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Conserved domains on  [gi|87083759|gb|ABD19440|]
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cytochrome oxidase subunit 3 (mitochondrion) [Daphnia pulex]

Protein Classification

cytochrome c oxidase subunit 3( domain architecture ID 10009592)

cytochrome c oxidase subunit 3 is one of main transmembrane subunits of cytochrome c oxidase, the last enzyme in the respiratory electron transport chain of mitochondria or bacteria located in the mitochondrial or bacterial membrane

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 4-258 1.16e-152

cytochrome c oxidase subunit III; Provisional


:

Pssm-ID: 214439  Cd Length: 255  Bit Score: 425.36  E-value: 1.16e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759    4 HMNHPFHLVDKSPWPILSAFSVMSLVSGLAKWFHTFNMDLAILGILSTTLVMIQWWRDVVREGTFQGLHTSKVGVGLRWG 83
Cdd:MTH00155   1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759   84 MILFIASEVLFFVSFFWAFFHSSLAPAIELGSAWPPLGIKPFNPFQIPLLNTAILLASGVTVTWAHHALMENNHTQAFQG 163
Cdd:MTH00155  81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759  164 LFLTVFLGFYFTSLQALEYFEAPFSIADAVYGTTFFVATGFHGLHVIIGTTFLLICLIRHTLHHFSFTHHFGFEAAAWYW 243
Cdd:MTH00155 161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240

                        250
                 ....*....|....*
gi 87083759  244 HFVDVVWLFLFISIY 258
Cdd:MTH00155 241 HFVDVVWLFLYISIY 255
 
Name Accession Description Interval E-value
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 4-258 1.16e-152

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 425.36  E-value: 1.16e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759    4 HMNHPFHLVDKSPWPILSAFSVMSLVSGLAKWFHTFNMDLAILGILSTTLVMIQWWRDVVREGTFQGLHTSKVGVGLRWG 83
Cdd:MTH00155   1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759   84 MILFIASEVLFFVSFFWAFFHSSLAPAIELGSAWPPLGIKPFNPFQIPLLNTAILLASGVTVTWAHHALMENNHTQAFQG 163
Cdd:MTH00155  81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759  164 LFLTVFLGFYFTSLQALEYFEAPFSIADAVYGTTFFVATGFHGLHVIIGTTFLLICLIRHTLHHFSFTHHFGFEAAAWYW 243
Cdd:MTH00155 161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240

                        250
                 ....*....|....*
gi 87083759  244 HFVDVVWLFLFISIY 258
Cdd:MTH00155 241 HFVDVVWLFLYISIY 255
COX3 pfam00510
Cytochrome c oxidase subunit III;
7-261 1.29e-117

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 337.08  E-value: 1.29e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759     7 HPFHLVDKSPWPILSAFSVMSLVSGLAKWFHTF--NMDLAILGILSTTLVMIQWWRDVVREGTFQGLHTSKVGVGLRWGM 84
Cdd:pfam00510   1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYsgNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759    85 ILFIASEVLFFVSFFWAFFHSSLAPAIELGSAWPPLGIKPFNPFQIPLLNTAILLASGVTVTWAHHALMENNHTQAFQGL 164
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759   165 FLTVFLGFYFTSLQALEYFEAPFSIADAVYGTTFFVATGFHGLHVIIGTTFLLICLIRHTLHHFSFTHHFGFEAAAWYWH 244
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240

                         250
                  ....*....|....*..
gi 87083759   245 FVDVVWLFLFISIYWWG 261
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWG 257
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 19-260 8.33e-117

Cytochrome c oxidase subunit III. 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. CcO 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, but subunit III, which is also conserved, is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. 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 III contains bound phospholipids in several crystal structures and is proposed to contain a "lipid pool." These phospholipids are believed to intrinsic constituents similar to cofactors of the enzyme.


