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Conserved domains on  [gi|2727871299|gb|XAM94802|]
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cytochrome c oxidase subunit II, partial (mitochondrion) [Eugryllacris ruficeps]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11475927)

cytochrome c oxidase subunit II, part of the functional core of the enzyme, transfers the electrons from cytochrome c via its binuclear copper A center to the bimetallic center of the catalytic subunit I

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-205 2.32e-100

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 289.81  E-value: 2.32e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727871299   1 LLFFHDHTHFILTMITILVAYIMGSLFFNPFTCHFLLKGQTIEIIWTILPAFTMIFIALPSLRLLYLLDESLDPMLSIKS 80
Cdd:MTH00154   20 LIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKT 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727871299  81 VGHQWYSSYEYSDFQKMsEFDSYLIPYNGMNQNEFWLLYVDYQTILPMNTQIHTLITSTDMINFWTVPALGVKVDATPGR 160
Cdd:MTH00154  100 IGHQWYWSYEYSDFKNI-EFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGR 178

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2727871299 161 LNQISFFMNRPGLFYGQCSTFFGANHSFKPIVIESMTMKTLISFM 205
Cdd:MTH00154  179 LNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWI 223
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-205 2.32e-100

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 289.81  E-value: 2.32e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727871299   1 LLFFHDHTHFILTMITILVAYIMGSLFFNPFTCHFLLKGQTIEIIWTILPAFTMIFIALPSLRLLYLLDESLDPMLSIKS 80
Cdd:MTH00154   20 LIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKT 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727871299  81 VGHQWYSSYEYSDFQKMsEFDSYLIPYNGMNQNEFWLLYVDYQTILPMNTQIHTLITSTDMINFWTVPALGVKVDATPGR 160
Cdd:MTH00154  100 IGHQWYWSYEYSDFKNI-EFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGR 178

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2727871299 161 LNQISFFMNRPGLFYGQCSTFFGANHSFKPIVIESMTMKTLISFM 205
Cdd:MTH00154  179 LNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWI 223
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 74-204 3.31e-59

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: 182.00  E-value: 3.31e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727871299  74 PMLSIKSVGHQWYSSYEYSDFQKmSEFDSYLIPYNGMNQNEFWLLYVDYQTILPMNTQIHTLITSTDMINFWTVPALGVK 153
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFND-LEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIK 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2727871299 154 VDATPGRLNQISFFMNRPGLFYGQCSTFFGANHSFKPIVIESMTMKTLISF 204
Cdd:cd13912    80 VDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
76-195 6.38e-56

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 173.36  E-value: 6.38e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727871299  76 LSIKSVGHQWYSSYEYSDFQKMsEFDSYLIPYNGMNQNEFWLLYVDYQTILPMNTQIHTLITSTDMINFWTVPALGVKVD 155
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDL-EFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2727871299 156 ATPGRLNQISFFMNRPGLFYGQCSTFFGANHSFKPIVIES 195
Cdd:pfam00116  80 AVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEA 119
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
41-197 1.94e-27

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 103.75  E-value: 1.94e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727871299  41 TIEIIWTILPAFTMIFIALPSLRLLYLLDESLDPMLSIKSVGHQWYSSYEYSDfqkmsefdsylipYNGMNQNEfwlLYV 120
Cdd:COG1622    78 KLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPD-------------QGIATVNE---LVL 141

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2727871299 121 dyqtilPMNTQIHTLITSTDMINFWTVPALGVKVDATPGRLNQISFFMNRPGLFYGQCSTFFGANHSFKPIVIESMT 197
Cdd:COG1622   142 ------PVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVS 212
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 42-196 3.72e-22

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: 89.36  E-value: 3.72e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727871299  42 IEIIWTILPAFTMIFIALPSLRLLYLLDESLDP-MLSIKSVGHQWYSSYEYSDFqkmsefdsylipyngmnqnefwLLYV 120
Cdd:TIGR02866  56 LEYVWTVIPLIIVVGLFAATAKGLLYLERPIPKdALKVKVTGYQWWWDFEYPES----------------------GFTT 113

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2727871299 121 DYQTILPMNTQIHTLITSTDMINFWTVPALGVKVDATPGRLNQISFFMNRPGLFYGQCSTFFGANHSFKPIVIESM 196
Cdd:TIGR02866 114 VNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVV 189
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-205 2.32e-100

