NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1904806552|ref|YP_009919801|]
View 

Cox2 (mitochondrion) [Metschnikowia agaves]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 14-240 3.50e-95

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 277.87  E-value: 3.50e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552  14 LQDSASPNQEGMHELYDHMMFYLALMLGLVSYMtyvvMVDFKNNKFAYKYLKHGQTLEMMWTMFPAVMLLLMAFPSFILT 93
Cdd:MTH00154    9 FQDSASPLMEQLIFFHDHTMMILIMITILVGYM----MISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552  94 YLCDEVLTPAMTMKVVGLQWYWKYEYSDFMSdkgetMEYESYIMPDDMLEEGQLRLLDTDTSIVLPVDTHVRFIVTANDV 173
Cdd:MTH00154   85 YLLDEVNNPSITLKTIGHQWYWSYEYSDFKN-----IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1904806552 174 IHSFAMPSLGMKIDATPGRLNQVSALIQRTGVYYGQCSELCGINHSLMPMKMECLSMTDFMEWLSDM 240
Cdd:MTH00154  160 IHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNM 226
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 14-240 3.50e-95

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 277.87  E-value: 3.50e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552  14 LQDSASPNQEGMHELYDHMMFYLALMLGLVSYMtyvvMVDFKNNKFAYKYLKHGQTLEMMWTMFPAVMLLLMAFPSFILT 93
Cdd:MTH00154    9 FQDSASPLMEQLIFFHDHTMMILIMITILVGYM----MISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552  94 YLCDEVLTPAMTMKVVGLQWYWKYEYSDFMSdkgetMEYESYIMPDDMLEEGQLRLLDTDTSIVLPVDTHVRFIVTANDV 173
Cdd:MTH00154   85 YLLDEVNNPSITLKTIGHQWYWSYEYSDFKN-----IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1904806552 174 IHSFAMPSLGMKIDATPGRLNQVSALIQRTGVYYGQCSELCGINHSLMPMKMECLSMTDFMEWLSDM 240
Cdd:MTH00154  160 IHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNM 226
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 102-236 1.70e-75

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: 224.37  E-value: 1.70e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552 102 PAMTMKVVGLQWYWKYEYSDFmsdkgETMEYESYIMPDDMLEEGQLRLLDTDTSIVLPVDTHVRFIVTANDVIHSFAMPS 181
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDF-----NDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPS 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1904806552 182 LGMKIDATPGRLNQVSALIQRTGVYYGQCSELCGINHSLMPMKMECLSMTDFMEW 236
Cdd:cd13912    76 LGIKVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
104-226 2.99e-69

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 208.42  E-value: 2.99e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552 104 MTMKVVGLQWYWKYEYSDFmsdkgETMEYESYIMPDDMLEEGQLRLLDTDTSIVLPVDTHVRFIVTANDVIHSFAMPSLG 183
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDF-----GDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLG 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1904806552 184 MKIDATPGRLNQVSALIQRTGVYYGQCSELCGINHSLMPMKME 226
Cdd:pfam00116  76 IKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIE 118
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
10-240 4.99e-54

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 173.48  E-value: 4.99e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552  10 WGVRLQDSASPNQEGMHELYDhMMFYLALMLGL-VSYMTYVVMVDF--KNNKFAYKYLKHGQTLEMMWTMFPAVMLLLMA 86
Cdd:COG1622    17 GQLSLPDPAGPIAEEIDDLFW-VSLIIMLVIFVlVFGLLLYFAIRYrrRKGDADPAQFHHNTKLEIVWTVIPIIIVIVLA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552  87 FPSFILTYLCDEVLTPAMTMKVVGLQWYWKYEYsdfmsdkgetmeyesyimpddmLEEGQLrlldTDTSIVLPVDTHVRF 166
Cdd:COG1622    96 VPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRY----------------------PDQGIA----TVNELVLPVGRPVRF 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1904806552 167 IVTANDVIHSFAMPSLGMKIDATPGRLNQVSALIQRTGVYYGQCSELCGINHSLMPMKMECLSMTDFMEWLSDM 240
Cdd:COG1622   150 LLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQ 223
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 20-238 1.38e-39

