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Conserved domains on  [gi|1901179613|dbj|GGC30853|]
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ubiquinol oxidase subunit 2 [Asaia siamensis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 110-208 1.07e-55

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: 174.66  E-value: 1.07e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901179613 110 LQVEVVALNWKWLFIYPEAHVASLDHLVLPQGREVEFHLTSDGTMQSFLIPSLGSQIYAMAGMVTHLHLQADRTGRLLGE 189
Cdd:cd04212     1 LEIQVVSLDWKWLFIYPEQGIATVNELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGL 80

                          90
                  ....*....|....*....
gi 1901179613 190 NTQFNGMGFQDQKFPVDIV 208
Cdd:cd04212    81 SANYSGEGFSDMKFKVLAV 99
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
8-224 1.47e-55

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


:

Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 178.87  E-value: 1.47e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901179613   8 ADHISFLDPAGPVAALQKHWFLLLSGGLLLVILPVLIGVPLCLWHYRASNRRARfLPDWDFALPLEFLVWGFPAVVVIAf 87
Cdd:COG1622    16 SGQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIRYRRRKGDAD-PAQFHHNTKLEIVWTVIPIIIVIV- 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901179613  88 sLLVWGperrFSPERAIGDAP--PLQVEVVALNWKWLFIYPEAHVASLDHLVLPQGREVEFHLTSDGTMQSFLIPSLGSQ 165
Cdd:COG1622    94 -LAVPT----LRVLHALDDAPedPLTVEVTGYQWKWLFRYPDQGIATVNELVLPVGRPVRFLLTSADVIHSFWVPALGGK 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1901179613 166 IYAMAGMVTHLHLQADRTGRLLGENTQFNGMGFQDQKFPVDIVSPDQFAQWLAKAGSSP 224
Cdd:COG1622   169 QDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQKASA 227
 
Name Accession Description Interval E-value
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 110-208 1.07e-55

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: 174.66  E-value: 1.07e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901179613 110 LQVEVVALNWKWLFIYPEAHVASLDHLVLPQGREVEFHLTSDGTMQSFLIPSLGSQIYAMAGMVTHLHLQADRTGRLLGE 189
Cdd:cd04212     1 LEIQVVSLDWKWLFIYPEQGIATVNELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGL 80

                          90
                  ....*....|....*....
gi 1901179613 190 NTQFNGMGFQDQKFPVDIV 208
Cdd:cd04212    81 SANYSGEGFSDMKFKVLAV 99
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
8-224 1.47e-55

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 178.87  E-value: 1.47e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901179613   8 ADHISFLDPAGPVAALQKHWFLLLSGGLLLVILPVLIGVPLCLWHYRASNRRARfLPDWDFALPLEFLVWGFPAVVVIAf 87
Cdd:COG1622    16 SGQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIRYRRRKGDAD-PAQFHHNTKLEIVWTVIPIIIVIV- 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901179613  88 sLLVWGperrFSPERAIGDAP--PLQVEVVALNWKWLFIYPEAHVASLDHLVLPQGREVEFHLTSDGTMQSFLIPSLGSQ 165
Cdd:COG1622    94 -LAVPT----LRVLHALDDAPedPLTVEVTGYQWKWLFRYPDQGIATVNELVLPVGRPVRFLLTSADVIHSFWVPALGGK 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1901179613 166 IYAMAGMVTHLHLQADRTGRLLGENTQFNGMGFQDQKFPVDIVSPDQFAQWLAKAGSSP 224
Cdd:COG1622   169 QDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQKASA 227
PRK10525 PRK10525
cytochrome o ubiquinol oxidase subunit II; Provisional
 51-278 1.22e-54

cytochrome o ubiquinol oxidase subunit II; Provisional


Pssm-ID: 182518 [Multi-domain]  Cd Length: 315  Bit Score: 179.22  E-value: 1.22e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901179613  51 WHYRASNRRARFLPDWDFALPLEFLVWGFPAVVVIAFSLLVWGPERRFSPERAI-GDAPPLQVEVVALNWKWLFIYPEAH 129
Cdd:PRK10525   67 WKYRASNKDAKYSPNWSHSNKVEAVVWTVPILIIIFLAVLTWKTTHALEPSKPLaHDEKPITIEVVSMDWKWFFIYPEQG 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901179613 130 VASLDHLVLPQGREVEFHLTSDGTMQSFLIPSLGSQIYAMAGMVTHLHLQADRTGRLLGENTQFNGMGFQDQKFPVdIVS 209
Cdd:PRK10525  147 IATVNEIAFPANVPVYFKVTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIANEPGTYDGISASYSGPGFSGMKFKA-IAT 225

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1901179613 210 PDQ--FAQWLAKAGSSPLQLDT-QSYDILrrqetgrksaqtllhdAKASD----AIFSSVPERFFQGIV---MHYDASM 278
Cdd:PRK10525  226 PDRaeFDQWVAKAKQSPNTMNDmAAFEKL----------------AAPSEynpvEYFSSVKPDLFKDVInkfMGHGKSM 288
CyoA TIGR01433
cytochrome o ubiquinol oxidase subunit II; This enzyme catalyzes the oxidation of ubiquinol ...
 51-220 4.75e-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: 175.01  E-value: 4.75e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901179613  51 WHYRASNRRARFLPDWDFALPLEFLVWGFPAVVVIAFSLLVWGPERRFSPERAI-GDAPPLQVEVVALNWKWLFIYPEAH 129
Cdd:TIGR01433  55 WKYRATNKDADYSPNWHHSTKIEIVVWTIPILIIIFLGVLTWITTHKLDPYRPLaSDVKPITIEVVALDWKWLFIYPEQG 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901179613 130 VASLDHLVLPQGREVEFHLTSDGTMQSFLIPSLGSQIYAMAGMVTHLHLQADRTGRLLGENTQFNGMGFQDQKFPVDIVS 209
Cdd:TIGR01433 135 IATVNEIAFPVNTPINFKITSNSVMNSFFIPQLGSQIYAMAGMQTKLHLIANEPGVYDGISANYSGPGFSGMKFKAIATD 214

                         170
                  ....*....|.
gi 1901179613 210 PDQFAQWLAKA 220
Cdd:TIGR01433 215 RAAFDQWVAKA 225
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 133-219 9.82e-04

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 39.84  E-value: 9.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901179613 133 LDH-LVLPQGREVEFHLTSDGTMQSFLIPSLGSQIYAMAGMVTHLHLQADRTGRLLGENTQFNGMGFQDQKFPVDIVSPD 211
Cdd:MTH00008  138 VDNrAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTK 217


                  ....*...
gi 1901179613 212 QFAQWLAK 219
Cdd:MTH00008  218 SFMKWVSS 225
 
Name Accession Description Interval E-value
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 110-208 1.07e-55

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: 174.66  E-value: 1.07e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901179613 110 LQVEVVALNWKWLFIYPEAHVASLDHLVLPQGREVEFHLTSDGTMQSFLIPSLGSQIYAMAGMVTHLHLQADRTGRLLGE 189
Cdd:cd04212     1 LEIQVVSLDWKWLFIYPEQGIATVNELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGL 80

                          90
                  ....*....|....*....
gi 1901179613 190 NTQFNGMGFQDQKFPVDIV 208
Cdd:cd04212    81 SANYSGEGFSDMKFKVLAV 99
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
8-224 1.47e-55

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 178.87  E-value: 1.47e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901179613   8 ADHISFLDPAGPVAALQKHWFLLLSGGLLLVILPVLIGVPLCLWHYRASNRRARfLPDWDFALPLEFLVWGFPAVVVIAf 87
Cdd:COG1622    16 SGQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIRYRRRKGDAD-PAQFHHNTKLEIVWTVIPIIIVIV- 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901179613  88 sLLVWGperrFSPERAIGDAP--PLQVEVVALNWKWLFIYPEAHVASLDHLVLPQGREVEFHLTSDGTMQSFLIPSLGSQ 165
Cdd:COG1622    94 -LAVPT----LRVLHALDDAPedPLTVEVTGYQWKWLFRYPDQGIATVNELVLPVGRPVRFLLTSADVIHSFWVPALGGK 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1901179613 166 IYAMAGMVTHLHLQADRTGRLLGENTQFNGMGFQDQKFPVDIVSPDQFAQWLAKAGSSP 224
Cdd:COG1622   169 QDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQKASA 227
PRK10525 PRK10525
cytochrome o ubiquinol oxidase subunit II; Provisional
 51-278 1.22e-54

cytochrome o ubiquinol oxidase subunit II; Provisional


Pssm-ID: 182518 [Multi-domain]  Cd Length: 315  Bit Score: 179.22  E-value: 1.22e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901179613  51 WHYRASNRRARFLPDWDFALPLEFLVWGFPAVVVIAFSLLVWGPERRFSPERAI-GDAPPLQVEVVALNWKWLFIYPEAH 129
Cdd:PRK10525   67 WKYRASNKDAKYSPNWSHSNKVEAVVWTVPILIIIFLAVLTWKTTHALEPSKPLaHDEKPITIEVVSMDWKWFFIYPEQG 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901179613 130 VASLDHLVLPQGREVEFHLTSDGTMQSFLIPSLGSQIYAMAGMVTHLHLQADRTGRLLGENTQFNGMGFQDQKFPVdIVS 209
Cdd:PRK10525  147 IATVNEIAFPANVPVYFKVTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIANEPGTYDGISASYSGPGFSGMKFKA-IAT 225

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1901179613 210 PDQ--FAQWLAKAGSSPLQLDT-QSYDILrrqetgrksaqtllhdAKASD----AIFSSVPERFFQGIV---MHYDASM 278
Cdd:PRK10525  226 PDRaeFDQWVAKAKQSPNTMNDmAAFEKL----------------AAPSEynpvEYFSSVKPDLFKDVInkfMGHGKSM 288
CyoA TIGR01433
cytochrome o ubiquinol oxidase subunit II; This enzyme catalyzes the oxidation of ubiquinol ...
 51-220 4.75e-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: 175.01  E-value: 4.75e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901179613  51 WHYRASNRRARFLPDWDFALPLEFLVWGFPAVVVIAFSLLVWGPERRFSPERAI-GDAPPLQVEVVALNWKWLFIYPEAH 129
Cdd:TIGR01433  55 WKYRATNKDADYSPNWHHSTKIEIVVWTIPILIIIFLGVLTWITTHKLDPYRPLaSDVKPITIEVVALDWKWLFIYPEQG 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901179613 130 VASLDHLVLPQGREVEFHLTSDGTMQSFLIPSLGSQIYAMAGMVTHLHLQADRTGRLLGENTQFNGMGFQDQKFPVDIVS 209
Cdd:TIGR01433 135 IATVNEIAFPVNTPINFKITSNSVMNSFFIPQLGSQIYAMAGMQTKLHLIANEPGVYDGISANYSGPGFSGMKFKAIATD 214

                         170
                  ....*....|.
gi 1901179613 210 PDQFAQWLAKA 220
Cdd:TIGR01433 215 RAAFDQWVAKA 225
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 84-218 1.82e-20

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: 86.67  E-value: 1.82e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901179613  84 VIAFSLLVWGPERRFSPERAIgDAPPLQVEVVALNWKWLFIYPEAHVASLDHLVLPQGREVEFHLTSDGTMQSFLIPSLG 163
Cdd:TIGR02866  66 IIVVGLFAATAKGLLYLERPI-PKDALKVKVTGYQWWWDFEYPESGFTTVNELVLPAGTPVELQVTSKDVIHSFWVPELG 144

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1901179613 164 SQIYAMAGMVTHLHLQADRTGRLLGENTQFNGMGFQDQKFPVDIVSPDQFAQWLA 218
Cdd:TIGR02866 145 GKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 111-217 2.50e-19

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


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 80.92  E-value: 2.50e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901179613 111 QVEVVALNWKWLFIYPEAHVASLDHLVLPQGREVEFHLTSDGTMQSFLIPSLGSQIYAMAGMVTHLHLQADRTGRLLGEN 190
Cdd:cd13914     2 EIEVEAYQWGWEFSYPEANVTTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAFPGQYNTIKTEATEEGEYQLYC 81

                          90       100
                  ....*....|....*....|....*..
gi 1901179613 191 TQFNGMGFQDQKFPVDIVSPDQFAQWL 217
Cdd:cd13914    82 AEYCGAGHSQMLSTVTVVSQDEYQQWL 108
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 110-205 6.39e-18

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: 76.95  E-value: 6.39e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901179613 110 LQVEVVALNWKWLFIYPEahVASLDHLVLPQGREVEFHLTSDGTMQSFLIPSLGSQIYAMAGMVTHLHLQADRTGRLLGE 189
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPN--VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDAVPGYTSELWFVADKPGTYTII 78

                          90
                  ....*....|....*.
gi 1901179613 190 NTQFNGMGFQDQKFPV 205
Cdd:cd13842    79 CAEYCGLGHSYMLGKV 94
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 109-205 3.25e-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: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 72.67  E-value: 3.25e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901179613 109 PLQVEVVALNWKWLFIYPEAHVAS-------LDHLVLPQGREVEFHLTSDGTMQSFLIPSLGSQIYAMAGMVTHLHLQAD 181
Cdd:cd13919     1 ALVVEVTAQQWAWTFRYPGGDGKLgtdddvtSPELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDAVPGRTTRLWFTPT 80

                          90       100
                  ....*....|....*....|....
gi 1901179613 182 RTGRLLGENTQFNGMGFQDQKFPV 205
Cdd:cd13919    81 REGEYEVRCAELCGLGHYRMRATV 104
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 109-198 5.10e-15

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: 69.19  E-value: 5.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901179613 109 PLQVEVVALNWKWLFIYPEAH---VASLDHLVLPQGREVEFHLTSDGTMQSFLIPSLGSQIYAMAGMVTHLHLQADRTGR 185
Cdd:cd04213     1 ALTIEVTGHQWWWEFRYPDEPgrgIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDMIPGRTNRLWLQADEPGV 80

                          90
                  ....*....|....*...
gi 1901179613 186 LLGENTQFNG-----MGF 198
Cdd:cd04213    81 YRGQCAEFCGashalMRF 98
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 110-184 1.06e-10

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: 57.25  E-value: 1.06e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1901179613 110 LQVEVVALNWKWLFIYPEAHVASlDHLVLPQGREVEFHLTSDGTMQSFLIPSLGSQIYAMAGMVTHLHLQADRTG 184
Cdd:cd13915     2 LEIQVTGRQWMWEFTYPNGKREI-NELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDVVPGRYTYLWFEATKPG 75
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 78-217 3.61e-10

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: 57.08  E-value: 3.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901179613  78 GFPAVVVIafSLLVWGPERRF----SPERAIGDapPLQVEVVALNWKWLFIYPEAhVASLDHLVLPQGREVEFHLTSDGT 153
Cdd:cd13918     1 GLSAIIVI--SLIVWTYGMLLyvedPPDEADED--ALEVEVEGFQFGWQFEYPNG-VTTGNTLRVPADTPIALRVTSTDV 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1901179613 154 MQSFLIPSLGSQIYAMAGMVTHLHLQADRTGRLLGENTQFNGMGFQDQKFPVDIVSPDQFAQWL 217
Cdd:cd13918    76 FHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAWY 139
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 133-219 9.82e-04

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 39.84  E-value: 9.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901179613 133 LDH-LVLPQGREVEFHLTSDGTMQSFLIPSLGSQIYAMAGMVTHLHLQADRTGRLLGENTQFNGMGFQDQKFPVDIVSPD 211
Cdd:MTH00008  138 VDNrAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTK 217


                  ....*...
gi 1901179613 212 QFAQWLAK 219
Cdd:MTH00008  218 SFMKWVSS 225
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 136-218 4.86e-03

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 37.45  E-value: 4.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901179613 136 LVLPQGREVEFHLTSDGTMQSFLIPSLGSQIYAMAGMVTHLHLQADRTGRLLGENTQFNGMGFQDQKFPVDIVSPDQFAQ 215
Cdd:MTH00051  146 LIVPIQTQVRVLVTAADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYIN 225


                  ...
gi 1901179613 216 WLA 218
Cdd:MTH00051  226 WVA 228
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 134-217 8.40e-03

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 36.62  E-value: 8.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901179613 134 DH-LVLPQGREVEFHLTSDGTMQSFLIPSLGSQIYAMAGMVTHLHLQADRTGRLLGENTQFNGMGFQDQKFPVDIVSPDQ 212
Cdd:MTH00139  139 DNrLVLPYKSNIRALITAADVLHSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKF 218


                  ....*
gi 1901179613 213 FAQWL 217
Cdd:MTH00139  219 FLEWI 223
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 108-217 8.55e-03

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 37.04  E-value: 8.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901179613 108 PPLQVEVVALNWKWLFIYPEAHVASLD-----------------------HLVLPQGREVEFHLTSDGTMQSFLIPSLGS 164
Cdd:MTH00023  102 PALTIKAIGHQWYWSYEYSDYEGETLEfdsymvptsdlnsgdfrllevdnRLVVPINTHVRILVTGADVLHSFAVPSLGL 181

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1901179613 165 QIYAMAGMVTHLHLQADRTGRLLGENTQFNGMGFQDQKFPVDIVSPDQFAQWL 217
Cdd:MTH00023  182 KIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWL 234
 
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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