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Conserved domains on  [gi|2296408317|gb|UWM12978|]
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cytochrome c oxidase subunit III (mitochondrion) [Paralepas cf. quadrata]

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-144

cytochrome c oxidase subunit III; Provisional


:

Pssm-ID: 214439  Cd Length: 255  Bit Score: 405.33  E-value: 1.16e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317   4 HWHHPFHMVDMSPWPLTASIGALTLTVGLSYWFHFNSMLILLLGLAIIIISSYQWWRDISREGTLQGLHSNMVMVNLRWG 83
Cdd:MTH00155    1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317  84 MILFIVSEVFFFLSFFWAFFHASLAPSVEIGTQWPPVGIIPFNPFQIPLLNTAILLASGVTVTWSHHSLMGGNHTQAMQS 163
Cdd:MTH00155   81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 164 LFVTILLGMYFTALQAYEYMEAPFSISEAVYGSTFFVATGFHGLHVIIGTTFLLICFYRLSKFHFSPAHHFGFEAAAWYW 243
Cdd:MTH00155  161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240

                         250
                  ....*....|....*
gi 2296408317 244 HFVDVVWLFLYVSIY 258
Cdd:MTH00155  241 HFVDVVWLFLYISIY 255
 
Name Accession Description Interval E-value
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 4-258 1.16e-144

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 405.33  E-value: 1.16e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317   4 HWHHPFHMVDMSPWPLTASIGALTLTVGLSYWFHFNSMLILLLGLAIIIISSYQWWRDISREGTLQGLHSNMVMVNLRWG 83
Cdd:MTH00155    1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317  84 MILFIVSEVFFFLSFFWAFFHASLAPSVEIGTQWPPVGIIPFNPFQIPLLNTAILLASGVTVTWSHHSLMGGNHTQAMQS 163
Cdd:MTH00155   81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 164 LFVTILLGMYFTALQAYEYMEAPFSISEAVYGSTFFVATGFHGLHVIIGTTFLLICFYRLSKFHFSPAHHFGFEAAAWYW 243
Cdd:MTH00155  161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240

                         250
                  ....*....|....*
gi 2296408317 244 HFVDVVWLFLYVSIY 258
Cdd:MTH00155  241 HFVDVVWLFLYISIY 255
COX3 pfam00510
Cytochrome c oxidase subunit III;
7-261 9.68e-119

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 339.77  E-value: 9.68e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317   7 HPFHMVDMSPWPLTASIGALTLTVGLSYWFHF--NSMLILLLGLAIIIISSYQWWRDISREGTLQGLHSNMVMVNLRWGM 84
Cdd:pfam00510   1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGysGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317  85 ILFIVSEVFFFLSFFWAFFHASLAPSVEIGTQWPPVGIIPFNPFQIPLLNTAILLASGVTVTWSHHSLMGGNHTQAMQSL 164
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 165 FVTILLGMYFTALQAYEYMEAPFSISEAVYGSTFFVATGFHGLHVIIGTTFLLICFYRLSKFHFSPAHHFGFEAAAWYWH 244
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240

                         250
                  ....*....|....*..
gi 2296408317 245 FVDVVWLFLYVSIYWWG 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 9.37e-114

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: 326.39  E-value: 9.37e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317  19 LTASIGALTLTVGLSYWFH-FNSMLILLLGLAIIIISSYQWWRDISREGTLQGLHSNMVMVNLRWGMILFIVSEVFFFLS 97
Cdd:cd01665     1 ILGSFGLLLLALGLVLWMHgYGGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317  98 FFWAFFHASLAPSVEIGTQWPPVGIIPFNPFQIPLLNTAILLASGVTVTWSHHSLMGGNHTQAMQSLFVTILLGMYFTAL 177
Cdd:cd01665    81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 178 QAYEYMEAPFSISEAVYGSTFFVATGFHGLHVIIGTTFLLICFYRLSKFHFSPAHHFGFEAAAWYWHFVDVVWLFLYVSI 257
Cdd:cd01665   161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240


                  ...
gi 2296408317 258 YWW 260
Cdd:cd01665   241 YWW 243
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
71-260 2.85e-47

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 155.78  E-value: 2.85e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317  71 LHSNMVMVNLRWGMILFIVSEVFFFLSFFWAFFHASLApsveigTQWPPVGIIPFNPFqIPLLNTAILLASGVTVTWSHH 150
Cdd:COG1845     7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS------APDWPAGAELLDLP-LPLINTLLLLLSSFTVALAVR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 151 SLMGGNHTQAMQSLFVTILLGMYFTALQAYEYME---APFSISEAVYGSTFFVATGFHGLHVIIGTTFLLICFYRLSKFH 227
Cdd:COG1845    80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHliaEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2296408317 228 FSPAHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 260
Cdd:COG1845   160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 121-261 1.91e-10

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: 58.71  E-value: 1.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 121 GIIPFNPFQIPLL--NTAILLASGVTVTWSHHSLMGGNHTQAMQSLFVTILLGMYFTALQAYE---YMEAPFSISEAVYG 195
Cdd:TIGR02897  43 GKMPAELFELPLVliMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYW 122

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2296408317 196 STFFVATGFHGLHVIIGTTFLLICFYRLSKFHFSPAHHFGFEAAAWYWHFVDVVWLFLYVSIYWWG 261
Cdd:TIGR02897 123 SSFFVLLGTHGCHVTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
 
Name Accession Description Interval E-value
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 4-258 1.16e-144

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 405.33  E-value: 1.16e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317   4 HWHHPFHMVDMSPWPLTASIGALTLTVGLSYWFHFNSMLILLLGLAIIIISSYQWWRDISREGTLQGLHSNMVMVNLRWG 83
Cdd:MTH00155    1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317  84 MILFIVSEVFFFLSFFWAFFHASLAPSVEIGTQWPPVGIIPFNPFQIPLLNTAILLASGVTVTWSHHSLMGGNHTQAMQS 163
Cdd:MTH00155   81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 164 LFVTILLGMYFTALQAYEYMEAPFSISEAVYGSTFFVATGFHGLHVIIGTTFLLICFYRLSKFHFSPAHHFGFEAAAWYW 243
Cdd:MTH00155  161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240

                         250
                  ....*....|....*
gi 2296408317 244 HFVDVVWLFLYVSIY 258
Cdd:MTH00155  241 HFVDVVWLFLYISIY 255
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 3-261 2.16e-138

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 389.70  E-value: 2.16e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317   3 NHWHHPFHMVDMSPWPLTASIGALTLTVGLSYWFHFNSMLILLLGLAIIIISSYQWWRDISREGTLQGLHSNMVMVNLRW 82
Cdd:MTH00118    2 THQAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317  83 GMILFIVSEVFFFLSFFWAFFHASLAPSVEIGTQWPPVGIIPFNPFQIPLLNTAILLASGVTVTWSHHSLMGGNHTQAMQ 162
Cdd:MTH00118   82 GMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 163 SLFVTILLGMYFTALQAYEYMEAPFSISEAVYGSTFFVATGFHGLHVIIGTTFLLICFYRLSKFHFSPAHHFGFEAAAWY 242
Cdd:MTH00118  162 ALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWY 241

                         250
                  ....*....|....*....
gi 2296408317 243 WHFVDVVWLFLYVSIYWWG 261
Cdd:MTH00118  242 WHFVDVVWLFLYISIYWWG 260
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 7-261 1.95e-130

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 369.69  E-value: 1.95e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317   7 HPFHMVDMSPWPLTASIGALTLTVGLSYWFHFNSMLILLLGLAIIIISSYQWWRDISREGTLQGLHSNMVMVNLRWGMIL 86
Cdd:MTH00189    5 HPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRYGMIL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317  87 FIVSEVFFFLSFFWAFFHASLAPSVEIGTQWPPVGIIPFNPFQIPLLNTAILLASGVTVTWSHHSLMGGNHTQAMQSLFV 166
Cdd:MTH00189   85 FITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQALTL 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 167 TILLGMYFTALQAYEYMEAPFSISEAVYGSTFFVATGFHGLHVIIGTTFLLICFYRLSKFHFSPAHHFGFEAAAWYWHFV 246
Cdd:MTH00189  165 TVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWYWHFV 244

                         250
                  ....*....|....*
gi 2296408317 247 DVVWLFLYVSIYWWG 261
Cdd:MTH00189  245 DVVWLFLYVSIYWWG 259
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 7-262 4.58e-127

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 360.75  E-value: 4.58e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317   7 HPFHMVDMSPWPLTASIGALTLTVGLSYWFHFNSMLILLLGLAIIIISSYQWWRDISREGTLQGLHSNMVMVNLRWGMIL 86
Cdd:MTH00141    4 NPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFIL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317  87 FIVSEVFFFLSFFWAFFHASLAPSVEIGTQWPPVGIIPFNPFQIPLLNTAILLASGVTVTWSHHSLMGGNHTQAMQSLFV 166
Cdd:MTH00141   84 FIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 167 TILLGMYFTALQAYEYMEAPFSISEAVYGSTFFVATGFHGLHVIIGTTFLLICFYRLSKFHFSPAHHFGFEAAAWYWHFV 246
Cdd:MTH00141  164 TIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFV 243

                         250
                  ....*....|....*.
gi 2296408317 247 DVVWLFLYVSIYWWGG 262
Cdd:MTH00141  244 DVVWLFLYLSIYWWGS 259
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 7-262 9.55e-124

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 352.49  E-value: 9.55e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317   7 HPFHMVDMSPWPLTASIGALTLTVGLSYWFHFNSMLILLLGLAIIIISSYQWWRDISREGTLQGLHSNMVMVNLRWGMIL 86
Cdd:MTH00039    5 HPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRYGMIL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317  87 FIVSEVFFFLSFFWAFFHASLAPSVEIGTQWPPVGIIPFNPFQIPLLNTAILLASGVTVTWSHHSLMGGNHTQAMQSLFV 166
Cdd:MTH00039   85 FITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQALFL 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 167 TILLGMYFTALQAYEYMEAPFSISEAVYGSTFFVATGFHGLHVIIGTTFLLICFYRLSKFHFSPAHHFGFEAAAWYWHFV 246
Cdd:MTH00039  165 TVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWYWHFV 244

                         250
                  ....*....|....*.
gi 2296408317 247 DVVWLFLYVSIYWWGG 262
Cdd:MTH00039  245 DVVWLFLYVCIYWWGS 260
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 4-261 4.87e-123

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 350.99  E-value: 4.87e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317   4 HWHHPFHMVDMSPWPLTASIGALTLTVGLSYWFHFNSMLILLLGLAIIIISSYQWWRDISREGTLQGLHSNMVMVNLRWG 83
Cdd:MTH00130    3 HQAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRYG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317  84 MILFIVSEVFFFLSFFWAFFHASLAPSVEIGTQWPPVGIIPFNPFQIPLLNTAILLASGVTVTWSHHSLMGGNHTQAMQS 163
Cdd:MTH00130   83 MILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQS 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 164 LFVTILLGMYFTALQAYEYMEAPFSISEAVYGSTFFVATGFHGLHVIIGTTFLLICFYRLSKFHFSPAHHFGFEAAAWYW 243
Cdd:MTH00130  163 LTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWYW 242

                         250
                  ....*....|....*...
gi 2296408317 244 HFVDVVWLFLYVSIYWWG 261
Cdd:MTH00130  243 HFVDVVWLFLYISIYWWG 260
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 4-261 2.70e-122

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 349.02  E-value: 2.70e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317   4 HWHHPFHMVDMSPWPLTASIGALTLTVGLSYWFHFNSMLILLLGLAIIIISSYQWWRDISREGTLQGLHSNMVMVNLRWG 83
Cdd:MTH00099    3 HQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRYG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317  84 MILFIVSEVFFFLSFFWAFFHASLAPSVEIGTQWPPVGIIPFNPFQIPLLNTAILLASGVTVTWSHHSLMGGNHTQAMQS 163
Cdd:MTH00099   83 MILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 164 LFVTILLGMYFTALQAYEYMEAPFSISEAVYGSTFFVATGFHGLHVIIGTTFLLICFYRLSKFHFSPAHHFGFEAAAWYW 243
Cdd:MTH00099  163 LFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWYW 242

                         250
                  ....*....|....*...
gi 2296408317 244 HFVDVVWLFLYVSIYWWG 261
Cdd:MTH00099  243 HFVDVVWLFLYVSIYWWG 260
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 4-261 9.58e-122

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 347.50  E-value: 9.58e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317   4 HWHHPFHMVDMSPWPLTASIGALTLTVGLSYWFHFNSMLILLLGLAIIIISSYQWWRDISREGTLQGLHSNMVMVNLRWG 83
Cdd:MTH00075    3 HQAHAFHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRYG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317  84 MILFIVSEVFFFLSFFWAFFHASLAPSVEIGTQWPPVGIIPFNPFQIPLLNTAILLASGVTVTWSHHSLMGGNHTQAMQS 163
Cdd:MTH00075   83 MILFITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQS 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 164 LFVTILLGMYFTALQAYEYMEAPFSISEAVYGSTFFVATGFHGLHVIIGTTFLLICFYRLSKFHFSPAHHFGFEAAAWYW 243
Cdd:MTH00075  163 LALTIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWYW 242

                         250
                  ....*....|....*...
gi 2296408317 244 HFVDVVWLFLYVSIYWWG 261
Cdd:MTH00075  243 HFVDVVWLFLYVSIYWWG 260
COX3 pfam00510
Cytochrome c oxidase subunit III;
7-261 9.68e-119

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 339.77  E-value: 9.68e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317   7 HPFHMVDMSPWPLTASIGALTLTVGLSYWFHF--NSMLILLLGLAIIIISSYQWWRDISREGTLQGLHSNMVMVNLRWGM 84
Cdd:pfam00510   1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGysGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317  85 ILFIVSEVFFFLSFFWAFFHASLAPSVEIGTQWPPVGIIPFNPFQIPLLNTAILLASGVTVTWSHHSLMGGNHTQAMQSL 164
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 165 FVTILLGMYFTALQAYEYMEAPFSISEAVYGSTFFVATGFHGLHVIIGTTFLLICFYRLSKFHFSPAHHFGFEAAAWYWH 244
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240

                         250
                  ....*....|....*..
gi 2296408317 245 FVDVVWLFLYVSIYWWG 261
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWG 257
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 7-261 1.52e-118

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 339.46  E-value: 1.52e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317   7 HPFHMVDMSPWPLTASIGALTLTVGLSYWFHFNSMLILLLGLAIIIISSYQWWRDISREGTLQGLHSNMVMVNLRWGMIL 86
Cdd:MTH00219    7 NPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLRIGMIL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317  87 FIVSEVFFFLSFFWAFFHASLAPSVEIGTQWPPVGIIPFNPFQIPLLNTAILLASGVTVTWSHHSLMGGNHTQAMQSLFV 166
Cdd:MTH00219   87 FIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQQGLLF 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 167 TILLGMYFTALQAYEYMEAPFSISEAVYGSTFFVATGFHGLHVIIGTTFLLICFYRLSKFHFSPAHHFGFEAAAWYWHFV 246
Cdd:MTH00219  167 TILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAAWYWHFV 246

                         250
                  ....*....|....*
gi 2296408317 247 DVVWLFLYVSIYWWG 261
Cdd:MTH00219  247 DVVWLFLYVSIYWWG 261
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 19-260 9.37e-114

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: 326.39  E-value: 9.37e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317  19 LTASIGALTLTVGLSYWFH-FNSMLILLLGLAIIIISSYQWWRDISREGTLQGLHSNMVMVNLRWGMILFIVSEVFFFLS 97
Cdd:cd01665     1 ILGSFGLLLLALGLVLWMHgYGGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317  98 FFWAFFHASLAPSVEIGTQWPPVGIIPFNPFQIPLLNTAILLASGVTVTWSHHSLMGGNHTQAMQSLFVTILLGMYFTAL 177
Cdd:cd01665    81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 178 QAYEYMEAPFSISEAVYGSTFFVATGFHGLHVIIGTTFLLICFYRLSKFHFSPAHHFGFEAAAWYWHFVDVVWLFLYVSI 257
Cdd:cd01665   161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240


                  ...
gi 2296408317 258 YWW 260
Cdd:cd01665   241 YWW 243
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 7-261 5.13e-108

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 312.54  E-value: 5.13e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317   7 HPFHMVDMSPWPLTASIGALTLTVGLSYWFHFNSMLILLLGLAIIIISSYQWWRDISREGTLQGLHSNMVMVNLRWGMIL 86
Cdd:MTH00009    4 QPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMIL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317  87 FIVSEVFFFLSFFWAFFHASLAPSVEIGTQWPPVGIIPFNPFQIPLLNTAILLASGVTVTWSHHSLMGGNHTQAMQSLFV 166
Cdd:MTH00009   84 FIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALIL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 167 TILLGMYFTALQAYEYMEAPFSISEAVYGSTFFVATGFHGLHVIIGTTFLLICFYRLSKFHFSPAHHFGFEAAAWYWHFV 246
Cdd:MTH00009  164 TVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFV 243

                         250
                  ....*....|....*
gi 2296408317 247 DVVWLFLYVSIYWWG 261
Cdd:MTH00009  244 DVVWIFLYLCIYWWG 258
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 6-261 8.39e-107

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 309.76  E-value: 8.39e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317   6 HHPFHMVDMSPWPLTASIGALTLTVGLSYWFHFNSMLILLLGLAIIIISSYQWWRDISREGTLQGLHSNMVMVNLRWGMI 85
Cdd:MTH00024    5 YHPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGML 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317  86 LFIVSEVFFFLSFFWAFFHASLAPSVEIGTQWPPVGIIPFNPFQIPLLNTAILLASGVTVTWSHHSLMGGNHTQAMQSLF 165
Cdd:MTH00024   85 LFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLF 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 166 VTILLGMYFTALQAYEYMEAPFSISEAVYGSTFFVATGFHGLHVIIGTTFLLICFYRLSKFHFSPAHHFGFEAAAWYWHF 245
Cdd:MTH00024  165 LTVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASWYWHF 244

                         250
                  ....*....|....*.
gi 2296408317 246 VDVVWLFLYVSIYWWG 261
Cdd:MTH00024  245 VDVVWLFLYLCIYWWG 260
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 1-261 1.32e-100

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 294.01  E-value: 1.32e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317   1 MKNHWHHPFHMVDMSPWPLTASIGALTLTVGLSYWFHFNSMLILLLGLAIIIISSYQWWRDISREGTLQGLHSNMVMVNL 80
Cdd:MTH00052    1 MMQQYYHPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317  81 RWGMILFIVSEVFFFLSFFWAFFHASLAPSVEIGTQWPPVGIIPFNPFQIPLLNTAILLASGVTVTWSHHSLMGGNHTQA 160
Cdd:MTH00052   81 KYGMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 161 MQSLFVTILLGMYFTALQAYEYMEAPFSISEAVYGSTFFVATGFHGLHVIIGTTFLLICFYRLSKFHFSPAHHFGFEAAA 240
Cdd:MTH00052  161 IIGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAA 240

                         250       260
                  ....*....|....*....|.
gi 2296408317 241 WYWHFVDVVWLFLYVSIYWWG 261
Cdd:MTH00052  241 WYWHFVDVVWLFLFIFMYWWG 261
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 6-261 2.27e-89

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 266.93  E-value: 2.27e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317   6 HHPFHMVDMSPWPLTASIGALTLTVGLSYWFHFNSMLILLLGLAIIIISSYQWWRDISREGTLQGLHSNMVMVNLRWGMI 85
Cdd:MTH00028    5 YHPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGML 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317  86 LFIVSEVFFFLSFFWAFFHASLAPSVEIGTQWPPVGIIPFNPFQIPLLNTAILLASGVTVTWSHHSLMGGNH-------- 157
Cdd:MTH00028   85 LFILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTGNpaslekgt 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 158 ----------------------------TQAMQSLFVTILLGMYFTALQAYEYMEAPFSISEAVYGSTFFVATGFHGLHV 209
Cdd:MTH00028  165 qgiegpnpsngappdpqkgptfllsdfrTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHV 244

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2296408317 210 IIGTTFLLICFYRLSKFHFSPAHHFGFEAAAWYWHFVDVVWLFLYVSIYWWG 261
Cdd:MTH00028  245 LVGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWG 296
PLN02194 PLN02194
cytochrome-c oxidase
 7-262 4.21e-78

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 236.87  E-value: 4.21e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317   7 HPFHMVDMSPWPLTASIGALTLTVGLSYWFH--FNSMLILLLGLAIIIISSYQWWRDISREGTLQGLHSNMVMVNLRWGM 84
Cdd:PLN02194    7 HSYHLVDPSPWPISGSLGALATTVGGVMYMHpfQGGARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGPRYGS 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317  85 ILFIVSEVFFFLSFFWAFFHASLAPSVEIGTQWPPVGIIPFNPFQIPLLNTAILLASGVTVTWSHHSLMGGNHTQAMQSL 164
Cdd:PLN02194   87 ILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEKRAVYAL 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 165 FVTILLGMYFTALQAYEYMEAPFSISEAVYGSTFFVATGFHGLHVIIGTTFLLICFYRLSKFHFSPAHHFGFEAAAWYWH 244
Cdd:PLN02194  167 VATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWYWH 246

                         250
                  ....*....|....*...
gi 2296408317 245 FVDVVWLFLYVSIYWWGG 262
Cdd:PLN02194  247 FVDVVWLFLFVSIYWWGG 264
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
 7-261 1.04e-66

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 207.50  E-value: 1.04e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317   7 HPFHMVDMSPWPLTASIGALTLTVGLSYWFHFNSMLILLLGLAIIIISSYQWWRDISREGtLQGLHSNMVMVNLRWGMIL 86
Cdd:MTH00083    3 HNFHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMIL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317  87 FIVSEVFFFLSFFWAFFHASLAPSVEIGTQWPPVGIIPFNPFQIPLLNTAILLASGVTVTWSHHSLMGGNHTQAMqSLFV 166
Cdd:MTH00083   82 FIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSNKSCTN-SLLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 167 TILLGMYFTALQAYEYMEAPFSISEAVYGSTFFVATGFHGLHVIIGTTFLLICFYRLSKFHFSPAHHFGFEAAAWYWHFV 246
Cdd:MTH00083  161 TCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFV 240

                         250
                  ....*....|....*
gi 2296408317 247 DVVWLFLYVSIYWWG 261
Cdd:MTH00083  241 DVVWLFLFVFVYWWS 255
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 72-260 3.23e-63

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: 196.27  E-value: 3.23e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317  72 HSNMVMVNLRWGMILFIVSEVFFFLSFFWAFFHASLAPSVEIGtqwppvgiIPFNPFQIPLLNTAILLASGVTVTWSHHS 151
Cdd:cd00386     1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFG--------AGLDPLDLPLLNTNTLLLSGSSVTWAHAS 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 152 LM--GGNHTQAMQSLFVTILLGMYFTALQAYEYMEAPFSISEAVYGSTFFVATGFHGLHVIIGTTFLLICFYRLSKFHFS 229
Cdd:cd00386    73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2296408317 230 PAHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 260
Cdd:cd00386   153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
71-260 2.85e-47

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 155.78  E-value: 2.85e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317  71 LHSNMVMVNLRWGMILFIVSEVFFFLSFFWAFFHASLApsveigTQWPPVGIIPFNPFqIPLLNTAILLASGVTVTWSHH 150
Cdd:COG1845     7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS------APDWPAGAELLDLP-LPLINTLLLLLSSFTVALAVR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 151 SLMGGNHTQAMQSLFVTILLGMYFTALQAYEYME---APFSISEAVYGSTFFVATGFHGLHVIIGTTFLLICFYRLSKFH 227
Cdd:COG1845    80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHliaEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2296408317 228 FSPAHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 260
Cdd:COG1845   160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
NorE_like cd02862
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ...
 132-258 1.70e-22

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: 91.14  E-value: 1.70e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 132 LLNTAILLASGVTVTWSHHSLMGGNHTQAMQSLFVTILLGMYFTALQAYEY---MEAPFSISEAVYGSTFFVATGFHGLH 208
Cdd:cd02862    55 ALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYahkIAAGIDPDAGLFFTLYFLLTGFHLLH 134

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2296408317 209 VIIGTTFLLICFYRLSKFHFSPAHHFGFEAAAWYWHFVDVVWLFLYVSIY 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 8.78e-18

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: 78.57  E-value: 8.78e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 131 PLLNTAILLASGVTVTWSHHSLMGGNHTQAMQSLFVTILLGMYFTALQAYEYMEAPFSI---SEAVYGSTFFVATGFHGL 207
Cdd:cd02865    52 LSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWHALNDAGygpTSNPAGSFFYLLTGLHGL 131

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2296408317 208 HVIIGTTFLLICFYRLSKFHFSPAHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 260
Cdd:cd02865   132 HVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVLLALLYGT 184
Ubiquinol_oxidase_III cd02863
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ...
 128-258 1.80e-17

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: 77.67  E-value: 1.80e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 128 FQIPL--LNTAILLASGVTVTWSHHSLMGGNHTQAMQSLFVTILLGMYFTALQAYE---YMEAPFSISEAVYGSTFFVAT 202
Cdd:cd02863    48 FELPLvfIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLV 127

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2296408317 203 GFHGLHVIIGTTFLLICFYRLSKFHFSPAHHFGFEAAAWYWHFVDVVWLFLYVSIY 258
Cdd:cd02863   128 GTHGLHVTFGLIWILVMIIQLKKRGLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
Heme_Cu_Oxidase_III_1 cd02864
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 115-260 6.08e-17

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: 76.77  E-value: 6.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 115 TQWPP---VGIIPFNPFQIPL----LNTAILLASGVTVTWSHHSLMGGNHTQAMQSLFVTILLGMYFTALQAYEYME--- 184
Cdd:cd02864    40 EPWPLpsdVFALRIGHFNIPLvliaIMTFILITSSGTMAMAVNFGYRGNRKAAARLMLATALLGATFVGMQAFEWTKliv 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 185 ------APFSISEAVYGSTFFVATGFHGLHVIIGTTFLLICFYRLSKFHFSPAHHF-GFEAAAWYWHFVDVVWLFLYVSI 257
Cdd:cd02864   120 eegvrpWGNPWGAAQFGASFFMITGFHGTHVTIGVIYLIIIARKVWRGKYQRIGRYeIVEIAGLYWHFVDLVWVFIFAFF 199


                  ...
gi 2296408317 258 YWW 260
Cdd:cd02864   200 YLW 202
COX3 MTH00049
cytochrome c oxidase subunit III; Validated
 127-258 6.24e-14

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177124  Cd Length: 215  Bit Score: 68.79  E-value: 6.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 127 PFQIPLLNTAILLASGVTVTwSHHSLMGGNHTQAMqsLFVTILLGMYFTALQAYEYMEAPFSISEAVYGSTFFVATGFHG 206
Cdd:MTH00049   89 SLEIPFVGCFLLLGSSITVT-AYHHLLGWKYCDLF--LYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHF 165

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2296408317 207 LHVIIGTTFLL-ICFYRLSKFHFSPAhhfgfEAAAWYWHFVDVVWLFLYVSIY 258
Cdd:MTH00049  166 SHVVLGVVGLStLLLVGSSSFGVYRS-----TVLTWYWHFVDYIWLLVYLIVY 213
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 121-261 1.91e-10

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: 58.71  E-value: 1.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 121 GIIPFNPFQIPLL--NTAILLASGVTVTWSHHSLMGGNHTQAMQSLFVTILLGMYFTALQAYE---YMEAPFSISEAVYG 195
Cdd:TIGR02897  43 GKMPAELFELPLVliMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYW 122

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2296408317 196 STFFVATGFHGLHVIIGTTFLLICFYRLSKFHFSPAHHFGFEAAAWYWHFVDVVWLFLYVSIYWWG 261
Cdd:TIGR02897 123 SSFFVLLGTHGCHVTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
PRK10663 PRK10663
cytochrome o ubiquinol oxidase subunit III; Provisional
 128-261 5.90e-10

cytochrome o ubiquinol oxidase subunit III; Provisional


Pssm-ID: 182628  Cd Length: 204  Bit Score: 57.48  E-value: 5.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 128 FQIP--LLNTAILLASGVTVTWSHHSLMGGNHTQAMQSLFVTILLGMYFTALQAYEY---MEAPFSISEAVYGSTFFVAT 202
Cdd:PRK10663   64 FELPfvLVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFhhlIVEGMGPDRSGFLSAFFALV 143

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2296408317 203 GFHGLHVIIGTTFLLICFYRLSKFHFSPAHHFGFEAAAWYWHFVDVVWLFLYVSIYWWG 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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