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Conserved domains on  [gi|270301148|gb|ACZ59763|]
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cytochrome c oxidase subunit III, partial (mitochondrion) [Peromyscus polionotus allophrys]

Protein Classification

cytochrome c oxidase subunit 3( domain architecture ID 10791085)

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 MTH00099
cytochrome c oxidase subunit III; Validated
 1-242 6.13e-162

cytochrome c oxidase subunit III; Validated


:

Pssm-ID: 177161  Cd Length: 261  Bit Score: 448.41  E-value: 6.13e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148   1 GAFSALLLTSGLVMWFHYNSYTLMTIGLLANTLTMYQWWRDIVREGTYQGHHTPIVQKGLRYGMILFIVSEVFFFAGFFW 80
Cdd:MTH00099  20 GALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRYGMILFIISEVFFFAGFFW 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148  81 AFYHSSLAPTHDLGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGKRSNMNQALLITILLGIYFTILQAS 160
Cdd:MTH00099 100 AFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQALFITILLGLYFTLLQAS 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148 161 EYFETPFSISDGVYGSTFFMATGFHGLHVIIGTTFLMVCLMRQLKYHFTSKHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 240
Cdd:MTH00099 180 EYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 259


                 ..
gi 270301148 241 GS 242
Cdd:MTH00099 260 GS 261
 
Name Accession Description Interval E-value
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 1-242 6.13e-162

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 448.41  E-value: 6.13e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148   1 GAFSALLLTSGLVMWFHYNSYTLMTIGLLANTLTMYQWWRDIVREGTYQGHHTPIVQKGLRYGMILFIVSEVFFFAGFFW 80
Cdd:MTH00099  20 GALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRYGMILFIISEVFFFAGFFW 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148  81 AFYHSSLAPTHDLGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGKRSNMNQALLITILLGIYFTILQAS 160
Cdd:MTH00099 100 AFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQALFITILLGLYFTLLQAS 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148 161 EYFETPFSISDGVYGSTFFMATGFHGLHVIIGTTFLMVCLMRQLKYHFTSKHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 240
Cdd:MTH00099 180 EYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 259


                 ..
gi 270301148 241 GS 242
Cdd:MTH00099 260 GS 261
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-240 1.63e-127

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: 360.68  E-value: 1.63e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148   1 GAFSALLLTSGLVMWFH-YNSYTLMTIGLLANTLTMYQWWRDIVREGTYQGHHTPIVQKGLRYGMILFIVSEVFFFAGFF 79
Cdd:cd01665    3 GSFGLLLLALGLVLWMHgYGGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFSFF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148  80 WAFYHSSLAPTHDLGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGKRSNMNQALLITILLGIYFTILQA 159
Cdd:cd01665   83 WAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGLQA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148 160 SEYFETPFSISDGVYGSTFFMATGFHGLHVIIGTTFLMVCLMRQLKYHFTSKHHFGFEAAAWYWHFVDVVWLFLYVSIYW 239
Cdd:cd01665  163 YEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFVYW 242


                 .
gi 270301148 240 W 240
Cdd:cd01665  243 W 243
COX3 pfam00510
Cytochrome c oxidase subunit III;
1-242 3.22e-126

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 357.88  E-value: 3.22e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148    1 GAFSALLLTSGLVMWFHY--NSYTLMTIGLLANTLTMYQWWRDIVREGTYQGHHTPIVQKGLRYGMILFIVSEVFFFAGF 78
Cdd:pfam00510  15 GSFALLLLTSGLVLWFHGysGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGMILFIISEVFFFLGI 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148   79 FWAFYHSSLAPTHDLGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGKRSNMNQALLITILLGIYFTILQ 158
Cdd:pfam00510  95 FWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGLILTILLAVYFTGLQ 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148  159 ASEYFETPFSISDGVYGSTFFMATGFHGLHVIIGTTFLMVCLMRQLKYHFTSKHHFGFEAAAWYWHFVDVVWLFLYVSIY 238
Cdd:pfam00510 175 AMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWHFVDVVWLFLYVSVY 254


                  ....
gi 270301148  239 WWGS 242
Cdd:pfam00510 255 WWGS 258
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
51-240 9.01e-50

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 161.17  E-value: 9.01e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148  51 HHTPIVQKGLRYGMILFIVSEVFF-FAGFFWAFYHSSLAPthdlggcWPPTGITPLNPLeVPLLNTSVLLASGVSITWAH 129
Cdd:COG1845    7 PHAPERRSPGKLGMWLFLASEVMLfAALFAAYFVLRASAP-------DWPAGAELLDLP-LPLINTLLLLLSSFTVALAV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148 130 HSLMEGKRSNMNQALLITILLGIYFTILQASEY---FETPFSISDGVYGSTFFMATGFHGLHVIIGTTFLMVCLMRQLKY 206
Cdd:COG1845   79 RAARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRG 158

                        170       180       190
                 ....*....|....*....|....*....|....
gi 270301148 207 HFTSKHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 240
Cdd:COG1845  159 GFTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 101-241 3.54e-11

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


Pssm-ID: 131943  Cd Length: 190  Bit Score: 60.25  E-value: 3.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148  101 GITPLNPLEVPLL--NTSVLLASGVSITWAHHSLMEGKRSNMNQALLITILLG---IYFTILQASEYFETPFSISDGVYG 175
Cdd:TIGR02897  43 GKMPAELFELPLVliMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGagfVGFEIYEFAHYASEGVTPQIGSYW 122

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 270301148  176 STFFMATGFHGLHVIIGTTFLMVCLMRQLKYHFTSKHHFGFEAAAWYWHFVDVVWLFLYVSIYWWG 241
Cdd:TIGR02897 123 SSFFVLLGTHGCHVTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
 
Name Accession Description Interval E-value
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 1-242 6.13e-162

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 448.41  E-value: 6.13e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148   1 GAFSALLLTSGLVMWFHYNSYTLMTIGLLANTLTMYQWWRDIVREGTYQGHHTPIVQKGLRYGMILFIVSEVFFFAGFFW 80
Cdd:MTH00099  20 GALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRYGMILFIISEVFFFAGFFW 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148  81 AFYHSSLAPTHDLGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGKRSNMNQALLITILLGIYFTILQAS 160
Cdd:MTH00099 100 AFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQALFITILLGLYFTLLQAS 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148 161 EYFETPFSISDGVYGSTFFMATGFHGLHVIIGTTFLMVCLMRQLKYHFTSKHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 240
Cdd:MTH00099 180 EYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 259


                 ..
gi 270301148 241 GS 242
Cdd:MTH00099 260 GS 261
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 1-242 3.96e-159

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 441.31  E-value: 3.96e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148   1 GAFSALLLTSGLVMWFHYNSYTLMTIGLLANTLTMYQWWRDIVREGTYQGHHTPIVQKGLRYGMILFIVSEVFFFAGFFW 80
Cdd:MTH00118  20 GAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRYGMILFITSEVFFFLGFFW 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148  81 AFYHSSLAPTHDLGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGKRSNMNQALLITILLGIYFTILQAS 160
Cdd:MTH00118 100 AFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQALTLTILLGLYFTALQAM 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148 161 EYFETPFSISDGVYGSTFFMATGFHGLHVIIGTTFLMVCLMRQLKYHFTSKHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 240
Cdd:MTH00118 180 EYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWYWHFVDVVWLFLYISIYWW 259


                 ..
gi 270301148 241 GS 242
Cdd:MTH00118 260 GS 261
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 1-242 8.81e-145

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 404.92  E-value: 8.81e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148   1 GAFSALLLTSGLVMWFHYNSYTLMTIGLLANTLTMYQWWRDIVREGTYQGHHTPIVQKGLRYGMILFIVSEVFFFAGFFW 80
Cdd:MTH00130  20 GAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRYGMILFITSEVFFFLGFFW 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148  81 AFYHSSLAPTHDLGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGKRSNMNQALLITILLGIYFTILQAS 160
Cdd:MTH00130 100 AFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQSLTLTILLGFYFTFLQAM 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148 161 EYFETPFSISDGVYGSTFFMATGFHGLHVIIGTTFLMVCLMRQLKYHFTSKHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 240
Cdd:MTH00130 180 EYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWYWHFVDVVWLFLYISIYWW 259


