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Conserved domains on  [gi|1035662989|gb|ANJ44365|]
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cytochrome c oxidase subunit III (mitochondrion) [Yunnanacris yunnaneus]

Protein Classification

cytochrome c oxidase subunit 3( domain architecture ID 10009592)

cytochrome c oxidase subunit 3 is one of main transmembrane subunits of cytochrome c oxidase, the last enzyme in the respiratory electron transport chain of mitochondria or bacteria located in the mitochondrial or bacterial membrane

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 5-259 1.21e-158

cytochrome c oxidase subunit III; Provisional


:

Pssm-ID: 214439  Cd Length: 255  Bit Score: 440.77  E-value: 1.21e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989   5 HSNHPFHLVDYSPWPLTGAIGAMVLVSGLAKWFHLFNINLFMIGMGITLLTMIQWWRDVVREGTYQGLHTSFVSIGLRWG 84
Cdd:MTH00155    1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989  85 MILFIASEVLFFMSFFWAFFSSSLAPTIELGMLWPPMGIQPFNPMQIPLLNTAILLASGVTVTWAHHSLMESNHTQALQG 164
Cdd:MTH00155   81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989 165 LFFTVLLGIYFTMLQAYEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTMFLLTCLMRHSMNQFSPNHHFGFEAAAWYW 244
Cdd:MTH00155  161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240

                         250
                  ....*....|....*
gi 1035662989 245 HFVDVVWLFLYISIY 259
Cdd:MTH00155  241 HFVDVVWLFLYISIY 255
 
Name Accession Description Interval E-value
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 5-259 1.21e-158

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 440.77  E-value: 1.21e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989   5 HSNHPFHLVDYSPWPLTGAIGAMVLVSGLAKWFHLFNINLFMIGMGITLLTMIQWWRDVVREGTYQGLHTSFVSIGLRWG 84
Cdd:MTH00155    1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989  85 MILFIASEVLFFMSFFWAFFSSSLAPTIELGMLWPPMGIQPFNPMQIPLLNTAILLASGVTVTWAHHSLMESNHTQALQG 164
Cdd:MTH00155   81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989 165 LFFTVLLGIYFTMLQAYEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTMFLLTCLMRHSMNQFSPNHHFGFEAAAWYW 244
Cdd:MTH00155  161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240

                         250
                  ....*....|....*
gi 1035662989 245 HFVDVVWLFLYISIY 259
Cdd:MTH00155  241 HFVDVVWLFLYISIY 255
COX3 pfam00510
Cytochrome c oxidase subunit III;
8-263 1.49e-122

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 349.40  E-value: 1.49e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989   8 HPFHLVDYSPWPLTGAIGAMVLVSGLAKWFHLF--NINLFMIGMGITLLTMIQWWRDVVREGTYQGLHTSFVSIGLRWGM 85
Cdd:pfam00510   1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYsgNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989  86 ILFIASEVLFFMSFFWAFFSSSLAPTIELGMLWPPMGIQPFNPMQIPLLNTAILLASGVTVTWAHHSLMESNHTQALQGL 165
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989 166 FFTVLLGIYFTMLQAYEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTMFLLTCLMRHSMNQFSPNHHFGFEAAAWYWH 245
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240

                         250
                  ....*....|....*...
gi 1035662989 246 FVDVVWLFLYISIYWWGS 263
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWGS 258
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 20-261 1.49e-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: 336.41  E-value: 1.49e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989  20 LTGAIGAMVLVSGLAKWFHLF-NINLFMIGMGITLLTMIQWWRDVVREGTYQGLHTSFVSIGLRWGMILFIASEVLFFMS 98
Cdd:cd01665     1 ILGSFGLLLLALGLVLWMHGYgGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989  99 FFWAFFSSSLAPTIELGMLWPPMGIQPFNPMQIPLLNTAILLASGVTVTWAHHSLMESNHTQALQGLFFTVLLGIYFTML 178
Cdd:cd01665    81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989 179 QAYEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTMFLLTCLMRHSMNQFSPNHHFGFEAAAWYWHFVDVVWLFLYISI 258
Cdd:cd01665   161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240


                  ...
gi 1035662989 259 YWW 261
Cdd:cd01665   241 YWW 243
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
72-261 6.89e-46

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 152.31  E-value: 6.89e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989  72 LHTSFVSIGLRWGMILFIASEVLFFMSFFWAFFSSSLAptielgMLWPPMGIQPFNPmQIPLLNTAILLASGVTVTWAHH 151
Cdd:COG1845     7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS------APDWPAGAELLDL-PLPLINTLLLLLSSFTVALAVR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989 152 SLMESNHTQALQGLFFTVLLGIYFTMLQAYEY---WEAPFTIADAVYGSTFFVATGFHGLHVIIGTMFLLTCLMRHSMNQ 228
Cdd:COG1845    80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1035662989 229 FSPNHHFGFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:COG1845   160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 133-262 8.00e-10

cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]


Pssm-ID: 131943  Cd Length: 190  Bit Score: 56.79  E-value: 8.00e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989 133 LLNTAILLASGVTVTWAHHSLMESNHTQALQGLFFTVLLGIYFTMLQAYE---YWEAPFTIADAVYGSTFFVATGFHGLH 209
Cdd:TIGR02897  56 LIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCH 135

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1035662989 210 VIIGTMFLLTCLMRHSMNQFSPNHHFGFEAAAWYWHFVDVVWLFLYISIYWWG 262
Cdd:TIGR02897 136 VTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
 
Name Accession Description Interval E-value
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 5-259 1.21e-158

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 440.77  E-value: 1.21e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989   5 HSNHPFHLVDYSPWPLTGAIGAMVLVSGLAKWFHLFNINLFMIGMGITLLTMIQWWRDVVREGTYQGLHTSFVSIGLRWG 84
Cdd:MTH00155    1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989  85 MILFIASEVLFFMSFFWAFFSSSLAPTIELGMLWPPMGIQPFNPMQIPLLNTAILLASGVTVTWAHHSLMESNHTQALQG 164
Cdd:MTH00155   81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989 165 LFFTVLLGIYFTMLQAYEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTMFLLTCLMRHSMNQFSPNHHFGFEAAAWYW 244
Cdd:MTH00155  161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240

                         250
                  ....*....|....*
gi 1035662989 245 HFVDVVWLFLYISIY 259
Cdd:MTH00155  241 HFVDVVWLFLYISIY 255
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 5-263 3.55e-141

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 396.63  E-value: 3.55e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989   5 HSNHPFHLVDYSPWPLTGAIGAMVLVSGLAKWFHLFNINLFMIGMGITLLTMIQWWRDVVREGTYQGLHTSFVSIGLRWG 84
Cdd:MTH00118    3 HQAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRYG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989  85 MILFIASEVLFFMSFFWAFFSSSLAPTIELGMLWPPMGIQPFNPMQIPLLNTAILLASGVTVTWAHHSLMESNHTQALQG 164
Cdd:MTH00118   83 MILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989 165 LFFTVLLGIYFTMLQAYEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTMFLLTCLMRHSMNQFSPNHHFGFEAAAWYW 244
Cdd:MTH00118  163 LTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWYW 242

                         250
                  ....*....|....*....
gi 1035662989 245 HFVDVVWLFLYISIYWWGS 263
Cdd:MTH00118  243 HFVDVVWLFLYISIYWWGS 261
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 4-263 5.59e-137

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 386.25  E-value: 5.59e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989   4 MHSNHPFHLVDYSPWPLTGAIGAMVLVSGLAKWFHLFNINLFMIGMGITLLTMIQWWRDVVREGTYQGLHTSFVSIGLRW 83
Cdd:MTH00189    1 MHQAHPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989  84 GMILFIASEVLFFMSFFWAFFSSSLAPTIELGMLWPPMGIQPFNPMQIPLLNTAILLASGVTVTWAHHSLMESNHTQALQ 163
Cdd:MTH00189   81 GMILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989 164 GLFFTVLLGIYFTMLQAYEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTMFLLTCLMRHSMNQFSPNHHFGFEAAAWY 243
Cdd:MTH00189  161 ALTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWY 240

                         250       260
                  ....*....|....*....|
gi 1035662989 244 WHFVDVVWLFLYISIYWWGS 263
Cdd:MTH00189  241 WHFVDVVWLFLYVSIYWWGS 260
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 4-263 5.36e-133

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 375.99  E-value: 5.36e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989   4 MHSNHPFHLVDYSPWPLTGAIGAMVLVSGLAKWFHLFNINLFMIGMGITLLTMIQWWRDVVREGTYQGLHTSFVSIGLRW 83
Cdd:MTH00039    1 MTHQHPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989  84 GMILFIASEVLFFMSFFWAFFSSSLAPTIELGMLWPPMGIQPFNPMQIPLLNTAILLASGVTVTWAHHSLMESNHTQALQ 163
Cdd:MTH00039   81 GMILFITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989 164 GLFFTVLLGIYFTMLQAYEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTMFLLTCLMRHSMNQFSPNHHFGFEAAAWY 243
Cdd:MTH00039  161 ALFLTVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWY 240

                         250       260
                  ....*....|....*....|
gi 1035662989 244 WHFVDVVWLFLYISIYWWGS 263
Cdd:MTH00039  241 WHFVDVVWLFLYVCIYWWGS 260
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 8-263 4.26e-130

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 368.45  E-value: 4.26e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989   8 HPFHLVDYSPWPLTGAIGAMVLVSGLAKWFHLFNINLFMIGMGITLLTMIQWWRDVVREGTYQGLHTSFVSIGLRWGMIL 87
Cdd:MTH00141    4 NPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFIL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989  88 FIASEVLFFMSFFWAFFSSSLAPTIELGMLWPPMGIQPFNPMQIPLLNTAILLASGVTVTWAHHSLMESNHTQALQGLFF 167
Cdd:MTH00141   84 FIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989 168 TVLLGIYFTMLQAYEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTMFLLTCLMRHSMNQFSPNHHFGFEAAAWYWHFV 247
Cdd:MTH00141  164 TIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFV 243

                         250
                  ....*....|....*.
gi 1035662989 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00141  244 DVVWLFLYLSIYWWGS 259
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 5-263 7.33e-128

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 362.93  E-value: 7.33e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989   5 HSNHPFHLVDYSPWPLTGAIGAMVLVSGLAKWFHLFNINLFMIGMGITLLTMIQWWRDVVREGTYQGLHTSFVSIGLRWG 84
Cdd:MTH00130    3 HQAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRYG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989  85 MILFIASEVLFFMSFFWAFFSSSLAPTIELGMLWPPMGIQPFNPMQIPLLNTAILLASGVTVTWAHHSLMESNHTQALQG 164
Cdd:MTH00130   83 MILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQS 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989 165 LFFTVLLGIYFTMLQAYEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTMFLLTCLMRHSMNQFSPNHHFGFEAAAWYW 244
Cdd:MTH00130  163 LTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWYW 242

                         250
                  ....*....|....*....
gi 1035662989 245 HFVDVVWLFLYISIYWWGS 263
Cdd:MTH00130  243 HFVDVVWLFLYISIYWWGS 261
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 5-263 8.94e-128

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 362.91  E-value: 8.94e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989   5 HSNHPFHLVDYSPWPLTGAIGAMVLVSGLAKWFHLFNINLFMIGMGITLLTMIQWWRDVVREGTYQGLHTSFVSIGLRWG 84
Cdd:MTH00075    3 HQAHAFHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRYG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989  85 MILFIASEVLFFMSFFWAFFSSSLAPTIELGMLWPPMGIQPFNPMQIPLLNTAILLASGVTVTWAHHSLMESNHTQALQG 164
Cdd:MTH00075   83 MILFITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQS 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989 165 LFFTVLLGIYFTMLQAYEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTMFLLTCLMRHSMNQFSPNHHFGFEAAAWYW 244
Cdd:MTH00075  163 LALTIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWYW 242

                         250
                  ....*....|....*....
gi 1035662989 245 HFVDVVWLFLYISIYWWGS 263
Cdd:MTH00075  243 HFVDVVWLFLYVSIYWWGS 261
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 8-263 5.42e-127

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 361.03  E-value: 5.42e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989   8 HPFHLVDYSPWPLTGAIGAMVLVSGLAKWFHLFNINLFMIGMGITLLTMIQWWRDVVREGTYQGLHTSFVSIGLRWGMIL 87
Cdd:MTH00219    7 NPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLRIGMIL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989  88 FIASEVLFFMSFFWAFFSSSLAPTIELGMLWPPMGIQPFNPMQIPLLNTAILLASGVTVTWAHHSLMESNHTQALQGLFF 167
Cdd:MTH00219   87 FIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQQGLLF 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989 168 TVLLGIYFTMLQAYEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTMFLLTCLMRHSMNQFSPNHHFGFEAAAWYWHFV 247
Cdd:MTH00219  167 TILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAAWYWHFV 246

                         250
                  ....*....|....*.
gi 1035662989 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00219  247 DVVWLFLYVSIYWWGS 262
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 5-263 1.40e-126

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 359.81  E-value: 1.40e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989   5 HSNHPFHLVDYSPWPLTGAIGAMVLVSGLAKWFHLFNINLFMIGMGITLLTMIQWWRDVVREGTYQGLHTSFVSIGLRWG 84
Cdd:MTH00099    3 HQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRYG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989  85 MILFIASEVLFFMSFFWAFFSSSLAPTIELGMLWPPMGIQPFNPMQIPLLNTAILLASGVTVTWAHHSLMESNHTQALQG 164
Cdd:MTH00099   83 MILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989 165 LFFTVLLGIYFTMLQAYEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTMFLLTCLMRHSMNQFSPNHHFGFEAAAWYW 244
Cdd:MTH00099  163 LFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWYW 242

                         250
                  ....*....|....*....
gi 1035662989 245 HFVDVVWLFLYISIYWWGS 263
Cdd:MTH00099  243 HFVDVVWLFLYVSIYWWGS 261
COX3 pfam00510
Cytochrome c oxidase subunit III;
8-263 1.49e-122

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 349.40  E-value: 1.49e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989   8 HPFHLVDYSPWPLTGAIGAMVLVSGLAKWFHLF--NINLFMIGMGITLLTMIQWWRDVVREGTYQGLHTSFVSIGLRWGM 85
Cdd:pfam00510   1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYsgNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989  86 ILFIASEVLFFMSFFWAFFSSSLAPTIELGMLWPPMGIQPFNPMQIPLLNTAILLASGVTVTWAHHSLMESNHTQALQGL 165
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989 166 FFTVLLGIYFTMLQAYEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTMFLLTCLMRHSMNQFSPNHHFGFEAAAWYWH 245
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240

                         250
                  ....*....|....*...
gi 1035662989 246 FVDVVWLFLYISIYWWGS 263
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWGS 258
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 8-263 1.40e-119

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 342.20  E-value: 1.40e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989   8 HPFHLVDYSPWPLTGAIGAMVLVSGLAKWFHLFNINLFMIGMGITLLTMIQWWRDVVREGTYQGLHTSFVSIGLRWGMIL 87
Cdd:MTH00009    4 QPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMIL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989  88 FIASEVLFFMSFFWAFFSSSLAPTIELGMLWPPMGIQPFNPMQIPLLNTAILLASGVTVTWAHHSLMESNHTQALQGLFF 167
Cdd:MTH00009   84 FIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALIL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989 168 TVLLGIYFTMLQAYEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTMFLLTCLMRHSMNQFSPNHHFGFEAAAWYWHFV 247
Cdd:MTH00009  164 TVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFV 243

                         250
                  ....*....|....*.
gi 1035662989 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00009  244 DVVWIFLYLCIYWWGS 259
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 20-261 1.49e-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: 336.41  E-value: 1.49e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989  20 LTGAIGAMVLVSGLAKWFHLF-NINLFMIGMGITLLTMIQWWRDVVREGTYQGLHTSFVSIGLRWGMILFIASEVLFFMS 98
Cdd:cd01665     1 ILGSFGLLLLALGLVLWMHGYgGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989  99 FFWAFFSSSLAPTIELGMLWPPMGIQPFNPMQIPLLNTAILLASGVTVTWAHHSLMESNHTQALQGLFFTVLLGIYFTML 178
Cdd:cd01665    81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989 179 QAYEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTMFLLTCLMRHSMNQFSPNHHFGFEAAAWYWHFVDVVWLFLYISI 258
Cdd:cd01665   161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240


                  ...
gi 1035662989 259 YWW 261
Cdd:cd01665   241 YWW 243
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 8-263 1.28e-109

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 317.08  E-value: 1.28e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989   8 HPFHLVDYSPWPLTGAIGAMVLVSGLAKWFHLFNINLFMIGMGITLLTMIQWWRDVVREGTYQGLHTSFVSIGLRWGMIL 87
Cdd:MTH00024    6 HPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGMLL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989  88 FIASEVLFFMSFFWAFFSSSLAPTIELGMLWPPMGIQPFNPMQIPLLNTAILLASGVTVTWAHHSLMESNHTQALQGLFF 167
Cdd:MTH00024   86 FILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989 168 TVLLGIYFTMLQAYEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTMFLLTCLMRHSMNQFSPNHHFGFEAAAWYWHFV 247
Cdd:MTH00024  166 TVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASWYWHFV 245

                         250
                  ....*....|....*.
gi 1035662989 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00024  246 DVVWLFLYLCIYWWGS 261
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 2-263 6.85e-106

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 307.49  E-value: 6.85e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989   2 LTMHSNHPFHLVDYSPWPLTGAIGAMVLVSGLAKWFHLFNINLFMIGMGITLLTMIQWWRDVVREGTYQGLHTSFVSIGL 81
Cdd:MTH00052    1 MMQQYYHPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989  82 RWGMILFIASEVLFFMSFFWAFFSSSLAPTIELGMLWPPMGIQPFNPMQIPLLNTAILLASGVTVTWAHHSLMESNHTQA 161
Cdd:MTH00052   81 KYGMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989 162 LQGLFFTVLLGIYFTMLQAYEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTMFLLTCLMRHSMNQFSPNHHFGFEAAA 241
Cdd:MTH00052  161 IIGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAA 240

                         250       260
                  ....*....|....*....|..
gi 1035662989 242 WYWHFVDVVWLFLYISIYWWGS 263
Cdd:MTH00052  241 WYWHFVDVVWLFLFIFMYWWGS 262
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 8-263 1.33e-91

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 272.71  E-value: 1.33e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989   8 HPFHLVDYSPWPLTGAIGAMVLVSGLAKWFHLFNINLFMIGMGITLLTMIQWWRDVVREGTYQGLHTSFVSIGLRWGMIL 87
Cdd:MTH00028    6 HPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989  88 FIASEVLFFMSFFWAFFSSSLAPTIELGMLWPPMGIQPFNPMQIPLLNTAILLASGVTVTWAHHSLMESNH--------- 158
Cdd:MTH00028   86 FILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTGNpaslekgtq 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989 159 ---------------------------TQALQGLFFTVLLGIYFTMLQAYEYWEAPFTIADAVYGSTFFVATGFHGLHVI 211
Cdd:MTH00028  166 giegpnpsngappdpqkgptfllsdfrTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVL 245

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1035662989 212 IGTMFLLTCLMRHSMNQFSPNHHFGFEAAAWYWHFVDVVWLFLYISIYWWGS 263
Cdd:MTH00028  246 VGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWGS 297
PLN02194 PLN02194
cytochrome-c oxidase
 8-262 3.32e-80

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 242.26  E-value: 3.32e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989   8 HPFHLVDYSPWPLTGAIGAMVLVSGLAKWFHLFN--INLFMIGMGITLLTMIQWWRDVVREGTYQGLHTSFVSIGLRWGM 85
Cdd:PLN02194    7 HSYHLVDPSPWPISGSLGALATTVGGVMYMHPFQggARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGPRYGS 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989  86 ILFIASEVLFFMSFFWAFFSSSLAPTIELGMLWPPMGIQPFNPMQIPLLNTAILLASGVTVTWAHHSLMESNHTQALQGL 165
Cdd:PLN02194   87 ILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEKRAVYAL 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989 166 FFTVLLGIYFTMLQAYEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTMFLLTCLMRHSMNQFSPNHHFGFEAAAWYWH 245
Cdd:PLN02194  167 VATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWYWH 246

                         250
                  ....*....|....*..
gi 1035662989 246 FVDVVWLFLYISIYWWG 262
Cdd:PLN02194  247 FVDVVWLFLFVSIYWWG 263
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
 8-263 1.16e-61

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 194.79  E-value: 1.16e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989   8 HPFHLVDYSPWPLTGAIGAMVLVSGLAKWFHLFNINLFMIGMGITLLTMIQWWRDVVREGtYQGLHTSFVSIGLRWGMIL 87
Cdd:MTH00083    3 HNFHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMIL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989  88 FIASEVLFFMSFFWAFFSSSLAPTIELGMLWPPMGIQPFNPMQIPLLNTAILLASGVTVTWAHHSLMESNhTQALQGLFF 167
Cdd:MTH00083   82 FIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSN-KSCTNSLLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989 168 TVLLGIYFTMLQAYEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTMFLLTCLMRHSMNQFSPNHHFGFEAAAWYWHFV 247
Cdd:MTH00083  161 TCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFV 240

                         250
                  ....*....|....*.
gi 1035662989 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00083  241 DVVWLFLFVFVYWWSY 256
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 73-261 7.72e-60

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


Pssm-ID: 238227  Cd Length: 183  Bit Score: 187.41  E-value: 7.72e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989  73 HTSFVSIGLRWGMILFIASEVLFFMSFFWAFFSSSLAPTIELGMlwppmgiqPFNPMQIPLLNTAILLASGVTVTWAHHS 152
Cdd:cd00386     1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFGA--------GLDPLDLPLLNTNTLLLSGSSVTWAHAS 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989 153 LM--ESNHTQALQGLFFTVLLGIYFTMLQAYEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTMFLLTCLMRHSMNQFS 230
Cdd:cd00386    73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1035662989 231 PNHHFGFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:cd00386   153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
72-261 6.89e-46

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 152.31  E-value: 6.89e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989  72 LHTSFVSIGLRWGMILFIASEVLFFMSFFWAFFSSSLAptielgMLWPPMGIQPFNPmQIPLLNTAILLASGVTVTWAHH 151
Cdd:COG1845     7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS------APDWPAGAELLDL-PLPLINTLLLLLSSFTVALAVR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989 152 SLMESNHTQALQGLFFTVLLGIYFTMLQAYEY---WEAPFTIADAVYGSTFFVATGFHGLHVIIGTMFLLTCLMRHSMNQ 228
Cdd:COG1845    80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1035662989 229 FSPNHHFGFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:COG1845   160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
NorE_like cd02862
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ...
 133-259 4.37e-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: 87.29  E-value: 4.37e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989 133 LLNTAILLASGVTVTWAHHSLMESNHTQALQGLFFTVLLGIYFTMLQAYEYWE---APFTIADAVYGSTFFVATGFHGLH 209
Cdd:cd02862    55 ALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYAHkiaAGIDPDAGLFFTLYFLLTGFHLLH 134

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1035662989 210 VIIGTMFLLTCLMRHSMNQFSPNHHFGFEAAAWYWHFVDVVWLFLYISIY 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 1.35e-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: 239216  Cd Length: 184  Bit Score: 72.79  E-value: 1.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989 132 PLLNTAILLASGVTVTWAHHSLMESNHTQALQGLFFTVLLGIYFTMLQAYEYWEAPF---TIADAVYGSTFFVATGFHGL 208
Cdd:cd02865    52 LSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWHALNDagyGPTSNPAGSFFYLLTGLHGL 131

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1035662989 209 HVIIGTMFLLTCLMRHSMNQFSPNHHFGFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:cd02865   132 HVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVLLALLYGT 184
Ubiquinol_oxidase_III cd02863
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ...
 133-259 5.49e-15

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


Pssm-ID: 239214  Cd Length: 186  Bit Score: 71.12  E-value: 5.49e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989 133 LLNTAILLASGVTVTWAHHSLMESNHTQALQGLFFTVLLGIYFTMLQAYE---YWEAPFTIADAVYGSTFFVATGFHGLH 209
Cdd:cd02863    54 FIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLVGTHGLH 133

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1035662989 210 VIIGTMFLLTCLMRHSMNQFSPNHHFGFEAAAWYWHFVDVVWLFLYISIY 259
Cdd:cd02863   134 VTFGLIWILVMIIQLKKRGLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
Heme_Cu_Oxidase_III_1 cd02864
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 136-261 4.40e-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: 69.07  E-value: 4.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989 136 TAILLASGVTVTWAHHSLMESNHTQALQGLFFTVLLGIYFTMLQAYEY-----------WEAPFTIAdaVYGSTFFVATG 204
Cdd:cd02864    67 TFILITSSGTMAMAVNFGYRGNRKAAARLMLATALLGATFVGMQAFEWtkliveegvrpWGNPWGAA--QFGASFFMITG 144

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1035662989 205 FHGLHVIIGTMFLLTCLMRHSMNQFSPNHHF-GFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:cd02864   145 FHGTHVTIGVIYLIIIARKVWRGKYQRIGRYeIVEIAGLYWHFVDLVWVFIFAFFYLW 202
COX3 MTH00049
cytochrome c oxidase subunit III; Validated
 128-259 7.00e-14

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177124  Cd Length: 215  Bit Score: 68.79  E-value: 7.00e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989 128 PMQIPLLNTAILLASGVTVTwAHHSLMESNHTQALqgLFFTVLLGIYFTMLQAYEYWEAPFTIADAVYGSTFFVATGFHG 207
Cdd:MTH00049   89 SLEIPFVGCFLLLGSSITVT-AYHHLLGWKYCDLF--LYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHF 165

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1035662989 208 LHVIIGTMFLLTCLMRHSMNqfspnhhFGF---EAAAWYWHFVDVVWLFLYISIY 259
Cdd:MTH00049  166 SHVVLGVVGLSTLLLVGSSS-------FGVyrsTVLTWYWHFVDYIWLLVYLIVY 213
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 133-262 8.00e-10

cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]


Pssm-ID: 131943  Cd Length: 190  Bit Score: 56.79  E-value: 8.00e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989 133 LLNTAILLASGVTVTWAHHSLMESNHTQALQGLFFTVLLGIYFTMLQAYE---YWEAPFTIADAVYGSTFFVATGFHGLH 209
Cdd:TIGR02897  56 LIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCH 135

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1035662989 210 VIIGTMFLLTCLMRHSMNQFSPNHHFGFEAAAWYWHFVDVVWLFLYISIYWWG 262
Cdd:TIGR02897 136 VTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
PRK10663 PRK10663
cytochrome o ubiquinol oxidase subunit III; Provisional
 133-263 3.18e-07

cytochrome o ubiquinol oxidase subunit III; Provisional


Pssm-ID: 182628  Cd Length: 204  Bit Score: 49.78  E-value: 3.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035662989 133 LLNTAILLASGVTVTWAHHSLMESNHTQALQGLFFTVLLGIYFTMLQAYEYW---EAPFTIADAVYGSTFFVATGFHGLH 209
Cdd:PRK10663   70 LVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFHhliVEGMGPDRSGFLSAFFALVGTHGLH 149

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1035662989 210 VIIGTMFLLTCLMRHSMNQFSPNHHFGFEAAAWYWHFVDVVWLFLYISIYWWGS 263
Cdd:PRK10663  150 VTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGA 203
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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