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Conserved domains on  [gi|688074697|ref|YP_009059109|]
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cytochrome c oxidase subunit III (mitochondrion) [Filchnerella beicki]

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 5.56e-161

cytochrome c oxidase subunit III; Provisional


:

Pssm-ID: 214439  Cd Length: 255  Bit Score: 446.55  E-value: 5.56e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697   5 HSNHPFHLVDYSPWPITGAIGAMVLVSGLAKWFHLFNINLLAIGFTITILTMIQWWRDVIREGTFQGLHTSFVSIGLRWG 84
Cdd:MTH00155   1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697  85 MILFIASEVLFFISFFWAFFNSSLAPAIELGMIWPPMGIQPFNPMQVPLLNTAILLASGVTVTWAHHSLMESNHTQALQG 164
Cdd:MTH00155  81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697 165 LFFTVLLGLYFTTLQAYEYWEAPFTIADAVYGSSFFVATGFHGLHVIIGTIFLSTCLLRHLMNQFSPSHHFGFEAAAWYW 244
Cdd:MTH00155 161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240

                        250
                 ....*....|....*
gi 688074697 245 HFVDVVWLFLYISIY 259
Cdd:MTH00155 241 HFVDVVWLFLYISIY 255
 
Name Accession Description Interval E-value
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 5-259 5.56e-161

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 446.55  E-value: 5.56e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697   5 HSNHPFHLVDYSPWPITGAIGAMVLVSGLAKWFHLFNINLLAIGFTITILTMIQWWRDVIREGTFQGLHTSFVSIGLRWG 84
Cdd:MTH00155   1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697  85 MILFIASEVLFFISFFWAFFNSSLAPAIELGMIWPPMGIQPFNPMQVPLLNTAILLASGVTVTWAHHSLMESNHTQALQG 164
Cdd:MTH00155  81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697 165 LFFTVLLGLYFTTLQAYEYWEAPFTIADAVYGSSFFVATGFHGLHVIIGTIFLSTCLLRHLMNQFSPSHHFGFEAAAWYW 244
Cdd:MTH00155 161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240

                        250
                 ....*....|....*
gi 688074697 245 HFVDVVWLFLYISIY 259
Cdd:MTH00155 241 HFVDVVWLFLYISIY 255
COX3 pfam00510
Cytochrome c oxidase subunit III;
8-263 9.22e-124

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 352.48  E-value: 9.22e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697    8 HPFHLVDYSPWPITGAIGAMVLVSGLAKWFHLF--NINLLAIGFTITILTMIQWWRDVIREGTFQGLHTSFVSIGLRWGM 85
Cdd:pfam00510   1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYsgNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697   86 ILFIASEVLFFISFFWAFFNSSLAPAIELGMIWPPMGIQPFNPMQVPLLNTAILLASGVTVTWAHHSLMESNHTQALQGL 165
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697  166 FFTVLLGLYFTTLQAYEYWEAPFTIADAVYGSSFFVATGFHGLHVIIGTIFLSTCLLRHLMNQFSPSHHFGFEAAAWYWH 245
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240

                         250
                  ....*....|....*...
gi 688074697  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 6.67e-120

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: 342.19  E-value: 6.67e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697  20 ITGAIGAMVLVSGLAKWFHLF-NINLLAIGFTITILTMIQWWRDVIREGTFQGLHTSFVSIGLRWGMILFIASEVLFFIS 98
Cdd:cd01665    1 ILGSFGLLLLALGLVLWMHGYgGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697  99 FFWAFFNSSLAPAIELGMIWPPMGIQPFNPMQVPLLNTAILLASGVTVTWAHHSLMESNHTQALQGLFFTVLLGLYFTTL 178
Cdd:cd01665   81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697 179 QAYEYWEAPFTIADAVYGSSFFVATGFHGLHVIIGTIFLSTCLLRHLMNQFSPSHHFGFEAAAWYWHFVDVVWLFLYISI 258
Cdd:cd01665  161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240


                 ...
gi 688074697 259 YWW 261
Cdd:cd01665  241 YWW 243
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
72-261 6.40e-47

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 154.62  E-value: 6.40e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697  72 LHTSFVSIGLRWGMILFIASEVLFFISFFWAFFNSSLAPAielgmiWPPMGIQPFNPmQVPLLNTAILLASGVTVTWAHH 151
Cdd:COG1845    7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRASAP------DWPAGAELLDL-PLPLINTLLLLLSSFTVALAVR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697 152 SLMESNHTQALQGLFFTVLLGLYFTTLQAYEY---WEAPFTIADAVYGSSFFVATGFHGLHVIIGTIFLSTCLLRHLMNQ 228
Cdd:COG1845   80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159

                        170       180       190
                 ....*....|....*....|....*....|...
gi 688074697 229 FSPSHHFGFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:COG1845  160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 133-262 1.75e-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: 1.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697  133 LLNTAILLASGVTVTWAHHSLMESNHTQALQGLFFTVLLGLYFTTLQAYE---YWEAPFTIADAVYGSSFFVATGFHGLH 209
Cdd:TIGR02897  56 LIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCH 135

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 688074697  210 VIIGTIFLSTCLLRHLMNQFSPSHHFGFEAAAWYWHFVDVVWLFLYISIYWWG 262
Cdd:TIGR02897 136 VTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
 
Name Accession Description Interval E-value
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 5-259 5.56e-161

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 446.55  E-value: 5.56e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697   5 HSNHPFHLVDYSPWPITGAIGAMVLVSGLAKWFHLFNINLLAIGFTITILTMIQWWRDVIREGTFQGLHTSFVSIGLRWG 84
Cdd:MTH00155   1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697  85 MILFIASEVLFFISFFWAFFNSSLAPAIELGMIWPPMGIQPFNPMQVPLLNTAILLASGVTVTWAHHSLMESNHTQALQG 164
Cdd:MTH00155  81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697 165 LFFTVLLGLYFTTLQAYEYWEAPFTIADAVYGSSFFVATGFHGLHVIIGTIFLSTCLLRHLMNQFSPSHHFGFEAAAWYW 244
Cdd:MTH00155 161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240

                        250
                 ....*....|....*
gi 688074697 245 HFVDVVWLFLYISIY 259
Cdd:MTH00155 241 HFVDVVWLFLYISIY 255
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 4-263 3.81e-144

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 404.33  E-value: 3.81e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697   4 THSNHPFHLVDYSPWPITGAIGAMVLVSGLAKWFHLFNINLLAIGFTITILTMIQWWRDVIREGTFQGLHTSFVSIGLRW 83
Cdd:MTH00118   2 THQAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697  84 GMILFIASEVLFFISFFWAFFNSSLAPAIELGMIWPPMGIQPFNPMQVPLLNTAILLASGVTVTWAHHSLMESNHTQALQ 163
Cdd:MTH00118  82 GMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQ 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697 164 GLFFTVLLGLYFTTLQAYEYWEAPFTIADAVYGSSFFVATGFHGLHVIIGTIFLSTCLLRHLMNQFSPSHHFGFEAAAWY 243
Cdd:MTH00118 162 ALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWY 241

                        250       260
                 ....*....|....*....|
gi 688074697 244 WHFVDVVWLFLYISIYWWGS 263
Cdd:MTH00118 242 WHFVDVVWLFLYISIYWWGS 261
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 4-263 7.80e-139

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 390.87  E-value: 7.80e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697   4 THSNHPFHLVDYSPWPITGAIGAMVLVSGLAKWFHLFNINLLAIGFTITILTMIQWWRDVIREGTFQGLHTSFVSIGLRW 83
Cdd:MTH00189   1 MHQAHPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697  84 GMILFIASEVLFFISFFWAFFNSSLAPAIELGMIWPPMGIQPFNPMQVPLLNTAILLASGVTVTWAHHSLMESNHTQALQ 163
Cdd:MTH00189  81 GMILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697 164 GLFFTVLLGLYFTTLQAYEYWEAPFTIADAVYGSSFFVATGFHGLHVIIGTIFLSTCLLRHLMNQFSPSHHFGFEAAAWY 243
Cdd:MTH00189 161 ALTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWY 240

                        250       260
                 ....*....|....*....|
gi 688074697 244 WHFVDVVWLFLYISIYWWGS 263
Cdd:MTH00189 241 WHFVDVVWLFLYVSIYWWGS 260
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 8-263 2.11e-133

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 377.15  E-value: 2.11e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697   8 HPFHLVDYSPWPITGAIGAMVLVSGLAKWFHLFNINLLAIGFTITILTMIQWWRDVIREGTFQGLHTSFVSIGLRWGMIL 87
Cdd:MTH00039   5 HPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRYGMIL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697  88 FIASEVLFFISFFWAFFNSSLAPAIELGMIWPPMGIQPFNPMQVPLLNTAILLASGVTVTWAHHSLMESNHTQALQGLFF 167
Cdd:MTH00039  85 FITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQALFL 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697 168 TVLLGLYFTTLQAYEYWEAPFTIADAVYGSSFFVATGFHGLHVIIGTIFLSTCLLRHLMNQFSPSHHFGFEAAAWYWHFV 247
Cdd:MTH00039 165 TVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWYWHFV 244

                        250
                 ....*....|....*.
gi 688074697 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00039 245 DVVWLFLYVCIYWWGS 260
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 8-263 1.99e-132

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 374.61  E-value: 1.99e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697   8 HPFHLVDYSPWPITGAIGAMVLVSGLAKWFHLFNINLLAIGFTITILTMIQWWRDVIREGTFQGLHTSFVSIGLRWGMIL 87
Cdd:MTH00141   4 NPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFIL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697  88 FIASEVLFFISFFWAFFNSSLAPAIELGMIWPPMGIQPFNPMQVPLLNTAILLASGVTVTWAHHSLMESNHTQALQGLFF 167
Cdd:MTH00141  84 FIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGL 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697 168 TVLLGLYFTTLQAYEYWEAPFTIADAVYGSSFFVATGFHGLHVIIGTIFLSTCLLRHLMNQFSPSHHFGFEAAAWYWHFV 247
Cdd:MTH00141 164 TIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFV 243

                        250
                 ....*....|....*.
gi 688074697 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00141 244 DVVWLFLYLSIYWWGS 259
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 4-263 6.22e-131

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 371.00  E-value: 6.22e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697   4 THSNHPFHLVDYSPWPITGAIGAMVLVSGLAKWFHLFNINLLAIGFTITILTMIQWWRDVIREGTFQGLHTSFVSIGLRW 83
Cdd:MTH00075   2 AHQAHAFHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697  84 GMILFIASEVLFFISFFWAFFNSSLAPAIELGMIWPPMGIQPFNPMQVPLLNTAILLASGVTVTWAHHSLMESNHTQALQ 163
Cdd:MTH00075  82 GMILFITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQ 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697 164 GLFFTVLLGLYFTTLQAYEYWEAPFTIADAVYGSSFFVATGFHGLHVIIGTIFLSTCLLRHLMNQFSPSHHFGFEAAAWY 243
Cdd:MTH00075 162 SLALTIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWY 241

                        250       260
                 ....*....|....*....|
gi 688074697 244 WHFVDVVWLFLYISIYWWGS 263
Cdd:MTH00075 242 WHFVDVVWLFLYVSIYWWGS 261
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 4-263 8.23e-130

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 367.94  E-value: 8.23e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697   4 THSNHPFHLVDYSPWPITGAIGAMVLVSGLAKWFHLFNINLLAIGFTITILTMIQWWRDVIREGTFQGLHTSFVSIGLRW 83
Cdd:MTH00130   2 AHQAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697  84 GMILFIASEVLFFISFFWAFFNSSLAPAIELGMIWPPMGIQPFNPMQVPLLNTAILLASGVTVTWAHHSLMESNHTQALQ 163
Cdd:MTH00130  82 GMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQ 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697 164 GLFFTVLLGLYFTTLQAYEYWEAPFTIADAVYGSSFFVATGFHGLHVIIGTIFLSTCLLRHLMNQFSPSHHFGFEAAAWY 243
Cdd:MTH00130 162 SLTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWY 241

                        250       260
                 ....*....|....*....|
gi 688074697 244 WHFVDVVWLFLYISIYWWGS 263
Cdd:MTH00130 242 WHFVDVVWLFLYISIYWWGS 261
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 8-263 1.26e-129

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 367.57  E-value: 1.26e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697   8 HPFHLVDYSPWPITGAIGAMVLVSGLAKWFHLFNINLLAIGFTITILTMIQWWRDVIREGTFQGLHTSFVSIGLRWGMIL 87
Cdd:MTH00219   7 NPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLRIGMIL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697  88 FIASEVLFFISFFWAFFNSSLAPAIELGMIWPPMGIQPFNPMQVPLLNTAILLASGVTVTWAHHSLMESNHTQALQGLFF 167
Cdd:MTH00219  87 FIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQQGLLF 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697 168 TVLLGLYFTTLQAYEYWEAPFTIADAVYGSSFFVATGFHGLHVIIGTIFLSTCLLRHLMNQFSPSHHFGFEAAAWYWHFV 247
Cdd:MTH00219 167 TILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAAWYWHFV 246

                        250
                 ....*....|....*.
gi 688074697 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00219 247 DVVWLFLYVSIYWWGS 262
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 4-263 1.19e-128

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 365.20  E-value: 1.19e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697   4 THSNHPFHLVDYSPWPITGAIGAMVLVSGLAKWFHLFNINLLAIGFTITILTMIQWWRDVIREGTFQGLHTSFVSIGLRW 83
Cdd:MTH00099   2 THQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697  84 GMILFIASEVLFFISFFWAFFNSSLAPAIELGMIWPPMGIQPFNPMQVPLLNTAILLASGVTVTWAHHSLMESNHTQALQ 163
Cdd:MTH00099  82 GMILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQ 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697 164 GLFFTVLLGLYFTTLQAYEYWEAPFTIADAVYGSSFFVATGFHGLHVIIGTIFLSTCLLRHLMNQFSPSHHFGFEAAAWY 243
Cdd:MTH00099 162 ALFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWY 241

                        250       260
                 ....*....|....*....|
gi 688074697 244 WHFVDVVWLFLYISIYWWGS 263
Cdd:MTH00099 242 WHFVDVVWLFLYVSIYWWGS 261
COX3 pfam00510
Cytochrome c oxidase subunit III;
8-263 9.22e-124

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 352.48  E-value: 9.22e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697    8 HPFHLVDYSPWPITGAIGAMVLVSGLAKWFHLF--NINLLAIGFTITILTMIQWWRDVIREGTFQGLHTSFVSIGLRWGM 85
Cdd:pfam00510   1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYsgNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697   86 ILFIASEVLFFISFFWAFFNSSLAPAIELGMIWPPMGIQPFNPMQVPLLNTAILLASGVTVTWAHHSLMESNHTQALQGL 165
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697  166 FFTVLLGLYFTTLQAYEYWEAPFTIADAVYGSSFFVATGFHGLHVIIGTIFLSTCLLRHLMNQFSPSHHFGFEAAAWYWH 245
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240

                         250
                  ....*....|....*...
gi 688074697  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 6.67e-120

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: 342.19  E-value: 6.67e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697  20 ITGAIGAMVLVSGLAKWFHLF-NINLLAIGFTITILTMIQWWRDVIREGTFQGLHTSFVSIGLRWGMILFIASEVLFFIS 98
Cdd:cd01665    1 ILGSFGLLLLALGLVLWMHGYgGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697  99 FFWAFFNSSLAPAIELGMIWPPMGIQPFNPMQVPLLNTAILLASGVTVTWAHHSLMESNHTQALQGLFFTVLLGLYFTTL 178
Cdd:cd01665   81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697 179 QAYEYWEAPFTIADAVYGSSFFVATGFHGLHVIIGTIFLSTCLLRHLMNQFSPSHHFGFEAAAWYWHFVDVVWLFLYISI 258
Cdd:cd01665  161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240


                 ...
gi 688074697 259 YWW 261
Cdd:cd01665  241 YWW 243
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 8-263 1.82e-119

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 341.82  E-value: 1.82e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697   8 HPFHLVDYSPWPITGAIGAMVLVSGLAKWFHLFNINLLAIGFTITILTMIQWWRDVIREGTFQGLHTSFVSIGLRWGMIL 87
Cdd:MTH00009   4 QPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMIL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697  88 FIASEVLFFISFFWAFFNSSLAPAIELGMIWPPMGIQPFNPMQVPLLNTAILLASGVTVTWAHHSLMESNHTQALQGLFF 167
Cdd:MTH00009  84 FIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALIL 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697 168 TVLLGLYFTTLQAYEYWEAPFTIADAVYGSSFFVATGFHGLHVIIGTIFLSTCLLRHLMNQFSPSHHFGFEAAAWYWHFV 247
Cdd:MTH00009 164 TVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFV 243

                        250
                 ....*....|....*.
gi 688074697 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00009 244 DVVWIFLYLCIYWWGS 259
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 8-263 3.03e-115

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 331.33  E-value: 3.03e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697   8 HPFHLVDYSPWPITGAIGAMVLVSGLAKWFHLFNINLLAIGFTITILTMIQWWRDVIREGTFQGLHTSFVSIGLRWGMIL 87
Cdd:MTH00024   6 HPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGMLL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697  88 FIASEVLFFISFFWAFFNSSLAPAIELGMIWPPMGIQPFNPMQVPLLNTAILLASGVTVTWAHHSLMESNHTQALQGLFF 167
Cdd:MTH00024  86 FILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFL 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697 168 TVLLGLYFTTLQAYEYWEAPFTIADAVYGSSFFVATGFHGLHVIIGTIFLSTCLLRHLMNQFSPSHHFGFEAAAWYWHFV 247
Cdd:MTH00024 166 TVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASWYWHFV 245

                        250
                 ....*....|....*.
gi 688074697 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00024 246 DVVWLFLYLCIYWWGS 261
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 2-263 7.18e-108

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 312.50  E-value: 7.18e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697   2 LTTHSNHPFHLVDYSPWPITGAIGAMVLVSGLAKWFHLFNINLLAIGFTITILTMIQWWRDVIREGTFQGLHTSFVSIGL 81
Cdd:MTH00052   1 MMQQYYHPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697  82 RWGMILFIASEVLFFISFFWAFFNSSLAPAIELGMIWPPMGIQPFNPMQVPLLNTAILLASGVTVTWAHHSLMESNHTQA 161
Cdd:MTH00052  81 KYGMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697 162 LQGLFFTVLLGLYFTTLQAYEYWEAPFTIADAVYGSSFFVATGFHGLHVIIGTIFLSTCLLRHLMNQFSPSHHFGFEAAA 241
Cdd:MTH00052 161 IIGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAA 240

                        250       260
                 ....*....|....*....|..
gi 688074697 242 WYWHFVDVVWLFLYISIYWWGS 263
Cdd:MTH00052 241 WYWHFVDVVWLFLFIFMYWWGS 262
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 8-263 4.35e-93

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 276.18  E-value: 4.35e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697   8 HPFHLVDYSPWPITGAIGAMVLVSGLAKWFHLFNINLLAIGFTITILTMIQWWRDVIREGTFQGLHTSFVSIGLRWGMIL 87
Cdd:MTH00028   6 HPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697  88 FIASEVLFFISFFWAFFNSSLAPAIELGMIWPPMGIQPFNPMQVPLLNTAILLASGVTVTWAHHSLMESNH--------- 158
Cdd:MTH00028  86 FILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTGNpaslekgtq 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697 159 ---------------------------TQALQGLFFTVLLGLYFTTLQAYEYWEAPFTIADAVYGSSFFVATGFHGLHVI 211
Cdd:MTH00028 166 giegpnpsngappdpqkgptfllsdfrTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVL 245

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 688074697 212 IGTIFLSTCLLRHLMNQFSPSHHFGFEAAAWYWHFVDVVWLFLYISIYWWGS 263
Cdd:MTH00028 246 VGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWGS 297
PLN02194 PLN02194
cytochrome-c oxidase
 8-262 2.32e-83

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 250.35  E-value: 2.32e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697   8 HPFHLVDYSPWPITGAIGAMVLVSGLAKWFHLFN--INLLAIGFTITILTMIQWWRDVIREGTFQGLHTSFVSIGLRWGM 85
Cdd:PLN02194   7 HSYHLVDPSPWPISGSLGALATTVGGVMYMHPFQggARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGPRYGS 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697  86 ILFIASEVLFFISFFWAFFNSSLAPAIELGMIWPPMGIQPFNPMQVPLLNTAILLASGVTVTWAHHSLMESNHTQALQGL 165
Cdd:PLN02194  87 ILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEKRAVYAL 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697 166 FFTVLLGLYFTTLQAYEYWEAPFTIADAVYGSSFFVATGFHGLHVIIGTIFLSTCLLRHLMNQFSPSHHFGFEAAAWYWH 245
Cdd:PLN02194 167 VATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWYWH 246

                        250
                 ....*....|....*..
gi 688074697 246 FVDVVWLFLYISIYWWG 262
Cdd:PLN02194 247 FVDVVWLFLFVSIYWWG 263
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
 8-263 1.25e-64

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 202.11  E-value: 1.25e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697   8 HPFHLVDYSPWPITGAIGAMVLVSGLAKWFHLFNINLLAIGFTITILTMIQWWRDVIREGtFQGLHTSFVSIGLRWGMIL 87
Cdd:MTH00083   3 HNFHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMIL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697  88 FIASEVLFFISFFWAFFNSSLAPAIELGMIWPPMGIQPFNPMQVPLLNTAILLASGVTVTWAHHSLMESNhTQALQGLFF 167
Cdd:MTH00083  82 FIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSN-KSCTNSLLL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697 168 TVLLGLYFTTLQAYEYWEAPFTIADAVYGSSFFVATGFHGLHVIIGTIFLSTCLLRHLMNQFSPSHHFGFEAAAWYWHFV 247
Cdd:MTH00083 161 TCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFV 240

                        250
                 ....*....|....*.
gi 688074697 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 2.19e-60

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


Pssm-ID: 238227  Cd Length: 183  Bit Score: 188.95  E-value: 2.19e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697  73 HTSFVSIGLRWGMILFIASEVLFFISFFWAFFNSSLAPAIELGMiwppmgiqPFNPMQVPLLNTAILLASGVTVTWAHHS 152
Cdd:cd00386    1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFGA--------GLDPLDLPLLNTNTLLLSGSSVTWAHAS 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697 153 LM--ESNHTQALQGLFFTVLLGLYFTTLQAYEYWEAPFTIADAVYGSSFFVATGFHGLHVIIGTIFLSTCLLRHLMNQFS 230
Cdd:cd00386   73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152

                        170       180       190
                 ....*....|....*....|....*....|.
gi 688074697 231 PSHHFGFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:cd00386  153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
72-261 6.40e-47

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 154.62  E-value: 6.40e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697  72 LHTSFVSIGLRWGMILFIASEVLFFISFFWAFFNSSLAPAielgmiWPPMGIQPFNPmQVPLLNTAILLASGVTVTWAHH 151
Cdd:COG1845    7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRASAP------DWPAGAELLDL-PLPLINTLLLLLSSFTVALAVR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697 152 SLMESNHTQALQGLFFTVLLGLYFTTLQAYEY---WEAPFTIADAVYGSSFFVATGFHGLHVIIGTIFLSTCLLRHLMNQ 228
Cdd:COG1845   80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159

                        170       180       190
                 ....*....|....*....|....*....|...
gi 688074697 229 FSPSHHFGFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:COG1845  160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
NorE_like cd02862
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ...
 133-259 1.70e-19

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: 83.05  E-value: 1.70e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697 133 LLNTAILLASGVTVTWAHHSLMESNHTQALQGLFFTVLLGLYFTTLQAYEYWE---APFTIADAVYGSSFFVATGFHGLH 209
Cdd:cd02862   55 ALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYAHkiaAGIDPDAGLFFTLYFLLTGFHLLH 134

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 688074697 210 VIIGTIFLSTCLLRHLMNQFSPSHHFGFEAAAWYWHFVDVVWLFLYISIY 259
Cdd:cd02862  135 VLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVLFPLLY 184
Heme_Cu_Oxidase_III_2 cd02865
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 131-261 1.32e-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: 1.32e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697 131 VPLLNTAILLASGVTVTWAHHSLMESNHTQALQGLFFTVLLGLYFTTLQAYEYWEAPF---TIADAVYGSSFFVATGFHG 207
Cdd:cd02865   51 LLSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWHALNDagyGPTSNPAGSFFYLLTGLHG 130

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 688074697 208 LHVIIGTIFLSTCLLRHLMNQFSPSHHFGFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:cd02865  131 LHVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVLLALLYGT 184
Ubiquinol_oxidase_III cd02863
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ...
 133-259 7.32e-16

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: 73.43  E-value: 7.32e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697 133 LLNTAILLASGVTVTWAHHSLMESNHTQALQGLFFTVLLGLYFTTLQAYE---YWEAPFTIADAVYGSSFFVATGFHGLH 209
Cdd:cd02863   54 FIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLVGTHGLH 133

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 688074697 210 VIIGTIFLSTCLLRHLMNQFSPSHHFGFEAAAWYWHFVDVVWLFLYISIY 259
Cdd:cd02863  134 VTFGLIWILVMIIQLKKRGLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
COX3 MTH00049
cytochrome c oxidase subunit III; Validated
 128-259 2.52e-15

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177124  Cd Length: 215  Bit Score: 72.64  E-value: 2.52e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697 128 PMQVPLLNTAILLASGVTVTwAHHSLMESNHTQALqgLFFTVLLGLYFTTLQAYEYWEAPFTIADAVYGSSFFVATGFHG 207
Cdd:MTH00049  89 SLEIPFVGCFLLLGSSITVT-AYHHLLGWKYCDLF--LYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHF 165

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 688074697 208 LHVIIGTIFLSTCLLRHLMNqFSPSHHfgfEAAAWYWHFVDVVWLFLYISIY 259
Cdd:MTH00049 166 SHVVLGVVGLSTLLLVGSSS-FGVYRS---TVLTWYWHFVDYIWLLVYLIVY 213
Heme_Cu_Oxidase_III_1 cd02864
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 136-261 2.50e-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: 69.84  E-value: 2.50e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697 136 TAILLASGVTVTWAHHSLMESNHTQALQGLFFTVLLGLYFTTLQAYEY-----------WEAPFTIAdaVYGSSFFVATG 204
Cdd:cd02864   67 TFILITSSGTMAMAVNFGYRGNRKAAARLMLATALLGATFVGMQAFEWtkliveegvrpWGNPWGAA--QFGASFFMITG 144

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 688074697 205 FHGLHVIIGTIFLSTCLLRHLMNQFSPSHHFG-FEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:cd02864  145 FHGTHVTIGVIYLIIIARKVWRGKYQRIGRYEiVEIAGLYWHFVDLVWVFIFAFFYLW 202
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 133-262 1.75e-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: 1.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697  133 LLNTAILLASGVTVTWAHHSLMESNHTQALQGLFFTVLLGLYFTTLQAYE---YWEAPFTIADAVYGSSFFVATGFHGLH 209
Cdd:TIGR02897  56 LIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCH 135

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 688074697  210 VIIGTIFLSTCLLRHLMNQFSPSHHFGFEAAAWYWHFVDVVWLFLYISIYWWG 262
Cdd:TIGR02897 136 VTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
PRK10663 PRK10663
cytochrome o ubiquinol oxidase subunit III; Provisional
 133-263 1.57e-07

cytochrome o ubiquinol oxidase subunit III; Provisional


Pssm-ID: 182628  Cd Length: 204  Bit Score: 50.55  E-value: 1.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688074697 133 LLNTAILLASGVTVTWAHHSLMESNHTQALQGLFFTVLLGLYFTTLQAYEYW---EAPFTIADAVYGSSFFVATGFHGLH 209
Cdd:PRK10663  70 LVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFHhliVEGMGPDRSGFLSAFFALVGTHGLH 149

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 688074697 210 VIIGTIFLSTCLLRHLMNQFSPSHHFGFEAAAWYWHFVDVVWLFLYISIYWWGS 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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