NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1681062982|gb|QDA23184|]
View 

cytochrome c oxidase subunit III (mitochondrion) [Systolederus spicupennis]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 5-259 2.33e-152

cytochrome c oxidase subunit III; Provisional


:

Pssm-ID: 214439  Cd Length: 255  Bit Score: 424.59  E-value: 2.33e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982   5 NHNHPYHLVDYSPWPLTGAIGGMIMTTGLAKWFYSSNMNLMLLGMMILIMTMFQWWRDVTREGTLQGLHTKNVSKGLRWG 84
Cdd:MTH00155    1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982  85 MIMFITSEVLFFMSFFWAFFNSSLASNVELGLMWPPVGIQPFNPINIPLLNTIILLSSGVTVTWAPHSLMESNKNQTNQS 164
Cdd:MTH00155   81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982 165 LTLTVMLGIYFTMLQAYEYIEAQFSIADSIYGTTFFMATGFHGIHVIIGTMFLLICFMRQLKFHFSSNHHLGFEAAAWYW 244
Cdd:MTH00155  161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240

                         250
                  ....*....|....*
gi 1681062982 245 HFVDVVWMFLYISIY 259
Cdd:MTH00155  241 HFVDVVWLFLYISIY 255
 
Name Accession Description Interval E-value
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 5-259 2.33e-152

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 424.59  E-value: 2.33e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982   5 NHNHPYHLVDYSPWPLTGAIGGMIMTTGLAKWFYSSNMNLMLLGMMILIMTMFQWWRDVTREGTLQGLHTKNVSKGLRWG 84
Cdd:MTH00155    1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982  85 MIMFITSEVLFFMSFFWAFFNSSLASNVELGLMWPPVGIQPFNPINIPLLNTIILLSSGVTVTWAPHSLMESNKNQTNQS 164
Cdd:MTH00155   81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982 165 LTLTVMLGIYFTMLQAYEYIEAQFSIADSIYGTTFFMATGFHGIHVIIGTMFLLICFMRQLKFHFSSNHHLGFEAAAWYW 244
Cdd:MTH00155  161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240

                         250
                  ....*....|....*
gi 1681062982 245 HFVDVVWMFLYISIY 259
Cdd:MTH00155  241 HFVDVVWLFLYISIY 255
COX3 pfam00510
Cytochrome c oxidase subunit III;
8-263 7.87e-123

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 350.17  E-value: 7.87e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982   8 HPYHLVDYSPWPLTGAIGGMIMTTGLAKWF--YSSNMNLMLLGMMILIMTMFQWWRDVTREGTLQGLHTKNVSKGLRWGM 85
Cdd:pfam00510   1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFhgYSGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982  86 IMFITSEVLFFMSFFWAFFNSSLASNVELGLMWPPVGIQPFNPINIPLLNTIILLSSGVTVTWAPHSLMESNKNQTNQSL 165
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982 166 TLTVMLGIYFTMLQAYEYIEAQFSIADSIYGTTFFMATGFHGIHVIIGTMFLLICFMRQLKFHFSSNHHLGFEAAAWYWH 245
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240

                         250
                  ....*....|....*...
gi 1681062982 246 FVDVVWMFLYISIYWWGS 263
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWGS 258
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 20-261 2.06e-117

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: 336.02  E-value: 2.06e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982  20 LTGAIGGMIMTTGLAKWF-YSSNMNLMLLGMMILIMTMFQWWRDVTREGTLQGLHTKNVSKGLRWGMIMFITSEVLFFMS 98
Cdd:cd01665     1 ILGSFGLLLLALGLVLWMhGYGGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982  99 FFWAFFNSSLASNVELGLMWPPVGIQPFNPINIPLLNTIILLSSGVTVTWAPHSLMESNKNQTNQSLTLTVMLGIYFTML 178
Cdd:cd01665    81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982 179 QAYEYIEAQFSIADSIYGTTFFMATGFHGIHVIIGTMFLLICFMRQLKFHFSSNHHLGFEAAAWYWHFVDVVWMFLYISI 258
Cdd:cd01665   161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240


                  ...
gi 1681062982 259 YWW 261
Cdd:cd01665   241 YWW 243
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
72-261 1.66e-47

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 156.16  E-value: 1.66e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982  72 LHTKNVSKGLRWGMIMFITSEVLFFMSFFWAFFNSSLASNVelglmWPPvGIQPFNPiNIPLLNTIILLSSGVTVTWAPH 151
Cdd:COG1845     7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRASAPD-----WPA-GAELLDL-PLPLINTLLLLLSSFTVALAVR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982 152 SLMESNKNQTNQSLTLTVMLGIYFTMLQAYEY---IEAQFSIADSIYGTTFFMATGFHGIHVIIGTMFLLICFMRQLKFH 228
Cdd:COG1845    80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1681062982 229 FSSNHHLGFEAAAWYWHFVDVVWMFLYISIYWW 261
Cdd:COG1845   160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 133-262 9.87e-09

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: 53.71  E-value: 9.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982 133 LLNTIILLSSGVTVTWAPHSLMESNKNQTNQSLTLTVMLGIYFTMLQAYE---YIEAQFSIADSIYGTTFFMATGFHGIH 209
Cdd:TIGR02897  56 LIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCH 135

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1681062982 210 VIIGtMFLLICFMRQLKFH-FSSNHHLGFEAAAWYWHFVDVVWMFLYISIYWWG 262
Cdd:TIGR02897 136 VTLG-IVWAICLLIQIQRRgLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
 
Name Accession Description Interval E-value
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 5-259 2.33e-152

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 424.59  E-value: 2.33e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982   5 NHNHPYHLVDYSPWPLTGAIGGMIMTTGLAKWFYSSNMNLMLLGMMILIMTMFQWWRDVTREGTLQGLHTKNVSKGLRWG 84
Cdd:MTH00155    1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982  85 MIMFITSEVLFFMSFFWAFFNSSLASNVELGLMWPPVGIQPFNPINIPLLNTIILLSSGVTVTWAPHSLMESNKNQTNQS 164
Cdd:MTH00155   81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982 165 LTLTVMLGIYFTMLQAYEYIEAQFSIADSIYGTTFFMATGFHGIHVIIGTMFLLICFMRQLKFHFSSNHHLGFEAAAWYW 244
Cdd:MTH00155  161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240

                         250
                  ....*....|....*
gi 1681062982 245 HFVDVVWMFLYISIY 259
Cdd:MTH00155  241 HFVDVVWLFLYISIY 255
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 4-263 1.24e-142

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 400.48  E-value: 1.24e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982   4 TNHNHPYHLVDYSPWPLTGAIGGMIMTTGLAKWFYSSNMNLMLLGMMILIMTMFQWWRDVTREGTLQGLHTKNVSKGLRW 83
Cdd:MTH00118    2 THQAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982  84 GMIMFITSEVLFFMSFFWAFFNSSLASNVELGLMWPPVGIQPFNPINIPLLNTIILLSSGVTVTWAPHSLMESNKNQTNQ 163
Cdd:MTH00118   82 GMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982 164 SLTLTVMLGIYFTMLQAYEYIEAQFSIADSIYGTTFFMATGFHGIHVIIGTMFLLICFMRQLKFHFSSNHHLGFEAAAWY 243
Cdd:MTH00118  162 ALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWY 241

                         250       260
                  ....*....|....*....|
gi 1681062982 244 WHFVDVVWMFLYISIYWWGS 263
Cdd:MTH00118  242 WHFVDVVWLFLYISIYWWGS 261
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 8-263 4.97e-138

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 388.95  E-value: 4.97e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982   8 HPYHLVDYSPWPLTGAIGGMIMTTGLAKWFYSSNMNLMLLGMMILIMTMFQWWRDVTREGTLQGLHTKNVSKGLRWGMIM 87
Cdd:MTH00189    5 HPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRYGMIL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982  88 FITSEVLFFMSFFWAFFNSSLASNVELGLMWPPVGIQPFNPINIPLLNTIILLSSGVTVTWAPHSLMESNKNQTNQSLTL 167
Cdd:MTH00189   85 FITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQALTL 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982 168 TVMLGIYFTMLQAYEYIEAQFSIADSIYGTTFFMATGFHGIHVIIGTMFLLICFMRQLKFHFSSNHHLGFEAAAWYWHFV 247
Cdd:MTH00189  165 TVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWYWHFV 244

                         250
                  ....*....|....*.
gi 1681062982 248 DVVWMFLYISIYWWGS 263
Cdd:MTH00189  245 DVVWLFLYVSIYWWGS 260
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 5-263 1.58e-130

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 369.83  E-value: 1.58e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982   5 NHNHPYHLVDYSPWPLTGAIGGMIMTTGLAKWFYSSNMNLMLLGMMILIMTMFQWWRDVTREGTLQGLHTKNVSKGLRWG 84
Cdd:MTH00039    2 THQHPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRYG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982  85 MIMFITSEVLFFMSFFWAFFNSSLASNVELGLMWPPVGIQPFNPINIPLLNTIILLSSGVTVTWAPHSLMESNKNQTNQS 164
Cdd:MTH00039   82 MILFITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982 165 LTLTVMLGIYFTMLQAYEYIEAQFSIADSIYGTTFFMATGFHGIHVIIGTMFLLICFMRQLKFHFSSNHHLGFEAAAWYW 244
Cdd:MTH00039  162 LFLTVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWYW 241

                         250
                  ....*....|....*....
gi 1681062982 245 HFVDVVWMFLYISIYWWGS 263
Cdd:MTH00039  242 HFVDVVWLFLYVCIYWWGS 260
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 8-263 4.04e-130

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 368.71  E-value: 4.04e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982   8 HPYHLVDYSPWPLTGAIGGMIMTTGLAKWFYSSNMNLMLLGMMILIMTMFQWWRDVTREGTLQGLHTKNVSKGLRWGMIM 87
Cdd:MTH00130    6 HAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRYGMIL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982  88 FITSEVLFFMSFFWAFFNSSLASNVELGLMWPPVGIQPFNPINIPLLNTIILLSSGVTVTWAPHSLMESNKNQTNQSLTL 167
Cdd:MTH00130   86 FITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQSLTL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982 168 TVMLGIYFTMLQAYEYIEAQFSIADSIYGTTFFMATGFHGIHVIIGTMFLLICFMRQLKFHFSSNHHLGFEAAAWYWHFV 247
Cdd:MTH00130  166 TILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWYWHFV 245

                         250
                  ....*....|....*.
gi 1681062982 248 DVVWMFLYISIYWWGS 263
Cdd:MTH00130  246 DVVWLFLYISIYWWGS 261
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 8-263 5.18e-130

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 368.73  E-value: 5.18e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982   8 HPYHLVDYSPWPLTGAIGGMIMTTGLAKWFYSSNMNLMLLGMMILIMTMFQWWRDVTREGTLQGLHTKNVSKGLRWGMIM 87
Cdd:MTH00219    7 NPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLRIGMIL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982  88 FITSEVLFFMSFFWAFFNSSLASNVELGLMWPPVGIQPFNPINIPLLNTIILLSSGVTVTWAPHSLMESNKNQTNQSLTL 167
Cdd:MTH00219   87 FIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQQGLLF 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982 168 TVMLGIYFTMLQAYEYIEAQFSIADSIYGTTFFMATGFHGIHVIIGTMFLLICFMRQLKFHFSSNHHLGFEAAAWYWHFV 247
Cdd:MTH00219  167 TILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAAWYWHFV 246

                         250
                  ....*....|....*.
gi 1681062982 248 DVVWMFLYISIYWWGS 263
Cdd:MTH00219  247 DVVWLFLYVSIYWWGS 262
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 8-263 1.17e-129

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 367.68  E-value: 1.17e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982   8 HPYHLVDYSPWPLTGAIGGMIMTTGLAKWFYSSNMNLMLLGMMILIMTMFQWWRDVTREGTLQGLHTKNVSKGLRWGMIM 87
Cdd:MTH00141    4 NPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFIL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982  88 FITSEVLFFMSFFWAFFNSSLASNVELGLMWPPVGIQPFNPINIPLLNTIILLSSGVTVTWAPHSLMESNKNQTNQSLTL 167
Cdd:MTH00141   84 FIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982 168 TVMLGIYFTMLQAYEYIEAQFSIADSIYGTTFFMATGFHGIHVIIGTMFLLICFMRQLKFHFSSNHHLGFEAAAWYWHFV 247
Cdd:MTH00141  164 TIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFV 243

                         250
                  ....*....|....*.
gi 1681062982 248 DVVWMFLYISIYWWGS 263
Cdd:MTH00141  244 DVVWLFLYLSIYWWGS 259
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 4-263 5.55e-129

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 365.97  E-value: 5.55e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982   4 TNHNHPYHLVDYSPWPLTGAIGGMIMTTGLAKWFYSSNMNLMLLGMMILIMTMFQWWRDVTREGTLQGLHTKNVSKGLRW 83
Cdd:MTH00099    2 THQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982  84 GMIMFITSEVLFFMSFFWAFFNSSLASNVELGLMWPPVGIQPFNPINIPLLNTIILLSSGVTVTWAPHSLMESNKNQTNQ 163
Cdd:MTH00099   82 GMILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982 164 SLTLTVMLGIYFTMLQAYEYIEAQFSIADSIYGTTFFMATGFHGIHVIIGTMFLLICFMRQLKFHFSSNHHLGFEAAAWY 243
Cdd:MTH00099  162 ALFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWY 241

                         250       260
                  ....*....|....*....|
gi 1681062982 244 WHFVDVVWMFLYISIYWWGS 263
Cdd:MTH00099  242 WHFVDVVWLFLYVSIYWWGS 261
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 4-263 1.44e-128

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 364.84  E-value: 1.44e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982   4 TNHNHPYHLVDYSPWPLTGAIGGMIMTTGLAKWFYSSNMNLMLLGMMILIMTMFQWWRDVTREGTLQGLHTKNVSKGLRW 83
Cdd:MTH00075    2 AHQAHAFHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982  84 GMIMFITSEVLFFMSFFWAFFNSSLASNVELGLMWPPVGIQPFNPINIPLLNTIILLSSGVTVTWAPHSLMESNKNQTNQ 163
Cdd:MTH00075   82 GMILFITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982 164 SLTLTVMLGIYFTMLQAYEYIEAQFSIADSIYGTTFFMATGFHGIHVIIGTMFLLICFMRQLKFHFSSNHHLGFEAAAWY 243
Cdd:MTH00075  162 SLALTIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWY 241

                         250       260
                  ....*....|....*....|
gi 1681062982 244 WHFVDVVWMFLYISIYWWGS 263
Cdd:MTH00075  242 WHFVDVVWLFLYVSIYWWGS 261
COX3 pfam00510
Cytochrome c oxidase subunit III;
8-263 7.87e-123

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 350.17  E-value: 7.87e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982   8 HPYHLVDYSPWPLTGAIGGMIMTTGLAKWF--YSSNMNLMLLGMMILIMTMFQWWRDVTREGTLQGLHTKNVSKGLRWGM 85
Cdd:pfam00510   1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFhgYSGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982  86 IMFITSEVLFFMSFFWAFFNSSLASNVELGLMWPPVGIQPFNPINIPLLNTIILLSSGVTVTWAPHSLMESNKNQTNQSL 165
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982 166 TLTVMLGIYFTMLQAYEYIEAQFSIADSIYGTTFFMATGFHGIHVIIGTMFLLICFMRQLKFHFSSNHHLGFEAAAWYWH 245
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240

                         250
                  ....*....|....*...
gi 1681062982 246 FVDVVWMFLYISIYWWGS 263
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWGS 258
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 20-261 2.06e-117

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: 336.02  E-value: 2.06e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982  20 LTGAIGGMIMTTGLAKWF-YSSNMNLMLLGMMILIMTMFQWWRDVTREGTLQGLHTKNVSKGLRWGMIMFITSEVLFFMS 98
Cdd:cd01665     1 ILGSFGLLLLALGLVLWMhGYGGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982  99 FFWAFFNSSLASNVELGLMWPPVGIQPFNPINIPLLNTIILLSSGVTVTWAPHSLMESNKNQTNQSLTLTVMLGIYFTML 178
Cdd:cd01665    81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982 179 QAYEYIEAQFSIADSIYGTTFFMATGFHGIHVIIGTMFLLICFMRQLKFHFSSNHHLGFEAAAWYWHFVDVVWMFLYISI 258
Cdd:cd01665   161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240


                  ...
gi 1681062982 259 YWW 261
Cdd:cd01665   241 YWW 243
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 8-263 3.96e-117

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 336.04  E-value: 3.96e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982   8 HPYHLVDYSPWPLTGAIGGMIMTTGLAKWFYSSNMNLMLLGMMILIMTMFQWWRDVTREGTLQGLHTKNVSKGLRWGMIM 87
Cdd:MTH00009    4 QPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMIL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982  88 FITSEVLFFMSFFWAFFNSSLASNVELGLMWPPVGIQPFNPINIPLLNTIILLSSGVTVTWAPHSLMESNKNQTNQSLTL 167
Cdd:MTH00009   84 FIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALIL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982 168 TVMLGIYFTMLQAYEYIEAQFSIADSIYGTTFFMATGFHGIHVIIGTMFLLICFMRQLKFHFSSNHHLGFEAAAWYWHFV 247
Cdd:MTH00009  164 TVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFV 243

                         250
                  ....*....|....*.
gi 1681062982 248 DVVWMFLYISIYWWGS 263
Cdd:MTH00009  244 DVVWIFLYLCIYWWGS 259
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 8-263 2.09e-113

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 326.32  E-value: 2.09e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982   8 HPYHLVDYSPWPLTGAIGGMIMTTGLAKWFYSSNMNLMLLGMMILIMTMFQWWRDVTREGTLQGLHTKNVSKGLRWGMIM 87
Cdd:MTH00024    6 HPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGMLL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982  88 FITSEVLFFMSFFWAFFNSSLASNVELGLMWPPVGIQPFNPINIPLLNTIILLSSGVTVTWAPHSLMESNKNQTNQSLTL 167
Cdd:MTH00024   86 FILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982 168 TVMLGIYFTMLQAYEYIEAQFSIADSIYGTTFFMATGFHGIHVIIGTMFLLICFMRQLKFHFSSNHHLGFEAAAWYWHFV 247
Cdd:MTH00024  166 TVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASWYWHFV 245

                         250
                  ....*....|....*.
gi 1681062982 248 DVVWMFLYISIYWWGS 263
Cdd:MTH00024  246 DVVWLFLYLCIYWWGS 261
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 8-263 3.36e-103

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 300.56  E-value: 3.36e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982   8 HPYHLVDYSPWPLTGAIGGMIMTTGLAKWFYSSNMNLMLLGMMILIMTMFQWWRDVTREGTLQGLHTKNVSKGLRWGMIM 87
Cdd:MTH00052    7 HPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGLKYGMIL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982  88 FITSEVLFFMSFFWAFFNSSLASNVELGLMWPPVGIQPFNPINIPLLNTIILLSSGVTVTWAPHSLMESNKNQTNQSLTL 167
Cdd:MTH00052   87 FIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEAIIGLAL 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982 168 TVMLGIYFTMLQAYEYIEAQFSIADSIYGTTFFMATGFHGIHVIIGTMFLLICFMRQLKFHFSSNHHLGFEAAAWYWHFV 247
Cdd:MTH00052  167 TVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAAWYWHFV 246

                         250
                  ....*....|....*.
gi 1681062982 248 DVVWMFLYISIYWWGS 263
Cdd:MTH00052  247 DVVWLFLFIFMYWWGS 262
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 8-263 6.53e-95

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 280.80  E-value: 6.53e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982   8 HPYHLVDYSPWPLTGAIGGMIMTTGLAKWFYSSNMNLMLLGMMILIMTMFQWWRDVTREGTLQGLHTKNVSKGLRWGMIM 87
Cdd:MTH00028    6 HPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982  88 FITSEVLFFMSFFWAFFNSSLASNVELGLMWPPVGIQPFNPINIPLLNTIILLSSGVTVTWAPHSLM------------- 154
Cdd:MTH00028   86 FILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIgtgnpaslekgtq 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982 155 -------------ESNKNQTNQS----------LTLTVMLGIYFTMLQAYEYIEAQFSIADSIYGTTFFMATGFHGIHVI 211
Cdd:MTH00028  166 giegpnpsngappDPQKGPTFLLsdfrtnavigLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVL 245

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1681062982 212 IGTMFLLICFMRQLKFHFSSNHHLGFEAAAWYWHFVDVVWMFLYISIYWWGS 263
Cdd:MTH00028  246 VGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWGS 297
PLN02194 PLN02194
cytochrome-c oxidase
 2-262 8.80e-84

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 251.51  E-value: 8.80e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982   2 LTTNHNHPYHLVDYSPWPLTGAIGGMIMTTGLAKWF--YSSNMNLMLLGMMILIMTMFQWWRDVTREGTLQGLHTKNVSK 79
Cdd:PLN02194    1 MIESQRHSYHLVDPSPWPISGSLGALATTVGGVMYMhpFQGGARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982  80 GLRWGMIMFITSEVLFFMSFFWAFFNSSLASNVELGLMWPPVGIQPFNPINIPLLNTIILLSSGVTVTWAPHSLMESNKN 159
Cdd:PLN02194   81 GPRYGSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982 160 QTNQSLTLTVMLGIYFTMLQAYEYIEAQFSIADSIYGTTFFMATGFHGIHVIIGTMFLLICFMRQLKFHFSSNHHLGFEA 239
Cdd:PLN02194  161 RAVYALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEA 240

                         250       260
                  ....*....|....*....|...
gi 1681062982 240 AAWYWHFVDVVWMFLYISIYWWG 262
Cdd:PLN02194  241 AAWYWHFVDVVWLFLFVSIYWWG 263
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
 8-263 7.19e-68

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 210.58  E-value: 7.19e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982   8 HPYHLVDYSPWPLTGAIGGMIMTTGLAKWFYSSNMNLMLLGMMILIMTMFQWWRDVTREGtLQGLHTKNVSKGLRWGMIM 87
Cdd:MTH00083    3 HNFHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMIL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982  88 FITSEVLFFMSFFWAFFNSSLASNVELGLMWPPVGIQPFNPINIPLLNTIILLSSGVTVTWAPHSLMESNKNQTNqSLTL 167
Cdd:MTH00083   82 FIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSNKSCTN-SLLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982 168 TVMLGIYFTMLQAYEYIEAQFSIADSIYGTTFFMATGFHGIHVIIGTMFLLICFMRQLKFHFSSNHHLGFEAAAWYWHFV 247
Cdd:MTH00083  161 TCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFV 240

                         250
                  ....*....|....*.
gi 1681062982 248 DVVWMFLYISIYWWGS 263
Cdd:MTH00083  241 DVVWLFLFVFVYWWSY 256
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 73-261 4.22e-62

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: 193.19  E-value: 4.22e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982  73 HTKNVSKGLRWGMIMFITSEVLFFMSFFWAFFNSSLASNVELGlmwppvgiQPFNPINIPLLNTIILLSSGVTVTWAPHS 152
Cdd:cd00386     1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFG--------AGLDPLDLPLLNTNTLLLSGSSVTWAHAS 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982 153 LM--ESNKNQTNQSLTLTVMLGIYFTMLQAYEYIEAQFSIADSIYGTTFFMATGFHGIHVIIGTMFLLICFMRQLKFHFS 230
Cdd:cd00386    73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1681062982 231 SNHHLGFEAAAWYWHFVDVVWMFLYISIYWW 261
Cdd:cd00386   153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
72-261 1.66e-47

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 156.16  E-value: 1.66e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982  72 LHTKNVSKGLRWGMIMFITSEVLFFMSFFWAFFNSSLASNVelglmWPPvGIQPFNPiNIPLLNTIILLSSGVTVTWAPH 151
Cdd:COG1845     7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRASAPD-----WPA-GAELLDL-PLPLINTLLLLLSSFTVALAVR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982 152 SLMESNKNQTNQSLTLTVMLGIYFTMLQAYEY---IEAQFSIADSIYGTTFFMATGFHGIHVIIGTMFLLICFMRQLKFH 228
Cdd:COG1845    80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1681062982 229 FSSNHHLGFEAAAWYWHFVDVVWMFLYISIYWW 261
Cdd:COG1845   160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
NorE_like cd02862
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ...
 133-259 2.80e-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: 93.45  E-value: 2.80e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982 133 LLNTIILLSSGVTVTWAPHSLMESNKNQTNQSLTLTVMLGIYFTMLQAYEY---IEAQFSIADSIYGTTFFMATGFHGIH 209
Cdd:cd02862    55 ALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYahkIAAGIDPDAGLFFTLYFLLTGFHLLH 134

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1681062982 210 VIIGTMFLLICFMRQLKFHFSSNHHLGFEAAAWYWHFVDVVWMFLYISIY 259
Cdd:cd02862   135 VLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVLFPLLY 184
Heme_Cu_Oxidase_III_1 cd02864
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 118-261 3.08e-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: 239215  Cd Length: 202  Bit Score: 80.24  E-value: 3.08e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982 118 WPP---VGIQPFNPINIPL----LNTIILLSSGVTVTWAPHSLMESNKNQTNQSLTLTVMLGIYFTMLQAYEYIE----- 185
Cdd:cd02864    42 WPLpsdVFALRIGHFNIPLvliaIMTFILITSSGTMAMAVNFGYRGNRKAAARLMLATALLGATFVGMQAFEWTKlivee 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982 186 ----AQFSIADSIYGTTFFMATGFHGIHVIIGTMFLLICFMRQLKFHFSS-NHHLGFEAAAWYWHFVDVVWMFLYISIYW 260
Cdd:cd02864   122 gvrpWGNPWGAAQFGASFFMITGFHGTHVTIGVIYLIIIARKVWRGKYQRiGRYEIVEIAGLYWHFVDLVWVFIFAFFYL 201


                  .
gi 1681062982 261 W 261
Cdd:cd02864   202 W 202
Ubiquinol_oxidase_III cd02863
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ...
 133-259 3.01e-16

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


Pssm-ID: 239214  Cd Length: 186  Bit Score: 74.58  E-value: 3.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982 133 LLNTIILLSSGVTVTWAPHSLMESNKNQTNQSLTLTVMLGIYFTMLQAYE---YIEAQFSIADSIYGTTFFMATGFHGIH 209
Cdd:cd02863    54 FIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLVGTHGLH 133

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1681062982 210 VIIGTMFLLICFMRQLKFHFSSNHHLGFEAAAWYWHFVDVVWMFLYISIY 259
Cdd:cd02863   134 VTFGLIWILVMIIQLKKRGLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
COX3 MTH00049
cytochrome c oxidase subunit III; Validated
 131-259 2.15e-14

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177124  Cd Length: 215  Bit Score: 69.94  E-value: 2.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982 131 IPLLNTIILLSSGVTVTwAPHSLMESNKNQTNqsLTLTVMLGIYFTMLQAYEYIEAQFSIADSIYGTTFFMATGFHGIHV 210
Cdd:MTH00049   92 IPFVGCFLLLGSSITVT-AYHHLLGWKYCDLF--LYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHFSHV 168

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1681062982 211 IIGTMFLLICFMRQLKFHFSSNHHLgfeaAAWYWHFVDVVWMFLYISIY 259
Cdd:MTH00049  169 VLGVVGLSTLLLVGSSSFGVYRSTV----LTWYWHFVDYIWLLVYLIVY 213
Heme_Cu_Oxidase_III_2 cd02865
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 125-261 5.12e-14

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: 68.55  E-value: 5.12e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982 125 PFNPINIPLLNTIILLSSGVTVTWAPHSLMESNKNQTNQSLTLTVMLGIYFTMLQAYEY---IEAQFSIADSIYGTTFFM 201
Cdd:cd02865    45 PLPLPNLLSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWhalNDAGYGPTSNPAGSFFYL 124

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982 202 ATGFHGIHVIIGTMFLLICFMRQLKFHFSSNHHLGFEAAAWYWHFVDVVWMFLYISIYWW 261
Cdd:cd02865   125 LTGLHGLHVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVLLALLYGT 184
PRK10663 PRK10663
cytochrome o ubiquinol oxidase subunit III; Provisional
 133-263 3.01e-10

cytochrome o ubiquinol oxidase subunit III; Provisional


Pssm-ID: 182628  Cd Length: 204  Bit Score: 58.25  E-value: 3.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982 133 LLNTIILLSSGVTVTWAPHSLMESNKNQTNQSLTLTVMLGIYFTMLQAYEY---IEAQFSIADSIYGTTFFMATGFHGIH 209
Cdd:PRK10663   70 LVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFhhlIVEGMGPDRSGFLSAFFALVGTHGLH 149

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1681062982 210 VIIGTMFLLICFMRQLKFHFSSNHHLGFEAAAWYWHFVDVVWMFLYISIYWWGS 263
Cdd:PRK10663  150 VTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGA 203
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 133-262 9.87e-09

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: 53.71  E-value: 9.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681062982 133 LLNTIILLSSGVTVTWAPHSLMESNKNQTNQSLTLTVMLGIYFTMLQAYE---YIEAQFSIADSIYGTTFFMATGFHGIH 209
Cdd:TIGR02897  56 LIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCH 135

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1681062982 210 VIIGtMFLLICFMRQLKFH-FSSNHHLGFEAAAWYWHFVDVVWMFLYISIYWWG 262
Cdd:TIGR02897 136 VTLG-IVWAICLLIQIQRRgLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH