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Conserved domains on  [gi|489927676|ref|WP_003831009|]
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MULTISPECIES: cytochrome o ubiquinol oxidase subunit II [Citrobacter]

Protein Classification

cytochrome ubiquinol oxidase subunit II( domain architecture ID 11484766)

subunit II of cytochrome ubiquinol oxidase, the terminal oxidase in the aerobic respiratory chain

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10525 PRK10525
cytochrome o ubiquinol oxidase subunit II; Provisional
 1-315 0e+00

cytochrome o ubiquinol oxidase subunit II; Provisional


:

Pssm-ID: 182518 [Multi-domain]  Cd Length: 315  Bit Score: 646.86  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927676   1 MRLRKYNKSLGWLSLIAGTALLSGCNSALLDPKGQIGLEQRSLILTAFGLMLIVVIPAILMAVGFAWKYRASNKDAKYSP 80
Cdd:PRK10525   1 MRLRKYNKSLGWLSLFAGTVLLSGCNSALLDPKGQIGLEQRSLILTAFGLMLIVVIPAILMAVGFAWKYRASNKDAKYSP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927676  81 NWSHSNKVEAVVWTVPILIIIFLAVLTWKTTHALEPSKPLAHDEKPITIEVVSMDWKWFFIYPEQGIATVNEIAFPANTP 160
Cdd:PRK10525  81 NWSHSNKVEAVVWTVPILIIIFLAVLTWKTTHALEPSKPLAHDEKPITIEVVSMDWKWFFIYPEQGIATVNEIAFPANVP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927676 161 VEFKVTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIANEVGTYDGISASYSGPGFSGMKFKAIATKDRAEFDQWVAKAKQ 240
Cdd:PRK10525 161 VYFKVTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIANEPGTYDGISASYSGPGFSGMKFKAIATPDRAEFDQWVAKAKQ 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489927676 241 STNTMSDMAAFEKVAAPSEYNQVEYFSNVKPDLFKDVINKFMAHGKSMDMSQPEGEHSAHEGMEGMDMSHAESAH 315
Cdd:PRK10525 241 SPNTMNDMAAFEKLAAPSEYNPVEYFSSVKPDLFKDVINKFMGHGKSMDMTQPEGEHSAHEGMEGMDMSHAESAH 315
 
Name Accession Description Interval E-value
PRK10525 PRK10525
cytochrome o ubiquinol oxidase subunit II; Provisional
 1-315 0e+00

cytochrome o ubiquinol oxidase subunit II; Provisional


Pssm-ID: 182518 [Multi-domain]  Cd Length: 315  Bit Score: 646.86  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927676   1 MRLRKYNKSLGWLSLIAGTALLSGCNSALLDPKGQIGLEQRSLILTAFGLMLIVVIPAILMAVGFAWKYRASNKDAKYSP 80
Cdd:PRK10525   1 MRLRKYNKSLGWLSLFAGTVLLSGCNSALLDPKGQIGLEQRSLILTAFGLMLIVVIPAILMAVGFAWKYRASNKDAKYSP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927676  81 NWSHSNKVEAVVWTVPILIIIFLAVLTWKTTHALEPSKPLAHDEKPITIEVVSMDWKWFFIYPEQGIATVNEIAFPANTP 160
Cdd:PRK10525  81 NWSHSNKVEAVVWTVPILIIIFLAVLTWKTTHALEPSKPLAHDEKPITIEVVSMDWKWFFIYPEQGIATVNEIAFPANVP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927676 161 VEFKVTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIANEVGTYDGISASYSGPGFSGMKFKAIATKDRAEFDQWVAKAKQ 240
Cdd:PRK10525 161 VYFKVTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIANEPGTYDGISASYSGPGFSGMKFKAIATPDRAEFDQWVAKAKQ 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489927676 241 STNTMSDMAAFEKVAAPSEYNQVEYFSNVKPDLFKDVINKFMAHGKSMDMSQPEGEHSAHEGMEGMDMSHAESAH 315
Cdd:PRK10525 241 SPNTMNDMAAFEKLAAPSEYNPVEYFSSVKPDLFKDVINKFMGHGKSMDMTQPEGEHSAHEGMEGMDMSHAESAH 315
CyoA TIGR01433
cytochrome o ubiquinol oxidase subunit II; This enzyme catalyzes the oxidation of ubiquinol ...
 13-239 2.81e-152

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: 425.78  E-value: 2.81e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927676   13 LSLIAGTALLSGCNSALLDPKGQIGLEQRSLILTAFGLMLIVVIPAILMAVGFAWKYRASNKDAKYSPNWSHSNKVEAVV 92
Cdd:TIGR01433   1 LSLIAASLLLSGCNLVLLDPKGQIGLEERSLILTAFGLMLLVVIPVILMTLFFAWKYRATNKDADYSPNWHHSTKIEIVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927676   93 WTVPILIIIFLAVLTWKTTHALEPSKPLAHDEKPITIEVVSMDWKWFFIYPEQGIATVNEIAFPANTPVEFKVTSNSVMN 172
Cdd:TIGR01433  81 WTIPILIIIFLGVLTWITTHKLDPYRPLASDVKPITIEVVALDWKWLFIYPEQGIATVNEIAFPVNTPINFKITSNSVMN 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489927676  173 SFFIPRLGSQIYAMAGMQTRLHLIANEVGTYDGISASYSGPGFSGMKFKAIATkDRAEFDQWVAKAK 239
Cdd:TIGR01433 161 SFFIPQLGSQIYAMAGMQTKLHLIANEPGVYDGISANYSGPGFSGMKFKAIAT-DRAAFDQWVAKAK 226
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
9-244 9.47e-96

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 282.49  E-value: 9.47e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927676   9 SLGWLSLIAGTALLSGcNSALLDPKGQIGLEQRSLILTAFGLMLIVVIPAILMAVGFAWKYRASNKDAKySPNWSHSNKV 88
Cdd:COG1622    2 KRLLLALLLLALLLSG-QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIRYRRRKGDAD-PAQFHHNTKL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927676  89 EAVVWTVPILIIIFLAVLTWKTTHALEPSkplahDEKPITIEVVSMDWKWFFIYPEQGIATVNEIAFPANTPVEFKVTSN 168
Cdd:COG1622   80 EIVWTVIPIIIVIVLAVPTLRVLHALDDA-----PEDPLTVEVTGYQWKWLFRYPDQGIATVNELVLPVGRPVRFLLTSA 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489927676 169 SVMNSFFIPRLGSQIYAMAGMQTRLHLIANEVGTYDGISASYSGPGFSGMKFKAIATkDRAEFDQWVAKAKQSTNT 244
Cdd:COG1622  155 DVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVV-SPEEFDAWLAEQKASAAT 229
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 127-225 8.49e-65

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: 198.93  E-value: 8.49e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927676 127 ITIEVVSMDWKWFFIYPEQGIATVNEIAFPANTPVEFKVTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIANEVGTYDGI 206
Cdd:cd04212    1 LEIQVVSLDWKWLFIYPEQGIATVNELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGL 80

                         90
                 ....*....|....*....
gi 489927676 207 SASYSGPGFSGMKFKAIAT 225
Cdd:cd04212   81 SANYSGEGFSDMKFKVLAV 99
COX_ARM pfam06481
COX Aromatic Rich Motif; COX2 (Cytochrome O ubiquinol OXidase 2) is a major component of the ...
 239-285 1.38e-16

COX Aromatic Rich Motif; COX2 (Cytochrome O ubiquinol OXidase 2) is a major component of the respiratory complex during vegetative growth. It transfers electrons from a quinol to the binuclear centre of the catalytic subunit 1. The function of this region is not known.


