLTIPKDRPVVFKLQAMDTMTSFWIPQLGGQKYAMTGMTMNWTLEASQTGTFRGRNSNFNGEGFSRQTFKVNAVS 218
Cdd:cd13912   44 LEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVS 123


                 ....*..
gi 581121380 219 QKDYDKW 225
Cdd:cd13912  124 LEDFLSW 130
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 27-227 2.63e-05

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 44.90  E-value: 2.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581121380  27 NAKGPVASSQKFLILYSIVFMLVICFVVLgMFAIFIYkysynknaeSGKMHHNAI-----IETIWFVIPIIIVAALAIPT 101
Cdd:MTH00117  11 DASSPIMEELLFFHDHALMVALLISSLVL-YLLTLML---------TTKLTHTNTvdaqeVELIWTILPAIVLILLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581121380 102 VKTLYDYEKPpkseKDP-MVVYAVsaGYKWFFAY--------------------PDEH---IETVNTLTIPKDRPVVFKL 157
Cdd:MTH00117  81 LRILYLMDEI----NNPhLTIKAI--GHQWYWSYeytdykdlsfdsymiptqdlPNGHfrlLEVDHRMVIPMESPIRILI 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581121380 158 QAMDTMTSFWIPQLGGQKYAMTGMTMNWTLEASQTGTFRGRNSNFNGEGFSRQTFKVNAVSQKDYDKWVK 227
Cdd:MTH00117 155 TAEDVLHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSS 224
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 44-172 3.35e-05

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 44.43  E-value: 3.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581121380  44 IVFMLVICFVVLGMFAIFIYKYSyNKNaesgkMHHNAIIETIWFVIPIIIVAALAIPTVKTLYDYEKppksEKDPMVVYA 123
Cdd:MTH00154  29 MILIMITILVGYMMISLLFNKFT-NRF-----LLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDE----VNNPSITLK 98

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 581121380 124 VsAGYKWFFAY---------------PDEH--------IETVNTLTIPKDRPVVFKLQAMDTMTSFWIPQLG 172
Cdd:MTH00154  99 T-IGHQWYWSYeysdfkniefdsymiPTNElenngfrlLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLG 169
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 44-227 4.16e-05

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 44.16  E-value: 4.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581121380  44 IVFMLVICFVVLGMFAIFIYKYSYNKNAESGKmhhnaiIETIWFVIPIIIVAALAIPTVKTLYDYEKPpkseKDPMVVya 123
Cdd:MTH00140  29 VVLVLIFSFVMYMLVLLLFNKFSCRTILEAQK------LETIWTIVPALILVFLALPSLRLLYLLDET----NNPLLT-- 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581121380 124 VSA-GYKWFFAY--PDEHIETVNTLTIPK-------------DRPVVFKLQ--------AMDTMTSFWIPQLGGQKYAMT 179
Cdd:MTH00140  97 VKAiGHQWYWSYeySDFSVIEFDSYMVPEnelelgdfrllevDNRLVLPYSvdtrvlvtSADVIHSWTVPSLGVKVDAIP 176

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 581121380 180 GMTMNWTLEASQTGTFRGRNSNFNGEGFSRQTFKVNAVSQKDYDKWVK 227
Cdd:MTH00140 177 GRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLE 224
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
119-217 3.16e-04

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 40.09  E-value: 3.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581121380  119 MVVYAVsaGYKWF--FAYPD---------------------EHIETVNTLTIPKDRPVVFKLQAMDTMTSFWIPQLGGQK 175
Cdd:pfam00116   1 LTIKAI--GHQWYwsYEYTDfgdlefdsymiptedleegqlRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKT 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 581121380  176 YAMTGMTMNWTLEASQTGTFRGRNSNFNGEGFSRQTFKVNAV 217
Cdd:pfam00116  79 DAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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