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Conserved domains on  [gi|2095950267|ref|WP_223157542|]
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cytochrome aa3 quinol oxidase subunit II [Listeria innocua]

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 ...
 6-230 5.71e-160

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: 447.05  E-value: 5.71e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095950267   6 LLGVTGLISGCGDLTVLNPKGPVAKGQSDLIIYSIIFMLVIVLTIFVLFTIMLVKYRERKDISNYEPDMHGSRKLEIFWT 85
Cdd:TIGR01432   2 LLTVVFVLSGCSNIEVLNPKGPVASSQSDLILYSIVFMLVIVFVVFVLFTIFLVKYRYRKDNGAYSPKMHGNAILETIWT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095950267  86 LIPVAIVIALAIPTVKTIYAGEEAPKVTSHKDPIVIYATSADWKWIFSYPDESIETVNYVNIPTDRPVLFKLTSADTMTS 165
Cdd:TIGR01432  82 VIPIIIVIALAIPTVKTIYDYEKAPKSTKEKDPMVVYATSADWKWFFSYPDEHIETVNYLNIPKDRPVLFKLQSADTMTS 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2095950267 166 FWVPQLGGQKYAMSGMTMNLYLQADEVGTYKGRNANFNGEGFADQRFDVVAQSEKDFKKWAKETK 230
Cdd:TIGR01432 162 FWIPQLGGQKYAMTGMTMNWYLQADEVGTYRGRNANFNGEGFADQTFDVNAVSEKDFDKWVKETK 226
 
Name Accession Description Interval E-value
QOXA TIGR01432
cytochrome aa3 quinol oxidase, subunit II; This enzyme catalyzes the oxidation of quinol with ...
 6-230 5.71e-160

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: 447.05  E-value: 5.71e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095950267   6 LLGVTGLISGCGDLTVLNPKGPVAKGQSDLIIYSIIFMLVIVLTIFVLFTIMLVKYRERKDISNYEPDMHGSRKLEIFWT 85
Cdd:TIGR01432   2 LLTVVFVLSGCSNIEVLNPKGPVASSQSDLILYSIVFMLVIVFVVFVLFTIFLVKYRYRKDNGAYSPKMHGNAILETIWT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095950267  86 LIPVAIVIALAIPTVKTIYAGEEAPKVTSHKDPIVIYATSADWKWIFSYPDESIETVNYVNIPTDRPVLFKLTSADTMTS 165
Cdd:TIGR01432  82 VIPIIIVIALAIPTVKTIYDYEKAPKSTKEKDPMVVYATSADWKWFFSYPDEHIETVNYLNIPKDRPVLFKLQSADTMTS 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2095950267 166 FWVPQLGGQKYAMSGMTMNLYLQADEVGTYKGRNANFNGEGFADQRFDVVAQSEKDFKKWAKETK 230
Cdd:TIGR01432 162 FWIPQLGGQKYAMTGMTMNWYLQADEVGTYRGRNANFNGEGFADQTFDVNAVSEKDFDKWVKETK 226
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-234 3.93e-91

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 272.47  E-value: 3.93e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095950267   1 MLLTVLLGVTGLISGCGDLTVLNPKGPVAKGQSDLIIYSIIFMLVIVLTIFVLFTIMLVKYRERKDiSNYEPDMHGSRKL 80
Cdd:COG1622     1 MKRLLLALLLLALLLSGQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIRYRRRKG-DADPAQFHHNTKL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095950267  81 EIFWTLIPVAIVIALAIPTVKTIYAGEEAPKvtshkDPIVIYATSADWKWIFSYPDESIETVNYVNIPTDRPVLFKLTSA 160
Cdd:COG1622    80 EIVWTVIPIIIVIVLAVPTLRVLHALDDAPE-----DPLTVEVTGYQWKWLFRYPDQGIATVNELVLPVGRPVRFLLTSA 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2095950267 161 DTMTSFWVPQLGGQKYAMSGMTMNLYLQADEVGTYKGRNANFNGEGFADQRFDVVAQSEKDFKKWAKETKANSP 234
Cdd:COG1622   155 DVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQKASAA 228
PRK10525 PRK10525
cytochrome o ubiquinol oxidase subunit II; Provisional
 6-255 1.25e-59

cytochrome o ubiquinol oxidase subunit II; Provisional


Pssm-ID: 182518 [Multi-domain]  Cd Length: 315  Bit Score: 195.02  E-value: 1.25e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095950267   6 LLGVTGLISGCgDLTVLNPKGPVAKGQSDLIIYSIIFMLVIVLTIFVLFTIMLVKYRERKDISNYEPDMHGSRKLE-IFW 84
Cdd:PRK10525   15 LFAGTVLLSGC-NSALLDPKGQIGLEQRSLILTAFGLMLIVVIPAILMAVGFAWKYRASNKDAKYSPNWSHSNKVEaVVW 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095950267  85 TlIPVAIVIALAIPTVKTIYAGEEAPKVTSHKDPIVIYATSADWKWIFSYPDESIETVNYVNIPTDRPVLFKLTSADTMT 164
Cdd:PRK10525   94 T-VPILIIIFLAVLTWKTTHALEPSKPLAHDEKPITIEVVSMDWKWFFIYPEQGIATVNEIAFPANVPVYFKVTSNSVMN 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095950267 165 SFWVPQLGGQKYAMSGMTMNLYLQADEVGTYKGRNANFNGEGFADQRFDVVAQ-SEKDFKKWAKETKANSPVI-TQDTYD 242
Cdd:PRK10525  173 SFFIPRLGSQIYAMAGMQTRLHLIANEPGTYDGISASYSGPGFSGMKFKAIATpDRAEFDQWVAKAKQSPNTMnDMAAFE 252

                         250
                  ....*....|...
gi 2095950267 243 RLLIPGSSKKKTY 255
Cdd:PRK10525  253 KLAAPSEYNPVEY 265
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 119-216 1.11e-56

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: 179.67  E-value: 1.11e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095950267 119 IVIYATSADWKWIFSYPDESIETVNYVNIPTDRPVLFKLTSADTMTSFWVPQLGGQKYAMSGMTMNLYLQADEVGTYKGR 198
Cdd:cd04212     1 LEIQVVSLDWKWLFIYPEQGIATVNELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGL 80

                          90
                  ....*....|....*...
gi 2095950267 199 NANFNGEGFADQRFDVVA 216
Cdd:cd04212    81 SANYSGEGFSDMKFKVLA 98
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 27-101 1.56e-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: 51.56  E-value: 1.56e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2095950267  27 PVAKGQSDLIIYSIIFMLVIVLTIFVLFTIMLVKYRERKDISNYEPDMHGSrKLEIFWTLIPVAIVIALAIPTVK 101
Cdd:pfam02790  15 PLMEGLLELHDYIMFILTLILILVLYILVTCLIRFNRRKNPITARYTTHGQ-TIEIIWTIIPAVILILIALPSFK 88
 
Name Accession Description Interval E-value
QOXA TIGR01432
cytochrome aa3 quinol oxidase, subunit II; This enzyme catalyzes the oxidation of quinol with ...
 6-230 5.71e-160

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: 447.05  E-value: 5.71e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095950267   6 LLGVTGLISGCGDLTVLNPKGPVAKGQSDLIIYSIIFMLVIVLTIFVLFTIMLVKYRERKDISNYEPDMHGSRKLEIFWT 85
Cdd:TIGR01432   2 LLTVVFVLSGCSNIEVLNPKGPVASSQSDLILYSIVFMLVIVFVVFVLFTIFLVKYRYRKDNGAYSPKMHGNAILETIWT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095950267  86 LIPVAIVIALAIPTVKTIYAGEEAPKVTSHKDPIVIYATSADWKWIFSYPDESIETVNYVNIPTDRPVLFKLTSADTMTS 165
Cdd:TIGR01432  82 VIPIIIVIALAIPTVKTIYDYEKAPKSTKEKDPMVVYATSADWKWFFSYPDEHIETVNYLNIPKDRPVLFKLQSADTMTS 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2095950267 166 FWVPQLGGQKYAMSGMTMNLYLQADEVGTYKGRNANFNGEGFADQRFDVVAQSEKDFKKWAKETK 230
Cdd:TIGR01432 162 FWIPQLGGQKYAMTGMTMNWYLQADEVGTYRGRNANFNGEGFADQTFDVNAVSEKDFDKWVKETK 226
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-234 3.93e-91

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 272.47  E-value: 3.93e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095950267   1 MLLTVLLGVTGLISGCGDLTVLNPKGPVAKGQSDLIIYSIIFMLVIVLTIFVLFTIMLVKYRERKDiSNYEPDMHGSRKL 80
Cdd:COG1622     1 MKRLLLALLLLALLLSGQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIRYRRRKG-DADPAQFHHNTKL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095950267  81 EIFWTLIPVAIVIALAIPTVKTIYAGEEAPKvtshkDPIVIYATSADWKWIFSYPDESIETVNYVNIPTDRPVLFKLTSA 160
Cdd:COG1622    80 EIVWTVIPIIIVIVLAVPTLRVLHALDDAPE-----DPLTVEVTGYQWKWLFRYPDQGIATVNELVLPVGRPVRFLLTSA 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2095950267 161 DTMTSFWVPQLGGQKYAMSGMTMNLYLQADEVGTYKGRNANFNGEGFADQRFDVVAQSEKDFKKWAKETKANSP 234
Cdd:COG1622   155 DVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQKASAA 228
CyoA TIGR01433
cytochrome o ubiquinol oxidase subunit II; This enzyme catalyzes the oxidation of ubiquinol ...
 6-230 1.69e-64

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: 204.29  E-value: 1.69e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095950267   6 LLGVTGLISGCgDLTVLNPKGPVAKGQSDLIIYSIIFMLVIVLTIFVLFTIMLVKYRERKDISNYEPDMHGSRKLEIFWT 85
Cdd:TIGR01433   3 LIAASLLLSGC-NLVLLDPKGQIGLEERSLILTAFGLMLLVVIPVILMTLFFAWKYRATNKDADYSPNWHHSTKIEIVVW 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095950267  86 LIPVAIVIALAIPTVKTIYAGEEAPKVTSHKDPIVIYATSADWKWIFSYPDESIETVNYVNIPTDRPVLFKLTSADTMTS 165
Cdd:TIGR01433  82 TIPILIIIFLGVLTWITTHKLDPYRPLASDVKPITIEVVALDWKWLFIYPEQGIATVNEIAFPVNTPINFKITSNSVMNS 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2095950267 166 FWVPQLGGQKYAMSGMTMNLYLQADEVGTYKGRNANFNGEGFADQRFDVVAQSEKDFKKWAKETK 230
Cdd:TIGR01433 162 FFIPQLGSQIYAMAGMQTKLHLIANEPGVYDGISANYSGPGFSGMKFKAIATDRAAFDQWVAKAK 226
PRK10525 PRK10525
cytochrome o ubiquinol oxidase subunit II; Provisional
 6-255 1.25e-59

cytochrome o ubiquinol oxidase subunit II; Provisional


Pssm-ID: 182518 [Multi-domain]  Cd Length: 315  Bit Score: 195.02  E-value: 1.25e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095950267   6 LLGVTGLISGCgDLTVLNPKGPVAKGQSDLIIYSIIFMLVIVLTIFVLFTIMLVKYRERKDISNYEPDMHGSRKLE-IFW 84
Cdd:PRK10525   15 LFAGTVLLSGC-NSALLDPKGQIGLEQRSLILTAFGLMLIVVIPAILMAVGFAWKYRASNKDAKYSPNWSHSNKVEaVVW 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095950267  85 TlIPVAIVIALAIPTVKTIYAGEEAPKVTSHKDPIVIYATSADWKWIFSYPDESIETVNYVNIPTDRPVLFKLTSADTMT 164
Cdd:PRK10525   94 T-VPILIIIFLAVLTWKTTHALEPSKPLAHDEKPITIEVVSMDWKWFFIYPEQGIATVNEIAFPANVPVYFKVTSNSVMN 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095950267 165 SFWVPQLGGQKYAMSGMTMNLYLQADEVGTYKGRNANFNGEGFADQRFDVVAQ-SEKDFKKWAKETKANSPVI-TQDTYD 242
Cdd:PRK10525  173 SFFIPRLGSQIYAMAGMQTRLHLIANEPGTYDGISASYSGPGFSGMKFKAIATpDRAEFDQWVAKAKQSPNTMnDMAAFE 252

                         250
                  ....*....|...
gi 2095950267 243 RLLIPGSSKKKTY 255
Cdd:PRK10525  253 KLAAPSEYNPVEY 265
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 119-216 1.11e-56

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: 179.67  E-value: 1.11e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095950267 119 IVIYATSADWKWIFSYPDESIETVNYVNIPTDRPVLFKLTSADTMTSFWVPQLGGQKYAMSGMTMNLYLQADEVGTYKGR 198
Cdd:cd04212     1 LEIQVVSLDWKWLFIYPEQGIATVNELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGL 80

                          90
                  ....*....|....*...
gi 2095950267 199 NANFNGEGFADQRFDVVA 216
Cdd:cd04212    81 SANYSGEGFSDMKFKVLA 98
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 24-225 1.38e-40

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: 141.75  E-value: 1.38e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095950267  24 PKGPVAKGQSDLIIYSIIFMLVIVLTIFVLFTIMLVKYRERKDisNYEPDM-HGSRKLEIFWTLIPVAIVIALAIPTVKT 102
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVWKFRRKGD--EEKPSQiHGNRRLEYVWTVIPLIIVVGLFAATAKG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095950267 103 IYAGEEAPKvtshKDPIVIYATSADWKWIFSYPDESIETVNYVNIPTDRPVLFKLTSADTMTSFWVPQLGGQKYAMSGMT 182
Cdd:TIGR02866  79 LLYLERPIP----KDALKVKVTGYQWWWDFEYPESGFTTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQT 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2095950267 183 MNLYLQADEVGTYKGRNANFNGEGFADQRFDVVAQSEKDFKKW 225
Cdd:TIGR02866 155 NALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAY 197
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 118-217 4.67e-28

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: 105.39  E-value: 4.67e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095950267 118 PIVIYATSADWKWIFSYPDES---IETVNYVNIPTDRPVLFKLTSADTMTSFWVPQLGGQKYAMSGMTMNLYLQADEVGT 194
Cdd:cd04213     1 ALTIEVTGHQWWWEFRYPDEPgrgIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDMIPGRTNRLWLQADEPGV 80

                          90       100
                  ....*....|....*....|...
gi 2095950267 195 YKGRNANFNGEGFADQRFDVVAQ 217
Cdd:cd04213    81 YRGQCAEFCGASHALMRFKVIAL 103
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 119-215 2.49e-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: 81.57  E-value: 2.49e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095950267 119 IVIYATSADWKWIFSYPDesIETVNYVNIPTDRPVLFKLTSADTMTSFWVPQLGGQKYAMSGMTMNLYLQADEVGTYKGR 198
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPN--VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDAVPGYTSELWFVADKPGTYTII 78

                          90
                  ....*....|....*..
gi 2095950267 199 NANFNGEGFADQRFDVV 215
Cdd:cd13842    79 CAEYCGLGHSYMLGKVE 95
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 118-215 1.06e-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: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 80.38  E-value: 1.06e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095950267 118 PIVIYATSADWKWIFSYPDE-------SIETVNYVNIPTDRPVLFKLTSADTMTSFWVPQLGGQKYAMSGMTMNLYLQAD 190
Cdd:cd13919     1 ALVVEVTAQQWAWTFRYPGGdgklgtdDDVTSPELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDAVPGRTTRLWFTPT 80

                          90       100
                  ....*....|....*....|....*
gi 2095950267 191 EVGTYKGRNANFNGEGFADQRFDVV 215
Cdd:cd13919    81 REGEYEVRCAELCGLGHYRMRATVK 105
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 128-225 1.31e-17

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: 77.45  E-value: 1.31e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095950267 128 WKWIFSYPDESIETVNYVNIPTDRPVLFKLTSADTMTSFWVPQLGGQKYAMSGMTMNLYLQADEVGTYKGRNANFNGEGF 207
Cdd:cd13914    10 WGWEFSYPEANVTTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAFPGQYNTIKTEATEEGEYQLYCAEYCGAGH 89

                          90
                  ....*....|....*...
gi 2095950267 208 ADQRFDVVAQSEKDFKKW 225
Cdd:cd13914    90 SQMLSTVTVVSQDEYQQW 107
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 91-225 3.50e-14

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: 69.02  E-value: 3.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095950267  91 IVIALAIPTV-KTIYAgeEAPKVTSHKDPIVIYATSADWKWIFSYPDEsIETVNYVNIPTDRPVLFKLTSADTMTSFWVP 169
Cdd:cd13918     6 IVISLIVWTYgMLLYV--EDPPDEADEDALEVEVEGFQFGWQFEYPNG-VTTGNTLRVPADTPIALRVTSTDVFHTFGIP 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2095950267 170 QLGGQKYAMSGMTMNLYLQADEVGTYKGRNANFNGEGFADQRFDVVAQSEKDFKKW 225
Cdd:cd13918    83 ELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAW 138
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 119-195 7.28e-11

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: 58.41  E-value: 7.28e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2095950267 119 IVIYATSADWKWIFSYPDESiETVNYVNIPTDRPVLFKLTSADTMTSFWVPQLGGQKYAMSGMTMNLYLQADEVGTY 195
Cdd:cd13915     2 LEIQVTGRQWMWEFTYPNGK-REINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDVVPGRYTYLWFEATKPGEY 77
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 40-228 1.46e-10

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 60.50  E-value: 1.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095950267  40 IIFMLVIVLTIFVLFTIMLVKYRERKDISNYEpdmhgsrkLEIFWTLIPVAIVIALAIPTVKTIYAGEEApkvtshKDP- 118
Cdd:MTH00139   29 VILIMILSFVGYISLSLMSNKFTSRSLLESQE--------VETIWTVLPAFILLFLALPSLRLLYLMDEV------SDPy 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095950267 119 IVIYATSADWKWIFSYPD-ESIETVNYVnIPTD--------------RPVL-------FKLTSADTMTSFWVPQLGGQKY 176
Cdd:MTH00139   95 LTFKAVGHQWYWSYEYSDfKNLSFDSYM-IPTEdlssgefrllevdnRLVLpyksnirALITAADVLHSWTVPSLGVKID 173

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2095950267 177 AMSGMTMNLYLQADEVGTYKGRNANFNGEGFADQRFDVVAQSEKDFKKWAKE 228
Cdd:MTH00139  174 AVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILE 225
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 40-197 8.59e-10

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 58.07  E-value: 8.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095950267  40 IIFMLVIVLTIFVLFTIMLVKYRERkdisNYEpdmhGSRKLEIFWTLIPVAIVIALAIPTVKTIYAGEEAPKvtSHkdpI 119
Cdd:MTH00168   29 LILVLILTLVLYSLLVLVTSKYTNR----FLL----DSQMIEFVWTIIPAFILISLALPSLRLLYLMDEIDK--PD---L 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095950267 120 VIYATSADWKWIFSY-------------PDESI--------ETVNYVNIPTDRPVLFKLTSADTMTSFWVPQLGGQKYAM 178
Cdd:MTH00168   96 TIKAVGHQWYWSYEYtdyndlefdsymvPTQDLspgqfrllEVDNRLVLPMDSKIRVLVTSADVLHSWTLPSLGLKMDAV 175

                         170
                  ....*....|....*....
gi 2095950267 179 SGMTMNLYLQADEVGTYKG 197
Cdd:MTH00168  176 PGRLNQLAFLSSRPGSFYG 194
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 14-172 1.11e-09

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 58.03  E-value: 1.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095950267  14 SGCGDLTVLNPKGPVakgQSDLIIYS----IIFMLVIVLTIFVLFTIMLVKYRERKdisnyepdMHGSRKLEIFWTLIPV 89
Cdd:MTH00140    2 SYWGQLGFQDPASPL---MEELIFFHdhamVVLVLIFSFVMYMLVLLLFNKFSCRT--------ILEAQKLETIWTIVPA 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095950267  90 AIVIALAIPTVKTIYAGEEAPKVTshkdpIVIYATSADWKWIFSYPD------------ESI---------ETVNYVNIP 148
Cdd:MTH00140   71 LILVFLALPSLRLLYLLDETNNPL-----LTVKAIGHQWYWSYEYSDfsviefdsymvpENElelgdfrllEVDNRLVLP 145

                         170       180
                  ....*....|....*....|....
gi 2095950267 149 TDRPVLFKLTSADTMTSFWVPQLG 172
Cdd:MTH00140  146 YSVDTRVLVTSADVIHSWTVPSLG 169
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 40-180 2.52e-09

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 57.07  E-value: 2.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095950267  40 IIFMLVIVLTIFVLFTIMLVKYRerkdisNYEPDMHGSRKLEIFWTLIPVAIVIALAIPTVKTIYAGEE--APKVTshkd 117
Cdd:MTH00023   36 IMFLLIIIITVVLWLIVEALNGK------FYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYLMDEvvSPALT---- 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095950267 118 pivIYATSADWKWIFSYPDESIETV-----------------------NYVNIPTDRPVLFKLTSADTMTSFWVPQLGGQ 174
Cdd:MTH00023  106 ---IKAIGHQWYWSYEYSDYEGETLefdsymvptsdlnsgdfrllevdNRLVVPINTHVRILVTGADVLHSFAVPSLGLK 182


                  ....*.
gi 2095950267 175 KYAMSG 180
Cdd:MTH00023  183 IDAVPG 188
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 40-225 1.25e-08

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 54.86  E-value: 1.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095950267  40 IIFMLVIVLTIFVLFTIMLVKYRERKDISnyepdmhgSRKLEIFWTLIPVAIVIALAIPTVKTIYAGEEAPKVTshkdpI 119
Cdd:MTH00008   29 LILTLVLTVVGYAMTSLMFNKLSNRYILE--------AQQIETIWTILPALILLFLAFPSLRLLYLMDEVSNPS-----I 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095950267 120 VIYATSADWKWIFSYPDES---------------------IETVNYVNIPTDRPVLFKLTSADTMTSFWVPQLGGQKYAM 178
Cdd:MTH00008   96 TLKTIGHQWYWSYEYSDFSnlefdsymlptsdlspgqfrlLEVDNRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDAV 175

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2095950267 179 SGMTMNLYLQADEVGTYKGRNANFNGEGFADQRFDVVAQSEKDFKKW 225
Cdd:MTH00008  176 PGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKW 222
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 38-198 1.36e-08

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 54.71  E-value: 1.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095950267  38 YSIIFM-LVIVLTIFVLFTIMLVKYRERKDISNYEpdmhgsrkLEIFWTLIPVAIVIALAIPTVKTIYAGEEAPkvtshk 116
Cdd:MTH00038   26 YALIILtLITILVFYGLASLLFSSPTNRFFLEGQE--------LETIWTIVPAFILIFIALPSLQLLYLMDEVN------ 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095950267 117 DP-IVIYATSADWKWIFSYPDES---------------------IETVNYVNIPTDRPVLFKLTSADTMTSFWVPQLGGQ 174
Cdd:MTH00038   92 NPfLTIKAIGHQWYWSYEYTDYNdlefdsymvptsdlstglprlLEVDNRLVLPYQTPIRVLVSSADVLHSWAVPSLGVK 171

                         170       180
                  ....*....|....*....|....
gi 2095950267 175 KYAMSGMTMNLYLQADEVGTYKGR 198
Cdd:MTH00038  172 MDAVPGRLNQTTFFISRTGLFYGQ 195
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 27-101 1.56e-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: 51.56  E-value: 1.56e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2095950267  27 PVAKGQSDLIIYSIIFMLVIVLTIFVLFTIMLVKYRERKDISNYEPDMHGSrKLEIFWTLIPVAIVIALAIPTVK 101
Cdd:pfam02790  15 PLMEGLLELHDYIMFILTLILILVLYILVTCLIRFNRRKNPITARYTTHGQ-TIEIIWTIIPAVILILIALPSFK 88
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 40-172 2.06e-08

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 54.06  E-value: 2.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095950267  40 IIFMLVIVLTIFVLFTIMLVKYRERKDISNYEpdmhgsrkLEIFWTLIPVAIVIALAIPTVKTIYAGEEApkvtshKDP- 118
Cdd:MTH00154   29 MILIMITILVGYMMISLLFNKFTNRFLLEGQE--------IEIIWTILPAIILIFIALPSLRLLYLLDEV------NNPs 94

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2095950267 119 IVIYATSADWKWIFSYPD------ES---------------IETVNYVNIPTDRPVLFKLTSADTMTSFWVPQLG 172
Cdd:MTH00154   95 ITLKTIGHQWYWSYEYSDfkniefDSymiptnelenngfrlLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLG 169
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 40-180 2.30e-08

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 54.02  E-value: 2.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095950267  40 IIFMLVIVLT--IFVLFTIMLVKYrerkdisnYEPDMHGSRKLEIFWTLIPVAIVIALAIPTVKTIYAGEEA--PKVTsh 115
Cdd:MTH00051   29 IMFILTIIITtvLWLIIRALTTKY--------YHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYLMDEVidPALT-- 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095950267 116 kdpivIYATSADWKWIFSYPDESIETV-----------------------NYVNIPTDRPVLFKLTSADTMTSFWVPQLG 172
Cdd:MTH00051   99 -----IKAIGHQWYWSYEYSDYGTDTIefdsymiptsdlnsgdlrllevdNRLIVPIQTQVRVLVTAADVLHSFAVPSLS 173


                  ....*...
gi 2095950267 173 GQKYAMSG 180
Cdd:MTH00051  174 VKIDAVPG 181
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 44-180 4.25e-08

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 53.35  E-value: 4.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095950267  44 LVIVLTIFVLFTIMLVKYRERKDISNYEPDmhgSRKLEIFWTLIPVAIVIALAIPTVKTIYAGEEApkvtshKDP-IVIY 122
Cdd:MTH00185   28 LMIVFLISTLVLYIIVAMVTTKLTNKYILD---SQEIEIVWTILPAIILIMIALPSLRILYLMDEI------NDPhLTIK 98

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2095950267 123 ATSADWKWIFSYPD-ESIETVNYVN--------------------IPTDRPVLFKLTSADTMTSFWVPQLGGQKYAMSG 180
Cdd:MTH00185   99 AMGHQWYWSYEYTDyEQLEFDSYMTptqdltpgqfrlletdhrmvVPMESPIRVLITAEDVLHSWTVPALGVKMDAVPG 177
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 43-172 1.12e-07

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 52.02  E-value: 1.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095950267  43 MLVIVLTIFVLFTIMLVkyrerkdISNYEPDMH--GSRKLEIFWTLIPVAIVIALAIPTVKTIYAGEEApkvtshKDP-I 119
Cdd:MTH00129   29 MIVFLISTLVLYIIVAM-------VSTKLTNKYilDSQEIEIIWTVLPAVILILIALPSLRILYLMDEI------NDPhL 95

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2095950267 120 VIYATSADWKWIFSYPDES---------------------IETVNYVNIPTDRPVLFKLTSADTMTSFWVPQLG 172
Cdd:MTH00129   96 TIKAMGHQWYWSYEYTDYEdlgfdsymiptqdltpgqfrlLEADHRMVVPVESPIRVLVSAEDVLHSWAVPALG 169
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 34-186 2.25e-07

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 51.16  E-value: 2.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095950267  34 DLIIYsIIFMLVIVLTIFVLFtIMLVKYRERKDISnyepdmhgSRKLEIFWTLIPVAIVIALAIPTVKTIYAGEE----- 108
Cdd:MTH00080   27 CSLLF-GEFVLAFVVFLFLYL-ISNNFYFKSKKIE--------YQFGELLCSVFPVLILLMQMVPSLSLLYYYGLmnlds 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095950267 109 --APKVTSHKdpiviyatsadWKWIFSYPD-------------------ES--IETVNYVNIPTDRPVLFKLTSADTMTS 165
Cdd:MTH00080   97 nlTVKVTGHQ-----------WYWSYEFSDipglefdsymksldqlrlgEPrlLEVDNRCVLPCDTNIRFCITSSDVIHS 165

                         170       180
                  ....*....|....*....|.
gi 2095950267 166 FWVPQLGGQKYAMSGMtMNLY 186
Cdd:MTH00080  166 WALPSLSIKMDAMSGI-LSTL 185
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 40-180 2.52e-07

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 51.18  E-value: 2.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095950267  40 IIFMLVIVLTIfVLFTIMLVKYRERKdISNYEPDMHGSRkLEIFWTLIPVAIVIALAIPTVKTIYAGEEApkvtSHKDPI 119
Cdd:MTH00027   55 ILFILTIIVGV-VLWLIIRILLGNNY-YSYYWNKLDGSL-IEVIWTLIPAFILILIAFPSLRLLYIMDEC----GFSANI 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095950267 120 VIYATSADWKWIFSYPDES-----------------------IETVNYVNIPTDRPVLFKLTSADTMTSFWVPQLGGQKY 176
Cdd:MTH00027  128 TIKVTGHQWYWSYSYEDYGekniefdsymiptadlefgdlrlLEVDNRLILPVDTNVRVLITAADVLHSWTVPSLAVKMD 207


                  ....
gi 2095950267 177 AMSG 180
Cdd:MTH00027  208 AVPG 211
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 119-225 4.00e-07

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: 48.72  E-value: 4.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095950267 119 IVIYATSADWKWIFSYPDES---------------------IETVNYVNIPTDRPVLFKLTSADTMTSFWVPQLGGQKYA 177
Cdd:cd13912     3 LTIKAIGHQWYWSYEYSDFNdlefdsymipeddlekgqlrlLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2095950267 178 MSGMTMNLYLQADEVGTYKGRNANFNGegfADQRF---DVVAQSEKDFKKW 225
Cdd:cd13912    83 VPGRLNQTSFFIERPGVYYGQCSEICG---ANHSFmpiVVEAVSLEDFLSW 130
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 43-172 4.12e-07

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 50.30  E-value: 4.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095950267  43 MLVIVLTIFVLFTIMLVkyrerkdISN--YEPDMHGSRKLEIFWTLIPVAIVIALAIPTVKTIYAGEEA--PKVTshkdp 118
Cdd:MTH00117   29 MVALLISSLVLYLLTLM-------LTTklTHTNTVDAQEVELIWTILPAIVLILLALPSLRILYLMDEInnPHLT----- 96

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2095950267 119 ivIYATSADWKWIFSYPDES---------------------IETVNYVNIPTDRPVLFKLTSADTMTSFWVPQLG 172
Cdd:MTH00117   97 --IKAIGHQWYWSYEYTDYKdlsfdsymiptqdlpnghfrlLEVDHRMVIPMESPIRILITAEDVLHSWAVPSLG 169
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 42-198 3.22e-06

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 47.79  E-value: 3.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095950267  42 FMLVIVLTIFVLFTIMLVKYRERKDISNYEpdmhgSRKLEIFWTLIPVAIVIALAIPTVKTIYAGEE--APKVTshkdpi 119
Cdd:MTH00098   28 LMIVFLISSLVLYIISLMLTTKLTHTSTMD-----AQEVETIWTILPAIILILIALPSLRILYMMDEinNPSLT------ 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095950267 120 vIYATSADWKWIFSYPDES---------------------IETVNYVNIPTDRPVLFKLTSADTMTSFWVPQLGGQKYAM 178
Cdd:MTH00098   97 -VKTMGHQWYWSYEYTDYEdlsfdsymiptsdlkpgelrlLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDAI 175

                         170       180
                  ....*....|....*....|
gi 2095950267 179 SGMTMNLYLQADEVGTYKGR 198
Cdd:MTH00098  176 PGRLNQTTLMSTRPGLYYGQ 195
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 43-228 2.30e-05

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 45.16  E-value: 2.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095950267  43 MLVIVLTIFVLFTI---MLVKYRERKDISNYEpdmhgsrkLEIFWTLIPVAIVIALAIPTVKTIYAGEE--APKVTshkd 117
Cdd:MTH00076   29 MAVFLISTLVLYIItimMTTKLTNTNTMDAQE--------IEMVWTIMPAIILIVIALPSLRILYLMDEinDPHLT---- 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095950267 118 pivIYATSADWKWIFSYPDES---------------------IETVNYVNIPTDRPVLFKLTSADTMTSFWVPQLGGQKY 176
Cdd:MTH00076   97 ---VKAIGHQWYWSYEYTDYEdlsfdsymiptqdltpgqfrlLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSLGIKTD 173

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2095950267 177 AMSGMTMNLYLQADEVGTYKGRNANFNGEGFADQRFDVVAQSEKDFKKWAKE 228
Cdd:MTH00076  174 AIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSS 225
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
119-197 4.96e-05

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 42.40  E-value: 4.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095950267 119 IVIYATSADWKWIFSYPD------ES---------------IETVNYVNIPTDRPVLFKLTSADTMTSFWVPQLGGQKYA 177
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDfgdlefDSymiptedleegqlrlLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100
                  ....*....|....*....|
gi 2095950267 178 MSGMTMNLYLQADEVGTYKG 197
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYG 100
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 77-197 1.51e-04

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 42.25  E-value: 1.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095950267  77 SRKLEIFWTLIPVAIVIALAIPTVKTIYAG-----EEAPKVTSHKdpiviyatsadWKWIFSYPDESI------ETVNYV 145
Cdd:MTH00047   46 NQVLELLWTVVPTLLVLVLCFLNLNFITSDldcfsSETIKVIGHQ-----------WYWSYEYSFGGSydsfmtDDIFGV 114

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2095950267 146 NIPT----DRPVLFKLTSADTMTSFWVPQLGGQKYAMSGMTMNLYLQADEVGTYKG 197
Cdd:MTH00047  115 DKPLrlvyGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVG 170
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 119-196 2.81e-03

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


Pssm-ID: 259983 [Multi-domain]  Cd Length: 93  Bit Score: 36.59  E-value: 2.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095950267 119 IVIYATSADWKWIFSyPDEsietvnyvnIPTDRPVLFKLTSADTMTSFWV----PQLGGQKYAMSGMTMNLYLQADEVGT 194
Cdd:cd13916     1 QVVAVTGHQWYWELS-RTE---------IPAGKPVEFRVTSADVNHGFGIydpdMRLLAQTQAMPGYTNVLRYTFDKPGT 70


                  ..
gi 2095950267 195 YK 196
Cdd:cd13916    71 YT 72
 
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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