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: 135.59  E-value: 1.38e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552  20 PNQEGMHELYDHMMFYLALML---GLVSYMTYVVMVDFKNNKFAYK--YLKHGQTLEMMWTMFPAVMLL-LMAFPSFILT 93
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTlisLLVAALLAYVVWKFRRKGDEEKpsQIHGNRRLEYVWTVIPLIIVVgLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552  94 YLCDEVLTPAMTMKVVGLQWYWKYEYSDFmsdkgetmeyesyimpddmleegqlrLLDTDTSIVLPVDTHVRFIVTANDV 173
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPES--------------------------GFTTVNELVLPAGTPVELQVTSKDV 134

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1904806552 174 IHSFAMPSLGMKIDATPGRLNQVSALIQRTGVYYGQCSELCGINHSLMPMKMECLSMTDFMEWLS 238
Cdd:TIGR02866 135 IHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 14-240 3.50e-95

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 277.87  E-value: 3.50e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552  14 LQDSASPNQEGMHELYDHMMFYLALMLGLVSYMtyvvMVDFKNNKFAYKYLKHGQTLEMMWTMFPAVMLLLMAFPSFILT 93
Cdd:MTH00154    9 FQDSASPLMEQLIFFHDHTMMILIMITILVGYM----MISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552  94 YLCDEVLTPAMTMKVVGLQWYWKYEYSDFMSdkgetMEYESYIMPDDMLEEGQLRLLDTDTSIVLPVDTHVRFIVTANDV 173
Cdd:MTH00154   85 YLLDEVNNPSITLKTIGHQWYWSYEYSDFKN-----IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1904806552 174 IHSFAMPSLGMKIDATPGRLNQVSALIQRTGVYYGQCSELCGINHSLMPMKMECLSMTDFMEWLSDM 240
Cdd:MTH00154  160 IHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNM 226
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 1-238 5.36e-90

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 265.46  E-value: 5.36e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552   1 MMWLDVPTPWGVRLQDSASPNQEGMHELYDHMMFYLALMLGLVSYMtyvvMVDFKNNKFAYKYLKHGQTLEMMWTMFPAV 80
Cdd:MTH00023    5 FFYRDIPEPWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWL----IVEALNGKFYDRFLVDGTFLEIVWTIIPAV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552  81 MLLLMAFPSFILTYLCDEVLTPAMTMKVVGLQWYWKYEYSDFmsdKGETMEYESYIMPDDMLEEGQLRLLDTDTSIVLPV 160
Cdd:MTH00023   81 ILVFIALPSLKLLYLMDEVVSPALTIKAIGHQWYWSYEYSDY---EGETLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPI 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1904806552 161 DTHVRFIVTANDVIHSFAMPSLGMKIDATPGRLNQVSALIQRTGVYYGQCSELCGINHSLMPMKMECLSMTDFMEWLS 238
Cdd:MTH00023  158 NTHVRILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLL 235
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 5-241 1.87e-85

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 253.55  E-value: 1.87e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552   5 DVPTPWGVRLQDSASPNQEGMHELYDHMMFYLALMLGLVSYMTYVVMVdfknNKFAYKYLKHGQTLEMMWTMFPAVMLLL 84
Cdd:MTH00051    2 DAPEPWQLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALT----TKYYHKYLFEGTLIEIIWTLIPAAILIF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552  85 MAFPSFILTYLCDEVLTPAMTMKVVGLQWYWKYEYSDFmsdKGETMEYESYIMPDDMLEEGQLRLLDTDTSIVLPVDTHV 164
Cdd:MTH00051   78 IAFPSLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDY---GTDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQV 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1904806552 165 RFIVTANDVIHSFAMPSLGMKIDATPGRLNQVSALIQRTGVYYGQCSELCGINHSLMPMKMECLSMTDFMEWLSDME 241
Cdd:MTH00051  155 RVLVTAADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQS 231
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 10-241 1.42e-84

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 251.01  E-value: 1.42e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552  10 WG-VRLQDSASPNQEGMHELYDHMMFYLALMLGLVSYMTYVVMVdfknNKFAYKYLKHGQTLEMMWTMFPAVMLLLMAFP 88
Cdd:MTH00140    4 WGqLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLF----NKFSCRTILEAQKLETIWTIVPALILVFLALP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552  89 SFILTYLCDEVLTPAMTMKVVGLQWYWKYEYSDFMSdkgetMEYESYIMPDDMLEEGQLRLLDTDTSIVLPVDTHVRFIV 168
Cdd:MTH00140   80 SLRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSV-----IEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLV 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1904806552 169 TANDVIHSFAMPSLGMKIDATPGRLNQVSALIQRTGVYYGQCSELCGINHSLMPMKMECLSMTDFMEWLSDME 241
Cdd:MTH00140  155 TSADVIHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELMS 227
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 8-238 2.25e-83

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 247.97  E-value: 2.25e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552   8 TPWGVRLQDSASPNQEGMHELYDHMMFYLALMLGLVSYMTYVVMvdfkNNKFAYKYLKHGQTLEMMWTMFPAVMLLLMAF 87
Cdd:MTH00168    3 TYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLV----TSKYTNRFLLDSQMIEFVWTIIPAFILISLAL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552  88 PSFILTYLCDEVLTPAMTMKVVGLQWYWKYEYSDFMSdkgetMEYESYIMPDDMLEEGQLRLLDTDTSIVLPVDTHVRFI 167
Cdd:MTH00168   79 PSLRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYND-----LEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVL 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1904806552 168 VTANDVIHSFAMPSLGMKIDATPGRLNQVSALIQRTGVYYGQCSELCGINHSLMPMKMECLSMTDFMEWLS 238
Cdd:MTH00168  154 VTSADVLHSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVD 224
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 10-240 1.58e-80

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 240.77  E-value: 1.58e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552  10 WG-VRLQDSASPNQEGMHELYDHMMFYLALMLGLVSYMTYVVMVdfknNKFAYKYLKHGQTLEMMWTMFPAVMLLLMAFP 88
Cdd:MTH00139    4 WGqLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMS----NKFTSRSLLESQEVETIWTVLPAFILLFLALP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552  89 SFILTYLCDEVLTPAMTMKVVGLQWYWKYEYSDFMSdkgetMEYESYIMPDDMLEEGQLRLLDTDTSIVLPVDTHVRFIV 168
Cdd:MTH00139   80 SLRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKN-----LSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALI 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1904806552 169 TANDVIHSFAMPSLGMKIDATPGRLNQVSALIQRTGVYYGQCSELCGINHSLMPMKMECLSMTDFMEWLSDM 240
Cdd:MTH00139  155 TAADVLHSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILEK 226
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 10-238 1.01e-77

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 233.98  E-value: 1.01e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552  10 WG-VRLQDSASPNQEGMHELYDHMMFYLALMLGLVSYMTYVVMVdfknNKFAYKYLKHGQTLEMMWTMFPAVMLLLMAFP 88
Cdd:MTH00008    4 WGqLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMF----NKLSNRYILEAQQIETIWTILPALILLFLAFP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552  89 SFILTYLCDEVLTPAMTMKVVGLQWYWKYEYSDFMSdkgetMEYESYIMPDDMLEEGQLRLLDTDTSIVLPVDTHVRFIV 168
Cdd:MTH00008   80 SLRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSN-----LEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLV 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552 169 TANDVIHSFAMPSLGMKIDATPGRLNQVSALIQRTGVYYGQCSELCGINHSLMPMKMECLSMTDFMEWLS 238
Cdd:MTH00008  155 TAADVIHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVS 224
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 102-236 1.70e-75

