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Conserved domains on  [gi|2431500951|ref|YP_010602065|]
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cytochrome c oxidase subunit III (mitochondrion) [Ocellarnaca braueri]

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
 10-261 2.49e-149

cytochrome c oxidase subunit III; Provisional


:

Pssm-ID: 214439  Cd Length: 255  Bit Score: 417.27  E-value: 2.49e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951  10 HPFHLVNASPWPITGAIGAFITVSGLIMWFHQYNYHLLMIGTTITILTMIQWWRDITREGTYQGLHTLVVNLGLRWGMIL 89
Cdd:MTH00155    4 HPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGMIL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951  90 FIISEIFFFISFFWAFFHSSLSPSIELGAMWPPAGIQPFNPFQIPLLNTAILLASGVTVTWAHHSLMESNQSQTTQGLFF 169
Cdd:MTH00155   84 FIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSLFF 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951 170 TVLLGLYFTMLQAYEYIEAPFTIADAVYGSTFFVATGFHGLHVIIGTTFLIICLLRHMFFHFSQSHHFGFEAAAWYWHFV 249
Cdd:MTH00155  164 TIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYWHFV 243

                         250
                  ....*....|..
gi 2431500951 250 DVVWLFLYISIY 261
Cdd:MTH00155  244 DVVWLFLYISIY 255
 
Name Accession Description Interval E-value
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 10-261 2.49e-149

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 417.27  E-value: 2.49e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951  10 HPFHLVNASPWPITGAIGAFITVSGLIMWFHQYNYHLLMIGTTITILTMIQWWRDITREGTYQGLHTLVVNLGLRWGMIL 89
Cdd:MTH00155    4 HPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGMIL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951  90 FIISEIFFFISFFWAFFHSSLSPSIELGAMWPPAGIQPFNPFQIPLLNTAILLASGVTVTWAHHSLMESNQSQTTQGLFF 169
Cdd:MTH00155   84 FIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSLFF 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951 170 TVLLGLYFTMLQAYEYIEAPFTIADAVYGSTFFVATGFHGLHVIIGTTFLIICLLRHMFFHFSQSHHFGFEAAAWYWHFV 249
Cdd:MTH00155  164 TIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYWHFV 243

                         250
                  ....*....|..
gi 2431500951 250 DVVWLFLYISIY 261
Cdd:MTH00155  244 DVVWLFLYISIY 255
COX3 pfam00510
Cytochrome c oxidase subunit III;
10-265 1.58e-118

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 339.39  E-value: 1.58e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951  10 HPFHLVNASPWPITGAIGAFITVSGLIMWFHQY--NYHLLMIGTTITILTMIQWWRDITREGTYQGLHTLVVNLGLRWGM 87
Cdd:pfam00510   1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYsgNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951  88 ILFIISEIFFFISFFWAFFHSSLSPSIELGAMWPPAGIQPFNPFQIPLLNTAILLASGVTVTWAHHSLMESNQSQTTQGL 167
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951 168 FFTVLLGLYFTMLQAYEYIEAPFTIADAVYGSTFFVATGFHGLHVIIGTTFLIICLLRHMFFHFSQSHHFGFEAAAWYWH 247
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240

                         250
                  ....*....|....*...
gi 2431500951 248 FVDVVWLFLYISIYWWGS 265
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWGS 258
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 22-263 3.17e-113

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: 325.24  E-value: 3.17e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951  22 ITGAIGAFITVSGLIMWFHQY-NYHLLMIGTTITILTMIQWWRDITREGTYQGLHTLVVNLGLRWGMILFIISEIFFFIS 100
Cdd:cd01665     1 ILGSFGLLLLALGLVLWMHGYgGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951 101 FFWAFFHSSLSPSIELGAMWPPAGIQPFNPFQIPLLNTAILLASGVTVTWAHHSLMESNQSQTTQGLFFTVLLGLYFTML 180
Cdd:cd01665    81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951 181 QAYEYIEAPFTIADAVYGSTFFVATGFHGLHVIIGTTFLIICLLRHMFFHFSQSHHFGFEAAAWYWHFVDVVWLFLYISI 260
Cdd:cd01665   161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240


                  ...
gi 2431500951 261 YWW 263
Cdd:cd01665   241 YWW 243
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
122-263 1.63e-46

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 153.85  E-value: 1.63e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951 122 PAGIQPFNPFqIPLLNTAILLASGVTVTWAHHSLMESNQSQTTQGLFFTVLLGLYFTMLQAYEY---IEAPFTIADAVYG 198
Cdd:COG1845    49 PAGAELLDLP-LPLINTLLLLLSSFTVALAVRAARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFG 127

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2431500951 199 STFFVATGFHGLHVIIGTTFLIICLLRHMFFHFSQSHHFGFEAAAWYWHFVDVVWLFLYISIYWW 263
Cdd:COG1845   128 SFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGFTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 123-264 1.87e-11

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: 61.41  E-value: 1.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951 123 AGIQPFNPFQIPLL--NTAILLASGVTVTWAHHSLMESNQSQTTQGLFFTVLLGLYFTMLQAYE---YIEAPFTIADAVY 197
Cdd:TIGR02897  42 AGKMPAELFELPLVliMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSY 121

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951 198 GSTFFVATGFHGLHV---IIGTTFLIICLLRHMFFHFSQSHHFgfeAAAWYWHFVDVVWLFLYISIYWWG 264
Cdd:TIGR02897 122 WSSFFVLLGTHGCHVtlgIVWAICLLIQIQRRGLTPYTAPKVF---IVSLYWHFLDVVWVFIFTAVYLIG 188
 
Name Accession Description Interval E-value
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 10-261 2.49e-149

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 417.27  E-value: 2.49e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951  10 HPFHLVNASPWPITGAIGAFITVSGLIMWFHQYNYHLLMIGTTITILTMIQWWRDITREGTYQGLHTLVVNLGLRWGMIL 89
Cdd:MTH00155    4 HPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGMIL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951  90 FIISEIFFFISFFWAFFHSSLSPSIELGAMWPPAGIQPFNPFQIPLLNTAILLASGVTVTWAHHSLMESNQSQTTQGLFF 169
Cdd:MTH00155   84 FIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSLFF 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951 170 TVLLGLYFTMLQAYEYIEAPFTIADAVYGSTFFVATGFHGLHVIIGTTFLIICLLRHMFFHFSQSHHFGFEAAAWYWHFV 249
Cdd:MTH00155  164 TIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYWHFV 243

                         250
                  ....*....|..
gi 2431500951 250 DVVWLFLYISIY 261
Cdd:MTH00155  244 DVVWLFLYISIY 255
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 9-265 3.28e-139

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 392.01  E-value: 3.28e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951   9 THPFHLVNASPWPITGAIGAFITVSGLIMWFHQYNYHLLMIGTTITILTMIQWWRDITREGTYQGLHTLVVNLGLRWGMI 88
Cdd:MTH00118    5 AHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRYGMI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951  89 LFIISEIFFFISFFWAFFHSSLSPSIELGAMWPPAGIQPFNPFQIPLLNTAILLASGVTVTWAHHSLMESNQSQTTQGLF 168
Cdd:MTH00118   85 LFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQALT 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951 169 FTVLLGLYFTMLQAYEYIEAPFTIADAVYGSTFFVATGFHGLHVIIGTTFLIICLLRHMFFHFSQSHHFGFEAAAWYWHF 248
Cdd:MTH00118  165 LTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWYWHF 244

                         250
                  ....*....|....*..
gi 2431500951 249 VDVVWLFLYISIYWWGS 265
Cdd:MTH00118  245 VDVVWLFLYISIYWWGS 261
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 9-265 1.33e-132

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 375.08  E-value: 1.33e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951   9 THPFHLVNASPWPITGAIGAFITVSGLIMWFHQYNYHLLMIGTTITILTMIQWWRDITREGTYQGLHTLVVNLGLRWGMI 88
Cdd:MTH00189    4 AHPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRYGMI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951  89 LFIISEIFFFISFFWAFFHSSLSPSIELGAMWPPAGIQPFNPFQIPLLNTAILLASGVTVTWAHHSLMESNQSQTTQGLF 168
Cdd:MTH00189   84 LFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQALT 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951 169 FTVLLGLYFTMLQAYEYIEAPFTIADAVYGSTFFVATGFHGLHVIIGTTFLIICLLRHMFFHFSQSHHFGFEAAAWYWHF 248
Cdd:MTH00189  164 LTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWYWHF 243

                         250
                  ....*....|....*..
gi 2431500951 249 VDVVWLFLYISIYWWGS 265
Cdd:MTH00189  244 VDVVWLFLYVSIYWWGS 260
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 9-265 2.24e-126

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 359.43  E-value: 2.24e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951   9 THPFHLVNASPWPITGAIGAFITVSGLIMWFHQYNYHLLMIGTTITILTMIQWWRDITREGTYQGLHTLVVNLGLRWGMI 88
Cdd:MTH00099    5 THAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRYGMI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951  89 LFIISEIFFFISFFWAFFHSSLSPSIELGAMWPPAGIQPFNPFQIPLLNTAILLASGVTVTWAHHSLMESNQSQTTQGLF 168
Cdd:MTH00099   85 LFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQALF 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951 169 FTVLLGLYFTMLQAYEYIEAPFTIADAVYGSTFFVATGFHGLHVIIGTTFLIICLLRHMFFHFSQSHHFGFEAAAWYWHF 248
Cdd:MTH00099  165 ITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWYWHF 244

                         250
                  ....*....|....*..
gi 2431500951 249 VDVVWLFLYISIYWWGS 265
Cdd:MTH00099  245 VDVVWLFLYVSIYWWGS 261
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 7-265 7.70e-126

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 357.89  E-value: 7.70e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951   7 TFTHPFHLVNASPWPITGAIGAFITVSGLIMWFHQYNYHLLMIGTTITILTMIQWWRDITREGTYQGLHTLVVNLGLRWG 86
Cdd:MTH00039    2 THQHPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRYG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951  87 MILFIISEIFFFISFFWAFFHSSLSPSIELGAMWPPAGIQPFNPFQIPLLNTAILLASGVTVTWAHHSLMESNQSQTTQG 166
Cdd:MTH00039   82 MILFITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951 167 LFFTVLLGLYFTMLQAYEYIEAPFTIADAVYGSTFFVATGFHGLHVIIGTTFLIICLLRHMFFHFSQSHHFGFEAAAWYW 246
Cdd:MTH00039  162 LFLTVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWYW 241

                         250
                  ....*....|....*....
gi 2431500951 247 HFVDVVWLFLYISIYWWGS 265
Cdd:MTH00039  242 HFVDVVWLFLYVCIYWWGS 260
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 10-265 1.76e-124

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 354.58  E-value: 1.76e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951  10 HPFHLVNASPWPITGAIGAFITVSGLIMWFHQYNYHLLMIGTTITILTMIQWWRDITREGTYQGLHTLVVNLGLRWGMIL 89
Cdd:MTH00141    4 NPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFIL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951  90 FIISEIFFFISFFWAFFHSSLSPSIELGAMWPPAGIQPFNPFQIPLLNTAILLASGVTVTWAHHSLMESNQSQTTQGLFF 169
Cdd:MTH00141   84 FIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951 170 TVLLGLYFTMLQAYEYIEAPFTIADAVYGSTFFVATGFHGLHVIIGTTFLIICLLRHMFFHFSQSHHFGFEAAAWYWHFV 249
Cdd:MTH00141  164 TIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFV 243

                         250
                  ....*....|....*.
gi 2431500951 250 DVVWLFLYISIYWWGS 265
Cdd:MTH00141  244 DVVWLFLYLSIYWWGS 259
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 10-265 1.79e-123

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 352.14  E-value: 1.79e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951  10 HPFHLVNASPWPITGAIGAFITVSGLIMWFHQYNYHLLMIGTTITILTMIQWWRDITREGTYQGLHTLVVNLGLRWGMIL 89
Cdd:MTH00130    6 HAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRYGMIL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951  90 FIISEIFFFISFFWAFFHSSLSPSIELGAMWPPAGIQPFNPFQIPLLNTAILLASGVTVTWAHHSLMESNQSQTTQGLFF 169
Cdd:MTH00130   86 FITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQSLTL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951 170 TVLLGLYFTMLQAYEYIEAPFTIADAVYGSTFFVATGFHGLHVIIGTTFLIICLLRHMFFHFSQSHHFGFEAAAWYWHFV 249
Cdd:MTH00130  166 TILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWYWHFV 245

                         250
                  ....*....|....*.
gi 2431500951 250 DVVWLFLYISIYWWGS 265
Cdd:MTH00130  246 DVVWLFLYISIYWWGS 261
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 10-265 1.02e-122

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 350.20  E-value: 1.02e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951  10 HPFHLVNASPWPITGAIGAFITVSGLIMWFHQYNYHLLMIGTTITILTMIQWWRDITREGTYQGLHTLVVNLGLRWGMIL 89
Cdd:MTH00075    6 HAFHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRYGMIL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951  90 FIISEIFFFISFFWAFFHSSLSPSIELGAMWPPAGIQPFNPFQIPLLNTAILLASGVTVTWAHHSLMESNQSQTTQGLFF 169
Cdd:MTH00075   86 FITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQSLAL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951 170 TVLLGLYFTMLQAYEYIEAPFTIADAVYGSTFFVATGFHGLHVIIGTTFLIICLLRHMFFHFSQSHHFGFEAAAWYWHFV 249
Cdd:MTH00075  166 TIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWYWHFV 245

                         250
                  ....*....|....*.
gi 2431500951 250 DVVWLFLYISIYWWGS 265
Cdd:MTH00075  246 DVVWLFLYVSIYWWGS 261
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 9-265 3.98e-121

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 346.00  E-value: 3.98e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951   9 THPFHLVNASPWPITGAIGAFITVSGLIMWFHQYNYHLLMIGTTITILTMIQWWRDITREGTYQGLHTLVVNLGLRWGMI 88
Cdd:MTH00219    6 TNPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLRIGMI 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951  89 LFIISEIFFFISFFWAFFHSSLSPSIELGAMWPPAGIQPFNPFQIPLLNTAILLASGVTVTWAHHSLMESNQSQTTQGLF 168
Cdd:MTH00219   86 LFIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQQGLL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951 169 FTVLLGLYFTMLQAYEYIEAPFTIADAVYGSTFFVATGFHGLHVIIGTTFLIICLLRHMFFHFSQSHHFGFEAAAWYWHF 248
Cdd:MTH00219  166 FTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAAWYWHF 245

                         250
                  ....*....|....*..
gi 2431500951 249 VDVVWLFLYISIYWWGS 265
Cdd:MTH00219  246 VDVVWLFLYVSIYWWGS 262
COX3 pfam00510
Cytochrome c oxidase subunit III;
10-265 1.58e-118

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 339.39  E-value: 1.58e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951  10 HPFHLVNASPWPITGAIGAFITVSGLIMWFHQY--NYHLLMIGTTITILTMIQWWRDITREGTYQGLHTLVVNLGLRWGM 87
Cdd:pfam00510   1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYsgNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951  88 ILFIISEIFFFISFFWAFFHSSLSPSIELGAMWPPAGIQPFNPFQIPLLNTAILLASGVTVTWAHHSLMESNQSQTTQGL 167
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951 168 FFTVLLGLYFTMLQAYEYIEAPFTIADAVYGSTFFVATGFHGLHVIIGTTFLIICLLRHMFFHFSQSHHFGFEAAAWYWH 247
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240

                         250
                  ....*....|....*...
gi 2431500951 248 FVDVVWLFLYISIYWWGS 265
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWGS 258
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 22-263 3.17e-113

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: 325.24  E-value: 3.17e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951  22 ITGAIGAFITVSGLIMWFHQY-NYHLLMIGTTITILTMIQWWRDITREGTYQGLHTLVVNLGLRWGMILFIISEIFFFIS 100
Cdd:cd01665     1 ILGSFGLLLLALGLVLWMHGYgGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951 101 FFWAFFHSSLSPSIELGAMWPPAGIQPFNPFQIPLLNTAILLASGVTVTWAHHSLMESNQSQTTQGLFFTVLLGLYFTML 180
Cdd:cd01665    81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951 181 QAYEYIEAPFTIADAVYGSTFFVATGFHGLHVIIGTTFLIICLLRHMFFHFSQSHHFGFEAAAWYWHFVDVVWLFLYISI 260
Cdd:cd01665   161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240


                  ...
gi 2431500951 261 YWW 263
Cdd:cd01665   241 YWW 243
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 10-265 4.82e-113

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 325.64  E-value: 4.82e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951  10 HPFHLVNASPWPITGAIGAFITVSGLIMWFHQYNYHLLMIGTTITILTMIQWWRDITREGTYQGLHTLVVNLGLRWGMIL 89
Cdd:MTH00009    4 QPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMIL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951  90 FIISEIFFFISFFWAFFHSSLSPSIELGAMWPPAGIQPFNPFQIPLLNTAILLASGVTVTWAHHSLMESNQSQTTQGLFF 169
Cdd:MTH00009   84 FIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALIL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951 170 TVLLGLYFTMLQAYEYIEAPFTIADAVYGSTFFVATGFHGLHVIIGTTFLIICLLRHMFFHFSQSHHFGFEAAAWYWHFV 249
Cdd:MTH00009  164 TVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFV 243

                         250
                  ....*....|....*.
gi 2431500951 250 DVVWLFLYISIYWWGS 265
Cdd:MTH00009  244 DVVWIFLYLCIYWWGS 259
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 10-265 8.11e-111

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 320.16  E-value: 8.11e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951  10 HPFHLVNASPWPITGAIGAFITVSGLIMWFHQYNYHLLMIGTTITILTMIQWWRDITREGTYQGLHTLVVNLGLRWGMIL 89
Cdd:MTH00024    6 HPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGMLL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951  90 FIISEIFFFISFFWAFFHSSLSPSIELGAMWPPAGIQPFNPFQIPLLNTAILLASGVTVTWAHHSLMESNQSQTTQGLFF 169
Cdd:MTH00024   86 FILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951 170 TVLLGLYFTMLQAYEYIEAPFTIADAVYGSTFFVATGFHGLHVIIGTTFLIICLLRHMFFHFSQSHHFGFEAAAWYWHFV 249
Cdd:MTH00024  166 TVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASWYWHFV 245

                         250
                  ....*....|....*.
gi 2431500951 250 DVVWLFLYISIYWWGS 265
Cdd:MTH00024  246 DVVWLFLYLCIYWWGS 261
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 10-265 7.97e-106

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 307.49  E-value: 7.97e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951  10 HPFHLVNASPWPITGAIGAFITVSGLIMWFHQYNYHLLMIGTTITILTMIQWWRDITREGTYQGLHTLVVNLGLRWGMIL 89
Cdd:MTH00052    7 HPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGLKYGMIL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951  90 FIISEIFFFISFFWAFFHSSLSPSIELGAMWPPAGIQPFNPFQIPLLNTAILLASGVTVTWAHHSLMESNQSQTTQGLFF 169
Cdd:MTH00052   87 FIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEAIIGLAL 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951 170 TVLLGLYFTMLQAYEYIEAPFTIADAVYGSTFFVATGFHGLHVIIGTTFLIICLLRHMFFHFSQSHHFGFEAAAWYWHFV 249
Cdd:MTH00052  167 TVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAAWYWHFV 246

                         250
                  ....*....|....*.
gi 2431500951 250 DVVWLFLYISIYWWGS 265
Cdd:MTH00052  247 DVVWLFLFIFMYWWGS 262
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 10-265 6.31e-91

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 270.78  E-value: 6.31e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951  10 HPFHLVNASPWPITGAIGAFITVSGLIMWFHQYNYHLLMIGTTITILTMIQWWRDITREGTYQGLHTLVVNLGLRWGMIL 89
Cdd:MTH00028    6 HPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951  90 FIISEIFFFISFFWAFFHSSLSPSIELGAMWPPAGIQPFNPFQIPLLNTAILLASGVTVTWAHHSLMESN---------- 159
Cdd:MTH00028   86 FILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTGnpaslekgtq 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951 160 --------------------------QSQTTQGLFFTVLLGLYFTMLQAYEYIEAPFTIADAVYGSTFFVATGFHGLHVI 213
Cdd:MTH00028  166 giegpnpsngappdpqkgptfllsdfRTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVL 245

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2431500951 214 IGTTFLIICLLRHMFFHFSQSHHFGFEAAAWYWHFVDVVWLFLYISIYWWGS 265
Cdd:MTH00028  246 VGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWGS 297
PLN02194 PLN02194
cytochrome-c oxidase
 10-264 2.60e-80

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 242.65  E-value: 2.60e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951  10 HPFHLVNASPWPITGAIGAFITVSGLIMWFH--QYNYHLLMIGTTITILTMIQWWRDITREGTYQGLHTLVVNLGLRWGM 87
Cdd:PLN02194    7 HSYHLVDPSPWPISGSLGALATTVGGVMYMHpfQGGARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGPRYGS 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951  88 ILFIISEIFFFISFFWAFFHSSLSPSIELGAMWPPAGIQPFNPFQIPLLNTAILLASGVTVTWAHHSLMESNQSQTTQGL 167
Cdd:PLN02194   87 ILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEKRAVYAL 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951 168 FFTVLLGLYFTMLQAYEYIEAPFTIADAVYGSTFFVATGFHGLHVIIGTTFLIICLLRHMFFHFSQSHHFGFEAAAWYWH 247
Cdd:PLN02194  167 VATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWYWH 246

                         250
                  ....*....|....*..
gi 2431500951 248 FVDVVWLFLYISIYWWG 264
Cdd:PLN02194  247 FVDVVWLFLFVSIYWWG 263
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
 10-265 3.37e-60

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 190.94  E-value: 3.37e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951  10 HPFHLVNASPWPITGAIGAFITVSGLIMWFHQYNYHLLMIGTTITILTMIQWWRDITREGtYQGLHTLVVNLGLRWGMIL 89
Cdd:MTH00083    3 HNFHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMIL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951  90 FIISEIFFFISFFWAFFHSSLSPSIELGAMWPPAGIQPFNPFQIPLLNTAILLASGVTVTWAHHSLMESNQSqTTQGLFF 169
Cdd:MTH00083   82 FIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSNKS-CTNSLLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951 170 TVLLGLYFTMLQAYEYIEAPFTIADAVYGSTFFVATGFHGLHVIIGTTFLIICLLRHMFFHFSQSHHFGFEAAAWYWHFV 249
Cdd:MTH00083  161 TCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFV 240

                         250
                  ....*....|....*.
gi 2431500951 250 DVVWLFLYISIYWWGS 265
Cdd:MTH00083  241 DVVWLFLFVFVYWWSY 256
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 107-263 4.45e-56

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: 178.17  E-value: 4.45e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951 107 HSSLSPSIELGAmwppagiqPFNPFQIPLLNTAILLASGVTVTWAHHSLM--ESNQSQTTQGLFFTVLLGLYFTMLQAYE 184
Cdd:cd00386    33 HSRLSPPVEFGA--------GLDPLDLPLLNTNTLLLSGSSVTWAHASLAarRGNRKKARLWLLLTILLGLAFLGLQAYE 104

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2431500951 185 YIEAPFTIADAVYGSTFFVATGFHGLHVIIGTTFLIICLLRHMFFHFSQSHHFGFEAAAWYWHFVDVVWLFLYISIYWW 263
Cdd:cd00386   105 YSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFTPRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
122-263 1.63e-46

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 153.85  E-value: 1.63e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951 122 PAGIQPFNPFqIPLLNTAILLASGVTVTWAHHSLMESNQSQTTQGLFFTVLLGLYFTMLQAYEY---IEAPFTIADAVYG 198
Cdd:COG1845    49 PAGAELLDLP-LPLINTLLLLLSSFTVALAVRAARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFG 127

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2431500951 199 STFFVATGFHGLHVIIGTTFLIICLLRHMFFHFSQSHHFGFEAAAWYWHFVDVVWLFLYISIYWW 263
Cdd:COG1845   128 SFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGFTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
NorE_like cd02862
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ...
 135-261 4.06e-21

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


Pssm-ID: 239213  Cd Length: 186  Bit Score: 87.68  E-value: 4.06e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951 135 LLNTAILLASGVTVTWAHHSLMESNQSQTTQGLFFTVLLGLYFTMLQAYEY---IEAPFTIADAVYGSTFFVATGFHGLH 211
Cdd:cd02862    55 ALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYahkIAAGIDPDAGLFFTLYFLLTGFHLLH 134

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2431500951 212 VIIGTTFLIICLLRHMFFHFSQSHHFGFEAAAWYWHFVDVVWLFLYISIY 261
Cdd:cd02862   135 VLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVLFPLLY 184
Ubiquinol_oxidase_III cd02863
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ...
 131-261 3.94e-17

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


Pssm-ID: 239214  Cd Length: 186  Bit Score: 76.90  E-value: 3.94e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951 131 FQIPL--LNTAILLASGVTVTWAHHSLMESNQSQTTQGLFFTVLLGLYFTMLQAYE---YIEAPFTIADAVYGSTFFVAT 205
Cdd:cd02863    48 FELPLvfIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLV 127

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2431500951 206 GFHGLHVIIGTTFLIICLLRHMFFHFSQSHHFGFEAAAWYWHFVDVVWLFLYISIY 261
Cdd:cd02863   128 GTHGLHVTFGLIWILVMIIQLKKRGLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
Heme_Cu_Oxidase_III_2 cd02865
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 134-263 1.12e-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: 75.48  E-value: 1.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951 134 PLLNTAILLASGVTVTWAHHSLMESNQSQTTQGLFFTVLLGLYFTMLQAYEYIEAPF---TIADAVYGSTFFVATGFHGL 210
Cdd:cd02865    52 LSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWHALNDagyGPTSNPAGSFFYLLTGLHGL 131

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2431500951 211 HVIIGTTFLIICLLRHMFFHFSQSHHFGFEAAAWYWHFVDVVWLFLYISIYWW 263
Cdd:cd02865   132 HVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVLLALLYGT 184
COX3 MTH00049
cytochrome c oxidase subunit III; Validated
 130-261 1.03e-14

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177124  Cd Length: 215  Bit Score: 71.10  E-value: 1.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951 130 PFQIPLLNTAILLASGVTVTwAHHSLMESNQSQTTqgLFFTVLLGLYFTMLQAYEYIEAPFTIADAVYGSTFFVATGFHG 209
Cdd:MTH00049   89 SLEIPFVGCFLLLGSSITVT-AYHHLLGWKYCDLF--LYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHF 165

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2431500951 210 LHVIIGTTFLIICLLrhmffhfSQSHHFGF---EAAAWYWHFVDVVWLFLYISIY 261
Cdd:MTH00049  166 SHVVLGVVGLSTLLL-------VGSSSFGVyrsTVLTWYWHFVDYIWLLVYLIVY 213
Heme_Cu_Oxidase_III_1 cd02864
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 127-263 1.78e-14

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


Pssm-ID: 239215  Cd Length: 202  Bit Score: 70.22  E-value: 1.78e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951 127 PFNPFQIPL----LNTAILLASGVTVTWAHHSLMESNQSQTTQGLFFTVLLGLYFTMLQAYEYIE---------APFTIA 193
Cdd:cd02864    52 RIGHFNIPLvliaIMTFILITSSGTMAMAVNFGYRGNRKAAARLMLATALLGATFVGMQAFEWTKliveegvrpWGNPWG 131

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2431500951 194 DAVYGSTFFVATGFHGLHVIIGTTFLIICLLRHMFFHFSQSHHF-GFEAAAWYWHFVDVVWLFLYISIYWW 263
Cdd:cd02864   132 AAQFGASFFMITGFHGTHVTIGVIYLIIIARKVWRGKYQRIGRYeIVEIAGLYWHFVDLVWVFIFAFFYLW 202
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 123-264 1.87e-11

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: 61.41  E-value: 1.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951 123 AGIQPFNPFQIPLL--NTAILLASGVTVTWAHHSLMESNQSQTTQGLFFTVLLGLYFTMLQAYE---YIEAPFTIADAVY 197
Cdd:TIGR02897  42 AGKMPAELFELPLVliMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSY 121

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951 198 GSTFFVATGFHGLHV---IIGTTFLIICLLRHMFFHFSQSHHFgfeAAAWYWHFVDVVWLFLYISIYWWG 264
Cdd:TIGR02897 122 WSSFFVLLGTHGCHVtlgIVWAICLLIQIQRRGLTPYTAPKVF---IVSLYWHFLDVVWVFIFTAVYLIG 188
PRK10663 PRK10663
cytochrome o ubiquinol oxidase subunit III; Provisional
 131-265 4.54e-09

cytochrome o ubiquinol oxidase subunit III; Provisional


Pssm-ID: 182628  Cd Length: 204  Bit Score: 54.79  E-value: 4.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951 131 FQIP--LLNTAILLASGVTVTWAHHSLMESNQSQTTQGLFFTVLLGLYFTMLQAYEY---IEAPFTIADAVYGSTFFVAT 205
Cdd:PRK10663   64 FELPfvLVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFhhlIVEGMGPDRSGFLSAFFALV 143

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431500951 206 GFHGLHVIIGTTFLIICLLRHMFFHFSQSHHFGFEAAAWYWHFVDVVWLFLYISIYWWGS 265
Cdd:PRK10663  144 GTHGLHVTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGA 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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