NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2057278918|gb|QWY15121|]
View 

cytochrome c oxidase subunit 3, partial [Chorthippus parallelus erythropus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 1-224 1.36e-131

cytochrome c oxidase subunit III; Provisional


:

Pssm-ID: 214439  Cd Length: 255  Bit Score: 370.66  E-value: 1.36e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278918   1 PWPLTGAIGAMVLVSGLAKWFHMFNINLFIIGLSITLLTMIQWWRDVIREGTYQGLHTGYVSIGLRWGMILFIASEVLFF 80
Cdd:MTH00155   13 PWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGMILFIVSEVFFF 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278918  81 FSFFWAFFSSSLTPTIELGMLWPPMGIQPFNPMQIPLLNTVILLASGVTVTWAHHSIMESNHNQTLQGLFFTVMLGLYFT 160
Cdd:MTH00155   93 ISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSLFFTIILGIYFT 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2057278918 161 MLQTYEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTIFLTTCMTRHLMNQFSPNHHFGFEAA 224
Cdd:MTH00155  173 MLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAA 236
 
Name Accession Description Interval E-value
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 1-224 1.36e-131

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 370.66  E-value: 1.36e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278918   1 PWPLTGAIGAMVLVSGLAKWFHMFNINLFIIGLSITLLTMIQWWRDVIREGTYQGLHTGYVSIGLRWGMILFIASEVLFF 80
Cdd:MTH00155   13 PWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGMILFIVSEVFFF 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278918  81 FSFFWAFFSSSLTPTIELGMLWPPMGIQPFNPMQIPLLNTVILLASGVTVTWAHHSIMESNHNQTLQGLFFTVMLGLYFT 160
Cdd:MTH00155   93 ISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSLFFTIILGIYFT 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2057278918 161 MLQTYEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTIFLTTCMTRHLMNQFSPNHHFGFEAA 224
Cdd:MTH00155  173 MLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAA 236
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 4-224 5.11e-99

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: 287.49  E-value: 5.11e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278918   4 LTGAIGAMVLVSGLAKWFHMF-NINLFIIGLSITLLTMIQWWRDVIREGTYQGLHTGYVSIGLRWGMILFIASEVLFFFS 82
Cdd:cd01665     1 ILGSFGLLLLALGLVLWMHGYgGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278918  83 FFWAFFSSSLTPTIELGMLWPPMGIQPFNPMQIPLLNTVILLASGVTVTWAHHSIMESNHNQTLQGLFFTVMLGLYFTML 162
Cdd:cd01665    81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2057278918 163 QTYEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTIFLTTCMTRHLMNQFSPNHHFGFEAA 224
Cdd:cd01665   161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAA 222
COX3 pfam00510
Cytochrome c oxidase subunit III;
1-224 2.57e-98

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 286.61  E-value: 2.57e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278918   1 PWPLTGAIGAMVLVSGLAKWFHMF--NINLFIIGLSITLLTMIQWWRDVIREGTYQGLHTGYVSIGLRWGMILFIASEVL 78
Cdd:pfam00510  10 PWPLFGSFALLLLTSGLVLWFHGYsgNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGMILFIISEVF 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278918  79 FFFSFFWAFFSSSLTPTIELGMLWPPMGIQPFNPMQIPLLNTVILLASGVTVTWAHHSIMESNHNQTLQGLFFTVMLGLY 158
Cdd:pfam00510  90 FFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGLILTILLAVY 169

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2057278918 159 FTMLQTYEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTIFLTTCMTRHLMNQFSPNHHFGFEAA 224
Cdd:pfam00510 170 FTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAA 235
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
56-224 1.28e-32

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 116.49  E-value: 1.28e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278918  56 LHTGYVSIGLRWGMILFIASEVLFFFSFFWAFFSSSLTptielgMLWPPMGIQPFNPmQIPLLNTVILLASGVTVTWAHH 135
Cdd:COG1845     7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS------APDWPAGAELLDL-PLPLINTLLLLLSSFTVALAVR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278918 136 SIMESNHNQTLQGLFFTVMLGLYFTMLQTYEY---WEAPFTIADAVYGSTFFVATGFHGLHVIIGTIFLTTCMTRHLMNQ 212
Cdd:COG1845    80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159

                         170
                  ....*....|..
gi 2057278918 213 FSPNHHFGFEAA 224
Cdd:COG1845   160 FTPENHTGVEAA 171
 
Name Accession Description Interval E-value
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 1-224 1.36e-131

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 370.66  E-value: 1.36e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278918   1 PWPLTGAIGAMVLVSGLAKWFHMFNINLFIIGLSITLLTMIQWWRDVIREGTYQGLHTGYVSIGLRWGMILFIASEVLFF 80
Cdd:MTH00155   13 PWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGMILFIVSEVFFF 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278918  81 FSFFWAFFSSSLTPTIELGMLWPPMGIQPFNPMQIPLLNTVILLASGVTVTWAHHSIMESNHNQTLQGLFFTVMLGLYFT 160
Cdd:MTH00155   93 ISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSLFFTIILGIYFT 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2057278918 161 MLQTYEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTIFLTTCMTRHLMNQFSPNHHFGFEAA 224
Cdd:MTH00155  173 MLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAA 236
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 1-224 4.42e-112

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 321.52  E-value: 4.42e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278918   1 PWPLTGAIGAMVLVSGLAKWFHMFNINLFIIGLSITLLTMIQWWRDVIREGTYQGLHTGYVSIGLRWGMILFIASEVLFF 80
Cdd:MTH00118   15 PWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRYGMILFITSEVFFF 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278918  81 FSFFWAFFSSSLTPTIELGMLWPPMGIQPFNPMQIPLLNTVILLASGVTVTWAHHSIMESNHNQTLQGLFFTVMLGLYFT 160
Cdd:MTH00118   95 LGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQALTLTILLGLYFT 174

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2057278918 161 MLQTYEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTIFLTTCMTRHLMNQFSPNHHFGFEAA 224
Cdd:MTH00118  175 ALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAA 238
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 1-224 4.44e-109

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 313.83  E-value: 4.44e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278918   1 PWPLTGAIGAMVLVSGLAKWFHMFNINLFIIGLSITLLTMIQWWRDVIREGTYQGLHTGYVSIGLRWGMILFIASEVLFF 80
Cdd:MTH00189   14 PWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRYGMILFITSEVFFF 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278918  81 FSFFWAFFSSSLTPTIELGMLWPPMGIQPFNPMQIPLLNTVILLASGVTVTWAHHSIMESNHNQTLQGLFFTVMLGLYFT 160
Cdd:MTH00189   94 LGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQALTLTVILGVYFT 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2057278918 161 MLQTYEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTIFLTTCMTRHLMNQFSPNHHFGFEAA 224
Cdd:MTH00189  174 LLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAA 237
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 1-224 3.95e-105

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 303.96  E-value: 3.95e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278918   1 PWPLTGAIGAMVLVSGLAKWFHMFNINLFIIGLSITLLTMIQWWRDVIREGTYQGLHTGYVSIGLRWGMILFIASEVLFF 80
Cdd:MTH00039   14 PWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRYGMILFITSEVCFF 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278918  81 FSFFWAFFSSSLTPTIELGMLWPPMGIQPFNPMQIPLLNTVILLASGVTVTWAHHSIMESNHNQTLQGLFFTVMLGLYFT 160
Cdd:MTH00039   94 FAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQALFLTVLLGLYFT 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2057278918 161 MLQTYEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTIFLTTCMTRHLMNQFSPNHHFGFEAA 224
Cdd:MTH00039  174 ALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAA 237
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 1-224 7.08e-105

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 303.25  E-value: 7.08e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278918   1 PWPLTGAIGAMVLVSGLAKWFHMFNINLFIIGLSITLLTMIQWWRDVIREGTYQGLHTGYVSIGLRWGMILFIASEVLFF 80
Cdd:MTH00219   16 PWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLRIGMILFIVSEILFF 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278918  81 FSFFWAFFSSSLTPTIELGMLWPPMGIQPFNPMQIPLLNTVILLASGVTVTWAHHSIMESNHNQTLQGLFFTVMLGLYFT 160
Cdd:MTH00219   96 FAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQQGLLFTILLGLYFT 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2057278918 161 MLQTYEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTIFLTTCMTRHLMNQFSPNHHFGFEAA 224
Cdd:MTH00219  176 MLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAA 239
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 1-224 2.09e-103

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 299.50  E-value: 2.09e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278918   1 PWPLTGAIGAMVLVSGLAKWFHMFNINLFIIGLSITLLTMIQWWRDVIREGTYQGLHTGYVSIGLRWGMILFIASEVLFF 80
Cdd:MTH00141   13 PWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFILFIVSEVCFF 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278918  81 FSFFWAFFSSSLTPTIELGMLWPPMGIQPFNPMQIPLLNTVILLASGVTVTWAHHSIMESNHNQTLQGLFFTVMLGLYFT 160
Cdd:MTH00141   93 FAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGLTIILGVYFT 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2057278918 161 MLQTYEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTIFLTTCMTRHLMNQFSPNHHFGFEAA 224
Cdd:MTH00141  173 FLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAA 236
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 1-224 1.42e-102

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 297.43  E-value: 1.42e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278918   1 PWPLTGAIGAMVLVSGLAKWFHMFNINLFIIGLSITLLTMIQWWRDVIREGTYQGLHTGYVSIGLRWGMILFIASEVLFF 80
Cdd:MTH00075   15 PWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRYGMILFITSEVFFF 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278918  81 FSFFWAFFSSSLTPTIELGMLWPPMGIQPFNPMQIPLLNTVILLASGVTVTWAHHSIMESNHNQTLQGLFFTVMLGLYFT 160
Cdd:MTH00075   95 LGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQSLALTIILGLYFT 174

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2057278918 161 MLQTYEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTIFLTTCMTRHLMNQFSPNHHFGFEAA 224
Cdd:MTH00075  175 LLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAA 238
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 1-224 1.76e-101

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 294.71  E-value: 1.76e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278918   1 PWPLTGAIGAMVLVSGLAKWFHMFNINLFIIGLSITLLTMIQWWRDVIREGTYQGLHTGYVSIGLRWGMILFIASEVLFF 80
Cdd:MTH00099   15 PWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRYGMILFIISEVFFF 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278918  81 FSFFWAFFSSSLTPTIELGMLWPPMGIQPFNPMQIPLLNTVILLASGVTVTWAHHSIMESNHNQTLQGLFFTVMLGLYFT 160
Cdd:MTH00099   95 AGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQALFITILLGLYFT 174

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2057278918 161 MLQTYEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTIFLTTCMTRHLMNQFSPNHHFGFEAA 224
Cdd:MTH00099  175 LLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAA 238
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 1-224 4.84e-101

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 293.59  E-value: 4.84e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278918   1 PWPLTGAIGAMVLVSGLAKWFHMFNINLFIIGLSITLLTMIQWWRDVIREGTYQGLHTGYVSIGLRWGMILFIASEVLFF 80
Cdd:MTH00130   15 PWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRYGMILFITSEVFFF 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278918  81 FSFFWAFFSSSLTPTIELGMLWPPMGIQPFNPMQIPLLNTVILLASGVTVTWAHHSIMESNHNQTLQGLFFTVMLGLYFT 160
Cdd:MTH00130   95 LGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQSLTLTILLGFYFT 174

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2057278918 161 MLQTYEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTIFLTTCMTRHLMNQFSPNHHFGFEAA 224
Cdd:MTH00130  175 FLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAA 238
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 4-224 5.11e-99