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: 224.37  E-value: 1.70e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552 102 PAMTMKVVGLQWYWKYEYSDFmsdkgETMEYESYIMPDDMLEEGQLRLLDTDTSIVLPVDTHVRFIVTANDVIHSFAMPS 181
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDF-----NDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPS 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1904806552 182 LGMKIDATPGRLNQVSALIQRTGVYYGQCSELCGINHSLMPMKMECLSMTDFMEW 236
Cdd:cd13912    76 LGIKVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 8-240 1.89e-74

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 225.35  E-value: 1.89e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552   8 TPWGVRLQDSASPNQEGMHELYDHMMFYLALMLGLVSYMTYVVMVDFKNNKFaykyLKHGQTLEMMWTMFPAVMLLLMAF 87
Cdd:MTH00038    3 TWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRF----FLEGQELETIWTIVPAFILIFIAL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552  88 PSFILTYLCDEVLTPAMTMKVVGLQWYWKYEYSDFMSdkgetMEYESYIMPDDMLEEGQLRLLDTDTSIVLPVDTHVRFI 167
Cdd:MTH00038   79 PSLQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYND-----LEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVL 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1904806552 168 VTANDVIHSFAMPSLGMKIDATPGRLNQVSALIQRTGVYYGQCSELCGINHSLMPMKMECLSMTDFMEWLSDM 240
Cdd:MTH00038  154 VSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNF 226
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 14-240 1.34e-73

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 223.25  E-value: 1.34e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552  14 LQDSASPNQEGMHELYDHMMFYLALMLGLVSYMTYVVMVdfknNKFAYKYLKHGQTLEMMWTMFPAVMLLLMAFPSFILT 93
Cdd:MTH00117    9 FQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLT----TKLTHTNTVDAQEVELIWTILPAIVLILLALPSLRIL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552  94 YLCDEVLTPAMTMKVVGLQWYWKYEYSDFmsdkgETMEYESYIMPDDMLEEGQLRLLDTDTSIVLPVDTHVRFIVTANDV 173
Cdd:MTH00117   85 YLMDEINNPHLTIKAIGHQWYWSYEYTDY-----KDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1904806552 174 IHSFAMPSLGMKIDATPGRLNQVSALIQRTGVYYGQCSELCGINHSLMPMKMECLSMTDFMEWLSDM 240
Cdd:MTH00117  160 LHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLL 226
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 14-240 3.04e-72

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 220.14  E-value: 3.04e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552  14 LQDSASPNQEGMHELYDHMMFYLALMLGLVSYMTyVVMVdfkNNKFAYKYLKHGQTLEMMWTMFPAVMLLLMAFPSFILT 93
Cdd:MTH00185    9 LQDAASPVMEELIHFHDHTLMIVFLISTLVLYII-VAMV---TTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLRIL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552  94 YLCDEVLTPAMTMKVVGLQWYWKYEYSDFmsdkgETMEYESYIMPDDMLEEGQLRLLDTDTSIVLPVDTHVRFIVTANDV 173
Cdd:MTH00185   85 YLMDEINDPHLTIKAMGHQWYWSYEYTDY-----EQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1904806552 174 IHSFAMPSLGMKIDATPGRLNQVSALIQRTGVYYGQCSELCGINHSLMPMKMECLSMTDFMEWLSDM 240
Cdd:MTH00185  160 LHSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLM 226
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 14-241 1.07e-70

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 215.80  E-value: 1.07e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552  14 LQDSASPNQEGMHELYDHMMFYLALMLGLVSYMTYVVMVdfknNKFAYKYLKHGQTLEMMWTMFPAVMLLLMAFPSFILT 93
Cdd:MTH00076    9 FQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMT----TKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRIL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552  94 YLCDEVLTPAMTMKVVGLQWYWKYEYSDFmsdkgETMEYESYIMPDDMLEEGQLRLLDTDTSIVLPVDTHVRFIVTANDV 173
Cdd:MTH00076   85 YLMDEINDPHLTVKAIGHQWYWSYEYTDY-----EDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1904806552 174 IHSFAMPSLGMKIDATPGRLNQVSALIQRTGVYYGQCSELCGINHSLMPMKMECLSMTDFMEWLSDME 241
Cdd:MTH00076  160 LHSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSML 227
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 14-240 1.17e-70

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 216.12  E-value: 1.17e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552  14 LQDSASPNQEGMHELYDHMMFYLALMLGLVSYMTyVVMVdfkNNKFAYKYLKHGQTLEMMWTMFPAVMLLLMAFPSFILT 93
Cdd:MTH00129    9 FQDAASPVMEELLHFHDHALMIVFLISTLVLYII-VAMV---STKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRIL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552  94 YLCDEVLTPAMTMKVVGLQWYWKYEYSDFmsdkgETMEYESYIMPDDMLEEGQLRLLDTDTSIVLPVDTHVRFIVTANDV 173
Cdd:MTH00129   85 YLMDEINDPHLTIKAMGHQWYWSYEYTDY-----EDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1904806552 174 IHSFAMPSLGMKIDATPGRLNQVSALIQRTGVYYGQCSELCGINHSLMPMKMECLSMTDFMEWLSDM 240
Cdd:MTH00129  160 LHSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLM 226
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
104-226 2.99e-69

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 208.42  E-value: 2.99e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552 104 MTMKVVGLQWYWKYEYSDFmsdkgETMEYESYIMPDDMLEEGQLRLLDTDTSIVLPVDTHVRFIVTANDVIHSFAMPSLG 183
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDF-----GDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLG 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1904806552 184 MKIDATPGRLNQVSALIQRTGVYYGQCSELCGINHSLMPMKME 226
Cdd:pfam00116  76 IKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIE 118
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 7-240 2.39e-67

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 207.26  E-value: 2.39e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552   7 PTPWGVRLQDSASPNQEGMHELYDHMMFYLALMLGLVSYMTYVVMvdfkNNKFAYKYLKHGQTLEMMWTMFPAVMLLLMA 86
Cdd:MTH00098    2 AYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLML----TTKLTHTSTMDAQEVETIWTILPAIILILIA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552  87 FPSFILTYLCDEVLTPAMTMKVVGLQWYWKYEYSDFmsdkgETMEYESYIMPDDMLEEGQLRLLDTDTSIVLPVDTHVRF 166
Cdd:MTH00098   78 LPSLRILYMMDEINNPSLTVKTMGHQWYWSYEYTDY-----EDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRM 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1904806552 167 IVTANDVIHSFAMPSLGMKIDATPGRLNQVSALIQRTGVYYGQCSELCGINHSLMPMKMECLSMTDFMEWLSDM 240
Cdd:MTH00098  153 LISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASM 226
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 5-237 5.20e-67

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 207.96  E-value: 5.20e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552   5 DVPTPWGVRLQDSASPNQEGMHELYDHMMFYLALMLGLVSYMtyVVMVDFKNNKFAYKYLK-HGQTLEMMWTMFPAVMLL 83
Cdd:MTH00027   28 DANEPWQLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWL--IIRILLGNNYYSYYWNKlDGSLIEVIWTLIPAFILI 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552  84 LMAFPSFILTYLCDE-VLTPAMTMKVVGLQWYWKYEYSDFMSdkgETMEYESYIMPDDMLEEGQLRLLDTDTSIVLPVDT 162
Cdd:MTH00027  106 LIAFPSLRLLYIMDEcGFSANITIKVTGHQWYWSYSYEDYGE---KNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDT 182

