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Conserved domains on  [gi|1707765480|gb|QDP18059|]
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cytochrome c oxidase subunit 3 (mitochondrion) [Phymateus morbillosus]

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
 5-259 1.45e-152

cytochrome c oxidase subunit III; Provisional


:

Pssm-ID: 214439  Cd Length: 255  Bit Score: 425.36  E-value: 1.45e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480   5 NQNHPFHLVDYSPWPITGAIGAMSLTSGLAKWFHLFNTNLIMIGLTIMTLTMIQWWRDIIREGTYQGLHTKLVSIGLRWG 84
Cdd:MTH00155    1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480  85 MILFITSEVLFFVSFFWAFFSSSINPTIELGMTWPPLGIQPFNPMQIPMLNTTILLASGVTITWAHHSMIESNHSQALQG 164
Cdd:MTH00155   81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480 165 LYFTVMLGIYFTMLQAYEYWEAPFTIADAIYGSTFFIATGFHGLHVIIGTVFLITCSVRHSMKQFSTNHHFGFEAAAWYW 244
Cdd:MTH00155  161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240

                         250
                  ....*....|....*
gi 1707765480 245 HFVDVIWLFLYISIY 259
Cdd:MTH00155  241 HFVDVVWLFLYISIY 255
 
Name Accession Description Interval E-value
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 5-259 1.45e-152

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 425.36  E-value: 1.45e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480   5 NQNHPFHLVDYSPWPITGAIGAMSLTSGLAKWFHLFNTNLIMIGLTIMTLTMIQWWRDIIREGTYQGLHTKLVSIGLRWG 84
Cdd:MTH00155    1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480  85 MILFITSEVLFFVSFFWAFFSSSINPTIELGMTWPPLGIQPFNPMQIPMLNTTILLASGVTITWAHHSMIESNHSQALQG 164
Cdd:MTH00155   81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480 165 LYFTVMLGIYFTMLQAYEYWEAPFTIADAIYGSTFFIATGFHGLHVIIGTVFLITCSVRHSMKQFSTNHHFGFEAAAWYW 244
Cdd:MTH00155  161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240

                         250
                  ....*....|....*
gi 1707765480 245 HFVDVIWLFLYISIY 259
Cdd:MTH00155  241 HFVDVVWLFLYISIY 255
COX3 pfam00510
Cytochrome c oxidase subunit III;
8-263 8.47e-122

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 347.48  E-value: 8.47e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480   8 HPFHLVDYSPWPITGAIGAMSLTSGLAKWFHLF--NTNLIMIGLTIMTLTMIQWWRDIIREGTYQGLHTKLVSIGLRWGM 85
Cdd:pfam00510   1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYsgNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480  86 ILFITSEVLFFVSFFWAFFSSSINPTIELGMTWPPLGIQPFNPMQIPMLNTTILLASGVTITWAHHSMIESNHSQALQGL 165
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480 166 YFTVMLGIYFTMLQAYEYWEAPFTIADAIYGSTFFIATGFHGLHVIIGTVFLITCSVRHSMKQFSTNHHFGFEAAAWYWH 245
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240

                         250
                  ....*....|....*...
gi 1707765480 246 FVDVIWLFLYISIYWWGS 263
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWGS 258
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 20-261 2.94e-115

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: 330.25  E-value: 2.94e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480  20 ITGAIGAMSLTSGLAKWFHLFNTNLIM-IGLTIMTLTMIQWWRDIIREGTYQGLHTKLVSIGLRWGMILFITSEVLFFVS 98
Cdd:cd01665     1 ILGSFGLLLLALGLVLWMHGYGGPLLLfLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480  99 FFWAFFSSSINPTIELGMTWPPLGIQPFNPMQIPMLNTTILLASGVTITWAHHSMIESNHSQALQGLYFTVMLGIYFTML 178
Cdd:cd01665    81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480 179 QAYEYWEAPFTIADAIYGSTFFIATGFHGLHVIIGTVFLITCSVRHSMKQFSTNHHFGFEAAAWYWHFVDVIWLFLYISI 258
Cdd:cd01665   161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240


                  ...
gi 1707765480 259 YWW 261
Cdd:cd01665   241 YWW 243
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
72-261 9.13e-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: 9.13e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480  72 LHTKLVSIGLRWGMILFITSEVLFFVSFFWAFFsssinpTIELGMTWPPLGIQPFNPmQIPMLNTTILLASGVTITWAHH 151
Cdd:COG1845     7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYF------VLRASAPDWPAGAELLDL-PLPLINTLLLLLSSFTVALAVR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480 152 SMIESNHSQALQGLYFTVMLGIYFTMLQAYEY---WEAPFTIADAIYGSTFFIATGFHGLHVIIGTVFLITCSVRHSMKQ 228
Cdd:COG1845    80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1707765480 229 FSTNHHFGFEAAAWYWHFVDVIWLFLYISIYWW 261
Cdd:COG1845   160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
 
Name Accession Description Interval E-value
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 5-259 1.45e-152

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 425.36  E-value: 1.45e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480   5 NQNHPFHLVDYSPWPITGAIGAMSLTSGLAKWFHLFNTNLIMIGLTIMTLTMIQWWRDIIREGTYQGLHTKLVSIGLRWG 84
Cdd:MTH00155    1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480  85 MILFITSEVLFFVSFFWAFFSSSINPTIELGMTWPPLGIQPFNPMQIPMLNTTILLASGVTITWAHHSMIESNHSQALQG 164
Cdd:MTH00155   81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480 165 LYFTVMLGIYFTMLQAYEYWEAPFTIADAIYGSTFFIATGFHGLHVIIGTVFLITCSVRHSMKQFSTNHHFGFEAAAWYW 244
Cdd:MTH00155  161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240

                         250
                  ....*....|....*
gi 1707765480 245 HFVDVIWLFLYISIY 259
Cdd:MTH00155  241 HFVDVVWLFLYISIY 255
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 4-263 8.06e-141

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 395.86  E-value: 8.06e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480   4 TNQNHPFHLVDYSPWPITGAIGAMSLTSGLAKWFHLFNTNLIMIGLTIMTLTMIQWWRDIIREGTYQGLHTKLVSIGLRW 83
Cdd:MTH00118    2 THQAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480  84 GMILFITSEVLFFVSFFWAFFSSSINPTIELGMTWPPLGIQPFNPMQIPMLNTTILLASGVTITWAHHSMIESNHSQALQ 163
Cdd:MTH00118   82 GMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480 164 GLYFTVMLGIYFTMLQAYEYWEAPFTIADAIYGSTFFIATGFHGLHVIIGTVFLITCSVRHSMKQFSTNHHFGFEAAAWY 243
Cdd:MTH00118  162 ALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWY 241

                         250       260
                  ....*....|....*....|
gi 1707765480 244 WHFVDVIWLFLYISIYWWGS 263
Cdd:MTH00118  242 WHFVDVVWLFLYISIYWWGS 261
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 6-263 9.72e-135

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 380.47  E-value: 9.72e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480   6 QNHPFHLVDYSPWPITGAIGAMSLTSGLAKWFHLFNTNLIMIGLTIMTLTMIQWWRDIIREGTYQGLHTKLVSIGLRWGM 85
Cdd:MTH00189    3 QAHPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRYGM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480  86 ILFITSEVLFFVSFFWAFFSSSINPTIELGMTWPPLGIQPFNPMQIPMLNTTILLASGVTITWAHHSMIESNHSQALQGL 165
Cdd:MTH00189   83 ILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQAL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480 166 YFTVMLGIYFTMLQAYEYWEAPFTIADAIYGSTFFIATGFHGLHVIIGTVFLITCSVRHSMKQFSTNHHFGFEAAAWYWH 245
Cdd:MTH00189  163 TLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWYWH 242

                         250
                  ....*....|....*...
gi 1707765480 246 FVDVIWLFLYISIYWWGS 263
Cdd:MTH00189  243 FVDVVWLFLYVSIYWWGS 260
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 5-263 8.48e-129

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 365.59  E-value: 8.48e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480   5 NQNHPFHLVDYSPWPITGAIGAMSLTSGLAKWFHLFNTNLIMIGLTIMTLTMIQWWRDIIREGTYQGLHTKLVSIGLRWG 84
Cdd:MTH00039    2 THQHPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRYG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480  85 MILFITSEVLFFVSFFWAFFSSSINPTIELGMTWPPLGIQPFNPMQIPMLNTTILLASGVTITWAHHSMIESNHSQALQG 164
Cdd:MTH00039   82 MILFITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480 165 LYFTVMLGIYFTMLQAYEYWEAPFTIADAIYGSTFFIATGFHGLHVIIGTVFLITCSVRHSMKQFSTNHHFGFEAAAWYW 244
Cdd:MTH00039  162 LFLTVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWYW 241

                         250
                  ....*....|....*....
gi 1707765480 245 HFVDVIWLFLYISIYWWGS 263
Cdd:MTH00039  242 HFVDVVWLFLYVCIYWWGS 260
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 6-263 7.38e-127

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 360.36  E-value: 7.38e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480   6 QNHPFHLVDYSPWPITGAIGAMSLTSGLAKWFHLFNTNLIMIGLTIMTLTMIQWWRDIIREGTYQGLHTKLVSIGLRWGM 85
Cdd:MTH00141    2 TRNPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480  86 ILFITSEVLFFVSFFWAFFSSSINPTIELGMTWPPLGIQPFNPMQIPMLNTTILLASGVTITWAHHSMIESNHSQALQGL 165
Cdd:MTH00141   82 ILFIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480 166 YFTVMLGIYFTMLQAYEYWEAPFTIADAIYGSTFFIATGFHGLHVIIGTVFLITCSVRHSMKQFSTNHHFGFEAAAWYWH 245
Cdd:MTH00141  162 GLTIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWH 241

                         250
                  ....*....|....*...
gi 1707765480 246 FVDVIWLFLYISIYWWGS 263
Cdd:MTH00141  242 FVDVVWLFLYLSIYWWGS 259
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 4-263 7.05e-126

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 357.90  E-value: 7.05e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480   4 TNQNHPFHLVDYSPWPITGAIGAMSLTSGLAKWFHLFNTNLIMIGLTIMTLTMIQWWRDIIREGTYQGLHTKLVSIGLRW 83
Cdd:MTH00075    2 AHQAHAFHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480  84 GMILFITSEVLFFVSFFWAFFSSSINPTIELGMTWPPLGIQPFNPMQIPMLNTTILLASGVTITWAHHSMIESNHSQALQ 163
Cdd:MTH00075   82 GMILFITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480 164 GLYFTVMLGIYFTMLQAYEYWEAPFTIADAIYGSTFFIATGFHGLHVIIGTVFLITCSVRHSMKQFSTNHHFGFEAAAWY 243
Cdd:MTH00075  162 SLALTIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWY 241

                         250       260
                  ....*....|....*....|
gi 1707765480 244 WHFVDVIWLFLYISIYWWGS 263
Cdd:MTH00075  242 WHFVDVVWLFLYVSIYWWGS 261
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 2-263 8.27e-126

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 357.94  E-value: 8.27e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480   2 MTTNQNHPFHLVDYSPWPITGAIGAMSLTSGLAKWFHLFNTNLIMIGLTIMTLTMIQWWRDIIREGTYQGLHTKLVSIGL 81
Cdd:MTH00219    1 MMFFQTNPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480  82 RWGMILFITSEVLFFVSFFWAFFSSSINPTIELGMTWPPLGIQPFNPMQIPMLNTTILLASGVTITWAHHSMIESNHSQA 161
Cdd:MTH00219   81 RIGMILFIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480 162 LQGLYFTVMLGIYFTMLQAYEYWEAPFTIADAIYGSTFFIATGFHGLHVIIGTVFLITCSVRHSMKQFSTNHHFGFEAAA 241
Cdd:MTH00219  161 QQGLLFTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAA 240

                         250       260
                  ....*....|....*....|..
gi 1707765480 242 WYWHFVDVIWLFLYISIYWWGS 263
Cdd:MTH00219  241 WYWHFVDVVWLFLYVSIYWWGS 262
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 4-263 1.73e-125

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 357.11  E-value: 1.73e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480   4 TNQNHPFHLVDYSPWPITGAIGAMSLTSGLAKWFHLFNTNLIMIGLTIMTLTMIQWWRDIIREGTYQGLHTKLVSIGLRW 83
Cdd:MTH00099    2 THQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480  84 GMILFITSEVLFFVSFFWAFFSSSINPTIELGMTWPPLGIQPFNPMQIPMLNTTILLASGVTITWAHHSMIESNHSQALQ 163
Cdd:MTH00099   82 GMILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480 164 GLYFTVMLGIYFTMLQAYEYWEAPFTIADAIYGSTFFIATGFHGLHVIIGTVFLITCSVRHSMKQFSTNHHFGFEAAAWY 243
Cdd:MTH00099  162 ALFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWY 241

                         250       260
                  ....*....|....*....|
gi 1707765480 244 WHFVDVIWLFLYISIYWWGS 263
Cdd:MTH00099  242 WHFVDVVWLFLYVSIYWWGS 261
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 4-263 5.16e-125

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 356.00  E-value: 5.16e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480   4 TNQNHPFHLVDYSPWPITGAIGAMSLTSGLAKWFHLFNTNLIMIGLTIMTLTMIQWWRDIIREGTYQGLHTKLVSIGLRW 83
Cdd:MTH00130    2 AHQAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480  84 GMILFITSEVLFFVSFFWAFFSSSINPTIELGMTWPPLGIQPFNPMQIPMLNTTILLASGVTITWAHHSMIESNHSQALQ 163
Cdd:MTH00130   82 GMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480 164 GLYFTVMLGIYFTMLQAYEYWEAPFTIADAIYGSTFFIATGFHGLHVIIGTVFLITCSVRHSMKQFSTNHHFGFEAAAWY 243
Cdd:MTH00130  162 SLTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWY 241

                         250       260
                  ....*....|....*....|
gi 1707765480 244 WHFVDVIWLFLYISIYWWGS 263
Cdd:MTH00130  242 WHFVDVVWLFLYISIYWWGS 261
COX3 pfam00510
Cytochrome c oxidase subunit III;
8-263 8.47e-122

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 347.48  E-value: 8.47e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480   8 HPFHLVDYSPWPITGAIGAMSLTSGLAKWFHLF--NTNLIMIGLTIMTLTMIQWWRDIIREGTYQGLHTKLVSIGLRWGM 85
Cdd:pfam00510   1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYsgNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480  86 ILFITSEVLFFVSFFWAFFSSSINPTIELGMTWPPLGIQPFNPMQIPMLNTTILLASGVTITWAHHSMIESNHSQALQGL 165
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480 166 YFTVMLGIYFTMLQAYEYWEAPFTIADAIYGSTFFIATGFHGLHVIIGTVFLITCSVRHSMKQFSTNHHFGFEAAAWYWH 245
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240

                         250
                  ....*....|....*...
gi 1707765480 246 FVDVIWLFLYISIYWWGS 263
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWGS 258
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 20-261 2.94e-115

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: 330.25  E-value: 2.94e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480  20 ITGAIGAMSLTSGLAKWFHLFNTNLIM-IGLTIMTLTMIQWWRDIIREGTYQGLHTKLVSIGLRWGMILFITSEVLFFVS 98
Cdd:cd01665     1 ILGSFGLLLLALGLVLWMHGYGGPLLLfLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480  99 FFWAFFSSSINPTIELGMTWPPLGIQPFNPMQIPMLNTTILLASGVTITWAHHSMIESNHSQALQGLYFTVMLGIYFTML 178
Cdd:cd01665    81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480 179 QAYEYWEAPFTIADAIYGSTFFIATGFHGLHVIIGTVFLITCSVRHSMKQFSTNHHFGFEAAAWYWHFVDVIWLFLYISI 258
Cdd:cd01665   161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240


                  ...
gi 1707765480 259 YWW 261
Cdd:cd01665   241 YWW 243
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 8-263 4.14e-115

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 330.65  E-value: 4.14e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480   8 HPFHLVDYSPWPITGAIGAMSLTSGLAKWFHLFNTNLIMIGLTIMTLTMIQWWRDIIREGTYQGLHTKLVSIGLRWGMIL 87
Cdd:MTH00009    4 QPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMIL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480  88 FITSEVLFFVSFFWAFFSSSINPTIELGMTWPPLGIQPFNPMQIPMLNTTILLASGVTITWAHHSMIESNHSQALQGLYF 167
Cdd:MTH00009   84 FIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALIL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480 168 TVMLGIYFTMLQAYEYWEAPFTIADAIYGSTFFIATGFHGLHVIIGTVFLITCSVRHSMKQFSTNHHFGFEAAAWYWHFV 247
Cdd:MTH00009  164 TVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFV 243

                         250
                  ....*....|....*.
gi 1707765480 248 DVIWLFLYISIYWWGS 263
Cdd:MTH00009  244 DVVWIFLYLCIYWWGS 259
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 4-263 1.04e-109

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 317.08  E-value: 1.04e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480   4 TNQNHPFHLVDYSPWPITGAIGAMSLTSGLAKWFHLFNTNLIMIGLTIMTLTMIQWWRDIIREGTYQGLHTKLVSIGLRW 83
Cdd:MTH00024    2 SKLYHPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480  84 GMILFITSEVLFFVSFFWAFFSSSINPTIELGMTWPPLGIQPFNPMQIPMLNTTILLASGVTITWAHHSMIESNHSQALQ 163
Cdd:MTH00024   82 GMLLFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAIL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480 164 GLYFTVMLGIYFTMLQAYEYWEAPFTIADAIYGSTFFIATGFHGLHVIIGTVFLITCSVRHSMKQFSTNHHFGFEAAAWY 243
Cdd:MTH00024  162 GLFLTVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASWY 241

                         250       260
                  ....*....|....*....|
gi 1707765480 244 WHFVDVIWLFLYISIYWWGS 263
Cdd:MTH00024  242 WHFVDVVWLFLYLCIYWWGS 261
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 2-263 3.00e-104

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 303.25  E-value: 3.00e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480   2 MTTNQNHPFHLVDYSPWPITGAIGAMSLTSGLAKWFHLFNTNLIMIGLTIMTLTMIQWWRDIIREGTYQGLHTKLVSIGL 81
Cdd:MTH00052    1 MMQQYYHPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480  82 RWGMILFITSEVLFFVSFFWAFFSSSINPTIELGMTWPPLGIQPFNPMQIPMLNTTILLASGVTITWAHHSMIESNHSQA 161
Cdd:MTH00052   81 KYGMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480 162 LQGLYFTVMLGIYFTMLQAYEYWEAPFTIADAIYGSTFFIATGFHGLHVIIGTVFLITCSVRHSMKQFSTNHHFGFEAAA 241
Cdd:MTH00052  161 IIGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAA 240

                         250       260
                  ....*....|....*....|..
gi 1707765480 242 WYWHFVDVIWLFLYISIYWWGS 263
Cdd:MTH00052  241 WYWHFVDVVWLFLFIFMYWWGS 262
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 8-263 8.90e-92

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 273.10  E-value: 8.90e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480   8 HPFHLVDYSPWPITGAIGAMSLTSGLAKWFHLFNTNLIMIGLTIMTLTMIQWWRDIIREGTYQGLHTKLVSIGLRWGMIL 87
Cdd:MTH00028    6 HPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480  88 FITSEVLFFVSFFWAFFSSSINPTIELGMTWPPLGIQPFNPMQIPMLNTTILLASGVTITWAHHSMIESNH--------- 158
Cdd:MTH00028   86 FILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTGNpaslekgtq 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480 159 ---------------------------SQALQGLYFTVMLGIYFTMLQAYEYWEAPFTIADAIYGSTFFIATGFHGLHVI 211
Cdd:MTH00028  166 giegpnpsngappdpqkgptfllsdfrTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVL 245

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1707765480 212 IGTVFLITCSVRHSMKQFSTNHHFGFEAAAWYWHFVDVIWLFLYISIYWWGS 263
Cdd:MTH00028  246 VGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWGS 297
PLN02194 PLN02194
cytochrome-c oxidase
 2-262 1.85e-84

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 253.05  E-value: 1.85e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480   2 MTTNQNHPFHLVDYSPWPITGAIGAMSLTSGLAKWFHLFN--TNLIMIGLTIMTLTMIQWWRDIIREGTYQGLHTKLVSI 79
Cdd:PLN02194    1 MIESQRHSYHLVDPSPWPISGSLGALATTVGGVMYMHPFQggARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480  80 GLRWGMILFITSEVLFFVSFFWAFFSSSINPTIELGMTWPPLGIQPFNPMQIPMLNTTILLASGVTITWAHHSMIESNHS 159
Cdd:PLN02194   81 GPRYGSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480 160 QALQGLYFTVMLGIYFTMLQAYEYWEAPFTIADAIYGSTFFIATGFHGLHVIIGTVFLITCSVRHSMKQFSTNHHFGFEA 239
Cdd:PLN02194  161 RAVYALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEA 240

                         250       260
                  ....*....|....*....|...
gi 1707765480 240 AAWYWHFVDVIWLFLYISIYWWG 262
Cdd:PLN02194  241 AAWYWHFVDVVWLFLFVSIYWWG 263
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
 8-263 1.77e-62

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 196.72  E-value: 1.77e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480   8 HPFHLVDYSPWPITGAIGAMSLTSGLAKWFHLFNTNLIMIGLTIMTLTMIQWWRDIIREGtYQGLHTKLVSIGLRWGMIL 87
Cdd:MTH00083    3 HNFHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMIL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480  88 FITSEVLFFVSFFWAFFSSSINPTIELGMTWPPLGIQPFNPMQIPMLNTTILLASGVTITWAHHSMIESNhSQALQGLYF 167
Cdd:MTH00083   82 FIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSN-KSCTNSLLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480 168 TVMLGIYFTMLQAYEYWEAPFTIADAIYGSTFFIATGFHGLHVIIGTVFLITCSVRHSMKQFSTNHHFGFEAAAWYWHFV 247
Cdd:MTH00083  161 TCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFV 240

                         250
                  ....*....|....*.
gi 1707765480 248 DVIWLFLYISIYWWGS 263
Cdd:MTH00083  241 DVVWLFLFVFVYWWSY 256
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 73-261 1.53e-58

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: 184.33  E-value: 1.53e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480  73 HTKLVSIGLRWGMILFITSEVLFFVSFFWAFFSSSINPTIELGMtwpplgiqPFNPMQIPMLNTTILLASGVTITWAHHS 152
Cdd:cd00386     1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFGA--------GLDPLDLPLLNTNTLLLSGSSVTWAHAS 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480 153 MI--ESNHSQALQGLYFTVMLGIYFTMLQAYEYWEAPFTIADAIYGSTFFIATGFHGLHVIIGTVFLITCSVRHSMKQFS 230
Cdd:cd00386    73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1707765480 231 TNHHFGFEAAAWYWHFVDVIWLFLYISIYWW 261
Cdd:cd00386   153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
72-261 9.13e-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: 9.13e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480  72 LHTKLVSIGLRWGMILFITSEVLFFVSFFWAFFsssinpTIELGMTWPPLGIQPFNPmQIPMLNTTILLASGVTITWAHH 151
Cdd:COG1845     7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYF------VLRASAPDWPAGAELLDL-PLPLINTLLLLLSSFTVALAVR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480 152 SMIESNHSQALQGLYFTVMLGIYFTMLQAYEY---WEAPFTIADAIYGSTFFIATGFHGLHVIIGTVFLITCSVRHSMKQ 228
Cdd:COG1845    80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1707765480 229 FSTNHHFGFEAAAWYWHFVDVIWLFLYISIYWW 261
Cdd:COG1845   160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
NorE_like cd02862
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ...
 134-259 2.49e-20

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: 85.36  E-value: 2.49e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480 134 LNTTILLASGVTITWAHHSMIESNHSQALQGLYFTVMLGIYFTMLQAYEYWE---APFTIADAIYGSTFFIATGFHGLHV 210
Cdd:cd02862    56 LNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYAHkiaAGIDPDAGLFFTLYFLLTGFHLLHV 135

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1707765480 211 IIGTVFLITCSVRHSMKQFSTNHHFGFEAAAWYWHFVDVIWLFLYISIY 259
Cdd:cd02862   136 LIGLGILLWVAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVLFPLLY 184
COX3 MTH00049
cytochrome c oxidase subunit III; Validated
 128-259 6.90e-15

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177124  Cd Length: 215  Bit Score: 71.49  E-value: 6.90e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480 128 PMQIPMLNTTILLASGVTITwAHHSMIESNHSQALqgLYFTVMLGIYFTMLQAYEYWEAPFTIADAIYGSTFFIATGFHG 207
Cdd:MTH00049   89 SLEIPFVGCFLLLGSSITVT-AYHHLLGWKYCDLF--LYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHF 165

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1707765480 208 LHVIIGTVFLITCSVRHSMKqfstnhhFGF---EAAAWYWHFVDVIWLFLYISIY 259
Cdd:MTH00049  166 SHVVLGVVGLSTLLLVGSSS-------FGVyrsTVLTWYWHFVDYIWLLVYLIVY 213
Heme_Cu_Oxidase_III_1 cd02864
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 136-261 1.37e-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: 70.22  E-value: 1.37e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480 136 TTILLASGVTITWAHHSMIESNHSQALQGLYFTVMLGIYFTMLQAYEY-----------WEAPFTIAdaIYGSTFFIATG 204
Cdd:cd02864    67 TFILITSSGTMAMAVNFGYRGNRKAAARLMLATALLGATFVGMQAFEWtkliveegvrpWGNPWGAA--QFGASFFMITG 144

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1707765480 205 FHGLHVIIGTVFLITCSVRHSMKQF-STNHHFGFEAAAWYWHFVDVIWLFLYISIYWW 261
Cdd:cd02864   145 FHGTHVTIGVIYLIIIARKVWRGKYqRIGRYEIVEIAGLYWHFVDLVWVFIFAFFYLW 202
Ubiquinol_oxidase_III cd02863
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ...
 133-259 2.70e-14

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: 69.19  E-value: 2.70e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480 133 MLNTTILLASGVTITWAHHSMIESNHSQALQGLYFTVMLGIYFTMLQAYE---YWEAPFTIADAIYGSTFFIATGFHGLH 209
Cdd:cd02863    54 FIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLVGTHGLH 133

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1707765480 210 VIIGTVFLITCSVRHSMKQFSTNHHFGFEAAAWYWHFVDVIWLFLYISIY 259
Cdd:cd02863   134 VTFGLIWILVMIIQLKKRGLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
Heme_Cu_Oxidase_III_2 cd02865
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 132-261 4.31e-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: 239216  Cd Length: 184  Bit Score: 68.55  E-value: 4.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480 132 PMLNTTILLASGVTITWAHHSMIESNHSQALQGLYFTVMLGIYFTMLQAYEYWEAPF---TIADAIYGSTFFIATGFHGL 208
Cdd:cd02865    52 LSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWHALNDagyGPTSNPAGSFFYLLTGLHGL 131

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1707765480 209 HVIIGTVFLITCSVRHSMKQFSTNHHFGFEAAAWYWHFVDVIWLFLYISIYWW 261
Cdd:cd02865   132 HVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVLLALLYGT 184
PRK10663 PRK10663
cytochrome o ubiquinol oxidase subunit III; Provisional
 133-263 1.09e-07

cytochrome o ubiquinol oxidase subunit III; Provisional


Pssm-ID: 182628  Cd Length: 204  Bit Score: 50.94  E-value: 1.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765480 133 MLNTTILLASGVTITWAHHSMIESNHSQALQGLYFTVMLGIYFTMLQAYEYW---EAPFTIADAIYGSTFFIATGFHGLH 209
Cdd:PRK10663   70 LVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFHhliVEGMGPDRSGFLSAFFALVGTHGLH 149

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1707765480 210 VIIGTVFLITCSVRHSMKQFSTNHHFGFEAAAWYWHFVDVIWLFLYISIYWWGS 263
Cdd:PRK10663  150 VTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGA 203
 
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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