                 ..
gi 270301148 241 GS 242
Cdd:MTH00130 260 GS 261
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 1-242 1.20e-141

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 397.04  E-value: 1.20e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148   1 GAFSALLLTSGLVMWFHYNSYTLMTIGLLANTLTMYQWWRDIVREGTYQGHHTPIVQKGLRYGMILFIVSEVFFFAGFFW 80
Cdd:MTH00189  19 GAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRYGMILFITSEVFFFLGFFW 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148  81 AFYHSSLAPTHDLGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGKRSNMNQALLITILLGIYFTILQAS 160
Cdd:MTH00189  99 AFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQALTLTVILGVYFTLLQAM 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148 161 EYFETPFSISDGVYGSTFFMATGFHGLHVIIGTTFLMVCLMRQLKYHFTSKHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 240
Cdd:MTH00189 179 EYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 258


                 ..
gi 270301148 241 GS 242
Cdd:MTH00189 259 GS 260
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 1-242 7.61e-140

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 392.57  E-value: 7.61e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148   1 GAFSALLLTSGLVMWFHYNSYTLMTIGLLANTLTMYQWWRDIVREGTYQGHHTPIVQKGLRYGMILFIVSEVFFFAGFFW 80
Cdd:MTH00075  20 GAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRYGMILFITSEVFFFLGFFW 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148  81 AFYHSSLAPTHDLGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGKRSNMNQALLITILLGIYFTILQAS 160
Cdd:MTH00075 100 AFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQSLALTIILGLYFTLLQAM 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148 161 EYFETPFSISDGVYGSTFFMATGFHGLHVIIGTTFLMVCLMRQLKYHFTSKHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 240
Cdd:MTH00075 180 EYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 259


                 ..
gi 270301148 241 GS 242
Cdd:MTH00075 260 GS 261
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 1-238 1.22e-134

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 379.14  E-value: 1.22e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148   1 GAFSALLLTSGLVMWFHYNSYTLMTIGLLANTLTMYQWWRDIVREGTYQGHHTPIVQKGLRYGMILFIVSEVFFFAGFFW 80
Cdd:MTH00155  18 GSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGMILFIVSEVFFFISFFW 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148  81 AFYHSSLAPTHDLGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGKRSNMNQALLITILLGIYFTILQAS 160
Cdd:MTH00155  98 AFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSLFFTIILGIYFTMLQAY 177

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 270301148 161 EYFETPFSISDGVYGSTFFMATGFHGLHVIIGTTFLMVCLMRQLKYHFTSKHHFGFEAAAWYWHFVDVVWLFLYVSIY 238
Cdd:MTH00155 178 EYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYWHFVDVVWLFLYISIY 255
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 1-242 1.06e-130

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 369.22  E-value: 1.06e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148   1 GAFSALLLTSGLVMWFHYNSYTLMTIGLLANTLTMYQWWRDIVREGTYQGHHTPIVQKGLRYGMILFIVSEVFFFAGFFW 80
Cdd:MTH00141  18 GSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFILFIVSEVCFFFAFFW 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148  81 AFYHSSLAPTHDLGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGKRSNMNQALLITILLGIYFTILQAS 160
Cdd:MTH00141  98 AYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGLTIILGVYFTFLQAG 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148 161 EYFETPFSISDGVYGSTFFMATGFHGLHVIIGTTFLMVCLMRQLKYHFTSKHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 240
Cdd:MTH00141 178 EYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFVDVVWLFLYLSIYWW 257


                 ..
gi 270301148 241 GS 242
Cdd:MTH00141 258 GS 259
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-240 1.63e-127

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: 360.68  E-value: 1.63e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148   1 GAFSALLLTSGLVMWFH-YNSYTLMTIGLLANTLTMYQWWRDIVREGTYQGHHTPIVQKGLRYGMILFIVSEVFFFAGFF 79
Cdd:cd01665    3 GSFGLLLLALGLVLWMHgYGGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFSFF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148  80 WAFYHSSLAPTHDLGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGKRSNMNQALLITILLGIYFTILQA 159
Cdd:cd01665   83 WAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGLQA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148 160 SEYFETPFSISDGVYGSTFFMATGFHGLHVIIGTTFLMVCLMRQLKYHFTSKHHFGFEAAAWYWHFVDVVWLFLYVSIYW 239
Cdd:cd01665  163 YEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFVYW 242


                 .
gi 270301148 240 W 240
Cdd:cd01665  243 W 243
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 1-242 1.98e-126

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 358.66  E-value: 1.98e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148   1 GAFSALLLTSGLVMWFHYNSYTLMTIGLLANTLTMYQWWRDIVREGTYQGHHTPIVQKGLRYGMILFIVSEVFFFAGFFW 80
Cdd:MTH00039  19 AAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRYGMILFITSEVCFFFAFFW 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148  81 AFYHSSLAPTHDLGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGKRSNMNQALLITILLGIYFTILQAS 160
Cdd:MTH00039  99 AFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQALFLTVLLGLYFTALQAW 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148 161 EYFETPFSISDGVYGSTFFMATGFHGLHVIIGTTFLMVCLMRQLKYHFTSKHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 240
Cdd:MTH00039 179 EYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWYWHFVDVVWLFLYVCIYWW 258


                 ..
gi 270301148 241 GS 242
Cdd:MTH00039 259 GS 260
COX3 pfam00510
Cytochrome c oxidase subunit III;
1-242 3.22e-126

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 357.88  E-value: 3.22e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148    1 GAFSALLLTSGLVMWFHY--NSYTLMTIGLLANTLTMYQWWRDIVREGTYQGHHTPIVQKGLRYGMILFIVSEVFFFAGF 78
Cdd:pfam00510  15 GSFALLLLTSGLVLWFHGysGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGMILFIISEVFFFLGI 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148   79 FWAFYHSSLAPTHDLGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGKRSNMNQALLITILLGIYFTILQ 158
Cdd:pfam00510  95 FWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGLILTILLAVYFTGLQ 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148  159 ASEYFETPFSISDGVYGSTFFMATGFHGLHVIIGTTFLMVCLMRQLKYHFTSKHHFGFEAAAWYWHFVDVVWLFLYVSIY 238
Cdd:pfam00510 175 AMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWHFVDVVWLFLYVSVY 254


                  ....
gi 270301148  239 WWGS 242
Cdd:pfam00510 255 WWGS 258
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 1-242 5.01e-123

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 349.86  E-value: 5.01e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148   1 GAFSALLLTSGLVMWFHYNSYTLMTIGLLANTLTMYQWWRDIVREGTYQGHHTPIVQKGLRYGMILFIVSEVFFFAGFFW 80
Cdd:MTH00219  21 GSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLRIGMILFIVSEILFFFAFFW 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148  81 AFYHSSLAPTHDLGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGKRSNMNQALLITILLGIYFTILQAS 160
Cdd:MTH00219 101 AFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQQGLLFTILLGLYFTMLQGM 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148 161 EYFETPFSISDGVYGSTFFMATGFHGLHVIIGTTFLMVCLMRQLKYHFTSKHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 240
Cdd:MTH00219 181 EYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 260


                 ..
gi 270301148 241 GS 242
Cdd:MTH00219 261 GS 262
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 1-242 8.09e-113

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 324.10  E-value: 8.09e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148   1 GAFSALLLTSGLVMWFHYNSYTLMTIGLLANTLTMYQWWRDIVREGTYQGHHTPIVQKGLRYGMILFIVSEVFFFAGFFW 80
Cdd:MTH00009  18 GSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMILFIASEVMFFFAFFW 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148  81 AFYHSSLAPTHDLGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGKRSNMNQALLITILLGIYFTILQAS 160
Cdd:MTH00009  98 AFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALILTVLLGAYFTFLQAG 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148 161 EYFETPFSISDGVYGSTFFMATGFHGLHVIIGTTFLMVCLMRQLKYHFTSKHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 240
Cdd:MTH00009 178 EYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFVDVVWIFLYLCIYWW 257


                 ..
gi 270301148 241 GS 242
Cdd:MTH00009 258 GS 259
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 1-242 4.13e-111

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 319.78  E-value: 4.13e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148   1 GAFSALLLTSGLVMWFHYNSYTLMTIGLLANTLTMYQWWRDIVREGTYQGHHTPIVQKGLRYGMILFIVSEVFFFAGFFW 80
Cdd:MTH00024  20 GAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGMLLFILSEVLFFFSFFW 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148  81 AFYHSSLAPTHDLGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGKRSNMNQALLITILLGIYFTILQAS 160
Cdd:MTH00024 100 AFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFLTVFLGVLFTGLQAI 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148 161 EYFETPFSISDGVYGSTFFMATGFHGLHVIIGTTFLMVCLMRQLKYHFTSKHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 240
Cdd:MTH00024 180 EYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASWYWHFVDVVWLFLYLCIYWW 259


                 ..
gi 270301148 241 GS 242
Cdd:MTH00024 260 GS 261
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 1-242 3.98e-109

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 314.81  E-value: 3.98e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148   1 GAFSALLLTSGLVMWFHYNSYTLMTIGLLANTLTMYQWWRDIVREGTYQGHHTPIVQKGLRYGMILFIVSEVFFFAGFFW 80
Cdd:MTH00052  21 GGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGLKYGMILFIVSEVCLFFSFFW 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148  81 AFYHSSLAPTHDLGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGKRSNMNQALLITILLGIYFTILQAS 160
Cdd:MTH00052 101 AFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEAIIGLALTVALGLLFTGLQAM 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148 161 EYFETPFSISDGVYGSTFFMATGFHGLHVIIGTTFLMVCLMRQLKYHFTSKHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 240
Cdd:MTH00052 181 EYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAAWYWHFVDVVWLFLFIFMYWW 260


                 ..
gi 270301148 241 GS 242
Cdd:MTH00052 261 GS 262
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 1-242 8.76e-96

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 282.34  E-value: 8.76e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148   1 GAFSALLLTSGLVMWFHYNSYTLMTIGLLANTLTMYQWWRDIVREGTYQGHHTPIVQKGLRYGMILFIVSEVFFFAGFFW 80
Cdd:MTH00028  20 GASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLLFILSEVCLFFAFFW 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148  81 AFYHSSLAPTHDLGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGK------------------------ 136
Cdd:MTH00028 100 AFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTGnpaslekgtqgiegpnpsngappd 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148 137 ------------RSNMNQALLITILLGIYFTILQASEYFETPFSISDGVYGSTFFMATGFHGLHVIIGTTFLMVCLMRQL 204
Cdd:MTH00028 180 pqkgptfllsdfRTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVLVGTTFLIVCFIRLL 259

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 270301148 205 KYHFTSKHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS 242
Cdd:MTH00028 260 SNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWGS 297
PLN02194 PLN02194
cytochrome-c oxidase
 1-241 1.63e-82

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 247.27  E-value: 1.63e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148   1 GAFSALLLTSGLVMWFH--YNSYTLMTIGLLANTLTMYQWWRDIVREGTYQGHHTPIVQKGLRYGMILFIVSEVFFFAGF 78
Cdd:PLN02194  21 GSLGALATTVGGVMYMHpfQGGARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGPRYGSILFIVSEVMFFFAF 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148  79 FWAFYHSSLAPTHDLGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGKRSNMNQALLITILLGIYFTILQ 158
Cdd:PLN02194 101 FWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEKRAVYALVATVLLALVFTGFQ 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148 159 ASEYFETPFSISDGVYGSTFFMATGFHGLHVIIGTTFLMVCLMRQLKYHFTSKHHFGFEAAAWYWHFVDVVWLFLYVSIY 238
Cdd:PLN02194 181 GMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWYWHFVDVVWLFLFVSIY 260


                 ...
gi 270301148 239 WWG 241
Cdd:PLN02194 261 WWG 263
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
 3-242 2.77e-73

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 223.68  E-value: 2.77e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148   3 FSALLLTSGLVMWFHYNSYTLMTIGLLANTLTMYQWWRDIVREGtYQGHHTPIVQKGLRYGMILFIVSEVFFFAGFFWAF 82
Cdd:MTH00083  19 FSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMILFIFSEFMFFFSIFWTF 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148  83 YHSSLAPTHDLGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGKrSNMNQALLITILLGIYFTILQASEY 162
Cdd:MTH00083  98 FDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSN-KSCTNSLLLTCFLGLYFTSFQLMEY 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148 163 FETPFSISDGVYGSTFFMATGFHGLHVIIGTTFLMVCLMRQLKYHFTSKHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS 242
Cdd:MTH00083 177 KEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFVDVVWLFLFVFVYWWSY 256
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 52-240 3.26e-65

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: 200.51  E-value: 3.26e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148  52 HTPIVQKGLRYGMILFIVSEVFFFAGFFWAFYHSSLAPTHDLGgcwpptgiTPLNPLEVPLLNTSVLLASGVSITWAHHS 131
Cdd:cd00386    1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFG--------AGLDPLDLPLLNTNTLLLSGSSVTWAHAS 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148 132 LM--EGKRSNMNQALLITILLGIYFTILQASEYFETPFSISDGVYGSTFFMATGFHGLHVIIGTTFLMVCLMRQLKYHFT 209
Cdd:cd00386   73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152

                        170       180       190
                 ....*....|....*....|....*....|.
gi 270301148 210 SKHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 240
Cdd:cd00386  153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
51-240 9.01e-50

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 161.17  E-value: 9.01e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148  51 HHTPIVQKGLRYGMILFIVSEVFF-FAGFFWAFYHSSLAPthdlggcWPPTGITPLNPLeVPLLNTSVLLASGVSITWAH 129
Cdd:COG1845    7 PHAPERRSPGKLGMWLFLASEVMLfAALFAAYFVLRASAP-------DWPAGAELLDLP-LPLINTLLLLLSSFTVALAV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148 130 HSLMEGKRSNMNQALLITILLGIYFTILQASEY---FETPFSISDGVYGSTFFMATGFHGLHVIIGTTFLMVCLMRQLKY 206
Cdd:COG1845   79 RAARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRG 158

                        170       180       190
                 ....*....|....*....|....*....|....
gi 270301148 207 HFTSKHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 240
Cdd:COG1845  159 GFTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
NorE_like cd02862
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ...
 112-238 3.20e-21

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


Pssm-ID: 239213  Cd Length: 186  Bit Score: 87.29  E-value: 3.20e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148 112 LLNTSVLLASGVSITWAHHSLMEGKRSNMNQALLITILLGIYFTILQASEY---FETPFSISDGVYGSTFFMATGFHGLH 188
Cdd:cd02862   55 ALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYahkIAAGIDPDAGLFFTLYFLLTGFHLLH 134

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 270301148 189 VIIGTTFLMVCLMRQLKYHFTSKHHFGFEAAAWYWHFVDVVWLFLYVSIY 238
Cdd:cd02862  135 VLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVLFPLLY 184
Heme_Cu_Oxidase_III_2 cd02865
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 104-240 1.42e-17

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: 77.41  E-value: 1.42e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148 104 PLNPLEVPLLNTSVLLASGVSITWAHHSLMEGKRSNMNQALLITILLGIYFTILQASEYFETPFSISDG---VYGSTFFM 180
Cdd:cd02865   45 PLPLPNLLSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWHALNDAGYGPtsnPAGSFFYL 124

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148 181 ATGFHGLHVIIGTTFLMVCLMRQLKYHFTSKHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 240
Cdd:cd02865  125 LTGLHGLHVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVLLALLYGT 184
COX3 MTH00049
cytochrome c oxidase subunit III; Validated
 107-238 1.30e-16

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177124  Cd Length: 215  Bit Score: 75.72  E-value: 1.30e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148 107 PLEVPLLNTSVLLASGVSITwAHHSLMEGKRSNMNqaLLITILLGIYFTILQASEYFETPFSISDGVYGSTFFMATGFHG 186
Cdd:MTH00049  89 SLEIPFVGCFLLLGSSITVT-AYHHLLGWKYCDLF--LYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHF 165

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 270301148 187 LHVIIGTTFLMVCLMRQLKYHFTSKHhfgfEAAAWYWHFVDVVWLFLYVSIY 238
Cdd:MTH00049 166 SHVVLGVVGLSTLLLVGSSSFGVYRS----TVLTWYWHFVDYIWLLVYLIVY 213
Heme_Cu_Oxidase_III_1 cd02864
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 107-240 1.68e-16

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


Pssm-ID: 239215  Cd Length: 202  Bit Score: 75.23  E-value: 1.68e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148 107 PLEVPLLNTSVLLASGVSITWAHHSLMEGKRSNMNQALLITILLGIYFTILQASEYfeTPFSISDGV-----------YG 175
Cdd:cd02864   59 PLVLIAIMTFILITSSGTMAMAVNFGYRGNRKAAARLMLATALLGATFVGMQAFEW--TKLIVEEGVrpwgnpwgaaqFG 136

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 270301148 176 STFFMATGFHGLHVIIGTTFLMVCLMRQLKYHFTSKHHF-GFEAAAWYWHFVDVVWLFLYVSIYWW 240
Cdd:cd02864  137 ASFFMITGFHGTHVTIGVIYLIIIARKVWRGKYQRIGRYeIVEIAGLYWHFVDLVWVFIFAFFYLW 202
Ubiquinol_oxidase_III cd02863
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ...
 112-238 2.45e-16

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


Pssm-ID: 239214  Cd Length: 186  Bit Score: 74.20  E-value: 2.45e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148 112 LLNTSVLLASGVSITWAHHSLMEGKRSNMNQALLITILLGIYFTILQASEYFE---TPFSISDGVYGSTFFMATGFHGLH 188
Cdd:cd02863   54 FIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEFHHliaEGAGPDRSAFLSAFFTLVGTHGLH 133

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 270301148 189 VIIGtTFLMVCLMRQLKYH-FTSKHHFGFEAAAWYWHFVDVVWLFLYVSIY 238
Cdd:cd02863  134 VTFG-LIWILVMIIQLKKRgLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 101-241 3.54e-11

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


Pssm-ID: 131943  Cd Length: 190  Bit Score: 60.25  E-value: 3.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148  101 GITPLNPLEVPLL--NTSVLLASGVSITWAHHSLMEGKRSNMNQALLITILLG---IYFTILQASEYFETPFSISDGVYG 175
Cdd:TIGR02897  43 GKMPAELFELPLVliMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGagfVGFEIYEFAHYASEGVTPQIGSYW 122

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 270301148  176 STFFMATGFHGLHVIIGTTFLMVCLMRQLKYHFTSKHHFGFEAAAWYWHFVDVVWLFLYVSIYWWG 241
Cdd:TIGR02897 123 SSFFVLLGTHGCHVTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
PRK10663 PRK10663
cytochrome o ubiquinol oxidase subunit III; Provisional
 112-242 3.94e-08

cytochrome o ubiquinol oxidase subunit III; Provisional


Pssm-ID: 182628  Cd Length: 204  Bit Score: 52.09  E-value: 3.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270301148 112 LLNTSVLLASGVSITWAHHSLMEGKRSNMNQALLITILLGIYFTilqASEYFETPFSISDGvYG-------STFFMATGF 184
Cdd:PRK10663  70 LVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFI---GMEIYEFHHLIVEG-MGpdrsgflSAFFALVGT 145

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 270301148 185 HGLHVIIGTTFLMVCLMRQLKYHFTSKHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS 242
Cdd:PRK10663 146 HGLHVTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGA 203
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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