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1904806552 163 HVRFIVTANDVIHSFAMPSLGMKIDATPGRLNQVSALIQRTGVYYGQCSELCGINHSLMPMKMECLSMTDFMEWL 237
Cdd:MTH00027  183 NVRVLITAADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWI 257
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 25-237 1.95e-55

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 177.12  E-value: 1.95e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552  25 MHELYDHMMFYLALMLGLVSYMTYVVMvdfkNNKFAYKYLKHGQTLEMMWTMFPAVMLLLMAFPSFILTYLCDEV-LTPA 103
Cdd:MTH00080   22 FHNFNCSLLFGEFVLAFVVFLFLYLIS----NNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMnLDSN 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552 104 MTMKVVGLQWYWKYEYSDFMSdkgetMEYESYIMPDDMLEEGQLRLLDTDTSIVLPVDTHVRFIVTANDVIHSFAMPSLG 183
Cdd:MTH00080   98 LTVKVTGHQWYWSYEFSDIPG-----LEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLS 172

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1904806552 184 MKIDATPGRLNQVSALIQRTGVYYGQCSELCGINHSLMPMKMECLSMTDFMEWL 237
Cdd:MTH00080  173 IKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWC 226
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
10-240 4.99e-54

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 173.48  E-value: 4.99e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552  10 WGVRLQDSASPNQEGMHELYDhMMFYLALMLGL-VSYMTYVVMVDF--KNNKFAYKYLKHGQTLEMMWTMFPAVMLLLMA 86
Cdd:COG1622    17 GQLSLPDPAGPIAEEIDDLFW-VSLIIMLVIFVlVFGLLLYFAIRYrrRKGDADPAQFHHNTKLEIVWTVIPIIIVIVLA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552  87 FPSFILTYLCDEVLTPAMTMKVVGLQWYWKYEYsdfmsdkgetmeyesyimpddmLEEGQLrlldTDTSIVLPVDTHVRF 166
Cdd:COG1622    96 VPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRY----------------------PDQGIA----TVNELVLPVGRPVRF 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1904806552 167 IVTANDVIHSFAMPSLGMKIDATPGRLNQVSALIQRTGVYYGQCSELCGINHSLMPMKMECLSMTDFMEWLSDM 240
Cdd:COG1622   150 LLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQ 223
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 20-238 1.38e-39

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: 135.59  E-value: 1.38e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552  20 PNQEGMHELYDHMMFYLALML---GLVSYMTYVVMVDFKNNKFAYK--YLKHGQTLEMMWTMFPAVMLL-LMAFPSFILT 93
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTlisLLVAALLAYVVWKFRRKGDEEKpsQIHGNRRLEYVWTVIPLIIVVgLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552  94 YLCDEVLTPAMTMKVVGLQWYWKYEYSDFmsdkgetmeyesyimpddmleegqlrLLDTDTSIVLPVDTHVRFIVTANDV 173
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPES--------------------------GFTTVNELVLPAGTPVELQVTSKDV 134

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1904806552 174 IHSFAMPSLGMKIDATPGRLNQVSALIQRTGVYYGQCSELCGINHSLMPMKMECLSMTDFMEWLS 238
Cdd:TIGR02866 135 IHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 68-226 2.33e-37

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 129.69  E-value: 2.33e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552  68 QTLEMMWTMFPAVMLLLMAFpsFILTYL-CDEVLTPAMTMKVVGLQWYWKYEYSDfmsdkgeTMEYESYIMPDDMLEEGQ 146
Cdd:MTH00047   47 QVLELLWTVVPTLLVLVLCF--LNLNFItSDLDCFSSETIKVIGHQWYWSYEYSF-------GGSYDSFMTDDIFGVDKP 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552 147 LRLLdtdtsivlpVDTHVRFIVTANDVIHSFAMPSLGMKIDATPGRLNQVSALIQRTGVYYGQCSELCGINHSLMPMKME 226
Cdd:MTH00047  118 LRLV---------YGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIE 188
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 132-229 2.99e-37

