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Conserved domains on  [gi|2091526573|ref|YP_010164365|]
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cytochrome c oxidase subunit III (mitochondrion) [Scyra compressipes]

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 3.35e-154

cytochrome c oxidase subunit III; Provisional


:

Pssm-ID: 214439  Cd Length: 255  Bit Score: 429.60  E-value: 3.35e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573   5 HGFHPYHLVNISPWPLTGSISAMMLTTGLVKWFHHYNFNLLALSLITTLLTMIQWWRDITREGTYQGSHTSVVKKGLRWG 84
Cdd:MTH00155    1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573  85 MILFIVSEILFFFSFFWAFFHSSLSPNIELGMFWPPQGIQPFNPFQIPLLNTTILLSSGVTVTWAHHAILESNYSQAIQG 164
Cdd:MTH00155   81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573 165 LGLTIILGVYFSMLQAFEYIEASFTIADSVFGSSFFVATGFHGLHVIIGTSFLFVCFMRLYSCHFSSNHHVGFEAAAWYW 244
Cdd:MTH00155  161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240

                         250
                  ....*....|....*
gi 2091526573 245 HFVDVVWLFLYVFIY 259
Cdd:MTH00155  241 HFVDVVWLFLYISIY 255
 
Name Accession Description Interval E-value
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 5-259 3.35e-154

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 429.60  E-value: 3.35e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573   5 HGFHPYHLVNISPWPLTGSISAMMLTTGLVKWFHHYNFNLLALSLITTLLTMIQWWRDITREGTYQGSHTSVVKKGLRWG 84
Cdd:MTH00155    1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573  85 MILFIVSEILFFFSFFWAFFHSSLSPNIELGMFWPPQGIQPFNPFQIPLLNTTILLSSGVTVTWAHHAILESNYSQAIQG 164
Cdd:MTH00155   81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573 165 LGLTIILGVYFSMLQAFEYIEASFTIADSVFGSSFFVATGFHGLHVIIGTSFLFVCFMRLYSCHFSSNHHVGFEAAAWYW 244
Cdd:MTH00155  161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240

                         250
                  ....*....|....*
gi 2091526573 245 HFVDVVWLFLYVFIY 259
Cdd:MTH00155  241 HFVDVVWLFLYISIY 255
COX3 pfam00510
Cytochrome c oxidase subunit III;
8-262 9.32e-119

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 339.77  E-value: 9.32e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573   8 HPYHLVNISPWPLTGSISAMMLTTGLVKWFHHY--NFNLLALSLITTLLTMIQWWRDITREGTYQGSHTSVVKKGLRWGM 85
Cdd:pfam00510   1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYsgNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573  86 ILFIVSEILFFFSFFWAFFHSSLSPNIELGMFWPPQGIQPFNPFQIPLLNTTILLSSGVTVTWAHHAILESNYSQAIQGL 165
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573 166 GLTIILGVYFSMLQAFEYIEASFTIADSVFGSSFFVATGFHGLHVIIGTSFLFVCFMRLYSCHFSSNHHVGFEAAAWYWH 245
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240

                         250
                  ....*....|....*..
gi 2091526573 246 FVDVVWLFLYVFIYWWG 262
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWG 257
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 20-261 2.16e-117

Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. CcO catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function, but subunit III, which is also conserved, is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit III contains bound phospholipids in several crystal structures and is proposed to contain a "lipid pool." These phospholipids are believed to intrinsic constituents similar to cofactors of the enzyme.


Pssm-ID: 238834  Cd Length: 243  Bit Score: 335.64  E-value: 2.16e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573  20 LTGSISAMMLTTGLVKWFHHY-NFNLLALSLITTLLTMIQWWRDITREGTYQGSHTSVVKKGLRWGMILFIVSEILFFFS 98
Cdd:cd01665     1 ILGSFGLLLLALGLVLWMHGYgGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573  99 FFWAFFHSSLSPNIELGMFWPPQGIQPFNPFQIPLLNTTILLSSGVTVTWAHHAILESNYSQAIQGLGLTIILGVYFSML 178
Cdd:cd01665    81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573 179 QAFEYIEASFTIADSVFGSSFFVATGFHGLHVIIGTSFLFVCFMRLYSCHFSSNHHVGFEAAAWYWHFVDVVWLFLYVFI 258
Cdd:cd01665   161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240


                  ...
gi 2091526573 259 YWW 261
Cdd:cd01665   241 YWW 243
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
73-261 8.47e-49

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 159.63  E-value: 8.47e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573  73 HTSVVKKGLRWGMILFIVSEILFFFSFFWAFFHSSLSpnielgMFWPPQGIQPFNPFqIPLLNTTILLSSGVTVTWAHHA 152
Cdd:COG1845     8 HAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS------APDWPAGAELLDLP-LPLINTLLLLLSSFTVALAVRA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573 153 ILESNYSQAIQGLGLTIILGVYFSMLQAFEY---IEASFTIADSVFGSSFFVATGFHGLHVIIGTSFLFVCFMRLYSCHF 229
Cdd:COG1845    81 ARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGF 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2091526573 230 SSNHHVGFEAAAWYWHFVDVVWLFLYVFIYWW 261
Cdd:COG1845   161 TPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 122-262 8.75e-08

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: 51.01  E-value: 8.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573 122 GIQPFNPFQIPLL--NTTILLSSGVTVTWAHHAILESNYSQAIQGLGLTIILGVYFSMLQAFE---YIEASFTIADSVFG 196
Cdd:TIGR02897  43 GKMPAELFELPLVliMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYW 122

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2091526573 197 SSFFVATGFHGLHVIIGTSFLFVCFMRLYSCHFSSNHHVGFEAAAWYWHFVDVVWLFLYVFIYWWG 262
Cdd:TIGR02897 123 SSFFVLLGTHGCHVTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
 
Name Accession Description Interval E-value
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 5-259 3.35e-154

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 429.60  E-value: 3.35e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573   5 HGFHPYHLVNISPWPLTGSISAMMLTTGLVKWFHHYNFNLLALSLITTLLTMIQWWRDITREGTYQGSHTSVVKKGLRWG 84
Cdd:MTH00155    1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573  85 MILFIVSEILFFFSFFWAFFHSSLSPNIELGMFWPPQGIQPFNPFQIPLLNTTILLSSGVTVTWAHHAILESNYSQAIQG 164
Cdd:MTH00155   81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573 165 LGLTIILGVYFSMLQAFEYIEASFTIADSVFGSSFFVATGFHGLHVIIGTSFLFVCFMRLYSCHFSSNHHVGFEAAAWYW 244
Cdd:MTH00155  161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240

                         250
                  ....*....|....*
gi 2091526573 245 HFVDVVWLFLYVFIY 259
Cdd:MTH00155  241 HFVDVVWLFLYISIY 255
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 4-262 1.15e-137

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 387.77  E-value: 1.15e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573   4 SHGFHPYHLVNISPWPLTGSISAMMLTTGLVKWFHHYNFNLLALSLITTLLTMIQWWRDITREGTYQGSHTSVVKKGLRW 83
Cdd:MTH00118    2 THQAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573  84 GMILFIVSEILFFFSFFWAFFHSSLSPNIELGMFWPPQGIQPFNPFQIPLLNTTILLSSGVTVTWAHHAILESNYSQAIQ 163
Cdd:MTH00118   82 GMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573 164 GLGLTIILGVYFSMLQAFEYIEASFTIADSVFGSSFFVATGFHGLHVIIGTSFLFVCFMRLYSCHFSSNHHVGFEAAAWY 243
Cdd:MTH00118  162 ALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWY 241

                         250
                  ....*....|....*....
gi 2091526573 244 WHFVDVVWLFLYVFIYWWG 262
Cdd:MTH00118  242 WHFVDVVWLFLYISIYWWG 260
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 5-262 1.38e-131

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 372.38  E-value: 1.38e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573   5 HGFHPYHLVNISPWPLTGSISAMMLTTGLVKWFHHYNFNLLALSLITTLLTMIQWWRDITREGTYQGSHTSVVKKGLRWG 84
Cdd:MTH00189    2 HQAHPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRYG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573  85 MILFIVSEILFFFSFFWAFFHSSLSPNIELGMFWPPQGIQPFNPFQIPLLNTTILLSSGVTVTWAHHAILESNYSQAIQG 164
Cdd:MTH00189   82 MILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573 165 LGLTIILGVYFSMLQAFEYIEASFTIADSVFGSSFFVATGFHGLHVIIGTSFLFVCFMRLYSCHFSSNHHVGFEAAAWYW 244
Cdd:MTH00189  162 LTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWYW 241

                         250
                  ....*....|....*...
gi 2091526573 245 HFVDVVWLFLYVFIYWWG 262
Cdd:MTH00189  242 HFVDVVWLFLYVSIYWWG 259
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 8-263 3.96e-130

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 368.67  E-value: 3.96e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573   8 HPYHLVNISPWPLTGSISAMMLTTGLVKWFHHYNFNLLALSLITTLLTMIQWWRDITREGTYQGSHTSVVKKGLRWGMIL 87
Cdd:MTH00039    5 HPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRYGMIL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573  88 FIVSEILFFFSFFWAFFHSSLSPNIELGMFWPPQGIQPFNPFQIPLLNTTILLSSGVTVTWAHHAILESNYSQAIQGLGL 167
Cdd:MTH00039   85 FITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQALFL 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573 168 TIILGVYFSMLQAFEYIEASFTIADSVFGSSFFVATGFHGLHVIIGTSFLFVCFMRLYSCHFSSNHHVGFEAAAWYWHFV 247
Cdd:MTH00039  165 TVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWYWHFV 244

                         250
                  ....*....|....*.
gi 2091526573 248 DVVWLFLYVFIYWWGG 263
Cdd:MTH00039  245 DVVWLFLYVCIYWWGS 260
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 8-263 1.68e-129

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 367.29  E-value: 1.68e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573   8 HPYHLVNISPWPLTGSISAMMLTTGLVKWFHHYNFNLLALSLITTLLTMIQWWRDITREGTYQGSHTSVVKKGLRWGMIL 87
Cdd:MTH00141    4 NPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFIL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573  88 FIVSEILFFFSFFWAFFHSSLSPNIELGMFWPPQGIQPFNPFQIPLLNTTILLSSGVTVTWAHHAILESNYSQAIQGLGL 167
Cdd:MTH00141   84 FIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573 168 TIILGVYFSMLQAFEYIEASFTIADSVFGSSFFVATGFHGLHVIIGTSFLFVCFMRLYSCHFSSNHHVGFEAAAWYWHFV 247
Cdd:MTH00141  164 TIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFV 243

                         250
                  ....*....|....*.
gi 2091526573 248 DVVWLFLYVFIYWWGG 263
Cdd:MTH00141  244 DVVWLFLYLSIYWWGS 259
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 4-262 3.27e-125

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 356.34  E-value: 3.27e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573   4 SHGFHPYHLVNISPWPLTGSISAMMLTTGLVKWFHHYNFNLLALSLITTLLTMIQWWRDITREGTYQGSHTSVVKKGLRW 83
Cdd:MTH00099    2 THQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573  84 GMILFIVSEILFFFSFFWAFFHSSLSPNIELGMFWPPQGIQPFNPFQIPLLNTTILLSSGVTVTWAHHAILESNYSQAIQ 163
Cdd:MTH00099   82 GMILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573 164 GLGLTIILGVYFSMLQAFEYIEASFTIADSVFGSSFFVATGFHGLHVIIGTSFLFVCFMRLYSCHFSSNHHVGFEAAAWY 243
Cdd:MTH00099  162 ALFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWY 241

                         250
                  ....*....|....*....
gi 2091526573 244 WHFVDVVWLFLYVFIYWWG 262
Cdd:MTH00099  242 WHFVDVVWLFLYVSIYWWG 260
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 8-262 5.44e-125

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 356.02  E-value: 5.44e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573   8 HPYHLVNISPWPLTGSISAMMLTTGLVKWFHHYNFNLLALSLITTLLTMIQWWRDITREGTYQGSHTSVVKKGLRWGMIL 87
Cdd:MTH00219    7 NPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLRIGMIL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573  88 FIVSEILFFFSFFWAFFHSSLSPNIELGMFWPPQGIQPFNPFQIPLLNTTILLSSGVTVTWAHHAILESNYSQAIQGLGL 167
Cdd:MTH00219   87 FIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQQGLLF 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573 168 TIILGVYFSMLQAFEYIEASFTIADSVFGSSFFVATGFHGLHVIIGTSFLFVCFMRLYSCHFSSNHHVGFEAAAWYWHFV 247
Cdd:MTH00219  167 TILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAAWYWHFV 246

                         250
                  ....*....|....*
gi 2091526573 248 DVVWLFLYVFIYWWG 262
Cdd:MTH00219  247 DVVWLFLYVSIYWWG 261
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 4-262 9.98e-123