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 289.81  E-value: 2.32e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727871299   1 LLFFHDHTHFILTMITILVAYIMGSLFFNPFTCHFLLKGQTIEIIWTILPAFTMIFIALPSLRLLYLLDESLDPMLSIKS 80
Cdd:MTH00154   20 LIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKT 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727871299  81 VGHQWYSSYEYSDFQKMsEFDSYLIPYNGMNQNEFWLLYVDYQTILPMNTQIHTLITSTDMINFWTVPALGVKVDATPGR 160
Cdd:MTH00154  100 IGHQWYWSYEYSDFKNI-EFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGR 178

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2727871299 161 LNQISFFMNRPGLFYGQCSTFFGANHSFKPIVIESMTMKTLISFM 205
Cdd:MTH00154  179 LNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWI 223
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-209 1.18e-83

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 247.54  E-value: 1.18e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727871299   1 LLFFHDHTHFILTMITILVAYIMGSLFFNPFTCHFLLKGQTIEIIWTILPAFTMIFIALPSLRLLYLLDESLDPMLSIKS 80
Cdd:MTH00140   20 LIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPSLRLLYLLDETNNPLLTVKA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727871299  81 VGHQWYSSYEYSDFQKMsEFDSYLIPYNGMNQNEFWLLYVDYQTILPMNTQIHTLITSTDMINFWTVPALGVKVDATPGR 160
Cdd:MTH00140  100 IGHQWYWSYEYSDFSVI-EFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVPSLGVKVDAIPGR 178

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2727871299 161 LNQISFFMNRPGLFYGQCSTFFGANHSFKPIVIESMTMKTLISFMTYSS 209
Cdd:MTH00140  179 LNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELMS 227
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-202 3.95e-81

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 241.16  E-value: 3.95e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727871299   1 LLFFHDHTHFILTMITILVAYIMGSLFFNPFTCHFLLKGQTIEIIWTILPAFTMIFIALPSLRLLYLLDESLDPMLSIKS 80
Cdd:MTH00139   20 LIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPSLRLLYLMDEVSDPYLTFKA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727871299  81 VGHQWYSSYEYSDFQKMsEFDSYLIPYNGMNQNEFWLLYVDYQTILPMNTQIHTLITSTDMINFWTVPALGVKVDATPGR 160
Cdd:MTH00139  100 VGHQWYWSYEYSDFKNL-SFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSWTVPSLGVKIDAVPGR 178

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2727871299 161 LNQISFFMNRPGLFYGQCSTFFGANHSFKPIVIESMTMKTLI 202
Cdd:MTH00139  179 LNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFL 220
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-200 1.69e-78

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 234.60  E-value: 1.69e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727871299   1 LLFFHDHTHFILTMITILVAYIMGSLFFNPFTCHFLLKGQTIEIIWTILPAFTMIFIALPSLRLLYLLDESLDPMLSIKS 80
Cdd:MTH00038   20 LIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPSLQLLYLMDEVNNPFLTIKA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727871299  81 VGHQWYSSYEYSDFQKMsEFDSYLIPYNGMNQNEFWLLYVDYQTILPMNTQIHTLITSTDMINFWTVPALGVKVDATPGR 160
Cdd:MTH00038  100 IGHQWYWSYEYTDYNDL-EFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLHSWAVPSLGVKMDAVPGR 178

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2727871299 161 LNQISFFMNRPGLFYGQCSTFFGANHSFKPIVIESMTMKT 200
Cdd:MTH00038  179 LNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNT 218
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-206 4.64e-78

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 233.59  E-value: 4.64e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727871299   1 LLFFHDHTHFILTMITILVAYIMGSLFFNPFTCHFLLKGQTIEIIWTILPAFTMIFIALPSLRLLYLLDESLDPMLSIKS 80
Cdd:MTH00008   20 LISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSLRLLYLMDEVSNPSITLKT 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727871299  81 VGHQWYSSYEYSDFQKMsEFDSYLIPYNGMNQNEFWLLYVDYQTILPMNTQIHTLITSTDMINFWTVPALGVKVDATPGR 160
Cdd:MTH00008  100 IGHQWYWSYEYSDFSNL-EFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPGR 178

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2727871299 161 LNQISFFMNRPGLFYGQCSTFFGANHSFKPIVIESMTMKTLISFMT 206
Cdd:MTH00008  179 LNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVS 224
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 1-205 4.04e-76

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 228.87  E-value: 4.04e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727871299   1 LLFFHDHTHFILTMITILVAYIMGSLFFNPFTCHFLLKGQTIEIIWTILPAFTMIFIALPSLRLLYLLDESLDPMLSIKS 80
Cdd:MTH00023   29 IIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYLMDEVVSPALTIKA 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727871299  81 VGHQWYSSYEYSDFQKMS-EFDSYLIPYNGMNQNEFWLLYVDYQTILPMNTQIHTLITSTDMINFWTVPALGVKVDATPG 159
Cdd:MTH00023  109 IGHQWYWSYEYSDYEGETlEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVPSLGLKIDAVPG 188

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2727871299 160 RLNQISFFMNRPGLFYGQCSTFFGANHSFKPIVIESMTMKTLISFM 205
Cdd:MTH00023  189 RLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWL 234
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-199 8.95e-74

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 222.48  E-value: 8.95e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727871299   1 LLFFHDHTHFILTMITILVAYIMGSLFFNPFTCHFLLKGQTIEIIWTILPAFTMIFIALPSLRLLYLLDESLDPMLSIKS 80
Cdd:MTH00117   20 LLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPSLRILYLMDEINNPHLTIKA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727871299  81 VGHQWYSSYEYSDFQKMSeFDSYLIPYNGMNQNEFWLLYVDYQTILPMNTQIHTLITSTDMINFWTVPALGVKVDATPGR 160
Cdd:MTH00117  100 IGHQWYWSYEYTDYKDLS-FDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVPSLGVKTDAVPGR 178

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2727871299 161 LNQISFFMNRPGLFYGQCSTFFGANHSFKPIVIESMTMK 199
Cdd:MTH00117  179 LNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLK 217
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-203 5.18e-72

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 217.93  E-value: 5.18e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727871299   1 LLFFHDHTHFILTMITILVAYIMGSLFFNPFTCHFLLKGQTIEIIWTILPAFTMIFIALPSLRLLYLLDESLDPMLSIKS 80
Cdd:MTH00168   20 LILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPSLRLLYLMDEIDKPDLTIKA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727871299  81 VGHQWYSSYEYSDFQKMsEFDSYLIPYNGMNQNEFWLLYVDYQTILPMNTQIHTLITSTDMINFWTVPALGVKVDATPGR 160
Cdd:MTH00168  100 VGHQWYWSYEYTDYNDL-EFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSWTLPSLGLKMDAVPGR 178

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2727871299 161 LNQISFFMNRPGLFYGQCSTFFGANHSFKPIVIESMTMKTLIS 203
Cdd:MTH00168  179 LNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFEN 221
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-199 1.99e-71

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 216.68  E-value: 1.99e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727871299   1 LLFFHDHTHFILTMITILVAYIMGSLFFNPFTCHFLLKGQTIEIIWTILPAFTMIFIALPSLRLLYLLDESLDPMLSIKS 80
Cdd:MTH00185   20 LIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLRILYLMDEINDPHLTIKA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727871299  81 VGHQWYSSYEYSDFQKMsEFDSYLIPYNGMNQNEFWLLYVDYQTILPMNTQIHTLITSTDMINFWTVPALGVKVDATPGR 160
Cdd:MTH00185  100 MGHQWYWSYEYTDYEQL-EFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVPALGVKMDAVPGR 178

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2727871299 161 LNQISFFMNRPGLFYGQCSTFFGANHSFKPIVIESMTMK 199
Cdd:MTH00185  179 LNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLE 217
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-199 9.43e-70

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 212.27  E-value: 9.43e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727871299   1 LLFFHDHTHFILTMITILVAYIMGSLFFNPFTCHFLLKGQTIEIIWTILPAFTMIFIALPSLRLLYLLDESLDPMLSIKS 80
Cdd:MTH00129   20 LLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRILYLMDEINDPHLTIKA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727871299  81 VGHQWYSSYEYSDFQKMsEFDSYLIPYNGMNQNEFWLLYVDYQTILPMNTQIHTLITSTDMINFWTVPALGVKVDATPGR 160
Cdd:MTH00129  100 MGHQWYWSYEYTDYEDL-GFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVPALGVKMDAVPGR 178

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2727871299 161 LNQISFFMNRPGLFYGQCSTFFGANHSFKPIVIESMTMK 199
Cdd:MTH00129  179 LNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLE 217
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 1-206 1.46e-68

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 209.64  E-value: 1.46e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727871299   1 LLFFHDHTHFILTMITILVAYIMGSLFFNPFTCHFLLKGQTIEIIWTILPAFTMIFIALPSLRLLYLLDESLDPMLSIKS 80
Cdd:MTH00051   22 IIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYLMDEVIDPALTIKA 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727871299  81 VGHQWYSSYEYSDFQKMS-EFDSYLIPYNGMNQNEFWLLYVDYQTILPMNTQIHTLITSTDMINFWTVPALGVKVDATPG 159
Cdd:MTH00051  102 IGHQWYWSYEYSDYGTDTiEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPSLSVKIDAVPG 181

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2727871299 160 RLNQISFFMNRPGLFYGQCSTFFGANHSFKPIVIESMTMKTLISFMT 206
Cdd:MTH00051  182 RLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVA 228
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-199 3.33e-68

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 208.42  E-value: 3.33e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727871299   1 LLFFHDHTHFILTMITILVAYIMGSLFFNPFTCHFLLKGQTIEIIWTILPAFTMIFIALPSLRLLYLLDESLDPMLSIKS 80
Cdd:MTH00098   20 LLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRILYMMDEINNPSLTVKT 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727871299  81 VGHQWYSSYEYSDFQKMSeFDSYLIPYNGMNQNEFWLLYVDYQTILPMNTQIHTLITSTDMINFWTVPALGVKVDATPGR 160
Cdd:MTH00098  100 MGHQWYWSYEYTDYEDLS-FDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDAIPGR 178

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2727871299 161 LNQISFFMNRPGLFYGQCSTFFGANHSFKPIVIESMTMK 199
Cdd:MTH00098  179 LNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLK 217
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-209 8.97e-67

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 204.63  E-value: 8.97e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727871299   1 LLFFHDHTHFILTMITILVAYIMGSLFFNPFTCHFLLKGQTIEIIWTILPAFTMIFIALPSLRLLYLLDESLDPMLSIKS 80
Cdd:MTH00076   20 LLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRILYLMDEINDPHLTVKA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727871299  81 VGHQWYSSYEYSDFQKMSeFDSYLIPYNGMNQNEFWLLYVDYQTILPMNTQIHTLITSTDMINFWTVPALGVKVDATPGR 160
Cdd:MTH00076  100 IGHQWYWSYEYTDYEDLS-FDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSLGIKTDAIPGR 178

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2727871299 161 LNQISFFMNRPGLFYGQCSTFFGANHSFKPIVIESMTMKTlisFMTYSS 209
Cdd:MTH00076  179 LNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNN---FLNWSS 224
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 74-204 3.31e-59

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: 182.00  E-value: 3.31e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727871299  74 PMLSIKSVGHQWYSSYEYSDFQKmSEFDSYLIPYNGMNQNEFWLLYVDYQTILPMNTQIHTLITSTDMINFWTVPALGVK 153
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFND-LEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIK 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2727871299 154 VDATPGRLNQISFFMNRPGLFYGQCSTFFGANHSFKPIVIESMTMKTLISF 204
Cdd:cd13912    80 VDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
76-195 6.38e-56

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 173.36  E-value: 6.38e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727871299  76 LSIKSVGHQWYSSYEYSDFQKMsEFDSYLIPYNGMNQNEFWLLYVDYQTILPMNTQIHTLITSTDMINFWTVPALGVKVD 155
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDL-EFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2727871299 156 ATPGRLNQISFFMNRPGLFYGQCSTFFGANHSFKPIVIES 195
Cdd:pfam00116  80 AVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEA 119
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 1-205 1.47e-52

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 169.82  E-value: 1.47e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727871299   1 LLFFHDHTHFILTMITILVAY-IMGSLFFNPFTCHFL--LKGQTIEIIWTILPAFTMIFIALPSLRLLYLLDES-LDPML 76
Cdd:MTH00027   48 IIMLHDQILFILTIIVGVVLWlIIRILLGNNYYSYYWnkLDGSLIEVIWTLIPAFILILIAFPSLRLLYIMDECgFSANI 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727871299  77 SIKSVGHQWYSSYEYSDF-QKMSEFDSYLIPYNGMNQNEFWLLYVDYQTILPMNTQIHTLITSTDMINFWTVPALGVKVD 155
Cdd:MTH00027  128 TIKVTGHQWYWSYSYEDYgEKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVLHSWTVPSLAVKMD 207

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2727871299 156 ATPGRLNQISFFMNRPGLFYGQCSTFFGANHSFKPIVIESMTMKTLISFM 205
Cdd:MTH00027  208 AVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWI 257
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 10-205 3.99e-41

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 139.37  E-value: 3.99e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727871299  10 FILTMITILVAYIMGSLFFNPFTCHFllkgQTIEIIWTILPAFTMIFIALPSLRLLYLLD-ESLDPMLSIKSVGHQWYSS 88
Cdd:MTH00080   35 VLAFVVFLFLYLISNNFYFKSKKIEY----QFGELLCSVFPVLILLMQMVPSLSLLYYYGlMNLDSNLTVKVTGHQWYWS 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727871299  89 YEYSDFQKMsEFDSYLIPYNGMNQNEFWLLYVDYQTILPMNTQIHTLITSTDMINFWTVPALGVKVDATPGRLNQISFFM 168
Cdd:MTH00080  111 YEFSDIPGL-EFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILSTLCYSF 189

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2727871299 169 NRPGLFYGQCSTFFGANHSFKPIVIESMTMKTLISFM 205
Cdd:MTH00080  190 PMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWC 226
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 2-194 4.54e-31

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 112.36  E-value: 4.54e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727871299   2 LFFHDHTHFILTMITILVAYIMGSLFFNPF----TCHFLLKGQTIEIIWTILPAFtMIFIALPSLRLLYLLDESLDPMLS 77
Cdd:MTH00047    5 LLYYDIVCYILALCVFIPCWVYIMLCWQVVsgngSVNFGSENQVLELLWTVVPTL-LVLVLCFLNLNFITSDLDCFSSET 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727871299  78 IKSVGHQWYSSYEYSDfqkMSEFDSYLIPYNGMnqnefwllyVDYQTILPMNTQIHTLITSTDMINFWTVPALGVKVDAT 157
Cdd:MTH00047   84 IKVIGHQWYWSYEYSF---GGSYDSFMTDDIFG---------VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAI 151

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2727871299 158 PGRLNQISFFMNRPGLFYGQCSTFFGANHSFKPIVIE 194
Cdd:MTH00047  152 PGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIE 188
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 84-197 4.69e-28

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 103.75  E-value: 4.69e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727871299  84 QWYSsyeysdFQKMSEFDSYLIPynGMNQNefwlLYVDYQTILPMNTQIHTLITSTDMINFWTVPALGVKVDATPGRLNQ 163
Cdd:PTZ00047   47 KYYS------FQSNLVTDEDLKP--GMLRQ----LEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHK 114

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2727871299 164 ISFFMNRPGLFYGQCSTFFGANHSFKPIVIESMT 197
Cdd:PTZ00047  115 INTFILREGVFYGQCSEMCGTLHGFMPIVVEAVS 148
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
41-197 1.94e-27

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 103.75  E-value: 1.94e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727871299  41 TIEIIWTILPAFTMIFIALPSLRLLYLLDESLDPMLSIKSVGHQWYSSYEYSDfqkmsefdsylipYNGMNQNEfwlLYV 120
Cdd:COG1622    78 KLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPD-------------QGIATVNE---LVL 141

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2727871299 121 dyqtilPMNTQIHTLITSTDMINFWTVPALGVKVDATPGRLNQISFFMNRPGLFYGQCSTFFGANHSFKPIVIESMT 197
Cdd:COG1622   142 ------PVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVS 212
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 42-196 3.72e-22

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: 89.36  E-value: 3.72e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727871299  42 IEIIWTILPAFTMIFIALPSLRLLYLLDESLDP-MLSIKSVGHQWYSSYEYSDFqkmsefdsylipyngmnqnefwLLYV 120
Cdd:TIGR02866  56 LEYVWTVIPLIIVVGLFAATAKGLLYLERPIPKdALKVKVTGYQWWWDFEYPES----------------------GFTT 113

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2727871299 121 DYQTILPMNTQIHTLITSTDMINFWTVPALGVKVDATPGRLNQISFFMNRPGLFYGQCSTFFGANHSFKPIVIESM 196
Cdd:TIGR02866 114 VNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVV 189
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 76-192 4.60e-15

The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of most bacteria, is a multi-chain transmembrane protein located in the inner membrane the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. Caa3 type of CcO Subunit II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the cytochromes a, a3 and CuB active site in subunit I.


Pssm-ID: 259875 [Multi-domain]  Cd Length: 103  Bit Score: 68.03  E-value: 4.60e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727871299  76 LSIKSVGHQWYSSYEYSDfqkmsefdsyLIPYNGMNQNEFWLlyvdyqtilPMNTQIHTLITSTDMI-NFWtVPALGVKV 154
Cdd:cd04213     2 LTIEVTGHQWWWEFRYPD----------EPGRGIVTANELHI---------PVGRPVRLRLTSADVIhSFW-VPSLAGKM 61

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2727871299 155 DATPGRLNQISFFMNRPGLFYGQCSTFFGANHS---FKPIV 192
Cdd:cd04213    62 DMIPGRTNRLWLQADEPGVYRGQCAEFCGASHAlmrFKVIA 102
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 76-194 3.19e-13

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: 63.08  E-value: 3.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727871299  76 LSIKSVGHQWYSSYEYSDFQKMSEFdsylipyngmnqnefwllyvdyqtILPMNTQIHTLITSTDMINFWTVPALGVKVD 155
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPNVRTPNEI------------------------VVPAGTPVRFRVTSPDVIHGFYIPNLGVKVD 56

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2727871299 156 ATPGRLNQISFFMNRPGLFYGQCSTFFGANHSFKPIVIE 194
Cdd:cd13842    57 AVPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-58 2.20e-12

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: 60.42  E-value: 2.20e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2727871299   1 LLFFHDHTHFILTMITILVAYIMGSLFF------NPFTCHFLLKGQTIEIIWTILPAFTMIFIA 58
Cdd:pfam02790  20 LLELHDYIMFILTLILILVLYILVTCLIrfnrrkNPITARYTTHGQTIEIIWTIIPAVILILIA 83
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 76-187 8.16e-12

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: 59.58  E-value: 8.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727871299  76 LSIKSVGHQWYSSYEYSDFqkmsefDSYLIPYNGMNQNEFWLlyvdyqtilPMNTQIHTLITSTDMI-NFWtVPALGVKV 154
Cdd:cd13919     2 LVVEVTAQQWAWTFRYPGG------DGKLGTDDDVTSPELHL---------PVGRPVLFNLRSKDVIhSFW-VPEFRVKQ 65

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2727871299 155 DATPGRLNQISFFMNRPGLFYGQCSTFFGANHS 187
Cdd:cd13919    66 DAVPGRTTRLWFTPTREGEYEVRCAELCGLGHY 98
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 76-187 1.32e-08

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: 50.71  E-value: 1.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727871299  76 LSIKSVGHQWYSSYEYsdfqkmsefdsyliPYNGMNQNEfwlLYVdyqtilPMNTQIHTLITSTDMINFWTVPALGVKVD 155
Cdd:cd13915     2 LEIQVTGRQWMWEFTY--------------PNGKREINE---LHV------PVGKPVRLILTSKDVIHSFYVPAFRIKQD 58

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2727871299 156 ATPGRLNQISFFMNRPGLFYGQCSTFFGANHS 187
Cdd:cd13915    59 VVPGRYTYLWFEATKPGEYDLFCTEYCGTGHS 90
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 126-184 1.33e-04

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: 39.45  E-value: 1.33e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727871299 126 LPMNTQIHTLITSTDMIN-FWtVPALGVKVDATPGRLNQISFFMNRPGLFYGQCSTFFGA 184
Cdd:cd04212    29 IPVGRPVNFRLTSDSVMNsFF-IPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGE 87
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 126-186 2.71e-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: 36.01  E-value: 2.71e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2727871299 126 LPMNTQIHTLITSTDMINFWTVPALGVKVDATPGRLNQISFFMNRPGLFYGQCSTFFGANH 186
Cdd:cd13913    29 VPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGH 89
 
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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