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Conserved domains on  [gi|1863124612|ref|YP_009860907|]
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cytochrome c oxidase subunit III (mitochondrion) [Nassarius siquijorensis]

Protein Classification

cytochrome c oxidase subunit 3( domain architecture ID 10791091)

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 MTH00141
cytochrome c oxidase subunit III; Provisional
 1-259 8.86e-156

cytochrome c oxidase subunit III; Provisional


:

Pssm-ID: 177199  Cd Length: 259  Bit Score: 433.55  E-value: 8.86e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612   1 MARNPFHLVEFSPWPLTGSMGALFLTSGLAGWFHGYGYISALLGVFLIVMTMIQWWRDVIREATYQGFHTIQVSKGLRWG 80
Cdd:MTH00141    1 MTRNPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612  81 MILFIVSEVCFFFAFFWAYFHSSLAPSMELGSCWPPAGITPLNPFEVPLLNTGVLLASGVTVTWAHHSLMEGDNPGGLQG 160
Cdd:MTH00141   81 FILFIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612 161 LLATVILGIYFTFLQACEYYEASFTIADGVYGSSFFVATGFHGLHVLIGSTFLLVCLIRVWLQHFSTGHHFGFEAAAWYW 240
Cdd:MTH00141  161 LGLTIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYW 240

                         250
                  ....*....|....*....
gi 1863124612 241 HFVDVVWLFLYLSIYWWGC 259
Cdd:MTH00141  241 HFVDVVWLFLYLSIYWWGS 259
 
Name Accession Description Interval E-value
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 1-259 8.86e-156

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 433.55  E-value: 8.86e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612   1 MARNPFHLVEFSPWPLTGSMGALFLTSGLAGWFHGYGYISALLGVFLIVMTMIQWWRDVIREATYQGFHTIQVSKGLRWG 80
Cdd:MTH00141    1 MTRNPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612  81 MILFIVSEVCFFFAFFWAYFHSSLAPSMELGSCWPPAGITPLNPFEVPLLNTGVLLASGVTVTWAHHSLMEGDNPGGLQG 160
Cdd:MTH00141   81 FILFIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612 161 LLATVILGIYFTFLQACEYYEASFTIADGVYGSSFFVATGFHGLHVLIGSTFLLVCLIRVWLQHFSTGHHFGFEAAAWYW 240
Cdd:MTH00141  161 LGLTIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYW 240

                         250
                  ....*....|....*....
gi 1863124612 241 HFVDVVWLFLYLSIYWWGC 259
Cdd:MTH00141  241 HFVDVVWLFLYLSIYWWGS 259
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 16-257 1.34e-121

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: 346.43  E-value: 1.34e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612  16 LTGSMGALFLTSGLAGWFHGY-GYISALLGVFLIVMTMIQWWRDVIREATYQGFHTIQVSKGLRWGMILFIVSEVCFFFA 94
Cdd:cd01665     1 ILGSFGLLLLALGLVLWMHGYgGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612  95 FFWAYFHSSLAPSMELGSCWPPAGITPLNPFEVPLLNTGVLLASGVTVTWAHHSLMEGDNPGGLQGLLATVILGIYFTFL 174
Cdd:cd01665    81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612 175 QACEYYEASFTIADGVYGSSFFVATGFHGLHVLIGSTFLLVCLIRVWLQHFSTGHHFGFEAAAWYWHFVDVVWLFLYLSI 254
Cdd:cd01665   161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240


                  ...
gi 1863124612 255 YWW 257
Cdd:cd01665   241 YWW 243
COX3 pfam00510
Cytochrome c oxidase subunit III;
5-258 3.25e-121

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 345.93  E-value: 3.25e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612   5 PFHLVEFSPWPLTGSMGALFLTSGLAGWFHGYGYISALLGVFLIVM--TMIQWWRDVIREATYQGFHTIQVSKGLRWGMI 82
Cdd:pfam00510   2 PFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYSGNMTLFIIALFSLllTMYLWFRDIIREGTFLGDHTFAVQKGLNLGMI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612  83 LFIVSEVCFFFAFFWAYFHSSLAPSMELGSCWPPAGITPLNPFEVPLLNTGVLLASGVTVTWAHHSLMEGDNPGGLQGLL 162
Cdd:pfam00510  82 LFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGLI 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612 163 ATVILGIYFTFLQACEYYEASFTIADGVYGSSFFVATGFHGLHVLIGSTFLLVCLIRVWLQHFSTGHHFGFEAAAWYWHF 242
Cdd:pfam00510 162 LTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWHF 241

                         250
                  ....*....|....*.
gi 1863124612 243 VDVVWLFLYLSIYWWG 258
Cdd:pfam00510 242 VDVVWLFLYVSVYWWG 257
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
69-257 5.53e-46

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 152.31  E-value: 5.53e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612  69 HTIQVSKGLRWGMILFIVSEVCF-FFAFFWAYFHSSLAPSMelgscwpPAGITPLNPFeVPLLNTGVLLASGVTVTWAHH 147
Cdd:COG1845     8 HAPERRSPGKLGMWLFLASEVMLfAALFAAYFVLRASAPDW-------PAGAELLDLP-LPLINTLLLLLSSFTVALAVR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612 148 SLMEGDNPGGLQGLLATVILGIYFTFLQACEYYEAS---FTIADGVYGSSFFVATGFHGLHVLIGSTFLLVCLIRVWLQH 224
Cdd:COG1845    80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHLIaegLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1863124612 225 FSTGHHFGFEAAAWYWHFVDVVWLFLYLSIYWW 257
Cdd:COG1845   160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 117-258 6.55e-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: 59.87  E-value: 6.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612 117 AGITPLNPFEVPLL--NTGVLLASGVTVTWAHHSLMEGDNPGGLQGLLATVILGIYFTFLQACE---YYEASFTIADGVY 191
Cdd:TIGR02897  42 AGKMPAELFELPLVliMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSY 121

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1863124612 192 GSSFFVATGFHGLHVLIGSTFLLVCLIRVWLQHFSTGHHFGFEAAAWYWHFVDVVWLFLYLSIYWWG 258
Cdd:TIGR02897 122 WSSFFVLLGTHGCHVTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
 
Name Accession Description Interval E-value
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 1-259 8.86e-156

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 433.55  E-value: 8.86e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612   1 MARNPFHLVEFSPWPLTGSMGALFLTSGLAGWFHGYGYISALLGVFLIVMTMIQWWRDVIREATYQGFHTIQVSKGLRWG 80
Cdd:MTH00141    1 MTRNPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612  81 MILFIVSEVCFFFAFFWAYFHSSLAPSMELGSCWPPAGITPLNPFEVPLLNTGVLLASGVTVTWAHHSLMEGDNPGGLQG 160
Cdd:MTH00141   81 FILFIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612 161 LLATVILGIYFTFLQACEYYEASFTIADGVYGSSFFVATGFHGLHVLIGSTFLLVCLIRVWLQHFSTGHHFGFEAAAWYW 240
Cdd:MTH00141  161 LGLTIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYW 240

                         250
                  ....*....|....*....
gi 1863124612 241 HFVDVVWLFLYLSIYWWGC 259
Cdd:MTH00141  241 HFVDVVWLFLYLSIYWWGS 259
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 1-255 7.19e-145

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 405.72  E-value: 7.19e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612   1 MARNPFHLVEFSPWPLTGSMGALFLTSGLAGWFHGYGYISALLGVFLIVMTMIQWWRDVIREATYQGFHTIQVSKGLRWG 80
Cdd:MTH00155    1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612  81 MILFIVSEVCFFFAFFWAYFHSSLAPSMELGSCWPPAGITPLNPFEVPLLNTGVLLASGVTVTWAHHSLMEGDNPGGLQG 160
Cdd:MTH00155   81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612 161 LLATVILGIYFTFLQACEYYEASFTIADGVYGSSFFVATGFHGLHVLIGSTFLLVCLIRVWLQHFSTGHHFGFEAAAWYW 240
Cdd:MTH00155  161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240

                         250
                  ....*....|....*
gi 1863124612 241 HFVDVVWLFLYLSIY 255
Cdd:MTH00155  241 HFVDVVWLFLYISIY 255
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 1-258 4.48e-143

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 401.27  E-value: 4.48e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612   1 MARNPFHLVEFSPWPLTGSMGALFLTSGLAGWFHGYGYISALLGVFLIVMTMIQWWRDVIREATYQGFHTIQVSKGLRWG 80
Cdd:MTH00189    2 HQAHPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRYG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612  81 MILFIVSEVCFFFAFFWAYFHSSLAPSMELGSCWPPAGITPLNPFEVPLLNTGVLLASGVTVTWAHHSLMEGDNPGGLQG 160
Cdd:MTH00189   82 MILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612 161 LLATVILGIYFTFLQACEYYEASFTIADGVYGSSFFVATGFHGLHVLIGSTFLLVCLIRVWLQHFSTGHHFGFEAAAWYW 240
Cdd:MTH00189  162 LTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWYW 241

                         250
                  ....*....|....*...
gi 1863124612 241 HFVDVVWLFLYLSIYWWG 258
Cdd:MTH00189  242 HFVDVVWLFLYVSIYWWG 259
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 5-258 1.64e-142

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 400.10  E-value: 1.64e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612   5 PFHLVEFSPWPLTGSMGALFLTSGLAGWFHGYGYISALLGVFLIVMTMIQWWRDVIREATYQGFHTIQVSKGLRWGMILF 84
Cdd:MTH00118    7 PYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRYGMILF 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612  85 IVSEVCFFFAFFWAYFHSSLAPSMELGSCWPPAGITPLNPFEVPLLNTGVLLASGVTVTWAHHSLMEGDNPGGLQGLLAT 164
Cdd:MTH00118   87 ITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQALTLT 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612 165 VILGIYFTFLQACEYYEASFTIADGVYGSSFFVATGFHGLHVLIGSTFLLVCLIRVWLQHFSTGHHFGFEAAAWYWHFVD 244
Cdd:MTH00118  167 ILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWYWHFVD 246

                         250
                  ....*....|....
gi 1863124612 245 VVWLFLYLSIYWWG 258
Cdd:MTH00118  247 VVWLFLYISIYWWG 260
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 1-258 5.90e-134

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 378.36  E-value: 5.90e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612   1 MARNPFHLVEFSPWPLTGSMGALFLTSGLAGWFHGYGYISALLGVFLIVMTMIQWWRDVIREATYQGFHTIQVSKGLRWG 80
Cdd:MTH00219    4 FQTNPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLRIG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612  81 MILFIVSEVCFFFAFFWAYFHSSLAPSMELGSCWPPAGITPLNPFEVPLLNTGVLLASGVTVTWAHHSLMEGDNPGGLQG 160
Cdd:MTH00219   84 MILFIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQQG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612 161 LLATVILGIYFTFLQACEYYEASFTIADGVYGSSFFVATGFHGLHVLIGSTFLLVCLIRVWLQHFSTGHHFGFEAAAWYW 240
Cdd:MTH00219  164 LLFTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAAWYW 243

                         250
                  ....*....|....*...
gi 1863124612 241 HFVDVVWLFLYLSIYWWG 258
Cdd:MTH00219  244 HFVDVVWLFLYVSIYWWG 261
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 1-258 2.18e-133

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 376.87  E-value: 2.18e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612   1 MARNPFHLVEFSPWPLTGSMGALFLTSGLAGWFHGYGYISALLGVFLIVMTMIQWWRDVIREATYQGFHTIQVSKGLRWG 80
Cdd:MTH00009    1 MIRQPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612  81 MILFIVSEVCFFFAFFWAYFHSSLAPSMELGSCWPPAGITPLNPFEVPLLNTGVLLASGVTVTWAHHSLMEGDNPGGLQG 160
Cdd:MTH00009   81 MILFIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612 161 LLATVILGIYFTFLQACEYYEASFTIADGVYGSSFFVATGFHGLHVLIGSTFLLVCLIRVWLQHFSTGHHFGFEAAAWYW 240
Cdd:MTH00009  161 LILTVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYW 240

                         250
                  ....*....|....*...
gi 1863124612 241 HFVDVVWLFLYLSIYWWG 258
Cdd:MTH00009  241 HFVDVVWIFLYLCIYWWG 258
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 5-258 3.15e-132

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 374.10  E-value: 3.15e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612   5 PFHLVEFSPWPLTGSMGALFLTSGLAGWFHGYGYISALLGVFLIVMTMIQWWRDVIREATYQGFHTIQVSKGLRWGMILF 84
Cdd:MTH00130    7 AYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRYGMILF 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612  85 IVSEVCFFFAFFWAYFHSSLAPSMELGSCWPPAGITPLNPFEVPLLNTGVLLASGVTVTWAHHSLMEGDNPGGLQGLLAT 164
Cdd:MTH00130   87 ITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQSLTLT 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612 165 VILGIYFTFLQACEYYEASFTIADGVYGSSFFVATGFHGLHVLIGSTFLLVCLIRVWLQHFSTGHHFGFEAAAWYWHFVD 244
Cdd:MTH00130  167 ILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWYWHFVD 246

                         250
                  ....*....|....
gi 1863124612 245 VVWLFLYLSIYWWG 258
Cdd:MTH00130  247 VVWLFLYISIYWWG 260
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 5-258 9.43e-132

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 372.91  E-value: 9.43e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612   5 PFHLVEFSPWPLTGSMGALFLTSGLAGWFHGYGYISALLGVFLIVMTMIQWWRDVIREATYQGFHTIQVSKGLRWGMILF 84
Cdd:MTH00039    6 PYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRYGMILF 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612  85 IVSEVCFFFAFFWAYFHSSLAPSMELGSCWPPAGITPLNPFEVPLLNTGVLLASGVTVTWAHHSLMEGDNPGGLQGLLAT 164
Cdd:MTH00039   86 ITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQALFLT 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612 165 VILGIYFTFLQACEYYEASFTIADGVYGSSFFVATGFHGLHVLIGSTFLLVCLIRVWLQHFSTGHHFGFEAAAWYWHFVD 244
Cdd:MTH00039  166 VLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWYWHFVD 245

                         250
                  ....*....|....
gi 1863124612 245 VVWLFLYLSIYWWG 258
Cdd:MTH00039  246 VVWLFLYVCIYWWG 259
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 5-258 3.37e-131

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 371.37  E-value: 3.37e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612   5 PFHLVEFSPWPLTGSMGALFLTSGLAGWFHGYGYISALLGVFLIVMTMIQWWRDVIREATYQGFHTIQVSKGLRWGMILF 84
Cdd:MTH00099    7 AYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRYGMILF 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612  85 IVSEVCFFFAFFWAYFHSSLAPSMELGSCWPPAGITPLNPFEVPLLNTGVLLASGVTVTWAHHSLMEGDNPGGLQGLLAT 164
Cdd:MTH00099   87 IISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQALFIT 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612 165 VILGIYFTFLQACEYYEASFTIADGVYGSSFFVATGFHGLHVLIGSTFLLVCLIRVWLQHFSTGHHFGFEAAAWYWHFVD 244
Cdd:MTH00099  167 ILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWYWHFVD 246

                         250
                  ....*....|....
gi 1863124612 245 VVWLFLYLSIYWWG 258
Cdd:MTH00099  247 VVWLFLYVSIYWWG 260
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 6-258 4.47e-131

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 371.00  E-value: 4.47e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612   6 FHLVEFSPWPLTGSMGALFLTSGLAGWFHGYGYISALLGVFLIVMTMIQWWRDVIREATYQGFHTIQVSKGLRWGMILFI 85
Cdd:MTH00075    8 FHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRYGMILFI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612  86 VSEVCFFFAFFWAYFHSSLAPSMELGSCWPPAGITPLNPFEVPLLNTGVLLASGVTVTWAHHSLMEGDNPGGLQGLLATV 165
Cdd:MTH00075   88 TSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQSLALTI 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612 166 ILGIYFTFLQACEYYEASFTIADGVYGSSFFVATGFHGLHVLIGSTFLLVCLIRVWLQHFSTGHHFGFEAAAWYWHFVDV 245
Cdd:MTH00075  168 ILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWYWHFVDV 247

                         250
                  ....*....|...
gi 1863124612 246 VWLFLYLSIYWWG 258
Cdd:MTH00075  248 VWLFLYVSIYWWG 260
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 16-257 1.34e-121

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: 346.43  E-value: 1.34e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612  16 LTGSMGALFLTSGLAGWFHGY-GYISALLGVFLIVMTMIQWWRDVIREATYQGFHTIQVSKGLRWGMILFIVSEVCFFFA 94
Cdd:cd01665     1 ILGSFGLLLLALGLVLWMHGYgGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612  95 FFWAYFHSSLAPSMELGSCWPPAGITPLNPFEVPLLNTGVLLASGVTVTWAHHSLMEGDNPGGLQGLLATVILGIYFTFL 174
Cdd:cd01665    81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612 175 QACEYYEASFTIADGVYGSSFFVATGFHGLHVLIGSTFLLVCLIRVWLQHFSTGHHFGFEAAAWYWHFVDVVWLFLYLSI 254
Cdd:cd01665   161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240


                  ...
gi 1863124612 255 YWW 257
Cdd:cd01665   241 YWW 243
COX3 pfam00510
Cytochrome c oxidase subunit III;
5-258 3.25e-121

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 345.93  E-value: 3.25e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612   5 PFHLVEFSPWPLTGSMGALFLTSGLAGWFHGYGYISALLGVFLIVM--TMIQWWRDVIREATYQGFHTIQVSKGLRWGMI 82
Cdd:pfam00510   2 PFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYSGNMTLFIIALFSLllTMYLWFRDIIREGTFLGDHTFAVQKGLNLGMI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612  83 LFIVSEVCFFFAFFWAYFHSSLAPSMELGSCWPPAGITPLNPFEVPLLNTGVLLASGVTVTWAHHSLMEGDNPGGLQGLL 162
Cdd:pfam00510  82 LFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGLI 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612 163 ATVILGIYFTFLQACEYYEASFTIADGVYGSSFFVATGFHGLHVLIGSTFLLVCLIRVWLQHFSTGHHFGFEAAAWYWHF 242
Cdd:pfam00510 162 LTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWHF 241

                         250
                  ....*....|....*.
gi 1863124612 243 VDVVWLFLYLSIYWWG 258
Cdd:pfam00510 242 VDVVWLFLYVSVYWWG 257
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 1-258 1.26e-115

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 332.10  E-value: 1.26e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612   1 MARNPFHLVEFSPWPLTGSMGALFLTSGLAGWFHGYGYISALLGVFLIVMTMIQWWRDVIREATYQGFHTIQVSKGLRWG 80
Cdd:MTH00024    3 KLYHPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612  81 MILFIVSEVCFFFAFFWAYFHSSLAPSMELGSCWPPAGITPLNPFEVPLLNTGVLLASGVTVTWAHHSLMEGDNPGGLQG 160
Cdd:MTH00024   83 MLLFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612 161 LLATVILGIYFTFLQACEYYEASFTIADGVYGSSFFVATGFHGLHVLIGSTFLLVCLIRVWLQHFSTGHHFGFEAAAWYW 240
Cdd:MTH00024  163 LFLTVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASWYW 242

                         250
                  ....*....|....*...
gi 1863124612 241 HFVDVVWLFLYLSIYWWG 258
Cdd:MTH00024  243 HFVDVVWLFLYLCIYWWG 260
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 5-258 1.19e-111

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 321.74  E-value: 1.19e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612   5 PFHLVEFSPWPLTGSMGALFLTSGLAGWFHgYGYISAL-LGVFLIVMTMIQWWRDVIREATYQGFHTIQVSKGLRWGMIL 83
Cdd:MTH00052    8 PYHLVDPSPWPYIGGCGALFTTVGGVMYFH-YSQSWVLiLGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGLKYGMIL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612  84 FIVSEVCFFFAFFWAYFHSSLAPSMELGSCWPPAGITPLNPFEVPLLNTGVLLASGVTVTWAHHSLMEGDNPGGLQGLLA 163
Cdd:MTH00052   87 FIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEAIIGLAL 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612 164 TVILGIYFTFLQACEYYEASFTIADGVYGSSFFVATGFHGLHVLIGSTFLLVCLIRVWLQHFSTGHHFGFEAAAWYWHFV 243
Cdd:MTH00052  167 TVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAAWYWHFV 246

                         250
                  ....*....|....*
gi 1863124612 244 DVVWLFLYLSIYWWG 258
Cdd:MTH00052  247 DVVWLFLFIFMYWWG 261
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 4-258 5.34e-99

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 291.20  E-value: 5.34e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612   4 NPFHLVEFSPWPLTGSMGALFLTSGLAGWFHGYGYISALLGVFLIVMTMIQWWRDVIREATYQGFHTIQVSKGLRWGMIL 83
Cdd:MTH00028    6 HPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612  84 FIVSEVCFFFAFFWAYFHSSLAPSMELGSCWPPAGITPLNPFEVPLLNTGVLLASGVTVTWAHHSLM------------- 150
Cdd:MTH00028   86 FILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIgtgnpaslekgtq 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612 151 --EGDNPGG---------------------LQGLLATVILGIYFTFLQACEYYEASFTIADGVYGSSFFVATGFHGLHVL 207
Cdd:MTH00028  166 giEGPNPSNgappdpqkgptfllsdfrtnaVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVL 245

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1863124612 208 IGSTFLLVCLIRVWLQHFSTGHHFGFEAAAWYWHFVDVVWLFLYLSIYWWG 258
Cdd:MTH00028  246 VGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWG 296
PLN02194 PLN02194
cytochrome-c oxidase
 3-258 1.87e-82

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 248.04  E-value: 1.87e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612   3 RNPFHLVEFSPWPLTGSMGALFLTSGLAGWFHGYGYISALL--GVFLIVMTMIQWWRDVIREATYQGFHTIQVSKGLRWG 80
Cdd:PLN02194    6 RHSYHLVDPSPWPISGSLGALATTVGGVMYMHPFQGGARLLslGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGPRYG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612  81 MILFIVSEVCFFFAFFWAYFHSSLAPSMELGSCWPPAGITPLNPFEVPLLNTGVLLASGVTVTWAHHSLMEGDNPGGLQG 160
Cdd:PLN02194   86 SILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEKRAVYA 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612 161 LLATVILGIYFTFLQACEYYEASFTIADGVYGSSFFVATGFHGLHVLIGSTFLLVCLIRVWLQHFSTGHHFGFEAAAWYW 240
Cdd:PLN02194  166 LVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWYW 245

                         250
                  ....*....|....*...
gi 1863124612 241 HFVDVVWLFLYLSIYWWG 258
Cdd:PLN02194  246 HFVDVVWLFLFVSIYWWG 263
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
 6-258 1.70e-69

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 214.43  E-value: 1.70e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612   6 FHLVEFSPWPLTGSMGALFLTSGLAGWFHGYGYISALLGVFLIVMTMIQWWRDVIREAtYQGFHTIQVSKGLRWGMILFI 85
Cdd:MTH00083    5 FHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMILFI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612  86 VSEVCFFFAFFWAYFHSSLAPSMELGSCWPPAGITPLNPFEVPLLNTGVLLASGVTVTWAHHSLMEgDNPGGLQGLLATV 165
Cdd:MTH00083   84 FSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCL-SNKSCTNSLLLTC 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612 166 ILGIYFTFLQACEYYEASFTIADGVYGSSFFVATGFHGLHVLIGSTFLLVCLIRVWLQHFSTGHHFGFEAAAWYWHFVDV 245
Cdd:MTH00083  163 FLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFVDV 242

                         250
                  ....*....|...
gi 1863124612 246 VWLFLYLSIYWWG 258
Cdd:MTH00083  243 VWLFLFVFVYWWS 255
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 69-257 1.58e-61

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: 191.65  E-value: 1.58e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612  69 HTIQVSKGLRWGMILFIVSEVCFFFAFFWAYFHSSLAPSMELGscwppagiTPLNPFEVPLLNTGVLLASGVTVTWAHHS 148
Cdd:cd00386     1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFG--------AGLDPLDLPLLNTNTLLLSGSSVTWAHAS 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612 149 LM--EGDNPGGLQGLLATVILGIYFTFLQACEYYEASFTIADGVYGSSFFVATGFHGLHVLIGSTFLLVCLIRVWLQHFS 226
Cdd:cd00386    73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1863124612 227 TGHHFGFEAAAWYWHFVDVVWLFLYLSIYWW 257
Cdd:cd00386   153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
69-257 5.53e-46

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 152.31  E-value: 5.53e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612  69 HTIQVSKGLRWGMILFIVSEVCF-FFAFFWAYFHSSLAPSMelgscwpPAGITPLNPFeVPLLNTGVLLASGVTVTWAHH 147
Cdd:COG1845     8 HAPERRSPGKLGMWLFLASEVMLfAALFAAYFVLRASAPDW-------PAGAELLDLP-LPLINTLLLLLSSFTVALAVR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612 148 SLMEGDNPGGLQGLLATVILGIYFTFLQACEYYEAS---FTIADGVYGSSFFVATGFHGLHVLIGSTFLLVCLIRVWLQH 224
Cdd:COG1845    80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHLIaegLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1863124612 225 FSTGHHFGFEAAAWYWHFVDVVWLFLYLSIYWW 257
Cdd:COG1845   160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
NorE_like cd02862
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ...
 129-255 2.98e-22

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: 90.37  E-value: 2.98e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612 129 LLNTGVLLASGVTVTWAHHSLMEGDNPGGLQGLLATVILGIYFTFLQACEYYE---ASFTIADGVYGSSFFVATGFHGLH 205
Cdd:cd02862    55 ALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYAHkiaAGIDPDAGLFFTLYFLLTGFHLLH 134

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1863124612 206 VLIGSTFLLVCLIRVWLQHFSTGHHFGFEAAAWYWHFVDVVWLFLYLSIY 255
Cdd:cd02862   135 VLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVLFPLLY 184
Heme_Cu_Oxidase_III_2 cd02865
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 76-257 2.11e-18

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


Pssm-ID: 239216  Cd Length: 184  Bit Score: 80.11  E-value: 2.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612  76 GLRWGMILFIVSEVCFFFAFFwayfhSSLAPSMELGSCWPPAGITPLNpfeVPLLNTGVLLASGVTVTWAHHSLMEGDNP 155
Cdd:cd02865     8 PGWWGLWVFMAVEGTLFALLI-----SAYFMRMTSGDWQPGAPLPLPN---LLSLNTAVLAASSVAMQWARRAARRNRRV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612 156 GGLQGLLATVILGIYFTFLQACEYYEASF---TIADGVYGSSFFVATGFHGLHVLIGSTFLLVCLIRVWLQHFSTGHHFG 232
Cdd:cd02865    80 LARLGLALAGALALAFLAGQLLAWHALNDagyGPTSNPAGSFFYLLTGLHGLHVIGGLVALAIVLAGLIRGHYGPRRRLP 159

                         170       180
                  ....*....|....*....|....*
gi 1863124612 233 FEAAAWYWHFVDVVWLFLYLSIYWW 257
Cdd:cd02865   160 VELCALYWHFLLLVWLVLLALLYGT 184
COX3 MTH00049
cytochrome c oxidase subunit III; Validated
 124-255 2.93e-16

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177124  Cd Length: 215  Bit Score: 74.95  E-value: 2.93e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612 124 PFEVPLLNTGVLLASGVTVTWAHHSLmeGDNPGGLQgLLATVILGIYFTFLQACEYYEASFTIADGVYGSSFFVATGFHG 203
Cdd:MTH00049   89 SLEIPFVGCFLLLGSSITVTAYHHLL--GWKYCDLF-LYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHF 165

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1863124612 204 LHVLIGStFLLVCLIRVWLQHFSTGHHfgfEAAAWYWHFVDVVWLFLYLSIY 255
Cdd:MTH00049  166 SHVVLGV-VGLSTLLLVGSSSFGVYRS---TVLTWYWHFVDYIWLLVYLIVY 213
Heme_Cu_Oxidase_III_1 cd02864
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 121-257 6.87e-15

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


Pssm-ID: 239215  Cd Length: 202  Bit Score: 70.99  E-value: 6.87e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612 121 PLNPFEVPL----LNTGVLLASGVTVTWAHHSLMEGDNPGGLQGLLATVILGIYFTFLQACEYYEASFTIADG------- 189
Cdd:cd02864    52 RIGHFNIPLvliaIMTFILITSSGTMAMAVNFGYRGNRKAAARLMLATALLGATFVGMQAFEWTKLIVEEGVRpwgnpwg 131

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1863124612 190 --VYGSSFFVATGFHGLHVLIGSTFLLVCLIRVWLQHF-STGHHFGFEAAAWYWHFVDVVWLFLYLSIYWW 257
Cdd:cd02864   132 aaQFGASFFMITGFHGTHVTIGVIYLIIIARKVWRGKYqRIGRYEIVEIAGLYWHFVDLVWVFIFAFFYLW 202
Ubiquinol_oxidase_III cd02863
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ...
 118-255 8.93e-15

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: 70.35  E-value: 8.93e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612 118 GITPLNPFEVPL--LNTGVLLASGVTVTWAHHSLMEGDNPGGLQGLLATVILGIYFTFLQACE---YYEASFTIADGVYG 192
Cdd:cd02863    41 GPPGHELFELPLvfIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFL 120

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1863124612 193 SSFFVATGFHGLHVLIGSTFLLVCLIRVWLQHFSTGHHFGFEAAAWYWHFVDVVWLFLYLSIY 255
Cdd:cd02863   121 SAFFTLVGTHGLHVTFGLIWILVMIIQLKKRGLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 117-258 6.55e-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: 59.87  E-value: 6.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612 117 AGITPLNPFEVPLL--NTGVLLASGVTVTWAHHSLMEGDNPGGLQGLLATVILGIYFTFLQACE---YYEASFTIADGVY 191
Cdd:TIGR02897  42 AGKMPAELFELPLVliMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSY 121

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1863124612 192 GSSFFVATGFHGLHVLIGSTFLLVCLIRVWLQHFSTGHHFGFEAAAWYWHFVDVVWLFLYLSIYWWG 258
Cdd:TIGR02897 122 WSSFFVLLGTHGCHVTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
PRK10663 PRK10663
cytochrome o ubiquinol oxidase subunit III; Provisional
 125-258 5.10e-07

cytochrome o ubiquinol oxidase subunit III; Provisional


Pssm-ID: 182628  Cd Length: 204  Bit Score: 49.01  E-value: 5.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863124612 125 FEVP--LLNTGVLLASGVTVTWAHHSLMEGDNPGGLQGLLATVILGIYFTflqACEYYEASFTIADGvYG-------SSF 195
Cdd:PRK10663   64 FELPfvLVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFI---GMEIYEFHHLIVEG-MGpdrsgflSAF 139

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1863124612 196 FVATGFHGLHVLIGSTFLLVCLIRVWLQHFSTGHHFGFEAAAWYWHFVDVVWLFLYLSIYWWG 258
Cdd:PRK10663  140 FALVGTHGLHVTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMG 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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