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 350.22  E-value: 9.98e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573   4 SHGFHPYHLVNISPWPLTGSISAMMLTTGLVKWFHHYNFNLLALSLITTLLTMIQWWRDITREGTYQGSHTSVVKKGLRW 83
Cdd:MTH00130    2 AHQAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573  84 GMILFIVSEILFFFSFFWAFFHSSLSPNIELGMFWPPQGIQPFNPFQIPLLNTTILLSSGVTVTWAHHAILESNYSQAIQ 163
Cdd:MTH00130   82 GMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573 164 GLGLTIILGVYFSMLQAFEYIEASFTIADSVFGSSFFVATGFHGLHVIIGTSFLFVCFMRLYSCHFSSNHHVGFEAAAWY 243
Cdd:MTH00130  162 SLTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWY 241

                         250
                  ....*....|....*....
gi 2091526573 244 WHFVDVVWLFLYVFIYWWG 262
Cdd:MTH00130  242 WHFVDVVWLFLYISIYWWG 260
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 4-262 3.76e-122

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 348.66  E-value: 3.76e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573   4 SHGFHPYHLVNISPWPLTGSISAMMLTTGLVKWFHHYNFNLLALSLITTLLTMIQWWRDITREGTYQGSHTSVVKKGLRW 83
Cdd:MTH00075    2 AHQAHAFHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573  84 GMILFIVSEILFFFSFFWAFFHSSLSPNIELGMFWPPQGIQPFNPFQIPLLNTTILLSSGVTVTWAHHAILESNYSQAIQ 163
Cdd:MTH00075   82 GMILFITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573 164 GLGLTIILGVYFSMLQAFEYIEASFTIADSVFGSSFFVATGFHGLHVIIGTSFLFVCFMRLYSCHFSSNHHVGFEAAAWY 243
Cdd:MTH00075  162 SLALTIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWY 241

                         250
                  ....*....|....*....
gi 2091526573 244 WHFVDVVWLFLYVFIYWWG 262
Cdd:MTH00075  242 WHFVDVVWLFLYVSIYWWG 260
COX3 pfam00510
Cytochrome c oxidase subunit III;
8-262 9.32e-119

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 339.77  E-value: 9.32e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573   8 HPYHLVNISPWPLTGSISAMMLTTGLVKWFHHY--NFNLLALSLITTLLTMIQWWRDITREGTYQGSHTSVVKKGLRWGM 85
Cdd:pfam00510   1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYsgNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573  86 ILFIVSEILFFFSFFWAFFHSSLSPNIELGMFWPPQGIQPFNPFQIPLLNTTILLSSGVTVTWAHHAILESNYSQAIQGL 165
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573 166 GLTIILGVYFSMLQAFEYIEASFTIADSVFGSSFFVATGFHGLHVIIGTSFLFVCFMRLYSCHFSSNHHVGFEAAAWYWH 245
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240

                         250
                  ....*....|....*..
gi 2091526573 246 FVDVVWLFLYVFIYWWG 262
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWG 257
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 20-261 2.16e-117

Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. CcO catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function, but subunit III, which is also conserved, is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit III contains bound phospholipids in several crystal structures and is proposed to contain a "lipid pool." These phospholipids are believed to intrinsic constituents similar to cofactors of the enzyme.


Pssm-ID: 238834  Cd Length: 243  Bit Score: 335.64  E-value: 2.16e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573  20 LTGSISAMMLTTGLVKWFHHY-NFNLLALSLITTLLTMIQWWRDITREGTYQGSHTSVVKKGLRWGMILFIVSEILFFFS 98
Cdd:cd01665     1 ILGSFGLLLLALGLVLWMHGYgGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573  99 FFWAFFHSSLSPNIELGMFWPPQGIQPFNPFQIPLLNTTILLSSGVTVTWAHHAILESNYSQAIQGLGLTIILGVYFSML 178
Cdd:cd01665    81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573 179 QAFEYIEASFTIADSVFGSSFFVATGFHGLHVIIGTSFLFVCFMRLYSCHFSSNHHVGFEAAAWYWHFVDVVWLFLYVFI 258
Cdd:cd01665   161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240


                  ...
gi 2091526573 259 YWW 261
Cdd:cd01665   241 YWW 243
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 7-262 1.69e-114

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 329.41  E-value: 1.69e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573   7 FHPYHLVNISPWPLTGSISAMMLTTGLVKWFHHYNFNLLALSLITTLLTMIQWWRDITREGTYQGSHTSVVKKGLRWGMI 86
Cdd:MTH00024    5 YHPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGML 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573  87 LFIVSEILFFFSFFWAFFHSSLSPNIELGMFWPPQGIQPFNPFQIPLLNTTILLSSGVTVTWAHHAILESNYSQAIQGLG 166
Cdd:MTH00024   85 LFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLF 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573 167 LTIILGVYFSMLQAFEYIEASFTIADSVFGSSFFVATGFHGLHVIIGTSFLFVCFMRLYSCHFSSNHHVGFEAAAWYWHF 246
Cdd:MTH00024  165 LTVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASWYWHF 244

                         250
                  ....*....|....*.
gi 2091526573 247 VDVVWLFLYVFIYWWG 262
Cdd:MTH00024  245 VDVVWLFLYLCIYWWG 260
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 8-262 1.04e-112

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 324.48  E-value: 1.04e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573   8 HPYHLVNISPWPLTGSISAMMLTTGLVKWFHHYNFNLLALSLITTLLTMIQWWRDITREGTYQGSHTSVVKKGLRWGMIL 87
Cdd:MTH00009    4 QPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMIL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573  88 FIVSEILFFFSFFWAFFHSSLSPNIELGMFWPPQGIQPFNPFQIPLLNTTILLSSGVTVTWAHHAILESNYSQAIQGLGL 167
Cdd:MTH00009   84 FIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALIL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573 168 TIILGVYFSMLQAFEYIEASFTIADSVFGSSFFVATGFHGLHVIIGTSFLFVCFMRLYSCHFSSNHHVGFEAAAWYWHFV 247
Cdd:MTH00009  164 TVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFV 243

                         250
                  ....*....|....*
gi 2091526573 248 DVVWLFLYVFIYWWG 262
Cdd:MTH00009  244 DVVWIFLYLCIYWWG 258
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 4-262 2.01e-109

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 316.35  E-value: 2.01e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573   4 SHGFHPYHLVNISPWPLTGSISAMMLTTGLVKWFHHYNFNLLALSLITTLLTMIQWWRDITREGTYQGSHTSVVKKGLRW 83
Cdd:MTH00052    3 QQYYHPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGLKY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573  84 GMILFIVSEILFFFSFFWAFFHSSLSPNIELGMFWPPQGIQPFNPFQIPLLNTTILLSSGVTVTWAHHAILESNYSQAIQ 163
Cdd:MTH00052   83 GMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEAII 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573 164 GLGLTIILGVYFSMLQAFEYIEASFTIADSVFGSSFFVATGFHGLHVIIGTSFLFVCFMRLYSCHFSSNHHVGFEAAAWY 243
Cdd:MTH00052  163 GLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAAWY 242

                         250
                  ....*....|....*....
gi 2091526573 244 WHFVDVVWLFLYVFIYWWG 262
Cdd:MTH00052  243 WHFVDVVWLFLFIFMYWWG 261
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 7-262 4.88e-97

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 286.19  E-value: 4.88e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573   7 FHPYHLVNISPWPLTGSISAMMLTTGLVKWFHHYNFNLLALSLITTLLTMIQWWRDITREGTYQGSHTSVVKKGLRWGMI 86
Cdd:MTH00028    5 YHPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGML 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573  87 LFIVSEILFFFSFFWAFFHSSLSPNIELGMFWPPQGIQPFNPFQIPLLNTTILLSSGVTVTWAHHAILESNY-------- 158
Cdd:MTH00028   85 LFILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTGNpaslekgt 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573 159 ----------------------------SQAIQGLGLTIILGVYFSMLQAFEYIEASFTIADSVFGSSFFVATGFHGLHV 210
Cdd:MTH00028  165 qgiegpnpsngappdpqkgptfllsdfrTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHV 244

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2091526573 211 IIGTSFLFVCFMRLYSCHFSSNHHVGFEAAAWYWHFVDVVWLFLYVFIYWWG 262
Cdd:MTH00028  245 LVGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWG 296
PLN02194 PLN02194
cytochrome-c oxidase
 8-263 1.78e-82

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 248.04  E-value: 1.78e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573   8 HPYHLVNISPWPLTGSISAMMLTTGLVKWFHHYN--FNLLALSLITTLLTMIQWWRDITREGTYQGSHTSVVKKGLRWGM 85
Cdd:PLN02194    7 HSYHLVDPSPWPISGSLGALATTVGGVMYMHPFQggARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGPRYGS 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573  86 ILFIVSEILFFFSFFWAFFHSSLSPNIELGMFWPPQGIQPFNPFQIPLLNTTILLSSGVTVTWAHHAILESNYSQAIQGL 165
Cdd:PLN02194   87 ILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEKRAVYAL 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573 166 GLTIILGVYFSMLQAFEYIEASFTIADSVFGSSFFVATGFHGLHVIIGTSFLFVCFMRLYSCHFSSNHHVGFEAAAWYWH 245
Cdd:PLN02194  167 VATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWYWH 246

                         250
                  ....*....|....*...
gi 2091526573 246 FVDVVWLFLYVFIYWWGG 263
Cdd:PLN02194  247 FVDVVWLFLFVSIYWWGG 264
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
 7-262 1.36e-67

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 209.81  E-value: 1.36e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573   7 FHPYHLVNISPWPLTGSISAMMLTTGLVKWFHHYNFNLLALSLITTLLTMIQWWRDITREGtYQGSHTSVVKKGLRWGMI 86
Cdd:MTH00083    2 FHNFHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573  87 LFIVSEILFFFSFFWAFFHSSLSPNIELGMFWPPQGIQPFNPFQIPLLNTTILLSSGVTVTWAHHAILESNySQAIQGLG 166
Cdd:MTH00083   81 LFIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSN-KSCTNSLL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573 167 LTIILGVYFSMLQAFEYIEASFTIADSVFGSSFFVATGFHGLHVIIGTSFLFVCFMRLYSCHFSSNHHVGFEAAAWYWHF 246
Cdd:MTH00083  160 LTCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHF 239

                         250
                  ....*....|....*.
gi 2091526573 247 VDVVWLFLYVFIYWWG 262
Cdd:MTH00083  240 VDVVWLFLFVFVYWWS 255
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 73-261 1.85e-62

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: 194.34  E-value: 1.85e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573  73 HTSVVKKGLRWGMILFIVSEILFFFSFFWAFFHSSLSPNIELGMfwppqgiqPFNPFQIPLLNTTILLSSGVTVTWAHHA 152
Cdd:cd00386     1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFGA--------GLDPLDLPLLNTNTLLLSGSSVTWAHAS 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573 153 IL--ESNYSQAIQGLGLTIILGVYFSMLQAFEYIEASFTIADSVFGSSFFVATGFHGLHVIIGTSFLFVCFMRLYSCHFS 230
Cdd:cd00386    73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2091526573 231 SNHHVGFEAAAWYWHFVDVVWLFLYVFIYWW 261
Cdd:cd00386   153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
73-261 8.47e-49

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 159.63  E-value: 8.47e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573  73 HTSVVKKGLRWGMILFIVSEILFFFSFFWAFFHSSLSpnielgMFWPPQGIQPFNPFqIPLLNTTILLSSGVTVTWAHHA 152
Cdd:COG1845     8 HAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS------APDWPAGAELLDLP-LPLINTLLLLLSSFTVALAVRA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573 153 ILESNYSQAIQGLGLTIILGVYFSMLQAFEY---IEASFTIADSVFGSSFFVATGFHGLHVIIGTSFLFVCFMRLYSCHF 229
Cdd:COG1845    81 ARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGF 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2091526573 230 SSNHHVGFEAAAWYWHFVDVVWLFLYVFIYWW 261
Cdd:COG1845   161 TPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
NorE_like cd02862
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ...
 133-259 1.01e-25

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: 99.62  E-value: 1.01e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573 133 LLNTTILLSSGVTVTWAHHAILESNYSQAIQGLGLTIILGVYFSMLQAFEY---IEASFTIADSVFGSSFFVATGFHGLH 209
Cdd:cd02862    55 ALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYahkIAAGIDPDAGLFFTLYFLLTGFHLLH 134

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2091526573 210 VIIGTSFLFVCFMRLYSCHFSSNHHVGFEAAAWYWHFVDVVWLFLYVFIY 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 4.17e-19

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: 82.03  E-value: 4.17e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573 132 PLLNTTILLSSGVTVTWAHHAILESNYSQAIQGLGLTIILGVYFSMLQAFEYIEASF---TIADSVFGSSFFVATGFHGL 208
Cdd:cd02865    52 LSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWHALNDagyGPTSNPAGSFFYLLTGLHGL 131

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2091526573 209 HVIIGTSFLFVCFMRLYSCHFSSNHHVGFEAAAWYWHFVDVVWLFLYVFIYWW 261
Cdd:cd02865   132 HVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVLLALLYGT 184
Ubiquinol_oxidase_III cd02863
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ...
 129-259 1.77e-18

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: 80.36  E-value: 1.77e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573 129 FQIPL--LNTTILLSSGVTVTWAHHAILESNYSQAIQGLGLTIILGVYFSMLQAFE---YIEASFTIADSVFGSSFFVAT 203
Cdd:cd02863    48 FELPLvfIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLV 127

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2091526573 204 GFHGLHVIIGTSFLFVCFMRLYSCHFSSNHHVGFEAAAWYWHFVDVVWLFLYVFIY 259
Cdd:cd02863   128 GTHGLHVTFGLIWILVMIIQLKKRGLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
Heme_Cu_Oxidase_III_1 cd02864
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 84-261 1.79e-15

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: 72.92  E-value: 1.79e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573  84 GMILFIVSEILFFFSFFWAFFHSSLSPNIELGMFWPPQGIqPFNPFQIPL----LNTTILLSSGVTVTWAHHAILESNYS 159
Cdd:cd02864    12 MMWFFLLSDAFIFSSFLIAYMTARISTTEPWPLPSDVFAL-RIGHFNIPLvliaIMTFILITSSGTMAMAVNFGYRGNRK 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573 160 QAIQGLGLTIILGVYFSMLQAFEYIE---------ASFTIADSVFGSSFFVATGFHGLHVIIGTSFL-FVCFMRLYSCHF 229
Cdd:cd02864    91 AAARLMLATALLGATFVGMQAFEWTKliveegvrpWGNPWGAAQFGASFFMITGFHGTHVTIGVIYLiIIARKVWRGKYQ 170

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2091526573 230 SSNHHVGFEAAAWYWHFVDVVWLFLYVFIYWW 261
Cdd:cd02864   171 RIGRYEIVEIAGLYWHFVDLVWVFIFAFFYLW 202
COX3 MTH00049
cytochrome c oxidase subunit III; Validated
 128-259 1.96e-15

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177124  Cd Length: 215  Bit Score: 73.03  E-value: 1.96e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573 128 PFQIPLLNTTILLSSGVTVTWAHHaILESNYSQAIqgLGLTIILGVYFSMLQAFEYIEASFTIADSVFGSSFFVATGFHG 207
Cdd:MTH00049   89 SLEIPFVGCFLLLGSSITVTAYHH-LLGWKYCDLF--LYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHF 165

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2091526573 208 LHVIIGtSFLFVCFMRLYSCHFSSNHHvgfEAAAWYWHFVDVVWLFLYVFIY 259
Cdd:MTH00049  166 SHVVLG-VVGLSTLLLVGSSSFGVYRS---TVLTWYWHFVDYIWLLVYLIVY 213
PRK10663 PRK10663
cytochrome o ubiquinol oxidase subunit III; Provisional
 129-262 1.46e-10

cytochrome o ubiquinol oxidase subunit III; Provisional


Pssm-ID: 182628  Cd Length: 204  Bit Score: 59.02  E-value: 1.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573 129 FQIP--LLNTTILLSSGVTVTWAHHAILESNYSQAIQGLGLTIILGVYFSMLQAFEY---IEASFTIADSVFGSSFFVAT 203
Cdd:PRK10663   64 FELPfvLVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFhhlIVEGMGPDRSGFLSAFFALV 143

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2091526573 204 GFHGLHVIIGTSFLFVCFMRLYSCHFSSNHHVGFEAAAWYWHFVDVVWLFLYVFIYWWG 262
Cdd:PRK10663  144 GTHGLHVTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMG 202
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 122-262 8.75e-08

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: 51.01  E-value: 8.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091526573 122 GIQPFNPFQIPLL--NTTILLSSGVTVTWAHHAILESNYSQAIQGLGLTIILGVYFSMLQAFE---YIEASFTIADSVFG 196
Cdd:TIGR02897  43 GKMPAELFELPLVliMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYW 122

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2091526573 197 SSFFVATGFHGLHVIIGTSFLFVCFMRLYSCHFSSNHHVGFEAAAWYWHFVDVVWLFLYVFIYWWG 262
Cdd:TIGR02897 123 SSFFVLLGTHGCHVTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
 
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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