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Conserved domains on  [gi|14141815|ref|NP_115279|]
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cytochrome c oxidase subunit III (mitochondrion) [Eudromia elegans]

Protein Classification

cytochrome c oxidase subunit 3( domain architecture ID 10791089)

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 MTH00118
cytochrome c oxidase subunit III; Provisional
 1-260 1.54e-175

cytochrome c oxidase subunit III; Provisional


:

Pssm-ID: 177179  Cd Length: 261  Bit Score: 483.68  E-value: 1.54e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815    1 MAHQAHSYHLVDPSPWPIFGAIAALLTTSGLIMWFHYNSTYLLTAGLLSMALVMLQWWRDIIRESTFQGHHTPTVQKGLR 80
Cdd:MTH00118   1 MTHQAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815   81 YGMILFITSEAFFFLGFFWAFFHSSLAPTPELGGLWPPTGIYPLNPLEVPLLNTAILLASGVTVTWAHHSITEGNRKQAT 160
Cdd:MTH00118  81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815  161 QALFLTILLGFYFTLLQAMEYHEASFSIADGVYGSTFFVATGFHGLHVIIGSTFLTVCLLRLIKFHFTSNHHFGFEAAAW 240
Cdd:MTH00118 161 QALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAW 240

                        250       260
                 ....*....|....*....|
gi 14141815  241 YWHFVDVIWLFLYMSIYWWG 260
Cdd:MTH00118 241 YWHFVDVVWLFLYISIYWWG 260
 
Name Accession Description Interval E-value
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 1-260 1.54e-175

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 483.68  E-value: 1.54e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815    1 MAHQAHSYHLVDPSPWPIFGAIAALLTTSGLIMWFHYNSTYLLTAGLLSMALVMLQWWRDIIRESTFQGHHTPTVQKGLR 80
Cdd:MTH00118   1 MTHQAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815   81 YGMILFITSEAFFFLGFFWAFFHSSLAPTPELGGLWPPTGIYPLNPLEVPLLNTAILLASGVTVTWAHHSITEGNRKQAT 160
Cdd:MTH00118  81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815  161 QALFLTILLGFYFTLLQAMEYHEASFSIADGVYGSTFFVATGFHGLHVIIGSTFLTVCLLRLIKFHFTSNHHFGFEAAAW 240
Cdd:MTH00118 161 QALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAW 240

                        250       260
                 ....*....|....*....|
gi 14141815  241 YWHFVDVIWLFLYMSIYWWG 260
Cdd:MTH00118 241 YWHFVDVVWLFLYISIYWWG 260
COX3 pfam00510
Cytochrome c oxidase subunit III;
6-260 2.24e-137

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 386.77  E-value: 2.24e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815     6 HSYHLVDPSPWPIFGAIAALLTTSGLIMWFHY--NSTYLLTAGLLSMALVMLQWWRDIIRESTFQGHHTPTVQKGLRYGM 83
Cdd:pfam00510   1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGysGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815    84 ILFITSEAFFFLGFFWAFFHSSLAPTPELGGLWPPTGIYPLNPLEVPLLNTAILLASGVTVTWAHHSITEGNRKQATQAL 163
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815   164 FLTILLGFYFTLLQAMEYHEASFSIADGVYGSTFFVATGFHGLHVIIGSTFLTVCLLRLIKFHFTSNHHFGFEAAAWYWH 243
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240

                         250
                  ....*....|....*..
gi 14141815   244 FVDVIWLFLYMSIYWWG 260
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWG 257
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 18-259 6.39e-129

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: 364.91  E-value: 6.39e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815  18 IFGAIAALLTTSGLIMWFH-YNSTYLLTAGLLSMALVMLQWWRDIIRESTFQGHHTPTVQKGLRYGMILFITSEAFFFLG 96
Cdd:cd01665   1 ILGSFGLLLLALGLVLWMHgYGGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815  97 FFWAFFHSSLAPTPELGGLWPPTGIYPLNPLEVPLLNTAILLASGVTVTWAHHSITEGNRKQATQALFLTILLGFYFTLL 176
Cdd:cd01665  81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815 177 QAMEYHEASFSIADGVYGSTFFVATGFHGLHVIIGSTFLTVCLLRLIKFHFTSNHHFGFEAAAWYWHFVDVIWLFLYMSI 256
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240


                ...
gi 14141815 257 YWW 259
Cdd:cd01665 241 YWW 243
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
70-259 7.40e-48

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 156.93  E-value: 7.40e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815  70 HHTPTVQKGLRYGMILFITSEAFFFLGFFWAFFHSSlAPTPELgglwpPTGIYPLNPLeVPLLNTAILLASGVTVTWAHH 149
Cdd:COG1845   7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLR-ASAPDW-----PAGAELLDLP-LPLINTLLLLLSSFTVALAVR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815 150 SITEGNRKQATQALFLTILLGFYFTLLQAMEYHEAS---FSIADGVYGSTFFVATGFHGLHVIIGSTFLTVCLLRLIKFH 226
Cdd:COG1845  80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHLIaegLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159

                       170       180       190
                ....*....|....*....|....*....|...
gi 14141815 227 FTSNHHFGFEAAAWYWHFVDVIWLFLYMSIYWW 259
Cdd:COG1845 160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
 
Name Accession Description Interval E-value
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 1-260 1.54e-175

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 483.68  E-value: 1.54e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815    1 MAHQAHSYHLVDPSPWPIFGAIAALLTTSGLIMWFHYNSTYLLTAGLLSMALVMLQWWRDIIRESTFQGHHTPTVQKGLR 80
Cdd:MTH00118   1 MTHQAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815   81 YGMILFITSEAFFFLGFFWAFFHSSLAPTPELGGLWPPTGIYPLNPLEVPLLNTAILLASGVTVTWAHHSITEGNRKQAT 160
Cdd:MTH00118  81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815  161 QALFLTILLGFYFTLLQAMEYHEASFSIADGVYGSTFFVATGFHGLHVIIGSTFLTVCLLRLIKFHFTSNHHFGFEAAAW 240
Cdd:MTH00118 161 QALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAW 240

                        250       260
                 ....*....|....*....|
gi 14141815  241 YWHFVDVIWLFLYMSIYWWG 260
Cdd:MTH00118 241 YWHFVDVVWLFLYISIYWWG 260
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 1-260 4.97e-158

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 439.16  E-value: 4.97e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815    1 MAHQAHSYHLVDPSPWPIFGAIAALLTTSGLIMWFHYNSTYLLTAGLLSMALVMLQWWRDIIRESTFQGHHTPTVQKGLR 80
Cdd:MTH00099   1 MTHQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815   81 YGMILFITSEAFFFLGFFWAFFHSSLAPTPELGGLWPPTGIYPLNPLEVPLLNTAILLASGVTVTWAHHSITEGNRKQAT 160
Cdd:MTH00099  81 YGMILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHML 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815  161 QALFLTILLGFYFTLLQAMEYHEASFSIADGVYGSTFFVATGFHGLHVIIGSTFLTVCLLRLIKFHFTSNHHFGFEAAAW 240
Cdd:MTH00099 161 QALFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAW 240

                        250       260
                 ....*....|....*....|
gi 14141815  241 YWHFVDVIWLFLYMSIYWWG 260
Cdd:MTH00099 241 YWHFVDVVWLFLYVSIYWWG 260
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 1-260 1.99e-157

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 437.66  E-value: 1.99e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815    1 MAHQAHSYHLVDPSPWPIFGAIAALLTTSGLIMWFHYNSTYLLTAGLLSMALVMLQWWRDIIRESTFQGHHTPTVQKGLR 80
Cdd:MTH00130   1 MAHQAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815   81 YGMILFITSEAFFFLGFFWAFFHSSLAPTPELGGLWPPTGIYPLNPLEVPLLNTAILLASGVTVTWAHHSITEGNRKQAT 160
Cdd:MTH00130  81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815  161 QALFLTILLGFYFTLLQAMEYHEASFSIADGVYGSTFFVATGFHGLHVIIGSTFLTVCLLRLIKFHFTSNHHFGFEAAAW 240
Cdd:MTH00130 161 QSLTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAW 240

                        250       260
                 ....*....|....*....|
gi 14141815  241 YWHFVDVIWLFLYMSIYWWG 260
Cdd:MTH00130 241 YWHFVDVVWLFLYISIYWWG 260
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 1-260 1.79e-153

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 427.62  E-value: 1.79e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815    1 MAHQAHSYHLVDPSPWPIFGAIAALLTTSGLIMWFHYNSTYLLTAGLLSMALVMLQWWRDIIRESTFQGHHTPTVQKGLR 80
Cdd:MTH00075   1 MAHQAHAFHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815   81 YGMILFITSEAFFFLGFFWAFFHSSLAPTPELGGLWPPTGIYPLNPLEVPLLNTAILLASGVTVTWAHHSITEGNRKQAT 160
Cdd:MTH00075  81 YGMILFITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815  161 QALFLTILLGFYFTLLQAMEYHEASFSIADGVYGSTFFVATGFHGLHVIIGSTFLTVCLLRLIKFHFTSNHHFGFEAAAW 240
Cdd:MTH00075 161 QSLALTIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAW 240

                        250       260
                 ....*....|....*....|
gi 14141815  241 YWHFVDVIWLFLYMSIYWWG 260
Cdd:MTH00075 241 YWHFVDVVWLFLYVSIYWWG 260
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 2-260 9.94e-153

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 425.93  E-value: 9.94e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815    2 AHQAHSYHLVDPSPWPIFGAIAALLTTSGLIMWFHYNSTYLLTAGLLSMALVMLQWWRDIIRESTFQGHHTPTVQKGLRY 81
Cdd:MTH00189   1 MHQAHPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815   82 GMILFITSEAFFFLGFFWAFFHSSLAPTPELGGLWPPTGIYPLNPLEVPLLNTAILLASGVTVTWAHHSITEGNRKQATQ 161
Cdd:MTH00189  81 GMILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815  162 ALFLTILLGFYFTLLQAMEYHEASFSIADGVYGSTFFVATGFHGLHVIIGSTFLTVCLLRLIKFHFTSNHHFGFEAAAWY 241
Cdd:MTH00189 161 ALTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWY 240

                        250
                 ....*....|....*....
gi 14141815  242 WHFVDVIWLFLYMSIYWWG 260
Cdd:MTH00189 241 WHFVDVVWLFLYVSIYWWG 259
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 3-257 3.44e-145

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 406.49  E-value: 3.44e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815    3 HQAHSYHLVDPSPWPIFGAIAALLTTSGLIMWFHYNSTYLLTAGLLSMALVMLQWWRDIIRESTFQGHHTPTVQKGLRYG 82
Cdd:MTH00155   1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815   83 MILFITSEAFFFLGFFWAFFHSSLAPTPELGGLWPPTGIYPLNPLEVPLLNTAILLASGVTVTWAHHSITEGNRKQATQA 162
Cdd:MTH00155  81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815  163 LFLTILLGFYFTLLQAMEYHEASFSIADGVYGSTFFVATGFHGLHVIIGSTFLTVCLLRLIKFHFTSNHHFGFEAAAWYW 242
Cdd:MTH00155 161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240

                        250
                 ....*....|....*
gi 14141815  243 HFVDVIWLFLYMSIY 257
Cdd:MTH00155 241 HFVDVVWLFLYISIY 255
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 6-260 1.34e-138

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 390.02  E-value: 1.34e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815    6 HSYHLVDPSPWPIFGAIAALLTTSGLIMWFHYNSTYLLTAGLLSMALVMLQWWRDIIRESTFQGHHTPTVQKGLRYGMIL 85
Cdd:MTH00141   4 NPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFIL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815   86 FITSEAFFFLGFFWAFFHSSLAPTPELGGLWPPTGIYPLNPLEVPLLNTAILLASGVTVTWAHHSITEGNRKQATQALFL 165
Cdd:MTH00141  84 FIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGL 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815  166 TILLGFYFTLLQAMEYHEASFSIADGVYGSTFFVATGFHGLHVIIGSTFLTVCLLRLIKFHFTSNHHFGFEAAAWYWHFV 245
Cdd:MTH00141 164 TIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFV 243

                        250
                 ....*....|....*
gi 14141815  246 DVIWLFLYMSIYWWG 260
Cdd:MTH00141 244 DVVWLFLYLSIYWWG 258
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 1-260 1.82e-137

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 387.16  E-value: 1.82e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815    1 MAHQaHSYHLVDPSPWPIFGAIAALLTTSGLIMWFHYNSTYLLTAGLLSMALVMLQWWRDIIRESTFQGHHTPTVQKGLR 80
Cdd:MTH00039   1 MTHQ-HPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815   81 YGMILFITSEAFFFLGFFWAFFHSSLAPTPELGGLWPPTGIYPLNPLEVPLLNTAILLASGVTVTWAHHSITEGNRKQAT 160
Cdd:MTH00039  80 YGMILFITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815  161 QALFLTILLGFYFTLLQAMEYHEASFSIADGVYGSTFFVATGFHGLHVIIGSTFLTVCLLRLIKFHFTSNHHFGFEAAAW 240
Cdd:MTH00039 160 QALFLTVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAW 239

                        250       260
                 ....*....|....*....|
gi 14141815  241 YWHFVDVIWLFLYMSIYWWG 260
Cdd:MTH00039 240 YWHFVDVVWLFLYVCIYWWG 259
COX3 pfam00510
Cytochrome c oxidase subunit III;
6-260 2.24e-137

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 386.77  E-value: 2.24e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815     6 HSYHLVDPSPWPIFGAIAALLTTSGLIMWFHY--NSTYLLTAGLLSMALVMLQWWRDIIRESTFQGHHTPTVQKGLRYGM 83
Cdd:pfam00510   1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGysGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815    84 ILFITSEAFFFLGFFWAFFHSSLAPTPELGGLWPPTGIYPLNPLEVPLLNTAILLASGVTVTWAHHSITEGNRKQATQAL 163
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815   164 FLTILLGFYFTLLQAMEYHEASFSIADGVYGSTFFVATGFHGLHVIIGSTFLTVCLLRLIKFHFTSNHHFGFEAAAWYWH 243
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240

                         250
                  ....*....|....*..
gi 14141815   244 FVDVIWLFLYMSIYWWG 260
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWG 257
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 18-259 6.39e-129

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: 364.91  E-value: 6.39e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815  18 IFGAIAALLTTSGLIMWFH-YNSTYLLTAGLLSMALVMLQWWRDIIRESTFQGHHTPTVQKGLRYGMILFITSEAFFFLG 96
Cdd:cd01665   1 ILGSFGLLLLALGLVLWMHgYGGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815  97 FFWAFFHSSLAPTPELGGLWPPTGIYPLNPLEVPLLNTAILLASGVTVTWAHHSITEGNRKQATQALFLTILLGFYFTLL 176
Cdd:cd01665  81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815 177 QAMEYHEASFSIADGVYGSTFFVATGFHGLHVIIGSTFLTVCLLRLIKFHFTSNHHFGFEAAAWYWHFVDVIWLFLYMSI 256
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240


                ...
gi 14141815 257 YWW 259
Cdd:cd01665 241 YWW 243
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 1-260 9.44e-128

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 362.57  E-value: 9.44e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815    1 MAHQAHSYHLVDPSPWPIFGAIAALLTTSGLIMWFHYNSTYLLTAGLLSMALVMLQWWRDIIRESTFQGHHTPTVQKGLR 80
Cdd:MTH00219   2 MFFQTNPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815   81 YGMILFITSEAFFFLGFFWAFFHSSLAPTPELGGLWPPTGIYPLNPLEVPLLNTAILLASGVTVTWAHHSITEGNRKQAT 160
Cdd:MTH00219  82 IGMILFIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQ 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815  161 QALFLTILLGFYFTLLQAMEYHEASFSIADGVYGSTFFVATGFHGLHVIIGSTFLTVCLLRLIKFHFTSNHHFGFEAAAW 240
Cdd:MTH00219 162 QGLLFTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAAW 241

                        250       260
                 ....*....|....*....|
gi 14141815  241 YWHFVDVIWLFLYMSIYWWG 260
Cdd:MTH00219 242 YWHFVDVVWLFLYVSIYWWG 261
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 1-260 3.77e-124

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 353.71  E-value: 3.77e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815    1 MAHQAHSYHLVDPSPWPIFGAIAALLTTSGLIMWFHYNSTYLLTAGLLSMALVMLQWWRDIIRESTFQGHHTPTVQKGLR 80
Cdd:MTH00052   2 MQQYYHPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGLK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815   81 YGMILFITSEAFFFLGFFWAFFHSSLAPTPELGGLWPPTGIYPLNPLEVPLLNTAILLASGVTVTWAHHSITEGNRKQAT 160
Cdd:MTH00052  82 YGMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEAI 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815  161 QALFLTILLGFYFTLLQAMEYHEASFSIADGVYGSTFFVATGFHGLHVIIGSTFLTVCLLRLIKFHFTSNHHFGFEAAAW 240
Cdd:MTH00052 162 IGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAAW 241

                        250       260
                 ....*....|....*....|
gi 14141815  241 YWHFVDVIWLFLYMSIYWWG 260
Cdd:MTH00052 242 YWHFVDVVWLFLFIFMYWWG 261
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 1-260 1.98e-123

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 351.75  E-value: 1.98e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815    1 MAHQAHSYHLVDPSPWPIFGAIAALLTTSGLIMWFHYNSTYLLTAGLLSMALVMLQWWRDIIRESTFQGHHTPTVQKGLR 80
Cdd:MTH00024   1 MSKLYHPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815   81 YGMILFITSEAFFFLGFFWAFFHSSLAPTPELGGLWPPTGIYPLNPLEVPLLNTAILLASGVTVTWAHHSITEGNRKQAT 160
Cdd:MTH00024  81 YGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815  161 QALFLTILLGFYFTLLQAMEYHEASFSIADGVYGSTFFVATGFHGLHVIIGSTFLTVCLLRLIKFHFTSNHHFGFEAAAW 240
Cdd:MTH00024 161 LGLFLTVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASW 240

                        250       260
                 ....*....|....*....|
gi 14141815  241 YWHFVDVIWLFLYMSIYWWG 260
Cdd:MTH00024 241 YWHFVDVVWLFLYLCIYWWG 260
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 6-260 8.02e-117

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 334.88  E-value: 8.02e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815    6 HSYHLVDPSPWPIFGAIAALLTTSGLIMWFHYNSTYLLTAGLLSMALVMLQWWRDIIRESTFQGHHTPTVQKGLRYGMIL 85
Cdd:MTH00009   4 QPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMIL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815   86 FITSEAFFFLGFFWAFFHSSLAPTPELGGLWPPTGIYPLNPLEVPLLNTAILLASGVTVTWAHHSITEGNRKQATQALFL 165
Cdd:MTH00009  84 FIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALIL 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815  166 TILLGFYFTLLQAMEYHEASFSIADGVYGSTFFVATGFHGLHVIIGSTFLTVCLLRLIKFHFTSNHHFGFEAAAWYWHFV 245
Cdd:MTH00009 164 TVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFV 243

                        250
                 ....*....|....*
gi 14141815  246 DVIWLFLYMSIYWWG 260
Cdd:MTH00009 244 DVVWIFLYLCIYWWG 258
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 6-260 2.88e-98

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 289.27  E-value: 2.88e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815    6 HSYHLVDPSPWPIFGAIAALLTTSGLIMWFHYNSTYLLTAGLLSMALVMLQWWRDIIRESTFQGHHTPTVQKGLRYGMIL 85
Cdd:MTH00028   6 HPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815   86 FITSEAFFFLGFFWAFFHSSLAPTPELGGLWPPTGIYPLNPLEVPLLNTAILLASGVTVTWAHHSITEGN---------- 155
Cdd:MTH00028  86 FILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTGnpaslekgtq 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815  156 --------------------------RKQATQALFLTILLGFYFTLLQAMEYHEASFSIADGVYGSTFFVATGFHGLHVI 209
Cdd:MTH00028 166 giegpnpsngappdpqkgptfllsdfRTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVL 245

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 14141815  210 IGSTFLTVCLLRLIKFHFTSNHHFGFEAAAWYWHFVDVIWLFLYMSIYWWG 260
Cdd:MTH00028 246 VGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWG 296
PLN02194 PLN02194
cytochrome-c oxidase
 4-260 9.00e-91

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 269.23  E-value: 9.00e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815    4 QAHSYHLVDPSPWPIFGAIAALLTTSGLIMWFH--YNSTYLLTAGLLSMALVMLQWWRDIIRESTFQGHHTPTVQKGLRY 81
Cdd:PLN02194   5 QRHSYHLVDPSPWPISGSLGALATTVGGVMYMHpfQGGARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGPRY 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815   82 GMILFITSEAFFFLGFFWAFFHSSLAPTPELGGLWPPTGIYPLNPLEVPLLNTAILLASGVTVTWAHHSITEGNRKQATQ 161
Cdd:PLN02194  85 GSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEKRAVY 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815  162 ALFLTILLGFYFTLLQAMEYHEASFSIADGVYGSTFFVATGFHGLHVIIGSTFLTVCLLRLIKFHFTSNHHFGFEAAAWY 241
Cdd:PLN02194 165 ALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWY 244

                        250
                 ....*....|....*....
gi 14141815  242 WHFVDVIWLFLYMSIYWWG 260
Cdd:PLN02194 245 WHFVDVVWLFLFVSIYWWG 263
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
 6-260 1.47e-78

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 237.55  E-value: 1.47e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815    6 HSYHLVDPSPWPIFGAIAALLTTSGLIMWFHYNSTYLLTAGLLSMALVMLQWWRDIIREStFQGHHTPTVQKGLRYGMIL 85
Cdd:MTH00083   3 HNFHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMIL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815   86 FITSEAFFFLGFFWAFFHSSLAPTPELGGLWPPTGIYPLNPLEVPLLNTAILLASGVTVTWAHHSITEGNrKQATQALFL 165
Cdd:MTH00083  82 FIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSN-KSCTNSLLL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815  166 TILLGFYFTLLQAMEYHEASFSIADGVYGSTFFVATGFHGLHVIIGSTFLTVCLLRLIKFHFTSNHHFGFEAAAWYWHFV 245
Cdd:MTH00083 161 TCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFV 240

                        250
                 ....*....|....*
gi 14141815  246 DVIWLFLYMSIYWWG 260
Cdd:MTH00083 241 DVVWLFLFVFVYWWS 255
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 71-259 1.26e-66

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: 204.74  E-value: 1.26e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815  71 HTPTVQKGLRYGMILFITSEAFFFLGFFWAFFHSSLAPTPELGGlwpptgiyPLNPLEVPLLNTAILLASGVTVTWAHHS 150
Cdd:cd00386   1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFGA--------GLDPLDLPLLNTNTLLLSGSSVTWAHAS 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815 151 IT--EGNRKQATQALFLTILLGFYFTLLQAMEYHEASFSIADGVYGSTFFVATGFHGLHVIIGSTFLTVCLLRLIKFHFT 228
Cdd:cd00386  73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152

                       170       180       190
                ....*....|....*....|....*....|.
gi 14141815 229 SNHHFGFEAAAWYWHFVDVIWLFLYMSIYWW 259
Cdd:cd00386 153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
70-259 7.40e-48

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 156.93  E-value: 7.40e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815  70 HHTPTVQKGLRYGMILFITSEAFFFLGFFWAFFHSSlAPTPELgglwpPTGIYPLNPLeVPLLNTAILLASGVTVTWAHH 149
Cdd:COG1845   7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLR-ASAPDW-----PAGAELLDLP-LPLINTLLLLLSSFTVALAVR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815 150 SITEGNRKQATQALFLTILLGFYFTLLQAMEYHEAS---FSIADGVYGSTFFVATGFHGLHVIIGSTFLTVCLLRLIKFH 226
Cdd:COG1845  80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHLIaegLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159

                       170       180       190
                ....*....|....*....|....*....|...
gi 14141815 227 FTSNHHFGFEAAAWYWHFVDVIWLFLYMSIYWW 259
Cdd:COG1845 160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
NorE_like cd02862
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ...
 131-257 5.15e-26

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: 100.39  E-value: 5.15e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815 131 LLNTAILLASGVTVTWAHHSITEGNRKQATQALFLTILLGFYFTLLQAMEYHE---ASFSIADGVYGSTFFVATGFHGLH 207
Cdd:cd02862  55 ALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYAHkiaAGIDPDAGLFFTLYFLLTGFHLLH 134

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 14141815 208 VIIGSTFLTVCLLRLIKFHFTSNHHFGFEAAAWYWHFVDVIWLFLYMSIY 257
Cdd:cd02862 135 VLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVLFPLLY 184
Heme_Cu_Oxidase_III_2 cd02865
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 123-259 8.05e-20

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: 83.96  E-value: 8.05e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815 123 PLNPLEVPLLNTAILLASGVTVTWAHHSITEGNRKQATQALFLTILLGFYFTLLQAMEYHEASFSI---ADGVYGSTFFV 199
Cdd:cd02865  45 PLPLPNLLSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWHALNDAGygpTSNPAGSFFYL 124

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815 200 ATGFHGLHVIIGSTFLTVCLLRLIKFHFTSNHHFGFEAAAWYWHFVDVIWLFLYMSIYWW 259
Cdd:cd02865 125 LTGLHGLHVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVLLALLYGT 184
Ubiquinol_oxidase_III cd02863
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ...
 131-257 2.15e-19

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: 83.06  E-value: 2.15e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815 131 LLNTAILLASGVTVTWAHHSITEGNRKQATQALFLTILLGFYFTLLQAMEYHE---ASFSIADGVYGSTFFVATGFHGLH 207
Cdd:cd02863  54 FIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEFHHliaEGAGPDRSAFLSAFFTLVGTHGLH 133

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 14141815 208 VIIGSTFLTVCLLRLIKFHFTSNHHFGFEAAAWYWHFVDVIWLFLYMSIY 257
Cdd:cd02863 134 VTFGLIWILVMIIQLKKRGLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
COX3 MTH00049
cytochrome c oxidase subunit III; Validated
 126-257 3.90e-18

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177124  Cd Length: 215  Bit Score: 80.35  E-value: 3.90e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815  126 PLEVPLLNTAILLASGVTVTWAHHSItegNRKQATQALFLTILLGFYFTLLQAMEYHEASFSIADGVYGSTFFVATGFHG 205
Cdd:MTH00049  89 SLEIPFVGCFLLLGSSITVTAYHHLL---GWKYCDLFLYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHF 165

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 14141815  206 LHVIIGStfltVCLLRLIKFHFTSNHHFGFEAAAWYWHFVDVIWLFLYMSIY 257
Cdd:MTH00049 166 SHVVLGV----VGLSTLLLVGSSSFGVYRSTVLTWYWHFVDYIWLLVYLIVY 213
Heme_Cu_Oxidase_III_1 cd02864
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 80-259 8.83e-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: 73.69  E-value: 8.83e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815  80 RYGMILFITSEAFFFLGFFWAFFHSSLApTPELGGLWPPTGIYPLNPLEVPL----LNTAILLASGVTVTWAHHSITEGN 155
Cdd:cd02864  10 KAMMWFFLLSDAFIFSSFLIAYMTARIS-TTEPWPLPSDVFALRIGHFNIPLvliaIMTFILITSSGTMAMAVNFGYRGN 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815 156 RKQATQALFLTILLGFYFTLLQAMEY-----HEASFSIAD----GVYGSTFFVATGFHGLHVIIGSTFLTVCLLRLIKFH 226
Cdd:cd02864  89 RKAAARLMLATALLGATFVGMQAFEWtklivEEGVRPWGNpwgaAQFGASFFMITGFHGTHVTIGVIYLIIIARKVWRGK 168

                       170       180       190
                ....*....|....*....|....*....|....
gi 14141815 227 FTSNHHFG-FEAAAWYWHFVDVIWLFLYMSIYWW 259
Cdd:cd02864 169 YQRIGRYEiVEIAGLYWHFVDLVWVFIFAFFYLW 202
PRK10663 PRK10663
cytochrome o ubiquinol oxidase subunit III; Provisional
 131-260 4.89e-10

cytochrome o ubiquinol oxidase subunit III; Provisional


Pssm-ID: 182628  Cd Length: 204  Bit Score: 57.48  E-value: 4.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141815  131 LLNTAILLASGVTVTWAHHSITEGNRKQATQALFLTILLGFYFTllqAMEYHEASFSIADGvYG-------STFFVATGF 203
Cdd:PRK10663  70 LVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFI---GMEIYEFHHLIVEG-MGpdrsgflSAFFALVGT 145

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 14141815  204 HGLHVIIGSTFLTVCLLRLIKFHFTSNHHFGFEAAAWYWHFVDVIWLFLYMSIYWWG 260
Cdd:PRK10663 146 HGLHVTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMG 202
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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