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Conserved domains on  [gi|1896069775|gb|QNJ47043|]
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cytochrome c oxidase subunit III, partial (mitochondrion) [Xya japonica]

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 6.48e-156

cytochrome c oxidase subunit III; Provisional


:

Pssm-ID: 214439  Cd Length: 255  Bit Score: 433.84  E-value: 6.48e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775   5 NTNHPFHLVDYSPWPLTGAIGALILTSGLSKWFHTFNINLLLVGSIISILTMIQWWRDISREGAFQGLHTLKVGVGLRWG 84
Cdd:MTH00155    1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775  85 MILFITSEVLFFISFFWAFFHSSLSPTIEIGSNWPPVGIISFNPLHIPLLNTAILLASGVTVTWAHHSLMSSNYTQAFQG 164
Cdd:MTH00155   81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775 165 LALTILLGLYFTILQAYEYLEAPFSIADSIYGSSFFMATGFHGLHVIIGTTFLLVCLIRLSMGQFSAAHHFGFEAAAWYW 244
Cdd:MTH00155  161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240

                         250
                  ....*....|....*
gi 1896069775 245 HFVDVVWLFLYLSIY 259
Cdd:MTH00155  241 HFVDVVWLFLYISIY 255
 
Name Accession Description Interval E-value
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 5-259 6.48e-156

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 433.84  E-value: 6.48e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775   5 NTNHPFHLVDYSPWPLTGAIGALILTSGLSKWFHTFNINLLLVGSIISILTMIQWWRDISREGAFQGLHTLKVGVGLRWG 84
Cdd:MTH00155    1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775  85 MILFITSEVLFFISFFWAFFHSSLSPTIEIGSNWPPVGIISFNPLHIPLLNTAILLASGVTVTWAHHSLMSSNYTQAFQG 164
Cdd:MTH00155   81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775 165 LALTILLGLYFTILQAYEYLEAPFSIADSIYGSSFFMATGFHGLHVIIGTTFLLVCLIRLSMGQFSAAHHFGFEAAAWYW 244
Cdd:MTH00155  161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240

                         250
                  ....*....|....*
gi 1896069775 245 HFVDVVWLFLYLSIY 259
Cdd:MTH00155  241 HFVDVVWLFLYISIY 255
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 20-261 3.11e-118

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: 337.95  E-value: 3.11e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775  20 LTGAIGALILTSGLSKWFHTF-NINLLLVGSIISILTMIQWWRDISREGAFQGLHTLKVGVGLRWGMILFITSEVLFFIS 98
Cdd:cd01665     1 ILGSFGLLLLALGLVLWMHGYgGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775  99 FFWAFFHSSLSPTIEIGSNWPPVGIISFNPLHIPLLNTAILLASGVTVTWAHHSLMSSNYTQAFQGLALTILLGLYFTIL 178
Cdd:cd01665    81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775 179 QAYEYLEAPFSIADSIYGSSFFMATGFHGLHVIIGTTFLLVCLIRLSMGQFSAAHHFGFEAAAWYWHFVDVVWLFLYLSI 258
Cdd:cd01665   161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240


                  ...
gi 1896069775 259 YWW 261
Cdd:cd01665   241 YWW 243
COX3 pfam00510
Cytochrome c oxidase subunit III;
8-262 3.16e-117

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 335.92  E-value: 3.16e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775   8 HPFHLVDYSPWPLTGAIGALILTSGLSKWFHTF--NINLLLVGSIISILTMIQWWRDISREGAFQGLHTLKVGVGLRWGM 85
Cdd:pfam00510   1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYsgNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775  86 ILFITSEVLFFISFFWAFFHSSLSPTIEIGSNWPPVGIISFNPLHIPLLNTAILLASGVTVTWAHHSLMSSNYTQAFQGL 165
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775 166 ALTILLGLYFTILQAYEYLEAPFSIADSIYGSSFFMATGFHGLHVIIGTTFLLVCLIRLSMGQFSAAHHFGFEAAAWYWH 245
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240

                         250
                  ....*....|....*..
gi 1896069775 246 FVDVVWLFLYLSIYWWG 262
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWG 257
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
72-261 5.81e-48

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 157.32  E-value: 5.81e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775  72 LHTLKVGVGLRWGMILFITSEVLFFISFFWAFFHSSLSptieigSNWPPVGIISFNPlHIPLLNTAILLASGVTVTWAHH 151
Cdd:COG1845     7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS------APDWPAGAELLDL-PLPLINTLLLLLSSFTVALAVR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775 152 SLMSSNYTQAFQGLALTILLGLYFTILQAYEY---LEAPFSIADSIYGSSFFMATGFHGLHVIIGTTFLLVCLIRLSMGQ 228
Cdd:COG1845    80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1896069775 229 FSAAHHFGFEAAAWYWHFVDVVWLFLYLSIYWW 261
Cdd:COG1845   160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 129-262 8.82e-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: 8.82e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775 129 LHIPLLNTAILLASGVTVTWAHHSLMSSNYTQAFQGLALTILLGLYFTILQAYE---YLEAPFSIADSIYGSSFFMATGF 205
Cdd:TIGR02897  52 LPLVLIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGT 131

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1896069775 206 HGLHVIIGTTFLLVCLIRLSMGQFSAAHHFGFEAAAWYWHFVDVVWLFLYLSIYWWG 262
Cdd:TIGR02897 132 HGCHVTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
 
Name Accession Description Interval E-value
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 5-259 6.48e-156

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 433.84  E-value: 6.48e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775   5 NTNHPFHLVDYSPWPLTGAIGALILTSGLSKWFHTFNINLLLVGSIISILTMIQWWRDISREGAFQGLHTLKVGVGLRWG 84
Cdd:MTH00155    1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775  85 MILFITSEVLFFISFFWAFFHSSLSPTIEIGSNWPPVGIISFNPLHIPLLNTAILLASGVTVTWAHHSLMSSNYTQAFQG 164
Cdd:MTH00155   81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775 165 LALTILLGLYFTILQAYEYLEAPFSIADSIYGSSFFMATGFHGLHVIIGTTFLLVCLIRLSMGQFSAAHHFGFEAAAWYW 244
Cdd:MTH00155  161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240

                         250
                  ....*....|....*
gi 1896069775 245 HFVDVVWLFLYLSIY 259
Cdd:MTH00155  241 HFVDVVWLFLYISIY 255
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 4-262 5.62e-141

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 396.24  E-value: 5.62e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775   4 NNTNHPFHLVDYSPWPLTGAIGALILTSGLSKWFHTFNINLLLVGSIISILTMIQWWRDISREGAFQGLHTLKVGVGLRW 83
Cdd:MTH00118    2 THQAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775  84 GMILFITSEVLFFISFFWAFFHSSLSPTIEIGSNWPPVGIISFNPLHIPLLNTAILLASGVTVTWAHHSLMSSNYTQAFQ 163
Cdd:MTH00118   82 GMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775 164 GLALTILLGLYFTILQAYEYLEAPFSIADSIYGSSFFMATGFHGLHVIIGTTFLLVCLIRLSMGQFSAAHHFGFEAAAWY 243
Cdd:MTH00118  162 ALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWY 241

                         250
                  ....*....|....*....
gi 1896069775 244 WHFVDVVWLFLYLSIYWWG 262
Cdd:MTH00118  242 WHFVDVVWLFLYISIYWWG 260
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 6-262 9.15e-137

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 385.48  E-value: 9.15e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775   6 TNHPFHLVDYSPWPLTGAIGALILTSGLSKWFHTFNINLLLVGSIISILTMIQWWRDISREGAFQGLHTLKVGVGLRWGM 85
Cdd:MTH00189    3 QAHPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRYGM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775  86 ILFITSEVLFFISFFWAFFHSSLSPTIEIGSNWPPVGIISFNPLHIPLLNTAILLASGVTVTWAHHSLMSSNYTQAFQGL 165
Cdd:MTH00189   83 ILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQAL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775 166 ALTILLGLYFTILQAYEYLEAPFSIADSIYGSSFFMATGFHGLHVIIGTTFLLVCLIRLSMGQFSAAHHFGFEAAAWYWH 245
Cdd:MTH00189  163 TLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWYWH 242

                         250
                  ....*....|....*..
gi 1896069775 246 FVDVVWLFLYLSIYWWG 262
Cdd:MTH00189  243 FVDVVWLFLYVSIYWWG 259
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 6-263 2.78e-133

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 376.54  E-value: 2.78e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775   6 TNHPFHLVDYSPWPLTGAIGALILTSGLSKWFHTFNINLLLVGSIISILTMIQWWRDISREGAFQGLHTLKVGVGLRWGM 85
Cdd:MTH00141    2 TRNPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775  86 ILFITSEVLFFISFFWAFFHSSLSPTIEIGSNWPPVGIISFNPLHIPLLNTAILLASGVTVTWAHHSLMSSNYTQAFQGL 165
Cdd:MTH00141   82 ILFIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775 166 ALTILLGLYFTILQAYEYLEAPFSIADSIYGSSFFMATGFHGLHVIIGTTFLLVCLIRLSMGQFSAAHHFGFEAAAWYWH 245
Cdd:MTH00141  162 GLTIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWH 241

                         250
                  ....*....|....*...
gi 1896069775 246 FVDVVWLFLYLSIYWWGG 263
Cdd:MTH00141  242 FVDVVWLFLYLSIYWWGS 259
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 8-263 1.04e-131

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 372.91  E-value: 1.04e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775   8 HPFHLVDYSPWPLTGAIGALILTSGLSKWFHTFNINLLLVGSIISILTMIQWWRDISREGAFQGLHTLKVGVGLRWGMIL 87
Cdd:MTH00039    5 HPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRYGMIL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775  88 FITSEVLFFISFFWAFFHSSLSPTIEIGSNWPPVGIISFNPLHIPLLNTAILLASGVTVTWAHHSLMSSNYTQAFQGLAL 167
Cdd:MTH00039   85 FITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQALFL 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775 168 TILLGLYFTILQAYEYLEAPFSIADSIYGSSFFMATGFHGLHVIIGTTFLLVCLIRLSMGQFSAAHHFGFEAAAWYWHFV 247
Cdd:MTH00039  165 TVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWYWHFV 244

                         250
                  ....*....|....*.
gi 1896069775 248 DVVWLFLYLSIYWWGG 263
Cdd:MTH00039  245 DVVWLFLYVCIYWWGS 260
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 8-262 1.74e-127

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 362.18  E-value: 1.74e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775   8 HPFHLVDYSPWPLTGAIGALILTSGLSKWFHTFNINLLLVGSIISILTMIQWWRDISREGAFQGLHTLKVGVGLRWGMIL 87
Cdd:MTH00219    7 NPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLRIGMIL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775  88 FITSEVLFFISFFWAFFHSSLSPTIEIGSNWPPVGIISFNPLHIPLLNTAILLASGVTVTWAHHSLMSSNYTQAFQGLAL 167
Cdd:MTH00219   87 FIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQQGLLF 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775 168 TILLGLYFTILQAYEYLEAPFSIADSIYGSSFFMATGFHGLHVIIGTTFLLVCLIRLSMGQFSAAHHFGFEAAAWYWHFV 247
Cdd:MTH00219  167 TILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAAWYWHFV 246

                         250
                  ....*....|....*
gi 1896069775 248 DVVWLFLYLSIYWWG 262
Cdd:MTH00219  247 DVVWLFLYVSIYWWG 261
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 8-262 2.07e-127

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 361.77  E-value: 2.07e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775   8 HPFHLVDYSPWPLTGAIGALILTSGLSKWFHTFNINLLLVGSIISILTMIQWWRDISREGAFQGLHTLKVGVGLRWGMIL 87
Cdd:MTH00130    6 HAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRYGMIL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775  88 FITSEVLFFISFFWAFFHSSLSPTIEIGSNWPPVGIISFNPLHIPLLNTAILLASGVTVTWAHHSLMSSNYTQAFQGLAL 167
Cdd:MTH00130   86 FITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQSLTL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775 168 TILLGLYFTILQAYEYLEAPFSIADSIYGSSFFMATGFHGLHVIIGTTFLLVCLIRLSMGQFSAAHHFGFEAAAWYWHFV 247
Cdd:MTH00130  166 TILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWYWHFV 245

                         250
                  ....*....|....*
gi 1896069775 248 DVVWLFLYLSIYWWG 262
Cdd:MTH00130  246 DVVWLFLYISIYWWG 260
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 8-262 1.29e-126

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 359.83  E-value: 1.29e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775   8 HPFHLVDYSPWPLTGAIGALILTSGLSKWFHTFNINLLLVGSIISILTMIQWWRDISREGAFQGLHTLKVGVGLRWGMIL 87
Cdd:MTH00075    6 HAFHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRYGMIL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775  88 FITSEVLFFISFFWAFFHSSLSPTIEIGSNWPPVGIISFNPLHIPLLNTAILLASGVTVTWAHHSLMSSNYTQAFQGLAL 167
Cdd:MTH00075   86 FITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQSLAL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775 168 TILLGLYFTILQAYEYLEAPFSIADSIYGSSFFMATGFHGLHVIIGTTFLLVCLIRLSMGQFSAAHHFGFEAAAWYWHFV 247
Cdd:MTH00075  166 TIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWYWHFV 245

                         250
                  ....*....|....*
gi 1896069775 248 DVVWLFLYLSIYWWG 262
Cdd:MTH00075  246 DVVWLFLYVSIYWWG 260
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 8-262 2.38e-125

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 356.73  E-value: 2.38e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775   8 HPFHLVDYSPWPLTGAIGALILTSGLSKWFHTFNINLLLVGSIISILTMIQWWRDISREGAFQGLHTLKVGVGLRWGMIL 87
Cdd:MTH00099    6 HAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRYGMIL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775  88 FITSEVLFFISFFWAFFHSSLSPTIEIGSNWPPVGIISFNPLHIPLLNTAILLASGVTVTWAHHSLMSSNYTQAFQGLAL 167
Cdd:MTH00099   86 FIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQALFI 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775 168 TILLGLYFTILQAYEYLEAPFSIADSIYGSSFFMATGFHGLHVIIGTTFLLVCLIRLSMGQFSAAHHFGFEAAAWYWHFV 247
Cdd:MTH00099  166 TILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWYWHFV 245

                         250
                  ....*....|....*
gi 1896069775 248 DVVWLFLYLSIYWWG 262
Cdd:MTH00099  246 DVVWLFLYVSIYWWG 260
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 20-261 3.11e-118

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: 337.95  E-value: 3.11e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775  20 LTGAIGALILTSGLSKWFHTF-NINLLLVGSIISILTMIQWWRDISREGAFQGLHTLKVGVGLRWGMILFITSEVLFFIS 98
Cdd:cd01665     1 ILGSFGLLLLALGLVLWMHGYgGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775  99 FFWAFFHSSLSPTIEIGSNWPPVGIISFNPLHIPLLNTAILLASGVTVTWAHHSLMSSNYTQAFQGLALTILLGLYFTIL 178
Cdd:cd01665    81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775 179 QAYEYLEAPFSIADSIYGSSFFMATGFHGLHVIIGTTFLLVCLIRLSMGQFSAAHHFGFEAAAWYWHFVDVVWLFLYLSI 258
Cdd:cd01665   161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240


                  ...
gi 1896069775 259 YWW 261
Cdd:cd01665   241 YWW 243
COX3 pfam00510
Cytochrome c oxidase subunit III;
8-262 3.16e-117

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 335.92  E-value: 3.16e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775   8 HPFHLVDYSPWPLTGAIGALILTSGLSKWFHTF--NINLLLVGSIISILTMIQWWRDISREGAFQGLHTLKVGVGLRWGM 85
Cdd:pfam00510   1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYsgNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775  86 ILFITSEVLFFISFFWAFFHSSLSPTIEIGSNWPPVGIISFNPLHIPLLNTAILLASGVTVTWAHHSLMSSNYTQAFQGL 165
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775 166 ALTILLGLYFTILQAYEYLEAPFSIADSIYGSSFFMATGFHGLHVIIGTTFLLVCLIRLSMGQFSAAHHFGFEAAAWYWH 245
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240

                         250
                  ....*....|....*..
gi 1896069775 246 FVDVVWLFLYLSIYWWG 262
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWG 257
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 6-262 1.10e-116

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 334.88  E-value: 1.10e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775   6 TNHPFHLVDYSPWPLTGAIGALILTSGLSKWFHTFNINLLLVGSIISILTMIQWWRDISREGAFQGLHTLKVGVGLRWGM 85
Cdd:MTH00009    2 IRQPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775  86 ILFITSEVLFFISFFWAFFHSSLSPTIEIGSNWPPVGIISFNPLHIPLLNTAILLASGVTVTWAHHSLMSSNYTQAFQGL 165
Cdd:MTH00009   82 ILFIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQAL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775 166 ALTILLGLYFTILQAYEYLEAPFSIADSIYGSSFFMATGFHGLHVIIGTTFLLVCLIRLSMGQFSAAHHFGFEAAAWYWH 245
Cdd:MTH00009  162 ILTVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWH 241

                         250
                  ....*....|....*..
gi 1896069775 246 FVDVVWLFLYLSIYWWG 262
Cdd:MTH00009  242 FVDVVWIFLYLCIYWWG 258
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 8-262 1.93e-114

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 329.02  E-value: 1.93e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775   8 HPFHLVDYSPWPLTGAIGALILTSGLSKWFHTFNINLLLVGSIISILTMIQWWRDISREGAFQGLHTLKVGVGLRWGMIL 87
Cdd:MTH00024    6 HPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGMLL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775  88 FITSEVLFFISFFWAFFHSSLSPTIEIGSNWPPVGIISFNPLHIPLLNTAILLASGVTVTWAHHSLMSSNYTQAFQGLAL 167
Cdd:MTH00024   86 FILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775 168 TILLGLYFTILQAYEYLEAPFSIADSIYGSSFFMATGFHGLHVIIGTTFLLVCLIRLSMGQFSAAHHFGFEAAAWYWHFV 247
Cdd:MTH00024  166 TVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASWYWHFV 245

                         250
                  ....*....|....*
gi 1896069775 248 DVVWLFLYLSIYWWG 262
Cdd:MTH00024  246 DVVWLFLYLCIYWWG 260
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 8-262 2.03e-106

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 308.65  E-value: 2.03e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775   8 HPFHLVDYSPWPLTGAIGALILTSGLSKWFHTFNINLLLVGSIISILTMIQWWRDISREGAFQGLHTLKVGVGLRWGMIL 87
Cdd:MTH00052    7 HPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGLKYGMIL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775  88 FITSEVLFFISFFWAFFHSSLSPTIEIGSNWPPVGIISFNPLHIPLLNTAILLASGVTVTWAHHSLMSSNYTQAFQGLAL 167
Cdd:MTH00052   87 FIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEAIIGLAL 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775 168 TILLGLYFTILQAYEYLEAPFSIADSIYGSSFFMATGFHGLHVIIGTTFLLVCLIRLSMGQFSAAHHFGFEAAAWYWHFV 247
Cdd:MTH00052  167 TVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAAWYWHFV 246

                         250
                  ....*....|....*
gi 1896069775 248 DVVWLFLYLSIYWWG 262
Cdd:MTH00052  247 DVVWLFLFIFMYWWG 261
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 8-262 1.74e-92

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 274.64  E-value: 1.74e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775   8 HPFHLVDYSPWPLTGAIGALILTSGLSKWFHTFNINLLLVGSIISILTMIQWWRDISREGAFQGLHTLKVGVGLRWGMIL 87
Cdd:MTH00028    6 HPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775  88 FITSEVLFFISFFWAFFHSSLSPTIEIGSNWPPVGIISFNPLHIPLLNTAILLASGVTVTWAHHSLMSSNY--------- 158
Cdd:MTH00028   86 FILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTGNpaslekgtq 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775 159 ---------------------------TQAFQGLALTILLGLYFTILQAYEYLEAPFSIADSIYGSSFFMATGFHGLHVI 211
Cdd:MTH00028  166 giegpnpsngappdpqkgptfllsdfrTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVL 245

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1896069775 212 IGTTFLLVCLIRLSMGQFSAAHHFGFEAAAWYWHFVDVVWLFLYLSIYWWG 262
Cdd:MTH00028  246 VGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWG 296
PLN02194 PLN02194
cytochrome-c oxidase
 2-263 1.48e-82

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 248.42  E-value: 1.48e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775   2 LTNNTNHPFHLVDYSPWPLTGAIGALILTSGLSKWFHTFN--INLLLVGSIISILTMIQWWRDISREGAFQGLHTLKVGV 79
Cdd:PLN02194    1 MIESQRHSYHLVDPSPWPISGSLGALATTVGGVMYMHPFQggARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775  80 GLRWGMILFITSEVLFFISFFWAFFHSSLSPTIEIGSNWPPVGIISFNPLHIPLLNTAILLASGVTVTWAHHSLMSSNYT 159
Cdd:PLN02194   81 GPRYGSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775 160 QAFQGLALTILLGLYFTILQAYEYLEAPFSIADSIYGSSFFMATGFHGLHVIIGTTFLLVCLIRLSMGQFSAAHHFGFEA 239
Cdd:PLN02194  161 RAVYALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEA 240

                         250       260
                  ....*....|....*....|....
gi 1896069775 240 AAWYWHFVDVVWLFLYLSIYWWGG 263
Cdd:PLN02194  241 AAWYWHFVDVVWLFLFVSIYWWGG 264
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
 8-262 1.03e-66

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 207.50  E-value: 1.03e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775   8 HPFHLVDYSPWPLTGAIGALILTSGLSKWFHtFNINLLLVGSIISIL-TMIQWWRDISREGaFQGLHTLKVGVGLRWGMI 86
Cdd:MTH00083    3 HNFHILSLSSYPYMMFFSSLGLTSSLVVFFK-YGLFYSFFFSLLYLLfISFLWGKDISMEG-LSGYHNFFVMDGFKFGMI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775  87 LFITSEVLFFISFFWAFFHSSLSPTIEIGSNWPPVGIISFNPLHIPLLNTAILLASGVTVTWAHHSLMSSNyTQAFQGLA 166
Cdd:MTH00083   81 LFIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSN-KSCTNSLL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775 167 LTILLGLYFTILQAYEYLEAPFSIADSIYGSSFFMATGFHGLHVIIGTTFLLVCLIRLSMGQFSAAHHFGFEAAAWYWHF 246
Cdd:MTH00083  160 LTCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHF 239

                         250
                  ....*....|....*.
gi 1896069775 247 VDVVWLFLYLSIYWWG 262
Cdd:MTH00083  240 VDVVWLFLFVFVYWWS 255
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 73-261 2.34e-63

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: 196.66  E-value: 2.34e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775  73 HTLKVGVGLRWGMILFITSEVLFFISFFWAFFHSSLSPTIEIGsnwppvgiISFNPLHIPLLNTAILLASGVTVTWAHHS 152
Cdd:cd00386     1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFG--------AGLDPLDLPLLNTNTLLLSGSSVTWAHAS 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775 153 LM--SSNYTQAFQGLALTILLGLYFTILQAYEYLEAPFSIADSIYGSSFFMATGFHGLHVIIGTTFLLVCLIRLSMGQFS 230
Cdd:cd00386    73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1896069775 231 AAHHFGFEAAAWYWHFVDVVWLFLYLSIYWW 261
Cdd:cd00386   153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
72-261 5.81e-48

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 157.32  E-value: 5.81e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775  72 LHTLKVGVGLRWGMILFITSEVLFFISFFWAFFHSSLSptieigSNWPPVGIISFNPlHIPLLNTAILLASGVTVTWAHH 151
Cdd:COG1845     7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS------APDWPAGAELLDL-PLPLINTLLLLLSSFTVALAVR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775 152 SLMSSNYTQAFQGLALTILLGLYFTILQAYEY---LEAPFSIADSIYGSSFFMATGFHGLHVIIGTTFLLVCLIRLSMGQ 228
Cdd:COG1845    80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1896069775 229 FSAAHHFGFEAAAWYWHFVDVVWLFLYLSIYWW 261
Cdd:COG1845   160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
NorE_like cd02862
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ...
 129-259 1.54e-23

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: 93.84  E-value: 1.54e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775 129 LHIPLLNTAILLASGVTVTWAHHSLMSSNYTQAFQGLALTILLGLYFTILQAYEYlEAPFSIADSIYGSSFFMA----TG 204
Cdd:cd02862    51 LLLGALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEY-AHKIAAGIDPDAGLFFTLyfllTG 129

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1896069775 205 FHGLHVIIGTTFLLVCLIRLSMGQFSAAHHFGFEAAAWYWHFVDVVWLFLYLSIY 259
Cdd:cd02862   130 FHLLHVLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVLFPLLY 184
Heme_Cu_Oxidase_III_2 cd02865
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 132-261 1.40e-18

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: 80.88  E-value: 1.40e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775 132 PLLNTAILLASGVTVTWAHHSLMSSNYTQAFQGLALTILLGLYFTILQAYEYLEAPFSI---ADSIYGSSFFMATGFHGL 208
Cdd:cd02865    52 LSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWHALNDAGygpTSNPAGSFFYLLTGLHGL 131

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1896069775 209 HVIIGTTFLLVCLIRLSMGQFSAAHHFGFEAAAWYWHFVDVVWLFLYLSIYWW 261
Cdd:cd02865   132 HVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVLLALLYGT 184
COX3 MTH00049
cytochrome c oxidase subunit III; Validated
 128-259 2.55e-18

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177124  Cd Length: 215  Bit Score: 80.73  E-value: 2.55e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775 128 PLHIPLLNTAILLASGVTVTwAHHSLMSSNYTQAFqgLALTILLGLYFTILQAYEYLEAPFSIADSIYGSSFFMATGFHG 207
Cdd:MTH00049   89 SLEIPFVGCFLLLGSSITVT-AYHHLLGWKYCDLF--LYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHF 165

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1896069775 208 LHVIIGTtFLLVCLIRLSMGQFSAAHHfgfEAAAWYWHFVDVVWLFLYLSIY 259
Cdd:MTH00049  166 SHVVLGV-VGLSTLLLVGSSSFGVYRS---TVLTWYWHFVDYIWLLVYLIVY 213
Ubiquinol_oxidase_III cd02863
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ...
 129-259 3.54e-17

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


Pssm-ID: 239214  Cd Length: 186  Bit Score: 76.90  E-value: 3.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775 129 LHIPLLNTAILLASGVTVTWAHHSLMSSNYTQAFQGLALTILLGLYFTILQAYE---YLEAPFSIADSIYGSSFFMATGF 205
Cdd:cd02863    50 LPLVFIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLVGT 129

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1896069775 206 HGLHVIIGTTFLLVCLIRLSMGQFSAAHHFGFEAAAWYWHFVDVVWLFLYLSIY 259
Cdd:cd02863   130 HGLHVTFGLIWILVMIIQLKKRGLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
Heme_Cu_Oxidase_III_1 cd02864
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 84-261 1.92e-15

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


Pssm-ID: 239215  Cd Length: 202  Bit Score: 72.53  E-value: 1.92e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775  84 GMILFITSEVLFFISFFWAFFHSSLSpTIEIGSNWPPVGIISFNPLHIPL----LNTAILLASGVTVTWAHHSLMSSNYT 159
Cdd:cd02864    12 MMWFFLLSDAFIFSSFLIAYMTARIS-TTEPWPLPSDVFALRIGHFNIPLvliaIMTFILITSSGTMAMAVNFGYRGNRK 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775 160 QAFQGLALTILLGLYFTILQAYEYLE---------APFSIADSIYGSSFFMATGFHGLHVIIGTTFLLVCLIRLSMGQFS 230
Cdd:cd02864    91 AAARLMLATALLGATFVGMQAFEWTKliveegvrpWGNPWGAAQFGASFFMITGFHGTHVTIGVIYLIIIARKVWRGKYQ 170

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1896069775 231 AAHHF-GFEAAAWYWHFVDVVWLFLYLSIYWW 261
Cdd:cd02864   171 RIGRYeIVEIAGLYWHFVDLVWVFIFAFFYLW 202
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 129-262 8.82e-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: 8.82e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775 129 LHIPLLNTAILLASGVTVTWAHHSLMSSNYTQAFQGLALTILLGLYFTILQAYE---YLEAPFSIADSIYGSSFFMATGF 205
Cdd:TIGR02897  52 LPLVLIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGT 131

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1896069775 206 HGLHVIIGTTFLLVCLIRLSMGQFSAAHHFGFEAAAWYWHFVDVVWLFLYLSIYWWG 262
Cdd:TIGR02897 132 HGCHVTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
PRK10663 PRK10663
cytochrome o ubiquinol oxidase subunit III; Provisional
 133-262 1.27e-09

cytochrome o ubiquinol oxidase subunit III; Provisional


Pssm-ID: 182628  Cd Length: 204  Bit Score: 56.33  E-value: 1.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069775 133 LLNTAILLASGVTVTWAHHSLMSSNYTQAFQGLALTILLGLYFTILQAYEY---LEAPFSIADSIYGSSFFMATGFHGLH 209
Cdd:PRK10663   70 LVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFhhlIVEGMGPDRSGFLSAFFALVGTHGLH 149

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1896069775 210 VIIGTTFLLVCLIRLSMGQFSAAHHFGFEAAAWYWHFVDVVWLFLYLSIYWWG 262
Cdd:PRK10663  150 VTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMG 202
 
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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