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Conserved domains on  [gi|346644600|dbj|BAK79073|]
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cytochrome oxidase subunit 2 (mitochondrion) [Vollenhovia emeryi]

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
 25-244 1.55e-124

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 352.59  E-value: 1.55e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346644600  25 TWL-LTLQNSNSPTYDMMIFFHDFTMILLIFITMMILSIMLSLSKNLLIDRYLLQGHKIEIIWTMAPMFILMFIALPSLK 103
Cdd:MTH00154   3 TWSnLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346644600 104 ILYLTDELHNNKLTIKTIGHQWYWSYEYSDFSNIEFDSFMIPTPELQSNEFRLLEVDNRCIMPFNFPIRILTTSMDVIHA 183
Cdd:MTH00154  83 LLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHS 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 346644600 184 WTLPSLGIKMDSTPGRLNQSFIYINRPGMFFGQCSEICGINHSFMPIVVESTNFSNLKNWL 244
Cdd:MTH00154 163 WTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWI 223
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 25-244 1.55e-124

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 352.59  E-value: 1.55e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346644600  25 TWL-LTLQNSNSPTYDMMIFFHDFTMILLIFITMMILSIMLSLSKNLLIDRYLLQGHKIEIIWTMAPMFILMFIALPSLK 103
Cdd:MTH00154   3 TWSnLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346644600 104 ILYLTDELHNNKLTIKTIGHQWYWSYEYSDFSNIEFDSFMIPTPELQSNEFRLLEVDNRCIMPFNFPIRILTTSMDVIHA 183
Cdd:MTH00154  83 LLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHS 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 346644600 184 WTLPSLGIKMDSTPGRLNQSFIYINRPGMFFGQCSEICGINHSFMPIVVESTNFSNLKNWL 244
Cdd:MTH00154 163 WTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWI 223
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 116-243 7.14e-85

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: 248.64  E-value: 7.14e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346644600 116 LTIKTIGHQWYWSYEYSDFSNIEFDSFMIPTPELQSNEFRLLEVDNRCIMPFNFPIRILTTSMDVIHAWTLPSLGIKMDS 195
Cdd:cd13912    3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 346644600 196 TPGRLNQSFIYINRPGMFFGQCSEICGINHSFMPIVVESTNFSNLKNW 243
Cdd:cd13912   83 VPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
116-235 1.25e-74

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 222.28  E-value: 1.25e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346644600  116 LTIKTIGHQWYWSYEYSDFSNIEFDSFMIPTPELQSNEFRLLEVDNRCIMPFNFPIRILTTSMDVIHAWTLPSLGIKMDS 195
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 346644600  196 TPGRLNQSFIYINRPGMFFGQCSEICGINHSFMPIVVEST 235
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
25-233 2.44e-43

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 146.51  E-value: 2.44e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346644600  25 TWLLTLQNSNSPTYDMMIFFHDFTMILLIFITMMILSIML-SL-----SKNLLIDRYLLQGHKIEIIWTMAPMFILMFIA 98
Cdd:COG1622   16 SGQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLyFAiryrrRKGDADPAQFHHNTKLEIVWTVIPIIIVIVLA 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346644600  99 LPSLKILYLTDELHNNKLTIKTIGHQWYWSYEYSDfsniefdsfmipTPELQSNEFRLlevdnrcimPFNFPIRILTTSM 178
Cdd:COG1622   96 VPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPD------------QGIATVNELVL---------PVGRPVRFLLTSA 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 346644600 179 DVIHAWTLPSLGIKMDSTPGRLNQSFIYINRPGMFFGQCSEICGINHSFMPIVVE 233
Cdd:COG1622  155 DVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVV 209
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 81-233 1.65e-35

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: 125.19  E-value: 1.65e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346644600   81 KIEIIWTMAPMFILM-FIALPSLKILYLTDELHNNKLTIKTIGHQWYWSYEYSDFsniefdsfmiptpelqsnefrLLEV 159
Cdd:TIGR02866  55 RLEYVWTVIPLIIVVgLFAATAKGLLYLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTT 113

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 346644600  160 DNRCIMPFNFPIRILTTSMDVIHAWTLPSLGIKMDSTPGRLNQSFIYINRPGMFFGQCSEICGINHSFMPIVVE 233
Cdd:TIGR02866 114 VNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVV 187
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 25-244 1.55e-124