Pssm-ID: 238834  Cd Length: 243  Bit Score: 334.48  E-value: 8.33e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759  19 ILSAFSVMSLVSGLAKWFHTF-NMDLAILGILSTTLVMIQWWRDVVREGTFQGLHTSKVGVGLRWGMILFIASEVLFFVS 97
Cdd:cd01665   1 ILGSFGLLLLALGLVLWMHGYgGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759  98 FFWAFFHSSLAPAIELGSAWPPLGIKPFNPFQIPLLNTAILLASGVTVTWAHHALMENNHTQAFQGLFLTVFLGFYFTSL 177
Cdd:cd01665  81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759 178 QALEYFEAPFSIADAVYGTTFFVATGFHGLHVIIGTTFLLICLIRHTLHHFSFTHHFGFEAAAWYWHFVDVVWLFLFISI 257
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240


                ...
gi 87083759 258 YWW 260
Cdd:cd01665 241 YWW 243
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
71-260 7.61e-46

Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];


Pssm-ID: 441450  Cd Length: 192  Bit Score: 151.93  E-value: 7.61e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759  71 LHTSKVGVGLRWGMILFIASEVLFFVSFFWAFFHSSLApaielgSAWPPLGIKPFNPFqIPLLNTAILLASGVTVTWAHH 150
Cdd:COG1845   7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS------APDWPAGAELLDLP-LPLINTLLLLLSSFTVALAVR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759 151 ALMENNHTQAFQGLFLTVFLGFYFTSLQALEY---FEAPFSIADAVYGTTFFVATGFHGLHVIIGTTFLLICLIRHTLHH 227
Cdd:COG1845  80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159

                       170       180       190
                ....*....|....*....|....*....|...
gi 87083759 228 FSFTHHFGFEAAAWYWHFVDVVWLFLFISIYWW 260
Cdd:COG1845 160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 121-261 1.28e-07

cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]


Pssm-ID: 131943  Cd Length: 190  Bit Score: 50.62  E-value: 1.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759   121 GIKPFNPFQIPLL--NTAILLASGVTVTWAHHALMENNHTQAFQGLFLTVFLGFYFTSLQALE---YFEAPFSIADAVYG 195
Cdd:TIGR02897  43 GKMPAELFELPLVliMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYW 122

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 87083759   196 TTFFVATGFHGLHV---IIGTTFLLICLIRHTLHHFSFTHHFgfeAAAWYWHFVDVVWLFLFISIYWWG 261
Cdd:TIGR02897 123 SSFFVLLGTHGCHVtlgIVWAICLLIQIQRRGLTPYTAPKVF---IVSLYWHFLDVVWVFIFTAVYLIG 188
 
Name Accession Description Interval E-value
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 4-258 1.16e-152

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 425.36  E-value: 1.16e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759    4 HMNHPFHLVDKSPWPILSAFSVMSLVSGLAKWFHTFNMDLAILGILSTTLVMIQWWRDVVREGTFQGLHTSKVGVGLRWG 83
Cdd:MTH00155   1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759   84 MILFIASEVLFFVSFFWAFFHSSLAPAIELGSAWPPLGIKPFNPFQIPLLNTAILLASGVTVTWAHHALMENNHTQAFQG 163
Cdd:MTH00155  81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759  164 LFLTVFLGFYFTSLQALEYFEAPFSIADAVYGTTFFVATGFHGLHVIIGTTFLLICLIRHTLHHFSFTHHFGFEAAAWYW 243
Cdd:MTH00155 161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240

                        250
                 ....*....|....*
gi 87083759  244 HFVDVVWLFLFISIY 258
Cdd:MTH00155 241 HFVDVVWLFLYISIY 255
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 3-261 7.71e-144

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 403.56  E-value: 7.71e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759    3 NHMNHPFHLVDKSPWPILSAFSVMSLVSGLAKWFHTFNMDLAILGILSTTLVMIQWWRDVVREGTFQGLHTSKVGVGLRW 82
Cdd:MTH00118   2 THQAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759   83 GMILFIASEVLFFVSFFWAFFHSSLAPAIELGSAWPPLGIKPFNPFQIPLLNTAILLASGVTVTWAHHALMENNHTQAFQ 162
Cdd:MTH00118  82 GMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQ 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759  163 GLFLTVFLGFYFTSLQALEYFEAPFSIADAVYGTTFFVATGFHGLHVIIGTTFLLICLIRHTLHHFSFTHHFGFEAAAWY 242
Cdd:MTH00118 162 ALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWY 241

                        250
                 ....*....|....*....
gi 87083759  243 WHFVDVVWLFLFISIYWWG 261
Cdd:MTH00118 242 WHFVDVVWLFLYISIYWWG 260
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 4-261 2.56e-134

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 379.32  E-value: 2.56e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759    4 HMNHPFHLVDKSPWPILSAFSVMSLVSGLAKWFHTFNMDLAILGILSTTLVMIQWWRDVVREGTFQGLHTSKVGVGLRWG 83
Cdd:MTH00189   2 HQAHPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRYG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759   84 MILFIASEVLFFVSFFWAFFHSSLAPAIELGSAWPPLGIKPFNPFQIPLLNTAILLASGVTVTWAHHALMENNHTQAFQG 163
Cdd:MTH00189  82 MILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759  164 LFLTVFLGFYFTSLQALEYFEAPFSIADAVYGTTFFVATGFHGLHVIIGTTFLLICLIRHTLHHFSFTHHFGFEAAAWYW 243
Cdd:MTH00189 162 LTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWYW 241

                        250
                 ....*....|....*...
gi 87083759  244 HFVDVVWLFLFISIYWWG 261
Cdd:MTH00189 242 HFVDVVWLFLYVSIYWWG 259
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 5-262 1.00e-131

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 372.69  E-value: 1.00e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759    5 MNHPFHLVDKSPWPILSAFSVMSLVSGLAKWFHTFNMDLAILGILSTTLVMIQWWRDVVREGTFQGLHTSKVGVGLRWGM 84
Cdd:MTH00141   2 TRNPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759   85 ILFIASEVLFFVSFFWAFFHSSLAPAIELGSAWPPLGIKPFNPFQIPLLNTAILLASGVTVTWAHHALMENNHTQAFQGL 164
Cdd:MTH00141  82 ILFIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759  165 FLTVFLGFYFTSLQALEYFEAPFSIADAVYGTTFFVATGFHGLHVIIGTTFLLICLIRHTLHHFSFTHHFGFEAAAWYWH 244
Cdd:MTH00141 162 GLTIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWH 241

                        250
                 ....*....|....*...
gi 87083759  245 FVDVVWLFLFISIYWWGN 262
Cdd:MTH00141 242 FVDVVWLFLYLSIYWWGS 259
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 7-261 6.25e-131

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 370.60  E-value: 6.25e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759    7 HPFHLVDKSPWPILSAFSVMSLVSGLAKWFHTFNMDLAILGILSTTLVMIQWWRDVVREGTFQGLHTSKVGVGLRWGMIL 86
Cdd:MTH00039   5 HPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRYGMIL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759   87 FIASEVLFFVSFFWAFFHSSLAPAIELGSAWPPLGIKPFNPFQIPLLNTAILLASGVTVTWAHHALMENNHTQAFQGLFL 166
Cdd:MTH00039  85 FITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQALFL 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759  167 TVFLGFYFTSLQALEYFEAPFSIADAVYGTTFFVATGFHGLHVIIGTTFLLICLIRHTLHHFSFTHHFGFEAAAWYWHFV 246
Cdd:MTH00039 165 TVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWYWHFV 244

                        250
                 ....*....|....*
gi 87083759  247 DVVWLFLFISIYWWG 261
Cdd:MTH00039 245 DVVWLFLYVCIYWWG 259
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 7-262 1.11e-126

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 360.26  E-value: 1.11e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759    7 HPFHLVDKSPWPILSAFSVMSLVSGLAKWFHTFNMDLAILGILSTTLVMIQWWRDVVREGTFQGLHTSKVGVGLRWGMIL 86
Cdd:MTH00219   7 NPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLRIGMIL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759   87 FIASEVLFFVSFFWAFFHSSLAPAIELGSAWPPLGIKPFNPFQIPLLNTAILLASGVTVTWAHHALMENNHTQAFQGLFL 166
Cdd:MTH00219  87 FIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQQGLLF 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759  167 TVFLGFYFTSLQALEYFEAPFSIADAVYGTTFFVATGFHGLHVIIGTTFLLICLIRHTLHHFSFTHHFGFEAAAWYWHFV 246
Cdd:MTH00219 167 TILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAAWYWHFV 246

                        250
                 ....*....|....*.
gi 87083759  247 DVVWLFLFISIYWWGN 262
Cdd:MTH00219 247 DVVWLFLYVSIYWWGS 262
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 4-262 1.72e-126

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 359.46  E-value: 1.72e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759    4 HMNHPFHLVDKSPWPILSAFSVMSLVSGLAKWFHTFNMDLAILGILSTTLVMIQWWRDVVREGTFQGLHTSKVGVGLRWG 83
Cdd:MTH00130   3 HQAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRYG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759   84 MILFIASEVLFFVSFFWAFFHSSLAPAIELGSAWPPLGIKPFNPFQIPLLNTAILLASGVTVTWAHHALMENNHTQAFQG 163
Cdd:MTH00130  83 MILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759  164 LFLTVFLGFYFTSLQALEYFEAPFSIADAVYGTTFFVATGFHGLHVIIGTTFLLICLIRHTLHHFSFTHHFGFEAAAWYW 243
Cdd:MTH00130 163 LTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWYW 242

                        250
                 ....*....|....*....
gi 87083759  244 HFVDVVWLFLFISIYWWGN 262
Cdd:MTH00130 243 HFVDVVWLFLYISIYWWGS 261
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 4-261 5.56e-125

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 355.57  E-value: 5.56e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759    4 HMNHPFHLVDKSPWPILSAFSVMSLVSGLAKWFHTFNMDLAILGILSTTLVMIQWWRDVVREGTFQGLHTSKVGVGLRWG 83
Cdd:MTH00099   3 HQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRYG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759   84 MILFIASEVLFFVSFFWAFFHSSLAPAIELGSAWPPLGIKPFNPFQIPLLNTAILLASGVTVTWAHHALMENNHTQAFQG 163
Cdd:MTH00099  83 MILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759  164 LFLTVFLGFYFTSLQALEYFEAPFSIADAVYGTTFFVATGFHGLHVIIGTTFLLICLIRHTLHHFSFTHHFGFEAAAWYW 243
Cdd:MTH00099 163 LFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWYW 242

                        250
                 ....*....|....*...
gi 87083759  244 HFVDVVWLFLFISIYWWG 261
Cdd:MTH00099 243 HFVDVVWLFLYVSIYWWG 260
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 4-261 7.27e-124

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 352.90  E-value: 7.27e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759    4 HMNHPFHLVDKSPWPILSAFSVMSLVSGLAKWFHTFNMDLAILGILSTTLVMIQWWRDVVREGTFQGLHTSKVGVGLRWG 83
Cdd:MTH00075   3 HQAHAFHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRYG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759   84 MILFIASEVLFFVSFFWAFFHSSLAPAIELGSAWPPLGIKPFNPFQIPLLNTAILLASGVTVTWAHHALMENNHTQAFQG 163
Cdd:MTH00075  83 MILFITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759  164 LFLTVFLGFYFTSLQALEYFEAPFSIADAVYGTTFFVATGFHGLHVIIGTTFLLICLIRHTLHHFSFTHHFGFEAAAWYW 243
Cdd:MTH00075 163 LALTIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWYW 242

                        250
                 ....*....|....*...
gi 87083759  244 HFVDVVWLFLFISIYWWG 261
Cdd:MTH00075 243 HFVDVVWLFLYVSIYWWG 260
COX3 pfam00510
Cytochrome c oxidase subunit III;
7-261 1.29e-117

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 337.08  E-value: 1.29e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759     7 HPFHLVDKSPWPILSAFSVMSLVSGLAKWFHTF--NMDLAILGILSTTLVMIQWWRDVVREGTFQGLHTSKVGVGLRWGM 84
Cdd:pfam00510   1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYsgNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759    85 ILFIASEVLFFVSFFWAFFHSSLAPAIELGSAWPPLGIKPFNPFQIPLLNTAILLASGVTVTWAHHALMENNHTQAFQGL 164
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759   165 FLTVFLGFYFTSLQALEYFEAPFSIADAVYGTTFFVATGFHGLHVIIGTTFLLICLIRHTLHHFSFTHHFGFEAAAWYWH 244
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240

                         250
                  ....*....|....*..
gi 87083759   245 FVDVVWLFLFISIYWWG 261
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWG 257
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 19-260 8.33e-117

Cytochrome c oxidase subunit III. 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. CcO 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, but subunit III, which is also conserved, is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. 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 III contains bound phospholipids in several crystal structures and is proposed to contain a "lipid pool." These phospholipids are believed to intrinsic constituents similar to cofactors of the enzyme.


Pssm-ID: 238834  Cd Length: 243  Bit Score: 334.48  E-value: 8.33e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759  19 ILSAFSVMSLVSGLAKWFHTF-NMDLAILGILSTTLVMIQWWRDVVREGTFQGLHTSKVGVGLRWGMILFIASEVLFFVS 97
Cdd:cd01665   1 ILGSFGLLLLALGLVLWMHGYgGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759  98 FFWAFFHSSLAPAIELGSAWPPLGIKPFNPFQIPLLNTAILLASGVTVTWAHHALMENNHTQAFQGLFLTVFLGFYFTSL 177
Cdd:cd01665  81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759 178 QALEYFEAPFSIADAVYGTTFFVATGFHGLHVIIGTTFLLICLIRHTLHHFSFTHHFGFEAAAWYWHFVDVVWLFLFISI 257
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240


                ...
gi 87083759 258 YWW 260
Cdd:cd01665 241 YWW 243
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 7-261 3.05e-116

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 333.73  E-value: 3.05e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759    7 HPFHLVDKSPWPILSAFSVMSLVSGLAKWFHTFNMDLAILGILSTTLVMIQWWRDVVREGTFQGLHTSKVGVGLRWGMIL 86
Cdd:MTH00009   4 QPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMIL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759   87 FIASEVLFFVSFFWAFFHSSLAPAIELGSAWPPLGIKPFNPFQIPLLNTAILLASGVTVTWAHHALMENNHTQAFQGLFL 166
Cdd:MTH00009  84 FIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALIL 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759  167 TVFLGFYFTSLQALEYFEAPFSIADAVYGTTFFVATGFHGLHVIIGTTFLLICLIRHTLHHFSFTHHFGFEAAAWYWHFV 246
Cdd:MTH00009 164 TVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFV 243

                        250
                 ....*....|....*
gi 87083759  247 DVVWLFLFISIYWWG 261
Cdd:MTH00009 244 DVVWIFLYLCIYWWG 258
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 7-261 3.26e-111

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 320.93  E-value: 3.26e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759    7 HPFHLVDKSPWPILSAFSVMSLVSGLAKWFHTFNMDLAILGILSTTLVMIQWWRDVVREGTFQGLHTSKVGVGLRWGMIL 86
Cdd:MTH00024   6 HPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGMLL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759   87 FIASEVLFFVSFFWAFFHSSLAPAIELGSAWPPLGIKPFNPFQIPLLNTAILLASGVTVTWAHHALMENNHTQAFQGLFL 166
Cdd:MTH00024  86 FILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFL 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759  167 TVFLGFYFTSLQALEYFEAPFSIADAVYGTTFFVATGFHGLHVIIGTTFLLICLIRHTLHHFSFTHHFGFEAAAWYWHFV 246
Cdd:MTH00024 166 TVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASWYWHFV 245

                        250
                 ....*....|....*
gi 87083759  247 DVVWLFLFISIYWWG 261
Cdd:MTH00024 246 DVVWLFLYLCIYWWG 260
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 1-262 8.05e-108

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 312.50  E-value: 8.05e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759    1 MSNHMNHPFHLVDKSPWPILSAFSVMSLVSGLAKWFHTFNMDLAILGILSTTLVMIQWWRDVVREGTFQGLHTSKVGVGL 80
Cdd:MTH00052   1 MMQQYYHPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759   81 RWGMILFIASEVLFFVSFFWAFFHSSLAPAIELGSAWPPLGIKPFNPFQIPLLNTAILLASGVTVTWAHHALMENNHTQA 160
Cdd:MTH00052  81 KYGMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759  161 FQGLFLTVFLGFYFTSLQALEYFEAPFSIADAVYGTTFFVATGFHGLHVIIGTTFLLICLIRHTLHHFSFTHHFGFEAAA 240
Cdd:MTH00052 161 IIGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAA 240

                        250       260
                 ....*....|....*....|..
gi 87083759  241 WYWHFVDVVWLFLFISIYWWGN 262
Cdd:MTH00052 241 WYWHFVDVVWLFLFIFMYWWGS 262
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 7-262 1.29e-89

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 267.32  E-value: 1.29e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759    7 HPFHLVDKSPWPILSAFSVMSLVSGLAKWFHTFNMDLAILGILSTTLVMIQWWRDVVREGTFQGLHTSKVGVGLRWGMIL 86
Cdd:MTH00028   6 HPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759   87 FIASEVLFFVSFFWAFFHSSLAPAIELGSAWPPLGIKPFNPFQIPLLNTAILLASGVTVTWAHHALM------------- 153
Cdd:MTH00028  86 FILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIgtgnpaslekgtq 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759  154 -----------------------ENNHTQAFQGLFLTVFLGFYFTSLQALEYFEAPFSIADAVYGTTFFVATGFHGLHVI 210
Cdd:MTH00028 166 giegpnpsngappdpqkgptfllSDFRTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVL 245

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 87083759  211 IGTTFLLICLIRHTLHHFSFTHHFGFEAAAWYWHFVDVVWLFLFISIYWWGN 262
Cdd:MTH00028 246 VGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWGS 297
PLN02194 PLN02194
cytochrome-c oxidase
 1-261 3.93e-82

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 247.27  E-value: 3.93e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759    1 MSNHMNHPFHLVDKSPWPILSAFSVMSLVSGLAKWFHTFN--MDLAILGILSTTLVMIQWWRDVVREGTFQGLHTSKVGV 78
Cdd:PLN02194   1 MIESQRHSYHLVDPSPWPISGSLGALATTVGGVMYMHPFQggARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759   79 GLRWGMILFIASEVLFFVSFFWAFFHSSLAPAIELGSAWPPLGIKPFNPFQIPLLNTAILLASGVTVTWAHHALMENNHT 158
Cdd:PLN02194  81 GPRYGSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759  159 QAFQGLFLTVFLGFYFTSLQALEYFEAPFSIADAVYGTTFFVATGFHGLHVIIGTTFLLICLIRHTLHHFSFTHHFGFEA 238
Cdd:PLN02194 161 RAVYALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEA 240

                        250       260
                 ....*....|....*....|...
gi 87083759  239 AAWYWHFVDVVWLFLFISIYWWG 261
Cdd:PLN02194 241 AAWYWHFVDVVWLFLFVSIYWWG 263
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
 5-261 3.86e-66

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 205.96  E-value: 3.86e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759    5 MNHPFHLVDKSPWPILSAFSVMSLVSGLAKWFHTFNMDLAILGILSTTLVMIQWWRDVVREGtFQGLHTSKVGVGLRWGM 84
Cdd:MTH00083   1 MFHNFHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGM 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759   85 ILFIASEVLFFVSFFWAFFHSSLAPAIELGSAWPPLGIKPFNPFQIPLLNTAILLASGVTVTWAHHALMENNhTQAFQGL 164
Cdd:MTH00083  80 ILFIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSN-KSCTNSL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759  165 FLTVFLGFYFTSLQALEYFEAPFSIADAVYGTTFFVATGFHGLHVIIGTTFLLICLIRHTLHHFSFTHHFGFEAAAWYWH 244
Cdd:MTH00083 159 LLTCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWH 238

                        250
                 ....*....|....*..
gi 87083759  245 FVDVVWLFLFISIYWWG 261
Cdd:MTH00083 239 FVDVVWLFLFVFVYWWS 255
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 72-260 5.05e-60

Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). 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. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. This group additionally contains proteins which are fusions between subunits I and III, such as Sulfolobus acidocaldarius SoxM, a subunit of the SoxM terminal oxidase complex. It also includes NorE which has been speculated to be a subunit of nitric oxide reductase. Some archaebacterial cytochrome oxidases lack subunit III. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria.


Pssm-ID: 238227  Cd Length: 183  Bit Score: 187.80  E-value: 5.05e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759  72 HTSKVGVGLRWGMILFIASEVLFFVSFFWAFFHSSLAPAIELGsawpplgiKPFNPFQIPLLNTAILLASGVTVTWAHHA 151
Cdd:cd00386   1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFG--------AGLDPLDLPLLNTNTLLLSGSSVTWAHAS 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759 152 LM--ENNHTQAFQGLFLTVFLGFYFTSLQALEYFEAPFSIADAVYGTTFFVATGFHGLHVIIGTTFLLICLIRHTLHHFS 229
Cdd:cd00386  73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152

                       170       180       190
                ....*....|....*....|....*....|.
gi 87083759 230 FTHHFGFEAAAWYWHFVDVVWLFLFISIYWW 260
Cdd:cd00386 153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
71-260 7.61e-46

Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];


Pssm-ID: 441450  Cd Length: 192  Bit Score: 151.93  E-value: 7.61e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759  71 LHTSKVGVGLRWGMILFIASEVLFFVSFFWAFFHSSLApaielgSAWPPLGIKPFNPFqIPLLNTAILLASGVTVTWAHH 150
Cdd:COG1845   7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS------APDWPAGAELLDLP-LPLINTLLLLLSSFTVALAVR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759 151 ALMENNHTQAFQGLFLTVFLGFYFTSLQALEY---FEAPFSIADAVYGTTFFVATGFHGLHVIIGTTFLLICLIRHTLHH 227
Cdd:COG1845  80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159

                       170       180       190
                ....*....|....*....|....*....|...
gi 87083759 228 FSFTHHFGFEAAAWYWHFVDVVWLFLFISIYWW 260
Cdd:COG1845 160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
NorE_like cd02862
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ...
 132-258 3.86e-21

NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include cytochrome c and ubiquinol oxidases. Alcaligenes faecalis norE is found in a gene cluster containing norCB. norCB encodes the cytochrome c and cytochrome b subunits of nitric oxide reductase (NOR). Based on this and on its similarity to subunit III of cytochrome c oxidase (CcO) and ubiquinol oxidase, NorE has been speculated to be a subunit of NOR.


Pssm-ID: 239213  Cd Length: 186  Bit Score: 87.68  E-value: 3.86e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759 132 LLNTAILLASGVTVTWAHHALMENNHTQAFQGLFLTVFLGFYFTSLQALEY---FEAPFSIADAVYGTTFFVATGFHGLH 208
Cdd:cd02862  55 ALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYahkIAAGIDPDAGLFFTLYFLLTGFHLLH 134

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 87083759 209 VIIGTTFLLICLIRHTLHHFSFTHHFGFEAAAWYWHFVDVVWLFLFISIY 258
Cdd:cd02862 135 VLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVLFPLLY 184
Heme_Cu_Oxidase_III_2 cd02865
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 131-260 5.89e-16

Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). 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. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria.


Pssm-ID: 239216  Cd Length: 184  Bit Score: 73.56  E-value: 5.89e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759 131 PLLNTAILLASGVTVTWAHHALMENNHTQAFQGLFLTVFLGFYFTSLQALEYFEAPFSI---ADAVYGTTFFVATGFHGL 207
Cdd:cd02865  52 LSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWHALNDAGygpTSNPAGSFFYLLTGLHGL 131

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 87083759 208 HVIIGTTFLLICLIRHTLHHFSFTHHFGFEAAAWYWHFVDVVWLFLFISIYWW 260
Cdd:cd02865 132 HVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVLLALLYGT 184
Ubiquinol_oxidase_III cd02863
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ...
 121-258 6.17e-15

Ubiquinol oxidase subunit III subfamily. 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. Ubiquinol oxidases feature four subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of bovine CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in bovine CcO. Although not required for catalytic activity, subunit III appears to be involved in assembly of the multimer complex.


Pssm-ID: 239214  Cd Length: 186  Bit Score: 70.73  E-value: 6.17e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759 121 GIKPFNPFQIPL--LNTAILLASGVTVTWAHHALMENNHTQAFQGLFLTVFLGFYFTSLQALEYFE---APFSIADAVYG 195
Cdd:cd02863  41 GPPGHELFELPLvfIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEFHHliaEGAGPDRSAFL 120

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 87083759 196 TTFFVATGFHGLHVIIGTTFLLICLIRHTLHHFSFTHHFGFEAAAWYWHFVDVVWLFLFISIY 258
Cdd:cd02863 121 SAFFTLVGTHGLHVTFGLIWILVMIIQLKKRGLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
Heme_Cu_Oxidase_III_1 cd02864
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 124-260 2.95e-14

Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). 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. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria.


Pssm-ID: 239215  Cd Length: 202  Bit Score: 69.45  E-value: 2.95e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759 124 PFNPFQIPL----LNTAILLASGVTVTWAHHALMENNHTQAFQGLFLTVFLGFYFTSLQALEYFE---------APFSIA 190
Cdd:cd02864  52 RIGHFNIPLvliaIMTFILITSSGTMAMAVNFGYRGNRKAAARLMLATALLGATFVGMQAFEWTKliveegvrpWGNPWG 131

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 87083759 191 DAVYGTTFFVATGFHGLHVIIGTTFLLIclIRHTLHHFSFTHHFGF---EAAAWYWHFVDVVWLFLFISIYWW 260
Cdd:cd02864 132 AAQFGASFFMITGFHGTHVTIGVIYLII--IARKVWRGKYQRIGRYeivEIAGLYWHFVDLVWVFIFAFFYLW 202
COX3 MTH00049
cytochrome c oxidase subunit III; Validated
 127-258 7.33e-14

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177124  Cd Length: 215  Bit Score: 68.40  E-value: 7.33e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759  127 PFQIPLLNTAILLASGVTVTWAHHaLMENNHTQAFqgLFLTVFLGFYFTSLQALEYFEAPFSIADAVYGTTFFVATGFHG 206
Cdd:MTH00049  89 SLEIPFVGCFLLLGSSITVTAYHH-LLGWKYCDLF--LYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHF 165

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 87083759  207 LHVIIGTtFLLICLIRHTLHHFSFTHHfgfEAAAWYWHFVDVVWLFLFISIY 258
Cdd:MTH00049 166 SHVVLGV-VGLSTLLLVGSSSFGVYRS---TVLTWYWHFVDYIWLLVYLIVY 213
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 121-261 1.28e-07

cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]


Pssm-ID: 131943  Cd Length: 190  Bit Score: 50.62  E-value: 1.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759   121 GIKPFNPFQIPLL--NTAILLASGVTVTWAHHALMENNHTQAFQGLFLTVFLGFYFTSLQALE---YFEAPFSIADAVYG 195
Cdd:TIGR02897  43 GKMPAELFELPLVliMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYW 122

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 87083759   196 TTFFVATGFHGLHV---IIGTTFLLICLIRHTLHHFSFTHHFgfeAAAWYWHFVDVVWLFLFISIYWWG 261
Cdd:TIGR02897 123 SSFFVLLGTHGCHVtlgIVWAICLLIQIQRRGLTPYTAPKVF---IVSLYWHFLDVVWVFIFTAVYLIG 188
PRK10663 PRK10663
cytochrome o ubiquinol oxidase subunit III; Provisional
 128-261 1.92e-07

cytochrome o ubiquinol oxidase subunit III; Provisional


Pssm-ID: 182628  Cd Length: 204  Bit Score: 50.16  E-value: 1.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87083759  128 FQIP--LLNTAILLASGVTVTWAHHALMENNHTQAFQGLFLTVFLGFYFTSLQALEY---FEAPFSIADAVYGTTFFVAT 202
Cdd:PRK10663  64 FELPfvLVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFhhlIVEGMGPDRSGFLSAFFALV 143

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 87083759  203 GFHGLHVIIGTTFLLICLIRHTLHHFSFTHHFGFEAAAWYWHFVDVVWLFLFISIYWWG 261
Cdd:PRK10663 144 GTHGLHVTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMG 202
 
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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