Pssm-ID: 428969  Cd Length: 46  Bit Score: 72.14  E-value: 1.38e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 489927676  239 KQSTNTMsDMAAFEKVAAPSEYNQVEYFSNVKPDLFKDVINKFMAHG 285
Cdd:pfam06481   1 KASPKTL-DRDEYLELAKPSENNPVEYFSSVDPGLFDAIVNKYMGPG 46
 
Name Accession Description Interval E-value
PRK10525 PRK10525
cytochrome o ubiquinol oxidase subunit II; Provisional
 1-315 0e+00

cytochrome o ubiquinol oxidase subunit II; Provisional


Pssm-ID: 182518 [Multi-domain]  Cd Length: 315  Bit Score: 646.86  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927676   1 MRLRKYNKSLGWLSLIAGTALLSGCNSALLDPKGQIGLEQRSLILTAFGLMLIVVIPAILMAVGFAWKYRASNKDAKYSP 80
Cdd:PRK10525   1 MRLRKYNKSLGWLSLFAGTVLLSGCNSALLDPKGQIGLEQRSLILTAFGLMLIVVIPAILMAVGFAWKYRASNKDAKYSP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927676  81 NWSHSNKVEAVVWTVPILIIIFLAVLTWKTTHALEPSKPLAHDEKPITIEVVSMDWKWFFIYPEQGIATVNEIAFPANTP 160
Cdd:PRK10525  81 NWSHSNKVEAVVWTVPILIIIFLAVLTWKTTHALEPSKPLAHDEKPITIEVVSMDWKWFFIYPEQGIATVNEIAFPANVP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927676 161 VEFKVTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIANEVGTYDGISASYSGPGFSGMKFKAIATKDRAEFDQWVAKAKQ 240
Cdd:PRK10525 161 VYFKVTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIANEPGTYDGISASYSGPGFSGMKFKAIATPDRAEFDQWVAKAKQ 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489927676 241 STNTMSDMAAFEKVAAPSEYNQVEYFSNVKPDLFKDVINKFMAHGKSMDMSQPEGEHSAHEGMEGMDMSHAESAH 315
Cdd:PRK10525 241 SPNTMNDMAAFEKLAAPSEYNPVEYFSSVKPDLFKDVINKFMGHGKSMDMTQPEGEHSAHEGMEGMDMSHAESAH 315
CyoA TIGR01433
cytochrome o ubiquinol oxidase subunit II; This enzyme catalyzes the oxidation of ubiquinol ...
 13-239 2.81e-152

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: 425.78  E-value: 2.81e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927676   13 LSLIAGTALLSGCNSALLDPKGQIGLEQRSLILTAFGLMLIVVIPAILMAVGFAWKYRASNKDAKYSPNWSHSNKVEAVV 92
Cdd:TIGR01433   1 LSLIAASLLLSGCNLVLLDPKGQIGLEERSLILTAFGLMLLVVIPVILMTLFFAWKYRATNKDADYSPNWHHSTKIEIVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927676   93 WTVPILIIIFLAVLTWKTTHALEPSKPLAHDEKPITIEVVSMDWKWFFIYPEQGIATVNEIAFPANTPVEFKVTSNSVMN 172
Cdd:TIGR01433  81 WTIPILIIIFLGVLTWITTHKLDPYRPLASDVKPITIEVVALDWKWLFIYPEQGIATVNEIAFPVNTPINFKITSNSVMN 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489927676  173 SFFIPRLGSQIYAMAGMQTRLHLIANEVGTYDGISASYSGPGFSGMKFKAIATkDRAEFDQWVAKAK 239
Cdd:TIGR01433 161 SFFIPQLGSQIYAMAGMQTKLHLIANEPGVYDGISANYSGPGFSGMKFKAIAT-DRAAFDQWVAKAK 226
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
9-244 9.47e-96

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 282.49  E-value: 9.47e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927676   9 SLGWLSLIAGTALLSGcNSALLDPKGQIGLEQRSLILTAFGLMLIVVIPAILMAVGFAWKYRASNKDAKySPNWSHSNKV 88
Cdd:COG1622    2 KRLLLALLLLALLLSG-QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIRYRRRKGDAD-PAQFHHNTKL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927676  89 EAVVWTVPILIIIFLAVLTWKTTHALEPSkplahDEKPITIEVVSMDWKWFFIYPEQGIATVNEIAFPANTPVEFKVTSN 168
Cdd:COG1622   80 EIVWTVIPIIIVIVLAVPTLRVLHALDDA-----PEDPLTVEVTGYQWKWLFRYPDQGIATVNELVLPVGRPVRFLLTSA 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489927676 169 SVMNSFFIPRLGSQIYAMAGMQTRLHLIANEVGTYDGISASYSGPGFSGMKFKAIATkDRAEFDQWVAKAKQSTNT 244
Cdd:COG1622  155 DVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVV-SPEEFDAWLAEQKASAAT 229
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 127-225 8.49e-65

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: 198.93  E-value: 8.49e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927676 127 ITIEVVSMDWKWFFIYPEQGIATVNEIAFPANTPVEFKVTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIANEVGTYDGI 206
Cdd:cd04212    1 LEIQVVSLDWKWLFIYPEQGIATVNELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGL 80

                         90
                 ....*....|....*....
gi 489927676 207 SASYSGPGFSGMKFKAIAT 225
Cdd:cd04212   81 SANYSGEGFSDMKFKVLAV 99
QOXA TIGR01432
cytochrome aa3 quinol oxidase, subunit II; This enzyme catalyzes the oxidation of quinol with ...
 14-239 4.63e-61

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: 193.98  E-value: 4.63e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927676   14 SLIAGTALLSGC-NSALLDPKGQIGLEQRSLILTAFGLMLIVVIPAILMAVGFAWKYRASNKDAKYSPNWSHSNKVEaVV 92
Cdd:TIGR01432   1 ALLTVVFVLSGCsNIEVLNPKGPVASSQSDLILYSIVFMLVIVFVVFVLFTIFLVKYRYRKDNGAYSPKMHGNAILE-TI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927676   93 WTV-PILIIIFLAVLTWKTTHALEPSKPLAHDEKPITIEVVSMDWKWFFIYPEQGIATVNEIAFPANTPVEFKVTSNSVM 171
Cdd:TIGR01432  80 WTViPIIIVIALAIPTVKTIYDYEKAPKSTKEKDPMVVYATSADWKWFFSYPDEHIETVNYLNIPKDRPVLFKLQSADTM 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489927676  172 NSFFIPRLGSQIYAMAGMQTRLHLIANEVGTYDGISASYSGPGFSGMKFKAIATKDRaEFDQWVAKAK 239
Cdd:TIGR01432 160 TSFWIPQLGGQKYAMTGMTMNWYLQADEVGTYRGRNANFNGEGFADQTFDVNAVSEK-DFDKWVKETK 226
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 43-236 1.59e-41

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


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 142.90  E-value: 1.59e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927676   43 LILTAFGLMLIVVIPAILMAVgfAWKYRASNKDAKySPNWSHSNKVEaVVWTV-PILIIIFLAVLTWKTTHALEPSKPLA 121
Cdd:TIGR02866  14 LFVLAVSTLISLLVAALLAYV--VWKFRRKGDEEK-PSQIHGNRRLE-YVWTViPLIIVVGLFAATAKGLLYLERPIPKD 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927676  122 hdekPITIEVVSMDWKWFFIYPEQGIATVNEIAFPANTPVEFKVTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIANEVG 201
Cdd:TIGR02866  90 ----ALKVKVTGYQWWWDFEYPESGFTTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPG 165

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 489927676  202 TYDGISASYSGPGFSGMKFKAIATkDRAEFDQWVA 236
Cdd:TIGR02866 166 VYYGFCAELCGAGHSLMLFKVVVV-PKEEFDAYVE 199
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 127-223 2.03e-34