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 352.59  E-value: 1.55e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346644600  25 TWL-LTLQNSNSPTYDMMIFFHDFTMILLIFITMMILSIMLSLSKNLLIDRYLLQGHKIEIIWTMAPMFILMFIALPSLK 103
Cdd:MTH00154   3 TWSnLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346644600 104 ILYLTDELHNNKLTIKTIGHQWYWSYEYSDFSNIEFDSFMIPTPELQSNEFRLLEVDNRCIMPFNFPIRILTTSMDVIHA 183
Cdd:MTH00154  83 LLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHS 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 346644600 184 WTLPSLGIKMDSTPGRLNQSFIYINRPGMFFGQCSEICGINHSFMPIVVESTNFSNLKNWL 244
Cdd:MTH00154 163 WTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWI 223
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 28-244 1.46e-108

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 312.26  E-value: 1.46e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346644600  28 LTLQNSNSPTYDMMIFFHDFTMILLIFITMMILSIMLSLSKNLLIDRYLLQGHKIEIIWTMAPMFILMFIALPSLKILYL 107
Cdd:MTH00140   7 LGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPSLRLLYL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346644600 108 TDELHNNKLTIKTIGHQWYWSYEYSDFSNIEFDSFMIPTPELQSNEFRLLEVDNRCIMPFNFPIRILTTSMDVIHAWTLP 187
Cdd:MTH00140  87 LDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVP 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 346644600 188 SLGIKMDSTPGRLNQSFIYINRPGMFFGQCSEICGINHSFMPIVVESTNFSNLKNWL 244
Cdd:MTH00140 167 SLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWL 223
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 25-243 4.41e-107

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 308.55  E-value: 4.41e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346644600  25 TWL-LTLQNSNSPTYDMMIFFHDFTMILLIFITMMILSIMLSLSKNLLIDRYLLQGHKIEIIWTMAPMFILMFIALPSLK 103
Cdd:MTH00038   3 TWLqLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPSLQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346644600 104 ILYLTDELHNNKLTIKTIGHQWYWSYEYSDFSNIEFDSFMIPTPELQSNEFRLLEVDNRCIMPFNFPIRILTTSMDVIHA 183
Cdd:MTH00038  83 LLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLHS 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 346644600 184 WTLPSLGIKMDSTPGRLNQSFIYINRPGMFFGQCSEICGINHSFMPIVVESTNFSNLKNW 243
Cdd:MTH00038 163 WAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENW 222
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 28-245 1.39e-105

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 304.60  E-value: 1.39e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346644600  28 LTLQNSNSPTYDMMIFFHDFTMILLIFITMMILSIMLSLSKNLLIDRYLLQGHKIEIIWTMAPMFILMFIALPSLKILYL 107
Cdd:MTH00168   7 LGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPSLRLLYL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346644600 108 TDELHNNKLTIKTIGHQWYWSYEYSDFSNIEFDSFMIPTPELQSNEFRLLEVDNRCIMPFNFPIRILTTSMDVIHAWTLP 187
Cdd:MTH00168  87 MDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSWTLP 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 346644600 188 SLGIKMDSTPGRLNQSFIYINRPGMFFGQCSEICGINHSFMPIVVESTNFSNLKNWLL 245
Cdd:MTH00168 167 SLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVD 224
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 28-244 5.45e-104

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 300.68  E-value: 5.45e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346644600  28 LTLQNSNSPTYDMMIFFHDFTMILLIFITMMILSIMLSLSKNLLIDRYLLQGHKIEIIWTMAPMFILMFIALPSLKILYL 107
Cdd:MTH00117   7 LGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPSLRILYL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346644600 108 TDELHNNKLTIKTIGHQWYWSYEYSDFSNIEFDSFMIPTPELQSNEFRLLEVDNRCIMPFNFPIRILTTSMDVIHAWTLP 187
Cdd:MTH00117  87 MDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVP 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 346644600 188 SLGIKMDSTPGRLNQSFIYINRPGMFFGQCSEICGINHSFMPIVVESTNFSNLKNWL 244
Cdd:MTH00117 167 SLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWS 223
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 28-246 1.71e-102

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 297.01  E-value: 1.71e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346644600  28 LTLQNSNSPTYDMMIFFHDFTMILLIFITMMILSIMLSLSKNLLIDRYLLQGHKIEIIWTMAPMFILMFIALPSLKILYL 107
Cdd:MTH00139   7 LGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPSLRLLYL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346644600 108 TDELHNNKLTIKTIGHQWYWSYEYSDFSNIEFDSFMIPTPELQSNEFRLLEVDNRCIMPFNFPIRILTTSMDVIHAWTLP 187
Cdd:MTH00139  87 MDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSWTVP 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 346644600 188 SLGIKMDSTPGRLNQSFIYINRPGMFFGQCSEICGINHSFMPIVVESTNFSNLKNWLLF 246
Cdd:MTH00139 167 SLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILE 225
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 25-245 1.48e-96

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 282.41  E-value: 1.48e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346644600  25 TWLLTLQNSNSPTYDMMIFFHDFTMILLIFITMMILSIMLSLSKNLLIDRYLLQGHKIEIIWTMAPMFILMFIALPSLKI 104
Cdd:MTH00023  13 PWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKL 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346644600 105 LYLTDELHNNKLTIKTIGHQWYWSYEYSDF--SNIEFDSFMIPTPELQSNEFRLLEVDNRCIMPFNFPIRILTTSMDVIH 182
Cdd:MTH00023  93 LYLMDEVVSPALTIKAIGHQWYWSYEYSDYegETLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLH 172

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 346644600 183 AWTLPSLGIKMDSTPGRLNQSFIYINRPGMFFGQCSEICGINHSFMPIVVESTNFSNLKNWLL 245
Cdd:MTH00023 173 SFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLL 235
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 28-245 8.02e-95

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 277.51  E-value: 8.02e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346644600  28 LTLQNSNSPTYDMMIFFHDFTMILLIFITMMILSIMLSLSKNLLIDRYLLQGHKIEIIWTMAPMFILMFIALPSLKILYL 107
Cdd:MTH00008   7 LMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSLRLLYL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346644600 108 TDELHNNKLTIKTIGHQWYWSYEYSDFSNIEFDSFMIPTPELQSNEFRLLEVDNRCIMPFNFPIRILTTSMDVIHAWTLP 187
Cdd:MTH00008  87 MDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTVP 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 346644600 188 SLGIKMDSTPGRLNQSFIYINRPGMFFGQCSEICGINHSFMPIVVESTNFSNLKNWLL 245
Cdd:MTH00008 167 SLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVS 224
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 28-243 3.75e-94

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 275.82  E-value: 3.75e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346644600  28 LTLQNSNSPTYDMMIFFHDFTMILLIFITMMILSIMLSLSKNLLIDRYLLQGHKIEIIWTMAPMFILMFIALPSLKILYL 107
Cdd:MTH00129   7 LGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRILYL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346644600 108 TDELHNNKLTIKTIGHQWYWSYEYSDFSNIEFDSFMIPTPELQSNEFRLLEVDNRCIMPFNFPIRILTTSMDVIHAWTLP 187
Cdd:MTH00129  87 MDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVP 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 346644600 188 SLGIKMDSTPGRLNQSFIYINRPGMFFGQCSEICGINHSFMPIVVESTNFSNLKNW 243
Cdd:MTH00129 167 ALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 28-243 3.24e-93

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 273.68  E-value: 3.24e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346644600  28 LTLQNSNSPTYDMMIFFHDFTMILLIFITMMILSIMLSLSKNLLIDRYLLQGHKIEIIWTMAPMFILMFIALPSLKILYL 107
Cdd:MTH00185   7 LGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLRILYL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346644600 108 TDELHNNKLTIKTIGHQWYWSYEYSDFSNIEFDSFMIPTPELQSNEFRLLEVDNRCIMPFNFPIRILTTSMDVIHAWTLP 187
Cdd:MTH00185  87 MDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVP 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 346644600 188 SLGIKMDSTPGRLNQSFIYINRPGMFFGQCSEICGINHSFMPIVVESTNFSNLKNW 243
Cdd:MTH00185 167 ALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 28-248 3.16e-91

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 268.51  E-value: 3.16e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346644600  28 LTLQNSNSPTYDMMIFFHDFTMILLIFITMMILSIMLSLSKNLLIDRYLLQGHKIEIIWTMAPMFILMFIALPSLKILYL 107
Cdd:MTH00098   7 LGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRILYM 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346644600 108 TDELHNNKLTIKTIGHQWYWSYEYSDFSNIEFDSFMIPTPELQSNEFRLLEVDNRCIMPFNFPIRILTTSMDVIHAWTLP 187
Cdd:MTH00098  87 MDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVP 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 346644600 188 SLGIKMDSTPGRLNQSFIYINRPGMFFGQCSEICGINHSFMPIVVESTNFSNLKNWLLFTL 248
Cdd:MTH00098 167 SLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASML 227
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 26-244 1.39e-89

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 264.72  E-value: 1.39e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346644600  26 WLLTLQNSNSPTYDMMIFFHDFTMILLIFITMMILSIMLSLSKNLLIDRYLLQGHKIEIIWTMAPMFILMFIALPSLKIL 105
Cdd:MTH00051   7 WQLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346644600 106 YLTDELHNNKLTIKTIGHQWYWSYEYSDF--SNIEFDSFMIPTPELQSNEFRLLEVDNRCIMPFNFPIRILTTSMDVIHA 183
Cdd:MTH00051  87 YLMDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHS 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 346644600 184 WTLPSLGIKMDSTPGRLNQSFIYINRPGMFFGQCSEICGINHSFMPIVVESTNFSNLKNWL 244
Cdd:MTH00051 167 FAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWV 227
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 28-244 5.81e-89

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 262.79  E-value: 5.81e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346644600  28 LTLQNSNSPTYDMMIFFHDFTMILLIFITMMILSIMLSLSKNLLIDRYLLQGHKIEIIWTMAPMFILMFIALPSLKILYL 107
Cdd:MTH00076   7 LGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRILYL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346644600 108 TDELHNNKLTIKTIGHQWYWSYEYSDFSNIEFDSFMIPTPELQSNEFRLLEVDNRCIMPFNFPIRILTTSMDVIHAWTLP 187
Cdd:MTH00076  87 MDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVP 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 346644600 188 SLGIKMDSTPGRLNQSFIYINRPGMFFGQCSEICGINHSFMPIVVESTNFSNLKNWL 244
Cdd:MTH00076 167 SLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWS 223
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 116-243 7.14e-85

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: 248.64  E-value: 7.14e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346644600 116 LTIKTIGHQWYWSYEYSDFSNIEFDSFMIPTPELQSNEFRLLEVDNRCIMPFNFPIRILTTSMDVIHAWTLPSLGIKMDS 195
Cdd:cd13912    3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 346644600 196 TPGRLNQSFIYINRPGMFFGQCSEICGINHSFMPIVVESTNFSNLKNW 243
Cdd:cd13912   83 VPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
116-235 1.25e-74

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 222.28  E-value: 1.25e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346644600  116 LTIKTIGHQWYWSYEYSDFSNIEFDSFMIPTPELQSNEFRLLEVDNRCIMPFNFPIRILTTSMDVIHAWTLPSLGIKMDS 195
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 346644600  196 TPGRLNQSFIYINRPGMFFGQCSEICGINHSFMPIVVEST 235
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 26-244 1.92e-71

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 219.51  E-value: 1.92e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346644600  26 WLLTLQNSNSPTYDMMIFFHDFTMILLIFITMMILSIMLslsKNLLIDRYL------LQGHKIEIIWTMAPMFILMFIAL 99
Cdd:MTH00027  33 WQLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLII---RILLGNNYYsyywnkLDGSLIEVIWTLIPAFILILIAF 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346644600 100 PSLKILYLTDE-LHNNKLTIKTIGHQWYWSYEYSDF--SNIEFDSFMIPTPELQSNEFRLLEVDNRCIMPFNFPIRILTT 176
Cdd:MTH00027 110 PSLRLLYIMDEcGFSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLIT 189

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 346644600 177 SMDVIHAWTLPSLGIKMDSTPGRLNQSFIYINRPGMFFGQCSEICGINHSFMPIVVESTNFSNLKNWL 244
Cdd:MTH00027 190 AADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWI 257
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 30-248 5.78e-68

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 209.48  E-value: 5.78e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346644600  30 LQNSNSPTYDMMIFFHDFTMILL---IFITMMILSIMLSLSKNLLIDRYLLQGHKIEIIWTMAPMFILMFIALPSLKILY 106
Cdd:MTH00080   8 LNFSNSLFSSYMDWFHNFNCSLLfgeFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLY 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346644600 107 LTdELHN--NKLTIKTIGHQWYWSYEYSDFSNIEFDSFMIPTPELQSNEFRLLEVDNRCIMPFNFPIRILTTSMDVIHAW 184
Cdd:MTH00080  88 YY-GLMNldSNLTVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSW 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 346644600 185 TLPSLGIKMDSTPGRLNQSFIYINRPGMFFGQCSEICGINHSFMPIVVESTNFSNLKNWLLFTL 248
Cdd:MTH00080 167 ALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWCKLLL 230
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 82-239 6.07e-44

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 146.64  E-value: 6.07e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346644600  82 IEIIWTMAPMFILMFiaLPSLKILYLTDELHNN-KLTIKTIGHQWYWSYEYSDfsNIEFDSFMiptpelqsNEFRLLeVD 160
Cdd:MTH00047  49 LELLWTVVPTLLVLV--LCFLNLNFITSDLDCFsSETIKVIGHQWYWSYEYSF--GGSYDSFM--------TDDIFG-VD 115

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 346644600 161 NRCIMPFNFPIRILTTSMDVIHAWTLPSLGIKMDSTPGRLNQSFIYINRPGMFFGQCSEICGINHSFMPIVVESTNFSN 239
Cdd:MTH00047 116 KPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVVDVDS 194
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
25-233 2.44e-43

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 146.51  E-value: 2.44e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346644600  25 TWLLTLQNSNSPTYDMMIFFHDFTMILLIFITMMILSIML-SL-----SKNLLIDRYLLQGHKIEIIWTMAPMFILMFIA 98
Cdd:COG1622   16 SGQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLyFAiryrrRKGDADPAQFHHNTKLEIVWTVIPIIIVIVLA 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346644600  99 LPSLKILYLTDELHNNKLTIKTIGHQWYWSYEYSDfsniefdsfmipTPELQSNEFRLlevdnrcimPFNFPIRILTTSM 178
Cdd:COG1622   96 VPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPD------------QGIATVNELVL---------PVGRPVRFLLTSA 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 346644600 179 DVIHAWTLPSLGIKMDSTPGRLNQSFIYINRPGMFFGQCSEICGINHSFMPIVVE 233
Cdd:COG1622  155 DVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVV 209
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 81-233 1.65e-35

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: 125.19  E-value: 1.65e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346644600   81 KIEIIWTMAPMFILM-FIALPSLKILYLTDELHNNKLTIKTIGHQWYWSYEYSDFsniefdsfmiptpelqsnefrLLEV 159
Cdd:TIGR02866  55 RLEYVWTVIPLIIVVgLFAATAKGLLYLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTT 113

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 346644600  160 DNRCIMPFNFPIRILTTSMDVIHAWTLPSLGIKMDSTPGRLNQSFIYINRPGMFFGQCSEICGINHSFMPIVVE 233
Cdd:TIGR02866 114 VNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVV 187
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 139-234 3.23e-34

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 120.70  E-value: 3.23e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346644600 139 FDSFMIPTPELQSNEFRLLEVDNRCIMPFNFPIRILTTSMDVIHAWTLPSLGIKMDSTPGRLNQSFIYINRPGMFFGQCS 218
Cdd:PTZ00047  51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                         90
                 ....*....|....*.
gi 346644600 219 EICGINHSFMPIVVES 234
Cdd:PTZ00047 131 EMCGTLHGFMPIVVEA 146
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 116-233 2.27e-26

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: 98.14  E-value: 2.27e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346644600 116 LTIKTIGHQWYWSYEYSDfsniefdsfmiptpelqsnefrlLEVDNRCIMPFNFPIRILTTSMDVIHAWTLPSLGIKMDS 195
Cdd:cd13842    1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 346644600 196 TPGRLNQSFIYINRPGMFFGQCSEICGINHSFMPIVVE 233
Cdd:cd13842   58 VPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 116-228 6.62e-26

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: 97.31  E-value: 6.62e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346644600 116 LTIKTIGHQWYWSYEYSDFSNIEFDSfmiptpelqSNEFRLlevdnrcimPFNFPIRILTTSMDVIHAWTLPSLGIKMDS 195
Cdd:cd04213    2 LTIEVTGHQWWWEFRYPDEPGRGIVT---------ANELHI---------PVGRPVRLRLTSADVIHSFWVPSLAGKMDM 63

                         90       100       110
                 ....*....|....*....|....*....|...
gi 346644600 196 TPGRLNQSFIYINRPGMFFGQCSEICGINHSFM 228
Cdd:cd04213   64 IPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 116-233 5.71e-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: 87.31  E-value: 5.71e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346644600 116 LTIKTIGHQWYWSYEYSDfSNIEFdsfmIPTPELQSNEFRLlevdnrcimPFNFPIRILTTSMDVIHAWTLPSLGIKMDS 195
Cdd:cd13919    2 LVVEVTAQQWAWTFRYPG-GDGKL----GTDDDVTSPELHL---------PVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 346644600 196 TPGRLNQSFIYINRPGMFFGQCSEICGINHSFM--PIVVE 233
Cdd:cd13919   68 VPGRTTRLWFTPTREGEYEVRCAELCGLGHYRMraTVKVV 107
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 116-232 6.14e-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: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 81.52  E-value: 6.14e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346644600 116 LTIKTIGHQWYWSYEYsdfsniefdsfmiPTPELQSNEFRLlevdnrcimPFNFPIRILTTSMDVIHAWTLPSLGIKMDS 195
Cdd:cd13915    2 LEIQVTGRQWMWEFTY-------------PNGKREINELHV---------PVGKPVRLILTSKDVIHSFYVPAFRIKQDV 59

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 346644600 196 TPGRLNQSFIYINRPGMFFGQCSEICGINHSFMPIVV 232
Cdd:cd13915   60 VPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGMIGKV 96
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 117-244 2.41e-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: 75.14  E-value: 2.41e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346644600 117 TIKTIGHQWYWSYEYSDFSNIEFDSFMIPTpelqsnefrllevdnrcimpfNFPIRILTTSMDVIHAWTLPSLGIKMDST 196
Cdd:cd13914    2 EIEVEAYQWGWEFSYPEANVTTSEQLVIPA---------------------DRPVYFRITSRDVIHAFHVPELGLKQDAF 60

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 346644600 197 PGRLNQSFIYINRPGMFFGQCSEICGINHSFMPIVVESTNFSNLKNWL 244
Cdd:cd13914   61 PGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 84-244 6.52e-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: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 74.80  E-value: 6.52e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346644600  84 IIWTMapmFILMFIALPSlkilyltDELHNNKLTIKTIGHQWYWSYEYsdfsniefdsfmiPTPELQSNEFRLlevdnrc 163
Cdd:cd13918   11 IVWTY---GMLLYVEDPP-------DEADEDALEVEVEGFQFGWQFEY-------------PNGVTTGNTLRV------- 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346644600 164 imPFNFPIRILTTSMDVIHAWTLPSLGIKMDSTPGRLNQSFIYINRPGMFFGQCSEICGINHSFMPIVVESTNFSNLKNW 243
Cdd:cd13918   61 --PADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAW 138


                 .
gi 346644600 244 L 244
Cdd:cd13918  139 Y 139
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 26-104 6.64e-14

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: 65.43  E-value: 6.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346644600   26 WLLTLQNSNSPTYDMMIFFHDFTMILLIFITMMILSIMLSL------SKNLLIDRYLLQGHKIEIIWTMAPMFILMFIAL 99
Cdd:pfam02790   5 WGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTClirfnrRKNPITARYTTHGQTIEIIWTIIPAVILILIAL 84


                  ....*
gi 346644600  100 PSLKI 104
Cdd:pfam02790  85 PSFKL 89
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 166-233 1.37e-06

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: 45.64  E-value: 1.37e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346644600 166 PFNFPIRILTTSMDVIHAWTLPSLGIKMDSTPGRLNQSFIYINRPGMFFGQCSEICGINHSFM--PIVVE 233
Cdd:cd13913   30 PAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNMygKIIVE 99
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 172-233 8.79e-04

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: 259984 [Multi-domain]  Cd Length: 88  Bit Score: 37.35  E-value: 8.79e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 346644600 172 RILTTSMDVIHAWTLPSLGIKMDSTPGRLNQSFIYINRPGMFFGQCSEICGINHSFM--PIVVE 233
Cdd:cd13917   25 RLHLSSLDVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIICNEYCGIGHHTMhgRIIVE 88
 
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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