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 128.40  E-value: 2.99e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552 132 YESYIMPDDMLEEGQLRLLDTDTSIVLPVDTHVRFIVTANDVIHSFAMPSLGMKIDATPGRLNQVSALIQRTGVYYGQCS 211
Cdd:PTZ00047   51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                          90
                  ....*....|....*...
gi 1904806552 212 ELCGINHSLMPMKMECLS 229
Cdd:PTZ00047  131 EMCGTLHGFMPIVVEAVS 148
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 6-92 9.39e-29

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: 103.95  E-value: 9.39e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552   6 VPTPWGVRLQDSASPNQEGMHELYDHMMFYLALMLGLVSYMTYVVMVDF--KNNKFAYKYLKHGQTLEMMWTMFPAVMLL 83
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRFnrRKNPITARYTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 1904806552  84 LMAFPSFIL 92
Cdd:pfam02790  81 LIALPSFKL 89
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 103-224 9.81e-27

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: 99.23  E-value: 9.81e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552 103 AMTMKVVGLQWYWKYEYsdfmsdkgetmeyesyimpddmlEEGQLRLLDTDTSIVLPVDTHVRFIVTANDVIHSFAMPSL 182
Cdd:cd04213     1 ALTIEVTGHQWWWEFRY-----------------------PDEPGRGIVTANELHIPVGRPVRLRLTSADVIHSFWVPSL 57

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1904806552 183 GMKIDATPGRLNQVSALIQRTGVYYGQCSELCGINHSLMPMK 224
Cdd:cd04213    58 AGKMDMIPGRTNRLWLQADEPGVYRGQCAEFCGASHALMRFK 99
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 103-221 9.01e-26

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: 96.94  E-value: 9.01e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552 103 AMTMKVVGLQWYWKYEYSDfmsdkgetmeYESYIMPDDMLEEGQLrlldtdtsiVLPVDTHVRFIVTANDVIHSFAMPSL 182
Cdd:cd13919     1 ALVVEVTAQQWAWTFRYPG----------GDGKLGTDDDVTSPEL---------HLPVGRPVLFNLRSKDVIHSFWVPEF 61

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1904806552 183 GMKIDATPGRLNQVSALIQRTGVYYGQCSELCGINHSLM 221
Cdd:cd13919    62 RVKQDAVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 104-226 1.08e-25

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: 96.21  E-value: 1.08e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552 104 MTMKVVGLQWYWKYEYSDfmsdkgetmeyesyimpddmleegqlrlLDTDTSIVLPVDTHVRFIVTANDVIHSFAMPSLG 183
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPN----------------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLG 52

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1904806552 184 MKIDATPGRLNQVSALIQRTGVYYGQCSELCGINHSLMPMKME 226
Cdd:cd13842    53 VKVDAVPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 105-237 1.08e-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: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 89.00  E-value: 1.08e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552 105 TMKVVGLQWYWKYEYSdfmsdkgetmeyesyimpddmlEEGqlrlLDTDTSIVLPVDTHVRFIVTANDVIHSFAMPSLGM 184
Cdd:cd13914     2 EIEVEAYQWGWEFSYP----------------------EAN----VTTSEQLVIPADRPVYFRITSRDVIHAFHVPELGL 55

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1904806552 185 KIDATPGRLNQVSALIQRTGVYYGQCSELCGINHSLMPMKMECLSMTDFMEWL 237
Cdd:cd13914    56 KQDAFPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 103-221 2.49e-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: 82.29  E-value: 2.49e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552 103 AMTMKVVGLQWYWKYEYSDfmsDKGETMEyesyimpddmleegqlrlldtdtsIVLPVDTHVRFIVTANDVIHSFAMPSL 182
Cdd:cd13915     1 ALEIQVTGRQWMWEFTYPN---GKREINE------------------------LHVPVGKPVRLILTSKDVIHSFYVPAF 53

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1904806552 183 GMKIDATPGRLNQVSALIQRTGVYYGQCSELCGINHSLM 221
Cdd:cd13915    54 RIKQDVVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 103-237 8.60e-19

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


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 79.81  E-value: 8.60e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552 103 AMTMKVVGLQWYWKYEYsdfmSDKGETMEYesyimpddmleegqlrlldtdtsIVLPVDTHVRFIVTANDVIHSFAMPSL 182
Cdd:cd13918    32 ALEVEVEGFQFGWQFEY----PNGVTTGNT-----------------------LRVPADTPIALRVTSTDVFHTFGIPEL 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1904806552 183 GMKIDATPGRLNQVSALIQRTGVYYGQCSELCGINHSLMPMKMECLSMTDFMEWL 237
Cdd:cd13918    85 RVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAWY 139
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 152-226 1.80e-13

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: 64.13  E-value: 1.80e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1904806552 152 TDTSIVLPVDTHVRFIVTANDVIHSFAMPSLGMKIDATPGRLNQVSALIQRTGVYYGQCSELCGINHSLMPMKME 226
Cdd:cd13913    23 NPNEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNMYGKII 97
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 156-221 1.60e-06

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: 45.23  E-value: 1.60e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1904806552 156 IVLPVDTHVRFIVTANDVIHSFAMPSLGMKIDATPGRLNQVSALIQRTGVYYGQCSELCGINHSLM 221
Cdd:cd04212    27 LVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDM 92
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 150-221 4.35e-06

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


Pssm-ID: 259983 [Multi-domain]  Cd Length: 93  Bit Score: 43.91  E-value: 4.35e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1904806552 150 LDTDTsivLPVDTHVRFIVTANDVIHSFAMPSLGMKI----DATPGRLNQVSALIQRTGVYYGQCSELCGINHSLM 221
Cdd:cd13916    14 LSRTE---IPAGKPVEFRVTSADVNHGFGIYDPDMRLlaqtQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 156-221 3.39e-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: 38.51  E-value: 3.39e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1904806552 156 IVLPVDTHVRFIVTANDVIHSFAMPSLGMKIDATPGRLNQVSALIQRTGVYYGQCSELCGINHSLM 221
Cdd:cd13917    16 LVLKKGKTYRLHLSSLDVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIICNEYCGIGHHTM 81
PRK10525 PRK10525
cytochrome o ubiquinol oxidase subunit II; Provisional
 37-224 3.15e-03

cytochrome o ubiquinol oxidase subunit II; Provisional


Pssm-ID: 182518 [Multi-domain]  Cd Length: 315  Bit Score: 38.24  E-value: 3.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552  37 ALMLGLVSYMTYVVM-VDFKNNKFAYKY------------LKHGQTLE-MMWTMfPAVMLLLMAfpsfILTYLCDEVLTP 102
Cdd:PRK10525   42 SLILTAFGLMLIVVIpAILMAVGFAWKYrasnkdakyspnWSHSNKVEaVVWTV-PILIIIFLA----VLTWKTTHALEP 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806552 103 A---------MTMKVVGLQWYWKYEYSdfmsdkgetmeyesyimpddmlEEGqlrlLDTDTSIVLPVDTHVRFIVTANDV 173
Cdd:PRK10525  117 SkplahdekpITIEVVSMDWKWFFIYP----------------------EQG----IATVNEIAFPANVPVYFKVTSNSV 170

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1904806552 174 IHSFAMPSLGMKIDATPGRLNQVSALIQRTGVYYGQCSELCGINHSLMPMK 224
Cdd:PRK10525  171 MNSFFIPRLGSQIYAMAGMQTRLHLIANEPGTYDGISASYSGPGFSGMKFK 221
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH