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Conserved domains on  [gi|1824665764|ref|YP_009740633|]
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cytochrome c oxidase subunit III (mitochondrion) [Bryodemella holdereri holdereri]

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 2.31e-154

cytochrome c oxidase subunit III; Provisional


:

Pssm-ID: 214439  Cd Length: 255  Bit Score: 429.99  E-value: 2.31e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764   5 NSNHPFHMVDYSPWPLVGSIGTMVMLMGLAKWFHMYNINLLMIGMMITILTMIQWWRDVIRESTFQGLHTKLVSMGMRWG 84
Cdd:MTH00155    1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764  85 MILFIVSEVLFFISFFWAFFNSSLSPTIELGMMWPPMGIQSFNPMHIPLLNTAILLASGVTVTWAHHSIMESNHSQATQG 164
Cdd:MTH00155   81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764 165 LFFTVLLGVYFTMLQMYEYWEASFTIADAVYGSTFFVATGFHGLHVIIGTLFLFTCFIRHLMNQFSPSHHFGFEAAAWYW 244
Cdd:MTH00155  161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240

                         250
                  ....*....|....*
gi 1824665764 245 HFVDVVWLFLYLSIY 259
Cdd:MTH00155  241 HFVDVVWLFLYISIY 255
 
Name Accession Description Interval E-value
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 5-259 2.31e-154

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 429.99  E-value: 2.31e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764   5 NSNHPFHMVDYSPWPLVGSIGTMVMLMGLAKWFHMYNINLLMIGMMITILTMIQWWRDVIRESTFQGLHTKLVSMGMRWG 84
Cdd:MTH00155    1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764  85 MILFIVSEVLFFISFFWAFFNSSLSPTIELGMMWPPMGIQSFNPMHIPLLNTAILLASGVTVTWAHHSIMESNHSQATQG 164
Cdd:MTH00155   81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764 165 LFFTVLLGVYFTMLQMYEYWEASFTIADAVYGSTFFVATGFHGLHVIIGTLFLFTCFIRHLMNQFSPSHHFGFEAAAWYW 244
Cdd:MTH00155  161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240

                         250
                  ....*....|....*
gi 1824665764 245 HFVDVVWLFLYLSIY 259
Cdd:MTH00155  241 HFVDVVWLFLYISIY 255
COX3 pfam00510
Cytochrome c oxidase subunit III;
8-263 6.85e-121

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 345.16  E-value: 6.85e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764   8 HPFHMVDYSPWPLVGSIGTMVMLMGLAKWFHMY--NINLLMIGMMITILTMIQWWRDVIRESTFQGLHTKLVSMGMRWGM 85
Cdd:pfam00510   1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYsgNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764  86 ILFIVSEVLFFISFFWAFFNSSLSPTIELGMMWPPMGIQSFNPMHIPLLNTAILLASGVTVTWAHHSIMESNHSQATQGL 165
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764 166 FFTVLLGVYFTMLQMYEYWEASFTIADAVYGSTFFVATGFHGLHVIIGTLFLFTCFIRHLMNQFSPSHHFGFEAAAWYWH 245
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240

                         250
                  ....*....|....*...
gi 1824665764 246 FVDVVWLFLYLSIYWWGS 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 9.12e-119

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: 339.49  E-value: 9.12e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764  20 LVGSIGTMVMLMGLAKWFHMY-NINLLMIGMMITILTMIQWWRDVIRESTFQGLHTKLVSMGMRWGMILFIVSEVLFFIS 98
Cdd:cd01665     1 ILGSFGLLLLALGLVLWMHGYgGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764  99 FFWAFFNSSLSPTIELGMMWPPMGIQSFNPMHIPLLNTAILLASGVTVTWAHHSIMESNHSQATQGLFFTVLLGVYFTML 178
Cdd:cd01665    81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764 179 QMYEYWEASFTIADAVYGSTFFVATGFHGLHVIIGTLFLFTCFIRHLMNQFSPSHHFGFEAAAWYWHFVDVVWLFLYLSI 258
Cdd:cd01665   161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240


                  ...
gi 1824665764 259 YWW 261
Cdd:cd01665   241 YWW 243
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
72-261 4.10e-46

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 152.70  E-value: 4.10e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764  72 LHTKLVSMGMRWGMILFIVSEVLFFISFFWAFFNSSLSPTielgmmWPPMGIQSFNPmHIPLLNTAILLASGVTVTWAHH 151
Cdd:COG1845     7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRASAP------DWPAGAELLDL-PLPLINTLLLLLSSFTVALAVR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764 152 SIMESNHSQATQGLFFTVLLGVYFTMLQMYEY---WEASFTIADAVYGSTFFVATGFHGLHVIIGTLFLFTCFIRHLMNQ 228
Cdd:COG1845    80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1824665764 229 FSPSHHFGFEAAAWYWHFVDVVWLFLYLSIYWW 261
Cdd:COG1845   160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 133-262 1.41e-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: 59.10  E-value: 1.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764 133 LLNTAILLASGVTVTWAHHSIMESNHSQATQGLFFTVLLGVYFTMLQMYE---YWEASFTIADAVYGSTFFVATGFHGLH 209
Cdd:TIGR02897  56 LIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCH 135

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1824665764 210 VIIGTLFLFTCFIRHLMNQFSPSHHFGFEAAAWYWHFVDVVWLFLYLSIYWWG 262
Cdd:TIGR02897 136 VTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
 
Name Accession Description Interval E-value
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 5-259 2.31e-154

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 429.99  E-value: 2.31e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764   5 NSNHPFHMVDYSPWPLVGSIGTMVMLMGLAKWFHMYNINLLMIGMMITILTMIQWWRDVIRESTFQGLHTKLVSMGMRWG 84
Cdd:MTH00155    1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764  85 MILFIVSEVLFFISFFWAFFNSSLSPTIELGMMWPPMGIQSFNPMHIPLLNTAILLASGVTVTWAHHSIMESNHSQATQG 164
Cdd:MTH00155   81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764 165 LFFTVLLGVYFTMLQMYEYWEASFTIADAVYGSTFFVATGFHGLHVIIGTLFLFTCFIRHLMNQFSPSHHFGFEAAAWYW 244
Cdd:MTH00155  161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240

                         250
                  ....*....|....*
gi 1824665764 245 HFVDVVWLFLYLSIY 259
Cdd:MTH00155  241 HFVDVVWLFLYISIY 255
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 4-263 1.48e-137

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 387.77  E-value: 1.48e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764   4 NNSNHPFHMVDYSPWPLVGSIGTMVMLMGLAKWFHMYNINLLMIGMMITILTMIQWWRDVIRESTFQGLHTKLVSMGMRW 83
Cdd:MTH00118    2 THQAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764  84 GMILFIVSEVLFFISFFWAFFNSSLSPTIELGMMWPPMGIQSFNPMHIPLLNTAILLASGVTVTWAHHSIMESNHSQATQ 163
Cdd:MTH00118   82 GMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764 164 GLFFTVLLGVYFTMLQMYEYWEASFTIADAVYGSTFFVATGFHGLHVIIGTLFLFTCFIRHLMNQFSPSHHFGFEAAAWY 243
Cdd:MTH00118  162 ALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWY 241

                         250       260
                  ....*....|....*....|
gi 1824665764 244 WHFVDVVWLFLYLSIYWWGS 263
Cdd:MTH00118  242 WHFVDVVWLFLYISIYWWGS 261
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 8-263 1.21e-134

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 380.09  E-value: 1.21e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764   8 HPFHMVDYSPWPLVGSIGTMVMLMGLAKWFHMYNINLLMIGMMITILTMIQWWRDVIRESTFQGLHTKLVSMGMRWGMIL 87
Cdd:MTH00189    5 HPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRYGMIL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764  88 FIVSEVLFFISFFWAFFNSSLSPTIELGMMWPPMGIQSFNPMHIPLLNTAILLASGVTVTWAHHSIMESNHSQATQGLFF 167
Cdd:MTH00189   85 FITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQALTL 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764 168 TVLLGVYFTMLQMYEYWEASFTIADAVYGSTFFVATGFHGLHVIIGTLFLFTCFIRHLMNQFSPSHHFGFEAAAWYWHFV 247
Cdd:MTH00189  165 TVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWYWHFV 244

                         250
                  ....*....|....*.
gi 1824665764 248 DVVWLFLYLSIYWWGS 263
Cdd:MTH00189  245 DVVWLFLYVSIYWWGS 260
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 8-263 1.58e-131

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 372.30  E-value: 1.58e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764   8 HPFHMVDYSPWPLVGSIGTMVMLMGLAKWFHMYNINLLMIGMMITILTMIQWWRDVIRESTFQGLHTKLVSMGMRWGMIL 87
Cdd:MTH00141    4 NPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFIL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764  88 FIVSEVLFFISFFWAFFNSSLSPTIELGMMWPPMGIQSFNPMHIPLLNTAILLASGVTVTWAHHSIMESNHSQATQGLFF 167
Cdd:MTH00141   84 FIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764 168 TVLLGVYFTMLQMYEYWEASFTIADAVYGSTFFVATGFHGLHVIIGTLFLFTCFIRHLMNQFSPSHHFGFEAAAWYWHFV 247
Cdd:MTH00141  164 TIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFV 243

                         250
                  ....*....|....*.
gi 1824665764 248 DVVWLFLYLSIYWWGS 263
Cdd:MTH00141  244 DVVWLFLYLSIYWWGS 259
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 8-263 3.32e-130

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 369.06  E-value: 3.32e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764   8 HPFHMVDYSPWPLVGSIGTMVMLMGLAKWFHMYNINLLMIGMMITILTMIQWWRDVIRESTFQGLHTKLVSMGMRWGMIL 87
Cdd:MTH00039    5 HPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRYGMIL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764  88 FIVSEVLFFISFFWAFFNSSLSPTIELGMMWPPMGIQSFNPMHIPLLNTAILLASGVTVTWAHHSIMESNHSQATQGLFF 167
Cdd:MTH00039   85 FITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQALFL 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764 168 TVLLGVYFTMLQMYEYWEASFTIADAVYGSTFFVATGFHGLHVIIGTLFLFTCFIRHLMNQFSPSHHFGFEAAAWYWHFV 247
Cdd:MTH00039  165 TVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWYWHFV 244

                         250
                  ....*....|....*.
gi 1824665764 248 DVVWLFLYLSIYWWGS 263
Cdd:MTH00039  245 DVVWLFLYVCIYWWGS 260
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 8-263 2.79e-128

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 364.11  E-value: 2.79e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764   8 HPFHMVDYSPWPLVGSIGTMVMLMGLAKWFHMYNINLLMIGMMITILTMIQWWRDVIRESTFQGLHTKLVSMGMRWGMIL 87
Cdd:MTH00219    7 NPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLRIGMIL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764  88 FIVSEVLFFISFFWAFFNSSLSPTIELGMMWPPMGIQSFNPMHIPLLNTAILLASGVTVTWAHHSIMESNHSQATQGLFF 167
Cdd:MTH00219   87 FIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQQGLLF 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764 168 TVLLGVYFTMLQMYEYWEASFTIADAVYGSTFFVATGFHGLHVIIGTLFLFTCFIRHLMNQFSPSHHFGFEAAAWYWHFV 247
Cdd:MTH00219  167 TILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAAWYWHFV 246

                         250
                  ....*....|....*.
gi 1824665764 248 DVVWLFLYLSIYWWGS 263
Cdd:MTH00219  247 DVVWLFLYVSIYWWGS 262
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 8-263 5.99e-124

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 353.30  E-value: 5.99e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764   8 HPFHMVDYSPWPLVGSIGTMVMLMGLAKWFHMYNINLLMIGMMITILTMIQWWRDVIRESTFQGLHTKLVSMGMRWGMIL 87
Cdd:MTH00130    6 HAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRYGMIL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764  88 FIVSEVLFFISFFWAFFNSSLSPTIELGMMWPPMGIQSFNPMHIPLLNTAILLASGVTVTWAHHSIMESNHSQATQGLFF 167
Cdd:MTH00130   86 FITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQSLTL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764 168 TVLLGVYFTMLQMYEYWEASFTIADAVYGSTFFVATGFHGLHVIIGTLFLFTCFIRHLMNQFSPSHHFGFEAAAWYWHFV 247
Cdd:MTH00130  166 TILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWYWHFV 245

                         250
                  ....*....|....*.
gi 1824665764 248 DVVWLFLYLSIYWWGS 263
Cdd:MTH00130  246 DVVWLFLYISIYWWGS 261
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 8-263 7.39e-124

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 352.90  E-value: 7.39e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764   8 HPFHMVDYSPWPLVGSIGTMVMLMGLAKWFHMYNINLLMIGMMITILTMIQWWRDVIRESTFQGLHTKLVSMGMRWGMIL 87
Cdd:MTH00075    6 HAFHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRYGMIL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764  88 FIVSEVLFFISFFWAFFNSSLSPTIELGMMWPPMGIQSFNPMHIPLLNTAILLASGVTVTWAHHSIMESNHSQATQGLFF 167
Cdd:MTH00075   86 FITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQSLAL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764 168 TVLLGVYFTMLQMYEYWEASFTIADAVYGSTFFVATGFHGLHVIIGTLFLFTCFIRHLMNQFSPSHHFGFEAAAWYWHFV 247
Cdd:MTH00075  166 TIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWYWHFV 245

                         250
                  ....*....|....*.
gi 1824665764 248 DVVWLFLYLSIYWWGS 263
Cdd:MTH00075  246 DVVWLFLYVSIYWWGS 261
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 8-263 2.19e-123

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 351.72  E-value: 2.19e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764   8 HPFHMVDYSPWPLVGSIGTMVMLMGLAKWFHMYNINLLMIGMMITILTMIQWWRDVIRESTFQGLHTKLVSMGMRWGMIL 87
Cdd:MTH00099    6 HAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRYGMIL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764  88 FIVSEVLFFISFFWAFFNSSLSPTIELGMMWPPMGIQSFNPMHIPLLNTAILLASGVTVTWAHHSIMESNHSQATQGLFF 167
Cdd:MTH00099   86 FIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQALFI 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764 168 TVLLGVYFTMLQMYEYWEASFTIADAVYGSTFFVATGFHGLHVIIGTLFLFTCFIRHLMNQFSPSHHFGFEAAAWYWHFV 247
Cdd:MTH00099  166 TILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWYWHFV 245

                         250
                  ....*....|....*.
gi 1824665764 248 DVVWLFLYLSIYWWGS 263
Cdd:MTH00099  246 DVVWLFLYVSIYWWGS 261
COX3 pfam00510
Cytochrome c oxidase subunit III;
8-263 6.85e-121

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 345.16  E-value: 6.85e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764   8 HPFHMVDYSPWPLVGSIGTMVMLMGLAKWFHMY--NINLLMIGMMITILTMIQWWRDVIRESTFQGLHTKLVSMGMRWGM 85
Cdd:pfam00510   1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYsgNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764  86 ILFIVSEVLFFISFFWAFFNSSLSPTIELGMMWPPMGIQSFNPMHIPLLNTAILLASGVTVTWAHHSIMESNHSQATQGL 165
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764 166 FFTVLLGVYFTMLQMYEYWEASFTIADAVYGSTFFVATGFHGLHVIIGTLFLFTCFIRHLMNQFSPSHHFGFEAAAWYWH 245
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240

                         250
                  ....*....|....*...
gi 1824665764 246 FVDVVWLFLYLSIYWWGS 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 9.12e-119

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: 339.49  E-value: 9.12e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764  20 LVGSIGTMVMLMGLAKWFHMY-NINLLMIGMMITILTMIQWWRDVIRESTFQGLHTKLVSMGMRWGMILFIVSEVLFFIS 98
Cdd:cd01665     1 ILGSFGLLLLALGLVLWMHGYgGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764  99 FFWAFFNSSLSPTIELGMMWPPMGIQSFNPMHIPLLNTAILLASGVTVTWAHHSIMESNHSQATQGLFFTVLLGVYFTML 178
Cdd:cd01665    81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764 179 QMYEYWEASFTIADAVYGSTFFVATGFHGLHVIIGTLFLFTCFIRHLMNQFSPSHHFGFEAAAWYWHFVDVVWLFLYLSI 258
Cdd:cd01665   161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240


                  ...
gi 1824665764 259 YWW 261
Cdd:cd01665   241 YWW 243
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 8-263 7.72e-117

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 335.27  E-value: 7.72e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764   8 HPFHMVDYSPWPLVGSIGTMVMLMGLAKWFHMYNINLLMIGMMITILTMIQWWRDVIRESTFQGLHTKLVSMGMRWGMIL 87
Cdd:MTH00009    4 QPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMIL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764  88 FIVSEVLFFISFFWAFFNSSLSPTIELGMMWPPMGIQSFNPMHIPLLNTAILLASGVTVTWAHHSIMESNHSQATQGLFF 167
Cdd:MTH00009   84 FIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALIL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764 168 TVLLGVYFTMLQMYEYWEASFTIADAVYGSTFFVATGFHGLHVIIGTLFLFTCFIRHLMNQFSPSHHFGFEAAAWYWHFV 247
Cdd:MTH00009  164 TVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFV 243

                         250
                  ....*....|....*.
gi 1824665764 248 DVVWLFLYLSIYWWGS 263
Cdd:MTH00009  244 DVVWIFLYLCIYWWGS 259
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 8-263 6.08e-114

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 327.87  E-value: 6.08e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764   8 HPFHMVDYSPWPLVGSIGTMVMLMGLAKWFHMYNINLLMIGMMITILTMIQWWRDVIRESTFQGLHTKLVSMGMRWGMIL 87
Cdd:MTH00024    6 HPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGMLL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764  88 FIVSEVLFFISFFWAFFNSSLSPTIELGMMWPPMGIQSFNPMHIPLLNTAILLASGVTVTWAHHSIMESNHSQATQGLFF 167
Cdd:MTH00024   86 FILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764 168 TVLLGVYFTMLQMYEYWEASFTIADAVYGSTFFVATGFHGLHVIIGTLFLFTCFIRHLMNQFSPSHHFGFEAAAWYWHFV 247
Cdd:MTH00024  166 TVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASWYWHFV 245

                         250
                  ....*....|....*.
gi 1824665764 248 DVVWLFLYLSIYWWGS 263
Cdd:MTH00024  246 DVVWLFLYLCIYWWGS 261
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 8-263 1.58e-104

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 304.02  E-value: 1.58e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764   8 HPFHMVDYSPWPLVGSIGTMVMLMGLAKWFHMYNINLLMIGMMITILTMIQWWRDVIRESTFQGLHTKLVSMGMRWGMIL 87
Cdd:MTH00052    7 HPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGLKYGMIL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764  88 FIVSEVLFFISFFWAFFNSSLSPTIELGMMWPPMGIQSFNPMHIPLLNTAILLASGVTVTWAHHSIMESNHSQATQGLFF 167
Cdd:MTH00052   87 FIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEAIIGLAL 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764 168 TVLLGVYFTMLQMYEYWEASFTIADAVYGSTFFVATGFHGLHVIIGTLFLFTCFIRHLMNQFSPSHHFGFEAAAWYWHFV 247
Cdd:MTH00052  167 TVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAAWYWHFV 246

                         250
                  ....*....|....*.
gi 1824665764 248 DVVWLFLYLSIYWWGS 263
Cdd:MTH00052  247 DVVWLFLFIFMYWWGS 262
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 8-263 2.12e-94

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 279.64  E-value: 2.12e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764   8 HPFHMVDYSPWPLVGSIGTMVMLMGLAKWFHMYNINLLMIGMMITILTMIQWWRDVIRESTFQGLHTKLVSMGMRWGMIL 87
Cdd:MTH00028    6 HPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764  88 FIVSEVLFFISFFWAFFNSSLSPTIELGMMWPPMGIQSFNPMHIPLLNTAILLASGVTVTWAHHSIMESNH--------- 158
Cdd:MTH00028   86 FILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTGNpaslekgtq 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764 159 ---------------------------SQATQGLFFTVLLGVYFTMLQMYEYWEASFTIADAVYGSTFFVATGFHGLHVI 211
Cdd:MTH00028  166 giegpnpsngappdpqkgptfllsdfrTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVL 245

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1824665764 212 IGTLFLFTCFIRHLMNQFSPSHHFGFEAAAWYWHFVDVVWLFLYLSIYWWGS 263
Cdd:MTH00028  246 VGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWGS 297
PLN02194 PLN02194
cytochrome-c oxidase
 2-262 2.73e-83

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 250.35  E-value: 2.73e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764   2 LTNNSNHPFHMVDYSPWPLVGSIGTMVMLMGLAKWFHMYN--INLLMIGMMITILTMIQWWRDVIRESTFQGLHTKLVSM 79
Cdd:PLN02194    1 MIESQRHSYHLVDPSPWPISGSLGALATTVGGVMYMHPFQggARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764  80 GMRWGMILFIVSEVLFFISFFWAFFNSSLSPTIELGMMWPPMGIQSFNPMHIPLLNTAILLASGVTVTWAHHSIMESNHS 159
Cdd:PLN02194   81 GPRYGSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764 160 QATQGLFFTVLLGVYFTMLQMYEYWEASFTIADAVYGSTFFVATGFHGLHVIIGTLFLFTCFIRHLMNQFSPSHHFGFEA 239
Cdd:PLN02194  161 RAVYALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEA 240

                         250       260
                  ....*....|....*....|...
gi 1824665764 240 AAWYWHFVDVVWLFLYLSIYWWG 262
Cdd:PLN02194  241 AAWYWHFVDVVWLFLFVSIYWWG 263
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
 8-263 2.21e-63

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 199.03  E-value: 2.21e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764   8 HPFHMVDYSPWPLVGSIGTMVMLMGLAKWFHMYNINLLMIGMMITILTMIQWWRDVIREStFQGLHTKLVSMGMRWGMIL 87
Cdd:MTH00083    3 HNFHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMIL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764  88 FIVSEVLFFISFFWAFFNSSLSPTIELGMMWPPMGIQSFNPMHIPLLNTAILLASGVTVTWAHHSIMESNhSQATQGLFF 167
Cdd:MTH00083   82 FIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSN-KSCTNSLLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764 168 TVLLGVYFTMLQMYEYWEASFTIADAVYGSTFFVATGFHGLHVIIGTLFLFTCFIRHLMNQFSPSHHFGFEAAAWYWHFV 247
Cdd:MTH00083  161 TCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFV 240

                         250
                  ....*....|....*.
gi 1824665764 248 DVVWLFLYLSIYWWGS 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 3.65e-60

Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. This group additionally contains proteins which are fusions between subunits I and III, such as Sulfolobus acidocaldarius SoxM, a subunit of the SoxM terminal oxidase complex. It also includes NorE which has been speculated to be a subunit of nitric oxide reductase. Some archaebacterial cytochrome oxidases lack subunit III. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria.


Pssm-ID: 238227  Cd Length: 183  Bit Score: 188.18  E-value: 3.65e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764  73 HTKLVSMGMRWGMILFIVSEVLFFISFFWAFFNSSLSPTIELGMmwppmgiqSFNPMHIPLLNTAILLASGVTVTWAHHS 152
Cdd:cd00386     1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFGA--------GLDPLDLPLLNTNTLLLSGSSVTWAHAS 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764 153 IM--ESNHSQATQGLFFTVLLGVYFTMLQMYEYWEASFTIADAVYGSTFFVATGFHGLHVIIGTLFLFTCFIRHLMNQFS 230
Cdd:cd00386    73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1824665764 231 PSHHFGFEAAAWYWHFVDVVWLFLYLSIYWW 261
Cdd:cd00386   153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
72-261 4.10e-46

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 152.70  E-value: 4.10e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764  72 LHTKLVSMGMRWGMILFIVSEVLFFISFFWAFFNSSLSPTielgmmWPPMGIQSFNPmHIPLLNTAILLASGVTVTWAHH 151
Cdd:COG1845     7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRASAP------DWPAGAELLDL-PLPLINTLLLLLSSFTVALAVR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764 152 SIMESNHSQATQGLFFTVLLGVYFTMLQMYEY---WEASFTIADAVYGSTFFVATGFHGLHVIIGTLFLFTCFIRHLMNQ 228
Cdd:COG1845    80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1824665764 229 FSPSHHFGFEAAAWYWHFVDVVWLFLYLSIYWW 261
Cdd:COG1845   160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
NorE_like cd02862
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ...
 133-259 1.56e-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: 86.13  E-value: 1.56e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764 133 LLNTAILLASGVTVTWAHHSIMESNHSQATQGLFFTVLLGVYFTMLQMYEYWE---ASFTIADAVYGSTFFVATGFHGLH 209
Cdd:cd02862    55 ALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYAHkiaAGIDPDAGLFFTLYFLLTGFHLLH 134

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1824665764 210 VIIGTLFLFTCFIRHLMNQFSPSHHFGFEAAAWYWHFVDVVWLFLYLSIY 259
Cdd:cd02862   135 VLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVLFPLLY 184
Heme_Cu_Oxidase_III_2 cd02865
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 132-261 6.63e-16

Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria.


Pssm-ID: 239216  Cd Length: 184  Bit Score: 73.56  E-value: 6.63e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764 132 PLLNTAILLASGVTVTWAHHSIMESNHSQATQGLFFTVLLGVYFTMLQMYEYWEASF---TIADAVYGSTFFVATGFHGL 208
Cdd:cd02865    52 LSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWHALNDagyGPTSNPAGSFFYLLTGLHGL 131

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1824665764 209 HVIIGTLFLFTCFIRHLMNQFSPSHHFGFEAAAWYWHFVDVVWLFLYLSIYWW 261
Cdd:cd02865   132 HVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVLLALLYGT 184
Ubiquinol_oxidase_III cd02863
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ...
 133-259 8.16e-15

Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the respiratory chains of aerobic bacteria, is a multi-chain transmembrane protein located in the cell membrane. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. Ubiquinol oxidases feature four subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of bovine CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in bovine CcO. Although not required for catalytic activity, subunit III appears to be involved in assembly of the multimer complex.


Pssm-ID: 239214  Cd Length: 186  Bit Score: 70.73  E-value: 8.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764 133 LLNTAILLASGVTVTWAHHSIMESNHSQATQGLFFTVLLGVYFTMLQMYE---YWEASFTIADAVYGSTFFVATGFHGLH 209
Cdd:cd02863    54 FIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLVGTHGLH 133

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1824665764 210 VIIGTLFLFTCFIRHLMNQFSPSHHFGFEAAAWYWHFVDVVWLFLYLSIY 259
Cdd:cd02863   134 VTFGLIWILVMIIQLKKRGLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
COX3 MTH00049
cytochrome c oxidase subunit III; Validated
 131-259 1.72e-14

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177124  Cd Length: 215  Bit Score: 70.33  E-value: 1.72e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764 131 IPLLNTAILLASGVTVTWAHHSI-MESNHSQatqgLFFTVLLGVYFTMLQMYEYWEASFTIADAVYGSTFFVATGFHGLH 209
Cdd:MTH00049   92 IPFVGCFLLLGSSITVTAYHHLLgWKYCDLF----LYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHFSH 167

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1824665764 210 VIIGTLFLFTCFIRHLMNqFSPSHHfgfEAAAWYWHFVDVVWLFLYLSIY 259
Cdd:MTH00049  168 VVLGVVGLSTLLLVGSSS-FGVYRS---TVLTWYWHFVDYIWLLVYLIVY 213
Heme_Cu_Oxidase_III_1 cd02864
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 84-261 7.47e-13

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: 65.60  E-value: 7.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764  84 GMILFIVSEVLFFISFFWAFFNSSLSPTIELGMMWPPMGIQSFN---PMHIPLLNTAILLASGVTVTWAHHSIMESNHSQ 160
Cdd:cd02864    12 MMWFFLLSDAFIFSSFLIAYMTARISTTEPWPLPSDVFALRIGHfniPLVLIAIMTFILITSSGTMAMAVNFGYRGNRKA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764 161 ATQGLFFTVLLGVYFTMLQMYEYWE---------ASFTIADAVYGSTFFVATGFHGLHVIIGTLFLFTCFIRHLMNQFSP 231
Cdd:cd02864    92 AARLMLATALLGATFVGMQAFEWTKliveegvrpWGNPWGAAQFGASFFMITGFHGTHVTIGVIYLIIIARKVWRGKYQR 171

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1824665764 232 SHHF-GFEAAAWYWHFVDVVWLFLYLSIYWW 261
Cdd:cd02864   172 IGRYeIVEIAGLYWHFVDLVWVFIFAFFYLW 202
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 133-262 1.41e-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: 59.10  E-value: 1.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764 133 LLNTAILLASGVTVTWAHHSIMESNHSQATQGLFFTVLLGVYFTMLQMYE---YWEASFTIADAVYGSTFFVATGFHGLH 209
Cdd:TIGR02897  56 LIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCH 135

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1824665764 210 VIIGTLFLFTCFIRHLMNQFSPSHHFGFEAAAWYWHFVDVVWLFLYLSIYWWG 262
Cdd:TIGR02897 136 VTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
PRK10663 PRK10663
cytochrome o ubiquinol oxidase subunit III; Provisional
 133-263 3.28e-07

cytochrome o ubiquinol oxidase subunit III; Provisional


Pssm-ID: 182628  Cd Length: 204  Bit Score: 49.39  E-value: 3.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665764 133 LLNTAILLASGVTVTWAHHSIMESNHSQATQGLFFTVLLGVYFTMLQMYEYW---EASFTIADAVYGSTFFVATGFHGLH 209
Cdd:PRK10663   70 LVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFHhliVEGMGPDRSGFLSAFFALVGTHGLH 149

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1824665764 210 VIIGTLFLFTCFIRHLMNQFSPSHHFGFEAAAWYWHFVDVVWLFLYLSIYWWGS 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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