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: 120.86  E-value: 2.03e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927676 127 ITIEVVSMDWKWFFIYPEqgIATVNEIAFPANTPVEFKVTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIANEVGTYDGI 206
Cdd:cd13842    1 LTVYVTGVQWSWTFIYPN--VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDAVPGYTSELWFVADKPGTYTII 78

                         90
                 ....*....|....*..
gi 489927676 207 SASYSGPGFSGMKFKAI 223
Cdd:cd13842   79 CAEYCGLGHSYMLGKVE 95
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 127-235 5.28e-23

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


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 91.32  E-value: 5.28e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927676 127 ITIEVVSMDWKWFFIYPEQGIATVNEIAFPANTPVEFKVTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIANEVGTYDGI 206
Cdd:cd13914    1 VEIEVEAYQWGWEFSYPEANVTTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAFPGQYNTIKTEATEEGEYQLY 80

                         90       100
                 ....*....|....*....|....*....
gi 489927676 207 SASYSGPGFSGMKFKaIATKDRAEFDQWV 235
Cdd:cd13914   81 CAEYCGAGHSQMLST-VTVVSQDEYQQWL 108
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 126-224 1.77e-22

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: 89.99  E-value: 1.77e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927676 126 PITIEVVSMDWKWFFIYPE---QGIATVNEIAFPANTPVEFKVTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIANEVGT 202
Cdd:cd04213    1 ALTIEVTGHQWWWEFRYPDepgRGIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDMIPGRTNRLWLQADEPGV 80

                         90       100
                 ....*....|....*....|..
gi 489927676 203 YDGISASYSGPGFSGMKFKAIA 224
Cdd:cd04213   81 YRGQCAEFCGASHALMRFKVIA 102
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 126-223 2.12e-22

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


Pssm-ID: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 89.62  E-value: 2.12e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927676 126 PITIEVVSMDWKWFFIYPEQGI-------ATVNEIAFPANTPVEFKVTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIAN 198
Cdd:cd13919    1 ALVVEVTAQQWAWTFRYPGGDGklgtdddVTSPELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDAVPGRTTRLWFTPT 80

                         90       100
                 ....*....|....*....|....*
gi 489927676 199 EVGTYDGISASYSGPGFSGMKFKAI 223
Cdd:cd13919   81 REGEYEVRCAELCGLGHYRMRATVK 105
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 98-235 2.48e-20

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: 85.20  E-value: 2.48e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927676  98 LIIIFLAVLTWKTTHALEpSKPLAHDEKPITIEVVSMDWKWFFIYPeQGIATVNEIAFPANTPVEFKVTSNSVMNSFFIP 177
Cdd:cd13918    5 IIVISLIVWTYGMLLYVE-DPPDEADEDALEVEVEGFQFGWQFEYP-NGVTTGNTLRVPADTPIALRVTSTDVFHTFGIP 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489927676 178 RLGSQIYAMAGMQTRLHLIANEVGTYDGISASYSGPGFSGMKFKAIATkDRAEFDQWV 235
Cdd:cd13918   83 ELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVM-DEEEFEAWY 139
COX_ARM pfam06481
COX Aromatic Rich Motif; COX2 (Cytochrome O ubiquinol OXidase 2) is a major component of the ...
 239-285 1.38e-16

COX Aromatic Rich Motif; COX2 (Cytochrome O ubiquinol OXidase 2) is a major component of the respiratory complex during vegetative growth. It transfers electrons from a quinol to the binuclear centre of the catalytic subunit 1. The function of this region is not known.


Pssm-ID: 428969  Cd Length: 46  Bit Score: 72.14  E-value: 1.38e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 489927676  239 KQSTNTMsDMAAFEKVAAPSEYNQVEYFSNVKPDLFKDVINKFMAHG 285
Cdd:pfam06481   1 KASPKTL-DRDEYLELAKPSENNPVEYFSSVDPGLFDAIVNKYMGPG 46
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 127-218 4.02e-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: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 69.97  E-value: 4.02e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927676 127 ITIEVVSMDWKWFFIYPEqGIATVNEIAFPANTPVEFKVTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIANEVGTYDGI 206
Cdd:cd13915    2 LEIQVTGRQWMWEFTYPN-GKREINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDVVPGRYTYLWFEATKPGEYDLF 80

                         90
                 ....*....|..
gi 489927676 207 SASYSGPGFSGM 218
Cdd:cd13915   81 CTEYCGTGHSGM 92
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 127-218 2.32e-07

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


Pssm-ID: 259983 [Multi-domain]  Cd Length: 93  Bit Score: 48.15  E-value: 2.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927676 127 ITIEVVSMDWKWffiypeqgiaTVNEIAFPANTPVEFKVTSNSVMNSFFI----PRLGSQIYAMAGMQTRLHLIANEVGT 202
Cdd:cd13916    1 QVVAVTGHQWYW----------ELSRTEIPAGKPVEFRVTSADVNHGFGIydpdMRLLAQTQAMPGYTNVLRYTFDKPGT 70

                         90
                 ....*....|....*.
gi 489927676 203 YDGISASYSGPGFSGM 218
Cdd:cd13916   71 YTILCLEYCGLAHHVM 86
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 51-205 2.68e-06

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 47.40  E-value: 2.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927676  51 MLIVVIpaILMAVGFAWKYRASNKDAKYSPNWSHsnKVEaVVWTV-PILIIIFLAVLTWKTTHAL-EPSKPLahdekpIT 128
Cdd:MTH00139  28 MVILIM--ILSFVGYISLSLMSNKFTSRSLLESQ--EVE-TIWTVlPAFILLFLALPSLRLLYLMdEVSDPY------LT 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927676 129 IEVVSMDWKW-------------FFIYPEQGIA--------TVNEIAFPANTPVEFKVTSNSVMNSFFIPRLGSQIYAMA 187
Cdd:MTH00139  97 FKAVGHQWYWsyeysdfknlsfdSYMIPTEDLSsgefrlleVDNRLVLPYKSNIRALITAADVLHSWTVPSLGVKIDAVP 176

                        170
                 ....*....|....*...
gi 489927676 188 GMQTRLHLIANEVGTYDG 205
Cdd:MTH00139 177 GRLNQVGFFINRPGVFYG 194
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 127-205 5.79e-06

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: 44.87  E-value: 5.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927676 127 ITIEVVSMDWKWFFIYP-----------------EQG----IATVNEIAFPANTPVEFKVTSNSVMNSFFIPRLGSQIYA 185
Cdd:cd13912    3 LTIKAIGHQWYWSYEYSdfndlefdsymipeddlEKGqlrlLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                         90       100
                 ....*....|....*....|
gi 489927676 186 MAGMQTRLHLIANEVGTYDG 205
Cdd:cd13912   83 VPGRLNQTSFFIERPGVYYG 102
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 45-237 1.50e-04

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 42.54  E-value: 1.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927676  45 LTAFGLMLIVVIPAILMAVGFAWKYRASNKdakYSPNWSHSNKVEAVVWTV-PILIIIFLAVLTWKTTHAL-EPSKPlah 122
Cdd:MTH00008  20 LISFHDHALLILTLVLTVVGYAMTSLMFNK---LSNRYILEAQQIETIWTIlPALILLFLAFPSLRLLYLMdEVSNP--- 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927676 123 dekPITIEVVSMDWKWFFIY-------------------PEQG--IATVNEIAFPANTPVEFKVTSNSVMNSFFIPRLGS 181
Cdd:MTH00008  94 ---SITLKTIGHQWYWSYEYsdfsnlefdsymlptsdlsPGQFrlLEVDNRAVLPMQTEIRVLVTAADVIHSWTVPSLGV 170

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489927676 182 QIYAMAGMQTRLHLIANEVGTYDGISASYSGPGFSGMKFkAIATKDRAEFDQWVAK 237
Cdd:MTH00008 171 KVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPI-VLEAVDTKSFMKWVSS 225
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 50-205 4.92e-04

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 40.58  E-value: 4.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927676  50 LMLIVVIPAILMAVGFAWKYraSNKdakyspNWSHSNKVEaVVWTV-PILIIIFLAVLTWKTTHALEPSKplahdeKP-I 127
Cdd:MTH00154  31 LIMITILVGYMMISLLFNKF--TNR------FLLEGQEIE-IIWTIlPAIILIFIALPSLRLLYLLDEVN------NPsI 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927676 128 TIEVVSMDWKW-----------F--FIYPEQGIA--------TVNEIAFPANTPVEFKVTSNSVMNSFFIPRLGSQIYAM 186
Cdd:MTH00154  96 TLKTIGHQWYWsyeysdfknieFdsYMIPTNELEnngfrlldVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAV 175

                        170
                 ....*....|....*....
gi 489927676 187 AGMQTRLHLIANEVGTYDG 205
Cdd:MTH00154 176 PGRLNQLNFLINRPGLFFG 194
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
127-218 4.94e-04

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 39.32  E-value: 4.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927676  127 ITIEVVSMDWKWFFIYPEQG---------------------IATVNEIAFPANTPVEFKVTSNSVMNSFFIPRLGSQIYA 185
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGdlefdsymiptedleegqlrlLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 489927676  186 MAGMQTRLHLIANEVGTYDGISASYSGPGFSGM 218
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFM 113
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 83-205 1.24e-03

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 39.51  E-value: 1.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927676  83 SHSNKVEA----VVWTV-PILIIIFLAVLTWKTTHALEPSkplahDEKPITIEVVSMDWKWFFIY-------------PE 144
Cdd:MTH00117  51 THTNTVDAqeveLIWTIlPAIVLILLALPSLRILYLMDEI-----NNPHLTIKAIGHQWYWSYEYtdykdlsfdsymiPT 125

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489927676 145 QGIA--------TVNEIAFPANTPVEFKVTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIANEVGTYDG 205
Cdd:MTH00117 126 QDLPnghfrlleVDHRMVIPMESPIRILITAEDVLHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYG 194
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 131-218 1.50e-03

C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and some archaea, which catalyze the reduction of O2 and simultaneously pump protons across the membrane. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. The ba3 family contains oxidases that lack the conserved residues that form the D- and K-pathways in CcO and ubiquinol oxidase. Instead, they contain a potential alternative K-pathway. Additional proton channels have been proposed for this family of oxidases but none have been identified definitively.


Pssm-ID: 259980 [Multi-domain]  Cd Length: 99  Bit Score: 37.16  E-value: 1.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927676 131 VVSMDWKWffiypeqgiaTVNEIAFPANTPVEFKVTSNSVMNSFFIPrlGSQIYAMA--GMQTRLHLIANEVGTYDGISA 208
Cdd:cd13913   15 VVAQAFAF----------NPNEIEVPAGATVTFYVTSKDVIHGFEIA--GTNVNVMVipGQVSSVTYTFDKPGEYLIICN 82

                         90
                 ....*....|
gi 489927676 209 SYSGPGFSGM 218
Cdd:cd13913   83 EYCGAGHHNM 92
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 83-218 3.41e-03

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 38.01  E-value: 3.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927676  83 SHSNKVEaVVWT-VPILIIIFLAVLTwktTHALEPSKPLAHDEkpiTIEVVSMDWKWFFIYPEQGI------ATVNEIAF 155
Cdd:MTH00047  44 SENQVLE-LLWTvVPTLLVLVLCFLN---LNFITSDLDCFSSE---TIKVIGHQWYWSYEYSFGGSydsfmtDDIFGVDK 116

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489927676 156 PA----NTPVEFKVTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIANEVGTYDGISASYSGPGFSGM 218
Cdd:MTH00047 117 PLrlvyGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYM 183
 
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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