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: 287.49  E-value: 5.11e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278918   4 LTGAIGAMVLVSGLAKWFHMF-NINLFIIGLSITLLTMIQWWRDVIREGTYQGLHTGYVSIGLRWGMILFIASEVLFFFS 82
Cdd:cd01665     1 ILGSFGLLLLALGLVLWMHGYgGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278918  83 FFWAFFSSSLTPTIELGMLWPPMGIQPFNPMQIPLLNTVILLASGVTVTWAHHSIMESNHNQTLQGLFFTVMLGLYFTML 162
Cdd:cd01665    81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2057278918 163 QTYEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTIFLTTCMTRHLMNQFSPNHHFGFEAA 224
Cdd:cd01665   161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAA 222
COX3 pfam00510
Cytochrome c oxidase subunit III;
1-224 2.57e-98

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 286.61  E-value: 2.57e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278918   1 PWPLTGAIGAMVLVSGLAKWFHMF--NINLFIIGLSITLLTMIQWWRDVIREGTYQGLHTGYVSIGLRWGMILFIASEVL 78
Cdd:pfam00510  10 PWPLFGSFALLLLTSGLVLWFHGYsgNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGMILFIISEVF 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278918  79 FFFSFFWAFFSSSLTPTIELGMLWPPMGIQPFNPMQIPLLNTVILLASGVTVTWAHHSIMESNHNQTLQGLFFTVMLGLY 158
Cdd:pfam00510  90 FFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGLILTILLAVY 169

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2057278918 159 FTMLQTYEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTIFLTTCMTRHLMNQFSPNHHFGFEAA 224
Cdd:pfam00510 170 FTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAA 235
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 1-224 2.21e-96

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 281.72  E-value: 2.21e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278918   1 PWPLTGAIGAMVLVSGLAKWFHMFNINLFIIGLSITLLTMIQWWRDVIREGTYQGLHTGYVSIGLRWGMILFIASEVLFF 80
Cdd:MTH00009   13 PWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMILFIASEVMFF 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278918  81 FSFFWAFFSSSLTPTIELGMLWPPMGIQPFNPMQIPLLNTVILLASGVTVTWAHHSIMESNHNQTLQGLFFTVMLGLYFT 160
Cdd:MTH00009   93 FAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALILTVLLGAYFT 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2057278918 161 MLQTYEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTIFLTTCMTRHLMNQFSPNHHFGFEAA 224
Cdd:MTH00009  173 FLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAA 236
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 1-224 5.99e-88

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 260.46  E-value: 5.99e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278918   1 PWPLTGAIGAMVLVSGLAKWFHMFNINLFIIGLSITLLTMIQWWRDVIREGTYQGLHTGYVSIGLRWGMILFIASEVLFF 80
Cdd:MTH00024   15 PWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGMLLFILSEVLFF 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278918  81 FSFFWAFFSSSLTPTIELGMLWPPMGIQPFNPMQIPLLNTVILLASGVTVTWAHHSIMESNHNQTLQGLFFTVMLGLYFT 160
Cdd:MTH00024   95 FSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFLTVFLGVLFT 174

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2057278918 161 MLQTYEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTIFLTTCMTRHLMNQFSPNHHFGFEAA 224
Cdd:MTH00024  175 GLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAA 238
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 1-224 2.14e-82

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 246.24  E-value: 2.14e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278918   1 PWPLTGAIGAMVLVSGLAKWFHMFNINLFIIGLSITLLTMIQWWRDVIREGTYQGLHTGYVSIGLRWGMILFIASEVLFF 80
Cdd:MTH00052   16 PWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGLKYGMILFIVSEVCLF 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278918  81 FSFFWAFFSSSLTPTIELGMLWPPMGIQPFNPMQIPLLNTVILLASGVTVTWAHHSIMESNHNQTLQGLFFTVMLGLYFT 160
Cdd:MTH00052   96 FSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEAIIGLALTVALGLLFT 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2057278918 161 MLQTYEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTIFLTTCMTRHLMNQFSPNHHFGFEAA 224
Cdd:MTH00052  176 GLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAA 239
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 1-224 1.53e-67

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 209.54  E-value: 1.53e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278918   1 PWPLTGAIGAMVLVSGLAKWFHMFNINLFIIGLSITLLTMIQWWRDVIREGTYQGLHTGYVSIGLRWGMILFIASEVLFF 80
Cdd:MTH00028   15 PWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLLFILSEVCLF 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278918  81 FSFFWAFFSSSLTPTIELGMLWPPMGIQPFNPMQIPLLNTVILLASGVTVTWAHHSIMESNHNQTLQ------------- 147
Cdd:MTH00028   95 FAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTGNPASLEkgtqgiegpnpsn 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278918 148 -----------------------GLFFTVMLGLYFTMLQTYEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTIFLTTC 204
Cdd:MTH00028  175 gappdpqkgptfllsdfrtnaviGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVLVGTTFLIVC 254

                         250       260
                  ....*....|....*....|
gi 2057278918 205 MTRHLMNQFSPNHHFGFEAA 224
Cdd:MTH00028  255 FIRLLSNQFTNSHHLGLEAA 274
PLN02194 PLN02194
cytochrome-c oxidase
 1-224 7.46e-61

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 191.42  E-value: 7.46e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278918   1 PWPLTGAIGAMVLVSGLAKWFHMFN--INLFIIGLSITLLTMIQWWRDVIREGTYQGLHTGYVSIGLRWGMILFIASEVL 78
Cdd:PLN02194   16 PWPISGSLGALATTVGGVMYMHPFQggARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGPRYGSILFIVSEVM 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278918  79 FFFSFFWAFFSSSLTPTIELGMLWPPMGIQPFNPMQIPLLNTVILLASGVTVTWAHHSIMESNHNQTLQGLFFTVMLGLY 158
Cdd:PLN02194   96 FFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEKRAVYALVATVLLALV 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2057278918 159 FTMLQTYEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTIFLTTCMTRHLMNQFSPNHHFGFEAA 224
Cdd:PLN02194  176 FTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAA 241
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
 9-222 2.27e-48

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 159.35  E-value: 2.27e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278918   9 GAMVLVSGLAKWFHMFNINLFIIGLSITLLTMIQWWRDVIREGtYQGLHTGYVSIGLRWGMILFIASEVLFFFSFFWAFF 88
Cdd:MTH00083   20 SSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMILFIFSEFMFFFSIFWTFF 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278918  89 SSSLTPTIELGMLWPPMGIQPFNPMQIPLLNTVILLASGVTVTWAHHSIMESNhNQTLQGLFFTVMLGLYFTMLQTYEYW 168
Cdd:MTH00083   99 DAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSN-KSCTNSLLLTCFLGLYFTSFQLMEYK 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2057278918 169 EAPFTIADAVYGSTFFVATGFHGLHVIIGTIFLTTCMTRHLMNQFSPNHHFGFE 222
Cdd:MTH00083  178 EASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLE 231
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 57-224 1.37e-44

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: 146.96  E-value: 1.37e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278918  57 HTGYVSIGLRWGMILFIASEVLFFFSFFWAFFSSSLTPTIELGMlwppmgiqPFNPMQIPLLNTVILLASGVTVTWAHHS 136
Cdd:cd00386     1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFGA--------GLDPLDLPLLNTNTLLLSGSSVTWAHAS 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278918 137 IMESNHN--QTLQGLFFTVMLGLYFTMLQTYEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTIFLTTCMTRHLMNQFS 214
Cdd:cd00386    73 LAARRGNrkKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152

                         170
                  ....*....|
gi 2057278918 215 PNHHFGFEAA 224
Cdd:cd00386   153 PRHHLGLEAA 162
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
56-224 1.28e-32

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 116.49  E-value: 1.28e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278918  56 LHTGYVSIGLRWGMILFIASEVLFFFSFFWAFFSSSLTptielgMLWPPMGIQPFNPmQIPLLNTVILLASGVTVTWAHH 135
Cdd:COG1845     7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS------APDWPAGAELLDL-PLPLINTLLLLLSSFTVALAVR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278918 136 SIMESNHNQTLQGLFFTVMLGLYFTMLQTYEY---WEAPFTIADAVYGSTFFVATGFHGLHVIIGTIFLTTCMTRHLMNQ 212
Cdd:COG1845    80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159

                         170
                  ....*....|..
gi 2057278918 213 FSPNHHFGFEAA 224
Cdd:COG1845   160 FTPENHTGVEAA 171
NorE_like cd02862
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ...
 117-224 9.70e-12

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: 61.48  E-value: 9.70e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278918 117 LLNTVILLASGVTVTWAHHSIMESNHNQTLQGLFFTVMLGLYFTMLQTYEYWE---APFTIADAVYGSTFFVATGFHGLH 193
Cdd:cd02862    55 ALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYAHkiaAGIDPDAGLFFTLYFLLTGFHLLH 134

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2057278918 194 VIIGTIFLTTCMTRHLMNQFSPNHHFGFEAA 224
Cdd:cd02862   135 VLIGLGILLWVAWRARRGRYSARDYEGVEAA 165
Ubiquinol_oxidase_III cd02863
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ...
 117-205 9.20e-10

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: 56.09  E-value: 9.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278918 117 LLNTVILLASGVTVTWAHHSIMESNHNQTLQGLFFTVMLGLYFTMLQTYE---YWEAPFTIADAVYGSTFFVATGFHGLH 193
Cdd:cd02863    54 FIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLVGTHGLH 133

                          90
                  ....*....|..
gi 2057278918 194 VIIGTIFLTTCM 205
Cdd:cd02863   134 VTFGLIWILVMI 145
COX3 MTH00049
cytochrome c oxidase subunit III; Validated
 112-203 5.41e-09

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177124  Cd Length: 215  Bit Score: 54.15  E-value: 5.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278918 112 PMQIPLLNTVILLASGVTVTwAHHSIMESNHNQTLqgLFFTVMLGLYFTMLQTYEYWEAPFTIADAVYGSTFFVATGFHG 191
Cdd:MTH00049   89 SLEIPFVGCFLLLGSSITVT-AYHHLLGWKYCDLF--LYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHF 165

                          90
                  ....*....|..
gi 2057278918 192 LHVIIGTIFLTT 203
Cdd:MTH00049  166 SHVVLGVVGLST 177
Heme_Cu_Oxidase_III_1 cd02864
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 120-201 1.81e-06

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: 46.73  E-value: 1.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278918 120 TVILLASGVTVTWAHHSIMESNHNQTLQGLFFTVMLGLYFTMLQTYEY-----------WEAPFTIAdaVYGSTFFVATG 188
Cdd:cd02864    67 TFILITSSGTMAMAVNFGYRGNRKAAARLMLATALLGATFVGMQAFEWtkliveegvrpWGNPWGAA--QFGASFFMITG 144

                          90
                  ....*....|...
gi 2057278918 189 FHGLHVIIGTIFL 201
Cdd:cd02864   145 FHGTHVTIGVIYL 157
Heme_Cu_Oxidase_III_2 cd02865
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 116-201 2.69e-06

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: 46.21  E-value: 2.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278918 116 PLLNTVILLASGVTVTWAHHSIMESNHNQTLQGLFFTVMLGLYFTMLQTYEYWEAPF---TIADAVYGSTFFVATGFHGL 192
Cdd:cd02865    52 LSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWHALNDagyGPTSNPAGSFFYLLTGLHGL 131


                  ....*....
gi 2057278918 193 HVIIGTIFL 201
Cdd:cd02865   132 HVIGGLVAL 140
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH