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Conserved domains on  [gi|938339317|ref|YP_009171518|]
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cytochrome c oxidase subunit 3 (mitochondrion) [Pseudothericles compressifrons]

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
 1-236 2.03e-152

cytochrome c oxidase subunit III; Provisional


:

Pssm-ID: 214439  Cd Length: 255  Bit Score: 423.82  E-value: 2.03e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317   1 MGAMALTSGLAKWFHTFNINLFMIGMTITLLTMYQWWRDVVREGTMQGLHTSVVSVGLRWGMILFIASEVLFFVSFFWAY 80
Cdd:MTH00155  20 IGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGMILFIVSEVFFFISFFWAF 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317  81 FNSSLAPAVEMGLAWPPMGIKPFNPMQVPLLNTVVLLSSGVTVTWAHHSLMEANHSQTTQGLLATVILGLYFTMLQAYEY 160
Cdd:MTH00155 100 FHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSLFFTIILGIYFTMLQAYEY 179

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 938339317 161 WEAPFTIADAVYGSSFFMATGFHGIHVIIGTSFLLMCLIRHYSNHFSPTHHFGFEAAAWYWHFVDVVWLFLYVSIY 236
Cdd:MTH00155 180 YEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYWHFVDVVWLFLYISIY 255
 
Name Accession Description Interval E-value
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 1-236 2.03e-152

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 423.82  E-value: 2.03e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317   1 MGAMALTSGLAKWFHTFNINLFMIGMTITLLTMYQWWRDVVREGTMQGLHTSVVSVGLRWGMILFIASEVLFFVSFFWAY 80
Cdd:MTH00155  20 IGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGMILFIVSEVFFFISFFWAF 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317  81 FNSSLAPAVEMGLAWPPMGIKPFNPMQVPLLNTVVLLSSGVTVTWAHHSLMEANHSQTTQGLLATVILGLYFTMLQAYEY 160
Cdd:MTH00155 100 FHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSLFFTIILGIYFTMLQAYEY 179

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 938339317 161 WEAPFTIADAVYGSSFFMATGFHGIHVIIGTSFLLMCLIRHYSNHFSPTHHFGFEAAAWYWHFVDVVWLFLYVSIY 236
Cdd:MTH00155 180 YEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYWHFVDVVWLFLYISIY 255
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-238 1.90e-124

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: 352.59  E-value: 1.90e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317   1 MGAMALTSGLAKWFHTF-NINLFMIGMTITLLTMYQWWRDVVREGTMQGLHTSVVSVGLRWGMILFIASEVLFFVSFFWA 79
Cdd:cd01665    5 FGLLLLALGLVLWMHGYgGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFSFFWA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317  80 YFNSSLAPAVEMGLAWPPMGIKPFNPMQVPLLNTVVLLSSGVTVTWAHHSLMEANHSQTTQGLLATVILGLYFTMLQAYE 159
Cdd:cd01665   85 FFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGLQAYE 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 938339317 160 YWEAPFTIADAVYGSSFFMATGFHGIHVIIGTSFLLMCLIRHYSNHFSPTHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 238
Cdd:cd01665  165 YYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFVYWW 243
COX3 pfam00510
Cytochrome c oxidase subunit III;
2-240 6.32e-119

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 339.39  E-value: 6.32e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317    2 GAMALTSGLAKWFHTF--NINLFMIGMTITLLTMYQWWRDVVREGTMQGLHTSVVSVGLRWGMILFIASEVLFFVSFFWA 79
Cdd:pfam00510  18 ALLLLTSGLVLWFHGYsgNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGMILFIISEVFFFLGIFWA 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317   80 YFNSSLAPAVEMGLAWPPMGIKPFNPMQVPLLNTVVLLSSGVTVTWAHHSLMEANHSQTTQGLLATVILGLYFTMLQAYE 159
Cdd:pfam00510  98 FFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGLILTILLAVYFTGLQAME 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317  160 YWEAPFTIADAVYGSSFFMATGFHGIHVIIGTSFLLMCLIRHYSNHFSPTHHFGFEAAAWYWHFVDVVWLFLYVSIYWWG 239
Cdd:pfam00510 178 YTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWHFVDVVWLFLYVSVYWWG 257


                  .
gi 938339317  240 S 240
Cdd:pfam00510 258 S 258
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
49-238 6.07e-55

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 174.65  E-value: 6.07e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317  49 LHTSVVSVGLRWGMILFIASEVLFFVSFFWAYFNSSlapaveMGLAWPPMGIKPFNPmQVPLLNTVVLLSSGVTVTWAHH 128
Cdd:COG1845    7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLR------ASAPDWPAGAELLDL-PLPLINTLLLLLSSFTVALAVR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 129 SLMEANHSQTTQGLLATVILGLYFTMLQAYEY---WEAPFTIADAVYGSSFFMATGFHGIHVIIGTSFLLMCLIRHYSNH 205
Cdd:COG1845   80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159

                        170       180       190
                 ....*....|....*....|....*....|...
gi 938339317 206 FSPTHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 238
Cdd:COG1845  160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 61-239 3.19e-10

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: 57.56  E-value: 3.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317   61 GMILFIASEVLFFVSFFWAYFNSSLApavemGLAWPPMGIKPFNpMQVPLLNTVVLLSSGVTVTWAHHSLMEANHSQTTQ 140
Cdd:TIGR02897  13 GFWIFLGAEIALFATLFATYLVLQHG-----GDYAGKMPAELFE-LPLVLIMTFLLLFSSFTCGIAIYEMRKENQKLMMF 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317  141 GLLATVILGLYFTMLQAYE---YWEAPFTIADAVYGSSFFMATGFHGIHVIIGTSFLLMCLIRHYSNHFSPTHHFGFEAA 217
Cdd:TIGR02897  87 WMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCHVTLGIVWAICLLIQIQRRGLTPYTAPKVFIV 166

                         170       180
                  ....*....|....*....|..
gi 938339317  218 AWYWHFVDVVWLFLYVSIYWWG 239
Cdd:TIGR02897 167 SLYWHFLDVVWVFIFTAVYLIG 188
 
Name Accession Description Interval E-value
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 1-236 2.03e-152

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 423.82  E-value: 2.03e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317   1 MGAMALTSGLAKWFHTFNINLFMIGMTITLLTMYQWWRDVVREGTMQGLHTSVVSVGLRWGMILFIASEVLFFVSFFWAY 80
Cdd:MTH00155  20 IGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGMILFIVSEVFFFISFFWAF 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317  81 FNSSLAPAVEMGLAWPPMGIKPFNPMQVPLLNTVVLLSSGVTVTWAHHSLMEANHSQTTQGLLATVILGLYFTMLQAYEY 160
Cdd:MTH00155 100 FHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSLFFTIILGIYFTMLQAYEY 179

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 938339317 161 WEAPFTIADAVYGSSFFMATGFHGIHVIIGTSFLLMCLIRHYSNHFSPTHHFGFEAAAWYWHFVDVVWLFLYVSIY 236
Cdd:MTH00155 180 YEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYWHFVDVVWLFLYISIY 255
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 1-240 2.65e-138

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 388.54  E-value: 2.65e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317   1 MGAMALTSGLAKWFHTFNINLFMIGMTITLLTMYQWWRDVVREGTMQGLHTSVVSVGLRWGMILFIASEVLFFVSFFWAY 80
Cdd:MTH00118  22 MAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRYGMILFITSEVFFFLGFFWAF 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317  81 FNSSLAPAVEMGLAWPPMGIKPFNPMQVPLLNTVVLLSSGVTVTWAHHSLMEANHSQTTQGLLATVILGLYFTMLQAYEY 160
Cdd:MTH00118 102 YHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQALTLTILLGLYFTALQAMEY 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 161 WEAPFTIADAVYGSSFFMATGFHGIHVIIGTSFLLMCLIRHYSNHFSPTHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS 240
Cdd:MTH00118 182 YEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWYWHFVDVVWLFLYISIYWWGS 261
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 1-240 3.08e-129

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 365.45  E-value: 3.08e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317   1 MGAMALTSGLAKWFHTFNINLFMIGMTITLLTMYQWWRDVVREGTMQGLHTSVVSVGLRWGMILFIASEVLFFVSFFWAY 80
Cdd:MTH00189  21 IAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRYGMILFITSEVFFFLGFFWAF 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317  81 FNSSLAPAVEMGLAWPPMGIKPFNPMQVPLLNTVVLLSSGVTVTWAHHSLMEANHSQTTQGLLATVILGLYFTMLQAYEY 160
Cdd:MTH00189 101 FHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQALTLTVILGVYFTLLQAMEY 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 161 WEAPFTIADAVYGSSFFMATGFHGIHVIIGTSFLLMCLIRHYSNHFSPTHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS 240
Cdd:MTH00189 181 YEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS 260
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 1-240 2.12e-128

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 363.44  E-value: 2.12e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317   1 MGAMALTSGLAKWFHTFNINLFMIGMTITLLTMYQWWRDVVREGTMQGLHTSVVSVGLRWGMILFIASEVLFFVSFFWAY 80
Cdd:MTH00141  20 IGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFILFIVSEVCFFFAFFWAY 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317  81 FNSSLAPAVEMGLAWPPMGIKPFNPMQVPLLNTVVLLSSGVTVTWAHHSLMEANHSQTTQGLLATVILGLYFTMLQAYEY 160
Cdd:MTH00141 100 FHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGLTIILGVYFTFLQAGEY 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 161 WEAPFTIADAVYGSSFFMATGFHGIHVIIGTSFLLMCLIRHYSNHFSPTHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS 240
Cdd:MTH00141 180 YEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFVDVVWLFLYLSIYWWGS 259
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 1-240 3.50e-126

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 357.89  E-value: 3.50e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317   1 MGAMALTSGLAKWFHTFNINLFMIGMTITLLTMYQWWRDVVREGTMQGLHTSVVSVGLRWGMILFIASEVLFFVSFFWAY 80
Cdd:MTH00039  21 IGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRYGMILFITSEVCFFFAFFWAF 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317  81 FNSSLAPAVEMGLAWPPMGIKPFNPMQVPLLNTVVLLSSGVTVTWAHHSLMEANHSQTTQGLLATVILGLYFTMLQAYEY 160
Cdd:MTH00039 101 FHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQALFLTVLLGLYFTALQAWEY 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 161 WEAPFTIADAVYGSSFFMATGFHGIHVIIGTSFLLMCLIRHYSNHFSPTHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS 240
Cdd:MTH00039 181 YDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWYWHFVDVVWLFLYVCIYWWGS 260
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 1-240 2.28e-125

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 355.96  E-value: 2.28e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317   1 MGAMALTSGLAKWFHTFNINLFMIGMTITLLTMYQWWRDVVREGTMQGLHTSVVSVGLRWGMILFIASEVLFFVSFFWAY 80
Cdd:MTH00099  22 LSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRYGMILFIISEVFFFAGFFWAF 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317  81 FNSSLAPAVEMGLAWPPMGIKPFNPMQVPLLNTVVLLSSGVTVTWAHHSLMEANHSQTTQGLLATVILGLYFTMLQAYEY 160
Cdd:MTH00099 102 YHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQALFITILLGLYFTLLQASEY 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 161 WEAPFTIADAVYGSSFFMATGFHGIHVIIGTSFLLMCLIRHYSNHFSPTHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS 240
Cdd:MTH00099 182 YEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS 261
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-238 1.90e-124

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: 352.59  E-value: 1.90e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317   1 MGAMALTSGLAKWFHTF-NINLFMIGMTITLLTMYQWWRDVVREGTMQGLHTSVVSVGLRWGMILFIASEVLFFVSFFWA 79
Cdd:cd01665    5 FGLLLLALGLVLWMHGYgGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFSFFWA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317  80 YFNSSLAPAVEMGLAWPPMGIKPFNPMQVPLLNTVVLLSSGVTVTWAHHSLMEANHSQTTQGLLATVILGLYFTMLQAYE 159
Cdd:cd01665   85 FFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGLQAYE 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 938339317 160 YWEAPFTIADAVYGSSFFMATGFHGIHVIIGTSFLLMCLIRHYSNHFSPTHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 238
Cdd:cd01665  165 YYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFVYWW 243
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 1-240 7.13e-124

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 352.17  E-value: 7.13e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317   1 MGAMALTSGLAKWFHTFNINLFMIGMTITLLTMYQWWRDVVREGTMQGLHTSVVSVGLRWGMILFIASEVLFFVSFFWAY 80
Cdd:MTH00219  23 LGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLRIGMILFIVSEILFFFAFFWAF 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317  81 FNSSLAPAVEMGLAWPPMGIKPFNPMQVPLLNTVVLLSSGVTVTWAHHSLMEANHSQTTQGLLATVILGLYFTMLQAYEY 160
Cdd:MTH00219 103 FHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQQGLLFTILLGLYFTMLQGMEY 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 161 WEAPFTIADAVYGSSFFMATGFHGIHVIIGTSFLLMCLIRHYSNHFSPTHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS 240
Cdd:MTH00219 183 LEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS 262
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 3-240 3.11e-123

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 350.58  E-value: 3.11e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317   3 AMALTSGLAKWFHTFNINLFMIGMTITLLTMYQWWRDVVREGTMQGLHTSVVSVGLRWGMILFIASEVLFFVSFFWAYFN 82
Cdd:MTH00075  24 ALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRYGMILFITSEVFFFLGFFWAFYN 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317  83 SSLAPAVEMGLAWPPMGIKPFNPMQVPLLNTVVLLSSGVTVTWAHHSLMEANHSQTTQGLLATVILGLYFTMLQAYEYWE 162
Cdd:MTH00075 104 SSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQSLALTIILGLYFTLLQAMEYYE 183

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 938339317 163 APFTIADAVYGSSFFMATGFHGIHVIIGTSFLLMCLIRHYSNHFSPTHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS 240
Cdd:MTH00075 184 APFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS 261
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 1-240 3.95e-123

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 350.22  E-value: 3.95e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317   1 MGAMALTSGLAKWFHTFNINLFMIGMTITLLTMYQWWRDVVREGTMQGLHTSVVSVGLRWGMILFIASEVLFFVSFFWAY 80
Cdd:MTH00130  22 VAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRYGMILFITSEVFFFLGFFWAF 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317  81 FNSSLAPAVEMGLAWPPMGIKPFNPMQVPLLNTVVLLSSGVTVTWAHHSLMEANHSQTTQGLLATVILGLYFTMLQAYEY 160
Cdd:MTH00130 102 YHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQSLTLTILLGFYFTFLQAMEY 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 161 WEAPFTIADAVYGSSFFMATGFHGIHVIIGTSFLLMCLIRHYSNHFSPTHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS 240
Cdd:MTH00130 182 YEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWYWHFVDVVWLFLYISIYWWGS 261
COX3 pfam00510
Cytochrome c oxidase subunit III;
2-240 6.32e-119

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 339.39  E-value: 6.32e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317    2 GAMALTSGLAKWFHTF--NINLFMIGMTITLLTMYQWWRDVVREGTMQGLHTSVVSVGLRWGMILFIASEVLFFVSFFWA 79
Cdd:pfam00510  18 ALLLLTSGLVLWFHGYsgNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGMILFIISEVFFFLGIFWA 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317   80 YFNSSLAPAVEMGLAWPPMGIKPFNPMQVPLLNTVVLLSSGVTVTWAHHSLMEANHSQTTQGLLATVILGLYFTMLQAYE 159
Cdd:pfam00510  98 FFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGLILTILLAVYFTGLQAME 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317  160 YWEAPFTIADAVYGSSFFMATGFHGIHVIIGTSFLLMCLIRHYSNHFSPTHHFGFEAAAWYWHFVDVVWLFLYVSIYWWG 239
Cdd:pfam00510 178 YTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWHFVDVVWLFLYVSVYWWG 257


                  .
gi 938339317  240 S 240
Cdd:pfam00510 258 S 258
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 1-240 1.34e-115

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 331.03  E-value: 1.34e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317   1 MGAMALTSGLAKWFHTFNINLFMIGMTITLLTMYQWWRDVVREGTMQGLHTSVVSVGLRWGMILFIASEVLFFVSFFWAY 80
Cdd:MTH00009  20 IGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMILFIASEVMFFFAFFWAF 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317  81 FNSSLAPAVEMGLAWPPMGIKPFNPMQVPLLNTVVLLSSGVTVTWAHHSLMEANHSQTTQGLLATVILGLYFTMLQAYEY 160
Cdd:MTH00009 100 FHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALILTVLLGAYFTFLQAGEY 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 161 WEAPFTIADAVYGSSFFMATGFHGIHVIIGTSFLLMCLIRHYSNHFSPTHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS 240
Cdd:MTH00009 180 IEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFVDVVWIFLYLCIYWWGS 259
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 1-240 3.98e-110

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 317.08  E-value: 3.98e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317   1 MGAMALTSGLAKWFHTFNINLFMIGMTITLLTMYQWWRDVVREGTMQGLHTSVVSVGLRWGMILFIASEVLFFVSFFWAY 80
Cdd:MTH00024  22 GGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGMLLFILSEVLFFFSFFWAF 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317  81 FNSSLAPAVEMGLAWPPMGIKPFNPMQVPLLNTVVLLSSGVTVTWAHHSLMEANHSQTTQGLLATVILGLYFTMLQAYEY 160
Cdd:MTH00024 102 FHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFLTVFLGVLFTGLQAIEY 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 161 WEAPFTIADAVYGSSFFMATGFHGIHVIIGTSFLLMCLIRHYSNHFSPTHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS 240
Cdd:MTH00024 182 YEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASWYWHFVDVVWLFLYLCIYWWGS 261
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 2-240 3.62e-101

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 294.39  E-value: 3.62e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317   2 GAMALTSGLAKWFHTFNINLFMIGMTITLLTMYQWWRDVVREGTMQGLHTSVVSVGLRWGMILFIASEVLFFVSFFWAYF 81
Cdd:MTH00052  24 GALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGLKYGMILFIVSEVCLFFSFFWAFF 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317  82 NSSLAPAVEMGLAWPPMGIKPFNPMQVPLLNTVVLLSSGVTVTWAHHSLMEANHSQTTQGLLATVILGLYFTMLQAYEYW 161
Cdd:MTH00052 104 HSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEAIIGLALTVALGLLFTGLQAMEYY 183

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 938339317 162 EAPFTIADAVYGSSFFMATGFHGIHVIIGTSFLLMCLIRHYSNHFSPTHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS 240
Cdd:MTH00052 184 EAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAAWYWHFVDVVWLFLFIFMYWWGS 262
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 2-240 1.79e-89

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 266.16  E-value: 1.79e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317   2 GAMALTSGLAKWFHTFNINLFMIGMTITLLTMYQWWRDVVREGTMQGLHTSVVSVGLRWGMILFIASEVLFFVSFFWAYF 81
Cdd:MTH00028  23 GAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLLFILSEVCLFFAFFWAFF 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317  82 NSSLAPAVEMGLAWPPMGIKPFNPMQVPLLNTVVLLSSGVTVTWAHHSLMEANHSQTTQ--------------------- 140
Cdd:MTH00028 103 HSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTGNPASLEkgtqgiegpnpsngappdpqk 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 141 ---------------GLLATVILGLYFTMLQAYEYWEAPFTIADAVYGSSFFMATGFHGIHVIIGTSFLLMCLIRHYSNH 205
Cdd:MTH00028 183 gptfllsdfrtnaviGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVLVGTTFLIVCFIRLLSNQ 262

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 938339317 206 FSPTHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS 240
Cdd:MTH00028 263 FTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWGS 297
PLN02194 PLN02194
cytochrome-c oxidase
 1-239 8.39e-83

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 248.04  E-value: 8.39e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317   1 MGAMALTSGLAKWFHTFN--INLFMIGMTITLLTMYQWWRDVVREGTMQGLHTSVVSVGLRWGMILFIASEVLFFVSFFW 78
Cdd:PLN02194  23 LGALATTVGGVMYMHPFQggARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGPRYGSILFIVSEVMFFFAFFW 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317  79 AYFNSSLAPAVEMGLAWPPMGIKPFNPMQVPLLNTVVLLSSGVTVTWAHHSLMEANHSQTTQGLLATVILGLYFTMLQAY 158
Cdd:PLN02194 103 ASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEKRAVYALVATVLLALVFTGFQGM 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 159 EYWEAPFTIADAVYGSSFFMATGFHGIHVIIGTSFLLMCLIRHYSNHFSPTHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 238
Cdd:PLN02194 183 EYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWYWHFVDVVWLFLFVSIYWW 262


                 .
gi 938339317 239 G 239
Cdd:PLN02194 263 G 263
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
 1-240 1.22e-68

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 211.74  E-value: 1.22e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317   1 MGAMALTSGLAKWFHTFNINLFMIGMTITLLTMYQWWRDVVREGtMQGLHTSVVSVGLRWGMILFIASEVLFFVSFFWAY 80
Cdd:MTH00083  19 FSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMILFIFSEFMFFFSIFWTF 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317  81 FNSSLAPAVEMGLAWPPMGIKPFNPMQVPLLNTVVLLSSGVTVTWAHHSLMeANHSQTTQGLLATVILGLYFTMLQAYEY 160
Cdd:MTH00083  98 FDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLC-LSNKSCTNSLLLTCFLGLYFTSFQLMEY 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 161 WEAPFTIADAVYGSSFFMATGFHGIHVIIGTSFLLMCLIRHYSNHFSPTHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS 240
Cdd:MTH00083 177 KEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFVDVVWLFLFVFVYWWSY 256
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 50-238 6.48e-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: 207.06  E-value: 6.48e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317  50 HTSVVSVGLRWGMILFIASEVLFFVSFFWAYFNSSLAPAVEMGLawppmgikPFNPMQVPLLNTVVLLSSGVTVTWAHHS 129
Cdd:cd00386    1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFGA--------GLDPLDLPLLNTNTLLLSGSSVTWAHAS 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 130 LMEANHS--QTTQGLLATVILGLYFTMLQAYEYWEAPFTIADAVYGSSFFMATGFHGIHVIIGTSFLLMCLIRHYSNHFS 207
Cdd:cd00386   73 LAARRGNrkKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152

                        170       180       190
                 ....*....|....*....|....*....|.
gi 938339317 208 PTHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 238
Cdd:cd00386  153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
49-238 6.07e-55

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 174.65  E-value: 6.07e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317  49 LHTSVVSVGLRWGMILFIASEVLFFVSFFWAYFNSSlapaveMGLAWPPMGIKPFNPmQVPLLNTVVLLSSGVTVTWAHH 128
Cdd:COG1845    7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLR------ASAPDWPAGAELLDL-PLPLINTLLLLLSSFTVALAVR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 129 SLMEANHSQTTQGLLATVILGLYFTMLQAYEY---WEAPFTIADAVYGSSFFMATGFHGIHVIIGTSFLLMCLIRHYSNH 205
Cdd:COG1845   80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159

                        170       180       190
                 ....*....|....*....|....*....|...
gi 938339317 206 FSPTHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 238
Cdd:COG1845  160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
NorE_like cd02862
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ...
 61-236 1.01e-23

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: 93.84  E-value: 1.01e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317  61 GMILFIASEVLFFVSFFWAYF-NSSLAPAVEMGLAW---PPMGikpfnpmqvpLLNTVVLLSSGVTVTWAHHSLMEANHS 136
Cdd:cd02862   12 GMWVFILSELLAFGALFIAYAvYRALYPELFAAGSAhldLLLG----------ALNTLVLLTSSFTVALAVRAARAGRRR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 137 QTTQGLLATVILGLYFTMLQAYEYwEAPFTIADAVYGSSFFMA----TGFHGIHVIIGTSFLLMCLIRHYSNHFSPTHHF 212
Cdd:cd02862   82 RARRWLAAAVLLGLVFLVIKYFEY-AHKIAAGIDPDAGLFFTLyfllTGFHLLHVLIGLGILLWVAWRARRGRYSARDYE 160

                        170       180
                 ....*....|....*....|....
gi 938339317 213 GFEAAAWYWHFVDVVWLFLYVSIY 236
Cdd:cd02862  161 GVEAAALYWHMVDLVWIVLFPLLY 184
Heme_Cu_Oxidase_III_2 cd02865
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 57-238 6.55e-20

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


Pssm-ID: 239216  Cd Length: 184  Bit Score: 83.96  E-value: 6.55e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317  57 GLRWGMILFIASEVLFFVSFFWAYFNSSLapaveMGLAWPPmgiKPFNPMQVPLLNTVVLLSSGVTVTWAHHSLMEANHS 136
Cdd:cd02865    8 PGWWGLWVFMAVEGTLFALLISAYFMRMT-----SGDWQPG---APLPLPNLLSLNTAVLAASSVAMQWARRAARRNRRV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 137 QTTQGLLATVILGLYFTMLQAYEYWEAPF---TIADAVYGSSFFMATGFHGIHVIIGTSFLLMCLIRHYSNHFSPTHHFG 213
Cdd:cd02865   80 LARLGLALAGALALAFLAGQLLAWHALNDagyGPTSNPAGSFFYLLTGLHGLHVIGGLVALAIVLAGLIRGHYGPRRRLP 159

                        170       180
                 ....*....|....*....|....*
gi 938339317 214 FEAAAWYWHFVDVVWLFLYVSIYWW 238
Cdd:cd02865  160 VELCALYWHFLLLVWLVLLALLYGT 184
Heme_Cu_Oxidase_III_1 cd02864
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 61-238 1.01e-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: 78.31  E-value: 1.01e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317  61 GMILFIASEVLFFVSFFWAYFNSSLAPAVEMGLAWPPMGIkPFNPMQVPL----LNTVVLLSSGVTVTWAHHSLMEANHS 136
Cdd:cd02864   12 MMWFFLLSDAFIFSSFLIAYMTARISTTEPWPLPSDVFAL-RIGHFNIPLvliaIMTFILITSSGTMAMAVNFGYRGNRK 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 137 QTTQGLLATVILGLYFTMLQAYEY-----------WEAPFTIAdaVYGSSFFMATGFHGIHVIIGTSFLLMCLIRHYSNH 205
Cdd:cd02864   91 AAARLMLATALLGATFVGMQAFEWtkliveegvrpWGNPWGAA--QFGASFFMITGFHGTHVTIGVIYLIIIARKVWRGK 168

                        170       180       190
                 ....*....|....*....|....*....|....
gi 938339317 206 FSPTHHF-GFEAAAWYWHFVDVVWLFLYVSIYWW 238
Cdd:cd02864  169 YQRIGRYeIVEIAGLYWHFVDLVWVFIFAFFYLW 202
Ubiquinol_oxidase_III cd02863
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ...
 61-236 4.37e-16

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


Pssm-ID: 239214  Cd Length: 186  Bit Score: 73.43  E-value: 4.37e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317  61 GMILFIASEVLFFVSFFWAYFnsslapAVEMGLAWPPMGIKPFNPMQVpLLNTVVLLSSGVTVTWAHHSLMEANHSQTTQ 140
Cdd:cd02863   12 GFWIYLMSDCILFATLFATYA------VLSGNTAGGPPGHELFELPLV-FIETFLLLLSSFTCGLAMIAMNKNNKKKVIL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 141 GLLATVILGLYFTMLQAYE---YWEAPFTIADAVYGSSFFMATGFHGIHVIIGTSFLLMCLIRHYSNHFSPTHHFGFEAA 217
Cdd:cd02863   85 WLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLVGTHGLHVTFGLIWILVMIIQLKKRGLTPDTARRLFCL 164

                        170
                 ....*....|....*....
gi 938339317 218 AWYWHFVDVVWLFLYVSIY 236
Cdd:cd02863  165 SLFWHFLDIVWIFVFTVVY 183
COX3 MTH00049
cytochrome c oxidase subunit III; Validated
 64-236 1.13e-15

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177124  Cd Length: 215  Bit Score: 73.03  E-value: 1.13e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317  64 LFIASEVLFFVSFFWA------YFNSSLAPAVEmglawppmgikpfnpmqVPLLNTVVLLSSGVTVTWAHHSL-MEANHS 136
Cdd:MTH00049  59 LFILSEVIIFGSLLVCclwfddWSYISLSSSLE-----------------IPFVGCFLLLGSSITVTAYHHLLgWKYCDL 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 137 QttqgLLATVILGLYFTMLQAYEYWEAPFTIADAVYGSSFFMATGFHGIHVIIGtSFLLMCLIRHYSNHFSPTHHfgfEA 216
Cdd:MTH00049 122 F----LYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHFSHVVLG-VVGLSTLLLVGSSSFGVYRS---TV 193

                        170       180
                 ....*....|....*....|
gi 938339317 217 AAWYWHFVDVVWLFLYVSIY 236
Cdd:MTH00049 194 LTWYWHFVDYIWLLVYLIVY 213
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 61-239 3.19e-10

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: 57.56  E-value: 3.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317   61 GMILFIASEVLFFVSFFWAYFNSSLApavemGLAWPPMGIKPFNpMQVPLLNTVVLLSSGVTVTWAHHSLMEANHSQTTQ 140
Cdd:TIGR02897  13 GFWIFLGAEIALFATLFATYLVLQHG-----GDYAGKMPAELFE-LPLVLIMTFLLLFSSFTCGIAIYEMRKENQKLMMF 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317  141 GLLATVILGLYFTMLQAYE---YWEAPFTIADAVYGSSFFMATGFHGIHVIIGTSFLLMCLIRHYSNHFSPTHHFGFEAA 217
Cdd:TIGR02897  87 WMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCHVTLGIVWAICLLIQIQRRGLTPYTAPKVFIV 166

                         170       180
                  ....*....|....*....|..
gi 938339317  218 AWYWHFVDVVWLFLYVSIYWWG 239
Cdd:TIGR02897 167 SLYWHFLDVVWVFIFTAVYLIG 188
PRK10663 PRK10663
cytochrome o ubiquinol oxidase subunit III; Provisional
 110-240 7.57e-08

cytochrome o ubiquinol oxidase subunit III; Provisional


Pssm-ID: 182628  Cd Length: 204  Bit Score: 50.94  E-value: 7.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 110 LLNTVVLLSSGVTVTWAHHSLMEANHSQTTQGLLATVILGLYFTMLQAYEYW---EAPFTIADAVYGSSFFMATGFHGIH 186
Cdd:PRK10663  70 LVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFHhliVEGMGPDRSGFLSAFFALVGTHGLH 149

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 938339317 187 VIIGTSFLLMCLIRHYSNHFSPTHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS 240
Cdd:PRK10663 150 VTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGA 203
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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