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Conserved domains on  [gi|1829764514|ref|YP_009743052|]
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cytochrome c oxidase subunit III (mitochondrion) [Eurytemora affinis]

Protein Classification

cytochrome c oxidase subunit 3( domain architecture ID 10009592)

cytochrome c oxidase subunit 3 is one of main transmembrane subunits of cytochrome c oxidase, the last enzyme in the respiratory electron transport chain of mitochondria or bacteria located in the mitochondrial or bacterial membrane

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 4-258 3.68e-149

cytochrome c oxidase subunit III; Provisional


:

Pssm-ID: 214439  Cd Length: 255  Bit Score: 416.50  E-value: 3.68e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514   4 HIQHPYHIVDESPWPLYGSLGGLYLTSGMISWFHLNSMFLFFIGLGLLGMVMFQWWRDVSREGAVQGLHSAIVELGLRWG 83
Cdd:MTH00155    1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514  84 MLLFITSEVFFFLSFFWAYFHASLAPNVELGGLWPPLGVVPFNPFGVPLLNTIILVSSGVSVTWAHHALMVGEYGQVKNS 163
Cdd:MTH00155   81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514 164 LGLTIVLGLYFTGLQALEYYEASFSFADSIYGSTFFIATGFHGLHVIVGTLFLLVCWVRHLKGEFSAAHHFGFEAAAWYW 243
Cdd:MTH00155  161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240

                         250
                  ....*....|....*
gi 1829764514 244 HFVDVVWLFLYLALY 258
Cdd:MTH00155  241 HFVDVVWLFLYISIY 255
 
Name Accession Description Interval E-value
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 4-258 3.68e-149

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 416.50  E-value: 3.68e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514   4 HIQHPYHIVDESPWPLYGSLGGLYLTSGMISWFHLNSMFLFFIGLGLLGMVMFQWWRDVSREGAVQGLHSAIVELGLRWG 83
Cdd:MTH00155    1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514  84 MLLFITSEVFFFLSFFWAYFHASLAPNVELGGLWPPLGVVPFNPFGVPLLNTIILVSSGVSVTWAHHALMVGEYGQVKNS 163
Cdd:MTH00155   81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514 164 LGLTIVLGLYFTGLQALEYYEASFSFADSIYGSTFFIATGFHGLHVIVGTLFLLVCWVRHLKGEFSAAHHFGFEAAAWYW 243
Cdd:MTH00155  161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240

                         250
                  ....*....|....*
gi 1829764514 244 HFVDVVWLFLYLALY 258
Cdd:MTH00155  241 HFVDVVWLFLYISIY 255
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 19-260 3.38e-123

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: 350.66  E-value: 3.38e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514  19 LYGSLGGLYLTSGMISWFHL-NSMFLFFIGLGLLGMVMFQWWRDVSREGAVQGLHSAIVELGLRWGMLLFITSEVFFFLS 97
Cdd:cd01665     1 ILGSFGLLLLALGLVLWMHGyGGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514  98 FFWAYFHASLAPNVELGGLWPPLGVVPFNPFGVPLLNTIILVSSGVSVTWAHHALMVGEYGQVKNSLGLTIVLGLYFTGL 177
Cdd:cd01665    81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514 178 QALEYYEASFSFADSIYGSTFFIATGFHGLHVIVGTLFLLVCWVRHLKGEFSAAHHFGFEAAAWYWHFVDVVWLFLYLAL 257
Cdd:cd01665   161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240


                  ...
gi 1829764514 258 YWW 260
Cdd:cd01665   241 YWW 243
COX3 pfam00510
Cytochrome c oxidase subunit III;
7-261 7.22e-116

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 332.45  E-value: 7.22e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514   7 HPYHIVDESPWPLYGSLGGLYLTSGMISWFHLNSMFLFFIGLGLLGM--VMFQWWRDVSREGAVQGLHSAIVELGLRWGM 84
Cdd:pfam00510   1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYSGNMTLFIIALFSLllTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514  85 LLFITSEVFFFLSFFWAYFHASLAPNVELGGLWPPLGVVPFNPFGVPLLNTIILVSSGVSVTWAHHALMVGEYGQVKNSL 164
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514 165 GLTIVLGLYFTGLQALEYYEASFSFADSIYGSTFFIATGFHGLHVIVGTLFLLVCWVRHLKGEFSAAHHFGFEAAAWYWH 244
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240

                         250
                  ....*....|....*..
gi 1829764514 245 FVDVVWLFLYLALYWWG 261
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWG 257
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
67-260 1.54e-53

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 171.57  E-value: 1.54e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514  67 AVQGLHSAIVELGLRWGMLLFITSEVFFFLSFFWAYFHASLApnvelgGLWPPLGVVPFNPfGVPLLNTIILVSSGVSVT 146
Cdd:COG1845     3 DVEAPHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS------APDWPAGAELLDL-PLPLINTLLLLLSSFTVA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514 147 WAHHALMVGEYGQVKNSLGLTIVLGLYFTGLQALEYYEAS---FSFADSIYGSTFFIATGFHGLHVIVGTLFLLVCWVRH 223
Cdd:COG1845    76 LAVRAARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHLIaegLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRA 155

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1829764514 224 LKGEFSAAHHFGFEAAAWYWHFVDVVWLFLYLALYWW 260
Cdd:COG1845   156 LRGGFTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 83-261 4.78e-07

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: 49.08  E-value: 4.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514  83 GMLLFITSEVFFFLSFFWAYFhaslapnvELGGLWPPLGVVPFNPFGVPLL--NTIILVSSGVSVTWAHHALMVGEYGQV 160
Cdd:TIGR02897  13 GFWIFLGAEIALFATLFATYL--------VLQHGGDYAGKMPAELFELPLVliMTFLLLFSSFTCGIAIYEMRKENQKLM 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514 161 KNSLGLTIVLGLYFTGLQALE---YYEASFSFADSIYGSTFFIATGFHGLHVIVGTLFLLVCWVRHLKGEFSAAHHFGFE 237
Cdd:TIGR02897  85 MFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCHVTLGIVWAICLLIQIQRRGLTPYTAPKVF 164

                         170       180
                  ....*....|....*....|....
gi 1829764514 238 AAAWYWHFVDVVWLFLYLALYWWG 261
Cdd:TIGR02897 165 IVSLYWHFLDVVWVFIFTAVYLIG 188
 
Name Accession Description Interval E-value
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 4-258 3.68e-149

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 416.50  E-value: 3.68e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514   4 HIQHPYHIVDESPWPLYGSLGGLYLTSGMISWFHLNSMFLFFIGLGLLGMVMFQWWRDVSREGAVQGLHSAIVELGLRWG 83
Cdd:MTH00155    1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514  84 MLLFITSEVFFFLSFFWAYFHASLAPNVELGGLWPPLGVVPFNPFGVPLLNTIILVSSGVSVTWAHHALMVGEYGQVKNS 163
Cdd:MTH00155   81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514 164 LGLTIVLGLYFTGLQALEYYEASFSFADSIYGSTFFIATGFHGLHVIVGTLFLLVCWVRHLKGEFSAAHHFGFEAAAWYW 243
Cdd:MTH00155  161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240

                         250
                  ....*....|....*
gi 1829764514 244 HFVDVVWLFLYLALY 258
Cdd:MTH00155  241 HFVDVVWLFLYISIY 255
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 4-261 3.32e-135

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 381.63  E-value: 3.32e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514   4 HIQHPYHIVDESPWPLYGSLGGLYLTSGMISWFHLNSMFLFFIGLGLLGMVMFQWWRDVSREGAVQGLHSAIVELGLRWG 83
Cdd:MTH00189    2 HQAHPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRYG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514  84 MLLFITSEVFFFLSFFWAYFHASLAPNVELGGLWPPLGVVPFNPFGVPLLNTIILVSSGVSVTWAHHALMVGEYGQVKNS 163
Cdd:MTH00189   82 MILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514 164 LGLTIVLGLYFTGLQALEYYEASFSFADSIYGSTFFIATGFHGLHVIVGTLFLLVCWVRHLKGEFSAAHHFGFEAAAWYW 243
Cdd:MTH00189  162 LTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWYW 241

                         250
                  ....*....|....*...
gi 1829764514 244 HFVDVVWLFLYLALYWWG 261
Cdd:MTH00189  242 HFVDVVWLFLYVSIYWWG 259
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 3-261 5.24e-135

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 381.22  E-value: 5.24e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514   3 NHIQHPYHIVDESPWPLYGSLGGLYLTSGMISWFHLNSMFLFFIGLGLLGMVMFQWWRDVSREGAVQGLHSAIVELGLRW 82
Cdd:MTH00118    2 THQAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514  83 GMLLFITSEVFFFLSFFWAYFHASLAPNVELGGLWPPLGVVPFNPFGVPLLNTIILVSSGVSVTWAHHALMVGEYGQVKN 162
Cdd:MTH00118   82 GMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514 163 SLGLTIVLGLYFTGLQALEYYEASFSFADSIYGSTFFIATGFHGLHVIVGTLFLLVCWVRHLKGEFSAAHHFGFEAAAWY 242
Cdd:MTH00118  162 ALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWY 241

                         250
                  ....*....|....*....
gi 1829764514 243 WHFVDVVWLFLYLALYWWG 261
Cdd:MTH00118  242 WHFVDVVWLFLYISIYWWG 260
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 7-262 4.52e-131

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 371.15  E-value: 4.52e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514   7 HPYHIVDESPWPLYGSLGGLYLTSGMISWFHLNSMFLFFIGLGLLGMVMFQWWRDVSREGAVQGLHSAIVELGLRWGMLL 86
Cdd:MTH00141    4 NPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFIL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514  87 FITSEVFFFLSFFWAYFHASLAPNVELGGLWPPLGVVPFNPFGVPLLNTIILVSSGVSVTWAHHALMVGEYGQVKNSLGL 166
Cdd:MTH00141   84 FIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514 167 TIVLGLYFTGLQALEYYEASFSFADSIYGSTFFIATGFHGLHVIVGTLFLLVCWVRHLKGEFSAAHHFGFEAAAWYWHFV 246
Cdd:MTH00141  164 TIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFV 243

                         250
                  ....*....|....*.
gi 1829764514 247 DVVWLFLYLALYWWGG 262
Cdd:MTH00141  244 DVVWLFLYLSIYWWGS 259
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 4-261 2.69e-126

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 359.08  E-value: 2.69e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514   4 HIQHPYHIVDESPWPLYGSLGGLYLTSGMISWFHLNSMFLFFIGLGLLGMVMFQWWRDVSREGAVQGLHSAIVELGLRWG 83
Cdd:MTH00130    3 HQAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRYG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514  84 MLLFITSEVFFFLSFFWAYFHASLAPNVELGGLWPPLGVVPFNPFGVPLLNTIILVSSGVSVTWAHHALMVGEYGQVKNS 163
Cdd:MTH00130   83 MILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQS 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514 164 LGLTIVLGLYFTGLQALEYYEASFSFADSIYGSTFFIATGFHGLHVIVGTLFLLVCWVRHLKGEFSAAHHFGFEAAAWYW 243
Cdd:MTH00130  163 LTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWYW 242

                         250
                  ....*....|....*...
gi 1829764514 244 HFVDVVWLFLYLALYWWG 261
Cdd:MTH00130  243 HFVDVVWLFLYISIYWWG 260
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 6-262 5.52e-125

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 355.96  E-value: 5.52e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514   6 QHPYHIVDESPWPLYGSLGGLYLTSGMISWFHLNSMFLFFIGLGLLGMVMFQWWRDVSREGAVQGLHSAIVELGLRWGML 85
Cdd:MTH00039    4 QHPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRYGMI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514  86 LFITSEVFFFLSFFWAYFHASLAPNVELGGLWPPLGVVPFNPFGVPLLNTIILVSSGVSVTWAHHALMVGEYGQVKNSLG 165
Cdd:MTH00039   84 LFITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQALF 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514 166 LTIVLGLYFTGLQALEYYEASFSFADSIYGSTFFIATGFHGLHVIVGTLFLLVCWVRHLKGEFSAAHHFGFEAAAWYWHF 245
Cdd:MTH00039  164 LTVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWYWHF 243

                         250
                  ....*....|....*..
gi 1829764514 246 VDVVWLFLYLALYWWGG 262
Cdd:MTH00039  244 VDVVWLFLYVCIYWWGS 260
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 4-261 6.15e-124

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 353.26  E-value: 6.15e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514   4 HIQHPYHIVDESPWPLYGSLGGLYLTSGMISWFHLNSMFLFFIGLGLLGMVMFQWWRDVSREGAVQGLHSAIVELGLRWG 83
Cdd:MTH00099    3 HQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRYG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514  84 MLLFITSEVFFFLSFFWAYFHASLAPNVELGGLWPPLGVVPFNPFGVPLLNTIILVSSGVSVTWAHHALMVGEYGQVKNS 163
Cdd:MTH00099   83 MILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514 164 LGLTIVLGLYFTGLQALEYYEASFSFADSIYGSTFFIATGFHGLHVIVGTLFLLVCWVRHLKGEFSAAHHFGFEAAAWYW 243
Cdd:MTH00099  163 LFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWYW 242

                         250
                  ....*....|....*...
gi 1829764514 244 HFVDVVWLFLYLALYWWG 261
Cdd:MTH00099  243 HFVDVVWLFLYVSIYWWG 260
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 19-260 3.38e-123

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: 350.66  E-value: 3.38e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514  19 LYGSLGGLYLTSGMISWFHL-NSMFLFFIGLGLLGMVMFQWWRDVSREGAVQGLHSAIVELGLRWGMLLFITSEVFFFLS 97
Cdd:cd01665     1 ILGSFGLLLLALGLVLWMHGyGGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514  98 FFWAYFHASLAPNVELGGLWPPLGVVPFNPFGVPLLNTIILVSSGVSVTWAHHALMVGEYGQVKNSLGLTIVLGLYFTGL 177
Cdd:cd01665    81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514 178 QALEYYEASFSFADSIYGSTFFIATGFHGLHVIVGTLFLLVCWVRHLKGEFSAAHHFGFEAAAWYWHFVDVVWLFLYLAL 257
Cdd:cd01665   161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240


                  ...
gi 1829764514 258 YWW 260
Cdd:cd01665   241 YWW 243
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 5-261 3.95e-122

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 348.70  E-value: 3.95e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514   5 IQHPYHIVDESPWPLYGSLGGLYLTSGMISWFHLNSMFLFFIGLGLLGMVMFQWWRDVSREGAVQGLHSAIVELGLRWGM 84
Cdd:MTH00219    5 QTNPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLRIGM 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514  85 LLFITSEVFFFLSFFWAYFHASLAPNVELGGLWPPLGVVPFNPFGVPLLNTIILVSSGVSVTWAHHALMVGEYGQVKNSL 164
Cdd:MTH00219   85 ILFIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQQGL 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514 165 GLTIVLGLYFTGLQALEYYEASFSFADSIYGSTFFIATGFHGLHVIVGTLFLLVCWVRHLKGEFSAAHHFGFEAAAWYWH 244
Cdd:MTH00219  165 LFTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAAWYWH 244

                         250
                  ....*....|....*..
gi 1829764514 245 FVDVVWLFLYLALYWWG 261
Cdd:MTH00219  245 FVDVVWLFLYVSIYWWG 261
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 4-261 2.70e-121

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 346.35  E-value: 2.70e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514   4 HIQHPYHIVDESPWPLYGSLGGLYLTSGMISWFHLNSMFLFFIGLGLLGMVMFQWWRDVSREGAVQGLHSAIVELGLRWG 83
Cdd:MTH00075    3 HQAHAFHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRYG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514  84 MLLFITSEVFFFLSFFWAYFHASLAPNVELGGLWPPLGVVPFNPFGVPLLNTIILVSSGVSVTWAHHALMVGEYGQVKNS 163
Cdd:MTH00075   83 MILFITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQS 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514 164 LGLTIVLGLYFTGLQALEYYEASFSFADSIYGSTFFIATGFHGLHVIVGTLFLLVCWVRHLKGEFSAAHHFGFEAAAWYW 243
Cdd:MTH00075  163 LALTIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWYW 242

                         250
                  ....*....|....*...
gi 1829764514 244 HFVDVVWLFLYLALYWWG 261
Cdd:MTH00075  243 HFVDVVWLFLYVSIYWWG 260
COX3 pfam00510
Cytochrome c oxidase subunit III;
7-261 7.22e-116

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 332.45  E-value: 7.22e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514   7 HPYHIVDESPWPLYGSLGGLYLTSGMISWFHLNSMFLFFIGLGLLGM--VMFQWWRDVSREGAVQGLHSAIVELGLRWGM 84
Cdd:pfam00510   1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYSGNMTLFIIALFSLllTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514  85 LLFITSEVFFFLSFFWAYFHASLAPNVELGGLWPPLGVVPFNPFGVPLLNTIILVSSGVSVTWAHHALMVGEYGQVKNSL 164
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514 165 GLTIVLGLYFTGLQALEYYEASFSFADSIYGSTFFIATGFHGLHVIVGTLFLLVCWVRHLKGEFSAAHHFGFEAAAWYWH 244
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240

                         250
                  ....*....|....*..
gi 1829764514 245 FVDVVWLFLYLALYWWG 261
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWG 257
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 7-261 3.50e-115

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 330.95  E-value: 3.50e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514   7 HPYHIVDESPWPLYGSLGGLYLTSGMISWFHLNSMFLFFIGLGLLGMVMFQWWRDVSREGAVQGLHSAIVELGLRWGMLL 86
Cdd:MTH00024    6 HPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGMLL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514  87 FITSEVFFFLSFFWAYFHASLAPNVELGGLWPPLGVVPFNPFGVPLLNTIILVSSGVSVTWAHHALMVGEYGQVKNSLGL 166
Cdd:MTH00024   86 FILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514 167 TIVLGLYFTGLQALEYYEASFSFADSIYGSTFFIATGFHGLHVIVGTLFLLVCWVRHLKGEFSAAHHFGFEAAAWYWHFV 246
Cdd:MTH00024  166 TVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASWYWHFV 245

                         250
                  ....*....|....*
gi 1829764514 247 DVVWLFLYLALYWWG 261
Cdd:MTH00024  246 DVVWLFLYLCIYWWG 260
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 1-261 7.56e-111

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 320.20  E-value: 7.56e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514   1 MSNHIQHPYHIVDESPWPLYGSLGGLYLTSGMISWFHLNSMFLFFIGLGLLGMVMFQWWRDVSREGAVQGLHSAIVELGL 80
Cdd:MTH00052    1 MMQQYYHPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514  81 RWGMLLFITSEVFFFLSFFWAYFHASLAPNVELGGLWPPLGVVPFNPFGVPLLNTIILVSSGVSVTWAHHALMVGEYGQV 160
Cdd:MTH00052   81 KYGMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514 161 KNSLGLTIVLGLYFTGLQALEYYEASFSFADSIYGSTFFIATGFHGLHVIVGTLFLLVCWVRHLKGEFSAAHHFGFEAAA 240
Cdd:MTH00052  161 IIGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAA 240

                         250       260
                  ....*....|....*....|.
gi 1829764514 241 WYWHFVDVVWLFLYLALYWWG 261
Cdd:MTH00052  241 WYWHFVDVVWLFLFIFMYWWG 261
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 5-261 6.08e-108

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 312.54  E-value: 6.08e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514   5 IQHPYHIVDESPWPLYGSLGGLYLTSGMISWFHLNSMFLFFIGLGLLGMVMFQWWRDVSREGAVQGLHSAIVELGLRWGM 84
Cdd:MTH00009    2 IRQPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514  85 LLFITSEVFFFLSFFWAYFHASLAPNVELGGLWPPLGVVPFNPFGVPLLNTIILVSSGVSVTWAHHALMVGEYGQVKNSL 164
Cdd:MTH00009   82 ILFIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQAL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514 165 GLTIVLGLYFTGLQALEYYEASFSFADSIYGSTFFIATGFHGLHVIVGTLFLLVCWVRHLKGEFSAAHHFGFEAAAWYWH 244
Cdd:MTH00009  162 ILTVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWH 241

                         250
                  ....*....|....*..
gi 1829764514 245 FVDVVWLFLYLALYWWG 261
Cdd:MTH00009  242 FVDVVWIFLYLCIYWWG 258
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 5-261 1.75e-97

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 287.35  E-value: 1.75e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514   5 IQHPYHIVDESPWPLYGSLGGLYLTSGMISWFHLNSMFLFFIGLGLLGMVMFQWWRDVSREGAVQGLHSAIVELGLRWGM 84
Cdd:MTH00028    4 VYHPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGM 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514  85 LLFITSEVFFFLSFFWAYFHASLAPNVELGGLWPPLGVVPFNPFGVPLLNTIILVSSGVSVTWAHHALmVGEYGQVKNSL 164
Cdd:MTH00028   84 LLFILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAI-IGTGNPASLEK 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514 165 G-------------------------------------LTIVLGLYFTGLQALEYYEASFSFADSIYGSTFFIATGFHGL 207
Cdd:MTH00028  163 GtqgiegpnpsngappdpqkgptfllsdfrtnavigllMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGL 242

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1829764514 208 HVIVGTLFLLVCWVRHLKGEFSAAHHFGFEAAAWYWHFVDVVWLFLYLALYWWG 261
Cdd:MTH00028  243 HVLVGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWG 296
PLN02194 PLN02194
cytochrome-c oxidase
 6-263 1.95e-87

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 260.75  E-value: 1.95e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514   6 QHPYHIVDESPWPLYGSLGGLYLTSGMISWFH--LNSMFLFFIGLGLLGMVMFQWWRDVSREGAVQGLHSAIVELGLRWG 83
Cdd:PLN02194    6 RHSYHLVDPSPWPISGSLGALATTVGGVMYMHpfQGGARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGPRYG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514  84 MLLFITSEVFFFLSFFWAYFHASLAPNVELGGLWPPLGVVPFNPFGVPLLNTIILVSSGVSVTWAHHALMVGEYGQVKNS 163
Cdd:PLN02194   86 SILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEKRAVYA 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514 164 LGLTIVLGLYFTGLQALEYYEASFSFADSIYGSTFFIATGFHGLHVIVGTLFLLVCWVRHLKGEFSAAHHFGFEAAAWYW 243
Cdd:PLN02194  166 LVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWYW 245

                         250       260
                  ....*....|....*....|
gi 1829764514 244 HFVDVVWLFLYLALYWWGGI 263
Cdd:PLN02194  246 HFVDVVWLFLFVSIYWWGGI 265
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
 7-261 1.19e-77

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 235.62  E-value: 1.19e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514   7 HPYHIVDESPWPLYGSLGGLYLTSGMISWFHLNSMFLFFIGLGLLGMVMFQWWRDVSREGaVQGLHSAIVELGLRWGMLL 86
Cdd:MTH00083    3 HNFHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMIL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514  87 FITSEVFFFLSFFWAYFHASLAPNVELGGLWPPLGVVPFNPFGVPLLNTIILVSSGVSVTWAHHALMVGEyGQVKNSLGL 166
Cdd:MTH00083   82 FIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSN-KSCTNSLLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514 167 TIVLGLYFTGLQALEYYEASFSFADSIYGSTFFIATGFHGLHVIVGTLFLLVCWVRHLKGEFSAAHHFGFEAAAWYWHFV 246
Cdd:MTH00083  161 TCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFV 240

                         250
                  ....*....|....*
gi 1829764514 247 DVVWLFLYLALYWWG 261
Cdd:MTH00083  241 DVVWLFLFVFVYWWS 255
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 72-260 8.57e-68

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: 207.83  E-value: 8.57e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514  72 HSAIVELGLRWGMLLFITSEVFFFLSFFWAYFHASLAPNVELGGlwpplgvvPFNPFGVPLLNTIILVSSGVSVTWAHHA 151
Cdd:cd00386     1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFGA--------GLDPLDLPLLNTNTLLLSGSSVTWAHAS 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514 152 LMV--GEYGQVKNSLGLTIVLGLYFTGLQALEYYEASFSFADSIYGSTFFIATGFHGLHVIVGTLFLLVCWVRHLKGEFS 229
Cdd:cd00386    73 LAArrGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1829764514 230 AAHHFGFEAAAWYWHFVDVVWLFLYLALYWW 260
Cdd:cd00386   153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
67-260 1.54e-53

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 171.57  E-value: 1.54e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514  67 AVQGLHSAIVELGLRWGMLLFITSEVFFFLSFFWAYFHASLApnvelgGLWPPLGVVPFNPfGVPLLNTIILVSSGVSVT 146
Cdd:COG1845     3 DVEAPHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS------APDWPAGAELLDL-PLPLINTLLLLLSSFTVA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514 147 WAHHALMVGEYGQVKNSLGLTIVLGLYFTGLQALEYYEAS---FSFADSIYGSTFFIATGFHGLHVIVGTLFLLVCWVRH 223
Cdd:COG1845    76 LAVRAARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHLIaegLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRA 155

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1829764514 224 LKGEFSAAHHFGFEAAAWYWHFVDVVWLFLYLALYWW 260
Cdd:COG1845   156 LRGGFTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
NorE_like cd02862
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ...
 83-258 1.66e-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: 101.93  E-value: 1.66e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514  83 GMLLFITSEVFFFLSFFWAYFHA-SLAPNVELGG---LWPPLGvvpfnpfgvpLLNTIILVSSGVSVTWAHHALMVGEYG 158
Cdd:cd02862    12 GMWVFILSELLAFGALFIAYAVYrALYPELFAAGsahLDLLLG----------ALNTLVLLTSSFTVALAVRAARAGRRR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514 159 QVKNSLGLTIVLGLYFTGLQALEYYEaSFSFADSIYGSTFF----IATGFHGLHVIVGTLFLLVCWVRHLKGEFSAAHHF 234
Cdd:cd02862    82 RARRWLAAAVLLGLVFLVIKYFEYAH-KIAAGIDPDAGLFFtlyfLLTGFHLLHVLIGLGILLWVAWRARRGRYSARDYE 160

                         170       180
                  ....*....|....*....|....
gi 1829764514 235 GFEAAAWYWHFVDVVWLFLYLALY 258
Cdd:cd02862   161 GVEAAALYWHMVDLVWIVLFPLLY 184
Heme_Cu_Oxidase_III_2 cd02865
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 79-260 2.37e-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: 2.37e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514  79 GLRWGMLLFITSEVFFFLSFFWAYFHASLAPNVELGglwpplgvVPFNPFGVPLLNTIILVSSGVSVTWAHHALMVGEYG 158
Cdd:cd02865     8 PGWWGLWVFMAVEGTLFALLISAYFMRMTSGDWQPG--------APLPLPNLLSLNTAVLAASSVAMQWARRAARRNRRV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514 159 QVKNSLGLTIVLGLYFTGLQALEYYEASFSF---ADSIYGSTFFIATGFHGLHVIVGTLFLLVCWVRHLKGEFSAAHHFG 235
Cdd:cd02865    80 LARLGLALAGALALAFLAGQLLAWHALNDAGygpTSNPAGSFFYLLTGLHGLHVIGGLVALAIVLAGLIRGHYGPRRRLP 159

                         170       180
                  ....*....|....*....|....*
gi 1829764514 236 FEAAAWYWHFVDVVWLFLYLALYWW 260
Cdd:cd02865   160 VELCALYWHFLLLVWLVLLALLYGT 184
Heme_Cu_Oxidase_III_1 cd02864
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 83-260 6.78e-17

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


Pssm-ID: 239215  Cd Length: 202  Bit Score: 76.77  E-value: 6.78e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514  83 GMLLFITSEVFFFLSFFWAYFHASLApNVELGGLWPPLGVVPFNPFGVPL----LNTIILVSSGVSVTWAHHALMVGEYG 158
Cdd:cd02864    12 MMWFFLLSDAFIFSSFLIAYMTARIS-TTEPWPLPSDVFALRIGHFNIPLvliaIMTFILITSSGTMAMAVNFGYRGNRK 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514 159 QVKNSLGLTIVLGLYFTGLQALEYYE---------ASFSFADSIYGSTFFIATGFHGLHVIVGTLFLLVCWVRHLKGEFS 229
Cdd:cd02864    91 AAARLMLATALLGATFVGMQAFEWTKliveegvrpWGNPWGAAQFGASFFMITGFHGTHVTIGVIYLIIIARKVWRGKYQ 170

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1829764514 230 AAHHFG-FEAAAWYWHFVDVVWLFLYLALYWW 260
Cdd:cd02864   171 RIGRYEiVEIAGLYWHFVDLVWVFIFAFFYLW 202
Ubiquinol_oxidase_III cd02863
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ...
 83-258 1.48e-14

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: 69.96  E-value: 1.48e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514  83 GMLLFITSEVFFFLSFFWAYF--HASLAPnvelgglwpplGVVPFNPFGVPL--LNTIILVSSGVSVTWAHHALMVGEYG 158
Cdd:cd02863    12 GFWIYLMSDCILFATLFATYAvlSGNTAG-----------GPPGHELFELPLvfIETFLLLLSSFTCGLAMIAMNKNNKK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514 159 QVKNSLGLTIVLGLYFTGLQALE---YYEASFSFADSIYGSTFFIATGFHGLHVIVGTLFLLVCWVRHLKGEFSAAHHFG 235
Cdd:cd02863    81 KVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLVGTHGLHVTFGLIWILVMIIQLKKRGLTPDTARR 160

                         170       180
                  ....*....|....*....|...
gi 1829764514 236 FEAAAWYWHFVDVVWLFLYLALY 258
Cdd:cd02863   161 LFCLSLFWHFLDIVWIFVFTVVY 183
COX3 MTH00049
cytochrome c oxidase subunit III; Validated
 86-258 1.60e-12

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177124  Cd Length: 215  Bit Score: 64.94  E-value: 1.60e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514  86 LFITSEVFFFLSFFWAYFHASLAPNVELGglwpplgvvpfNPFGVPLLNTIILVSSGVSVTWAHHaLMVGEYGQVknSLG 165
Cdd:MTH00049   59 LFILSEVIIFGSLLVCCLWFDDWSYISLS-----------SSLEIPFVGCFLLLGSSITVTAYHH-LLGWKYCDL--FLY 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514 166 LTIVLGLYFTGLQALEYYEASFSFADSIYGSTFFIATGFHGLHVIVGTLFLLVCWvrhLKGEFSAAHHFGfEAAAWYWHF 245
Cdd:MTH00049  125 LTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHFSHVVLGVVGLSTLL---LVGSSSFGVYRS-TVLTWYWHF 200

                         170
                  ....*....|...
gi 1829764514 246 VDVVWLFLYLALY 258
Cdd:MTH00049  201 VDYIWLLVYLIVY 213
PRK10663 PRK10663
cytochrome o ubiquinol oxidase subunit III; Provisional
 132-263 1.69e-08

cytochrome o ubiquinol oxidase subunit III; Provisional


Pssm-ID: 182628  Cd Length: 204  Bit Score: 53.25  E-value: 1.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514 132 LLNTIILVSSGVSVTWAHHALMVGEYGQVKNSLGLTIVLGLYFTGLQALEYY---EASFSFADSIYGSTFFIATGFHGLH 208
Cdd:PRK10663   70 LVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFHhliVEGMGPDRSGFLSAFFALVGTHGLH 149

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1829764514 209 VIVGTLFLLVCWVRHLKGEFSAAHHFGFEAAAWYWHFVDVVWLFLYLALYWWGGI 263
Cdd:PRK10663  150 VTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGAM 204
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 83-261 4.78e-07

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: 49.08  E-value: 4.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514  83 GMLLFITSEVFFFLSFFWAYFhaslapnvELGGLWPPLGVVPFNPFGVPLL--NTIILVSSGVSVTWAHHALMVGEYGQV 160
Cdd:TIGR02897  13 GFWIFLGAEIALFATLFATYL--------VLQHGGDYAGKMPAELFELPLVliMTFLLLFSSFTCGIAIYEMRKENQKLM 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829764514 161 KNSLGLTIVLGLYFTGLQALE---YYEASFSFADSIYGSTFFIATGFHGLHVIVGTLFLLVCWVRHLKGEFSAAHHFGFE 237
Cdd:TIGR02897  85 MFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCHVTLGIVWAICLLIQIQRRGLTPYTAPKVF 164

                         170       180
                  ....*....|....*....|....
gi 1829764514 238 AAAWYWHFVDVVWLFLYLALYWWG 261
Cdd:TIGR02897 165 IVSLYWHFLDVVWVFIFTAVYLIG 188
 
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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