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Conserved domains on  [gi|1331215853|ref|YP_009454603|]
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cytochrome c oxidase subunit III (mitochondrion) [Caryanda elegans]

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
 5-259 1.15e-156

cytochrome c oxidase subunit III; Provisional


:

Pssm-ID: 214439  Cd Length: 255  Bit Score: 435.76  E-value: 1.15e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853   5 HSNHPFHLVDYSPWPLTGAIGAMVLVSGLAKWFHLFNINLFTIGISITLLTMIQWWRDIIREGTYQGLHTGFVSIGLRWG 84
Cdd:MTH00155    1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853  85 MILFIASEVLFFLSFFWAFFSSSLAPTIELGMLWPPMGIQPFNPMQIPLLNTAILLASGVTVTWAHHSLMESNHTQALQG 164
Cdd:MTH00155   81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853 165 LFFTVMLGFYFTLLQAYEYWEAPFTIADAVYGSTFFIATGFHGLHVIIGTMFLLTCLMRHSKNQFSPSHHFGFEAAAWYW 244
Cdd:MTH00155  161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240

                         250
                  ....*....|....*
gi 1331215853 245 HFVDVVWLFLYISIY 259
Cdd:MTH00155  241 HFVDVVWLFLYISIY 255
 
Name Accession Description Interval E-value
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 5-259 1.15e-156

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 435.76  E-value: 1.15e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853   5 HSNHPFHLVDYSPWPLTGAIGAMVLVSGLAKWFHLFNINLFTIGISITLLTMIQWWRDIIREGTYQGLHTGFVSIGLRWG 84
Cdd:MTH00155    1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853  85 MILFIASEVLFFLSFFWAFFSSSLAPTIELGMLWPPMGIQPFNPMQIPLLNTAILLASGVTVTWAHHSLMESNHTQALQG 164
Cdd:MTH00155   81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853 165 LFFTVMLGFYFTLLQAYEYWEAPFTIADAVYGSTFFIATGFHGLHVIIGTMFLLTCLMRHSKNQFSPSHHFGFEAAAWYW 244
Cdd:MTH00155  161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240

                         250
                  ....*....|....*
gi 1331215853 245 HFVDVVWLFLYISIY 259
Cdd:MTH00155  241 HFVDVVWLFLYISIY 255
COX3 pfam00510
Cytochrome c oxidase subunit III;
8-263 2.64e-121

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 346.32  E-value: 2.64e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853   8 HPFHLVDYSPWPLTGAIGAMVLVSGLAKWFHLF--NINLFTIGISITLLTMIQWWRDIIREGTYQGLHTGFVSIGLRWGM 85
Cdd:pfam00510   1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYsgNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853  86 ILFIASEVLFFLSFFWAFFSSSLAPTIELGMLWPPMGIQPFNPMQIPLLNTAILLASGVTVTWAHHSLMESNHTQALQGL 165
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853 166 FFTVMLGFYFTLLQAYEYWEAPFTIADAVYGSTFFIATGFHGLHVIIGTMFLLTCLMRHSKNQFSPSHHFGFEAAAWYWH 245
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240

                         250
                  ....*....|....*...
gi 1331215853 246 FVDVVWLFLYISIYWWGS 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 3.24e-115

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: 330.25  E-value: 3.24e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853  20 LTGAIGAMVLVSGLAKWFHLF-NINLFTIGISITLLTMIQWWRDIIREGTYQGLHTGFVSIGLRWGMILFIASEVLFFLS 98
Cdd:cd01665     1 ILGSFGLLLLALGLVLWMHGYgGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853  99 FFWAFFSSSLAPTIELGMLWPPMGIQPFNPMQIPLLNTAILLASGVTVTWAHHSLMESNHTQALQGLFFTVMLGFYFTLL 178
Cdd:cd01665    81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853 179 QAYEYWEAPFTIADAVYGSTFFIATGFHGLHVIIGTMFLLTCLMRHSKNQFSPSHHFGFEAAAWYWHFVDVVWLFLYISI 258
Cdd:cd01665   161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240


                  ...
gi 1331215853 259 YWW 261
Cdd:cd01665   241 YWW 243
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
72-261 9.84e-46

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 151.93  E-value: 9.84e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853  72 LHTGFVSIGLRWGMILFIASEVLFFLSFFWAFFssslapTIELGMLWPPMGIQPFNPmQIPLLNTAILLASGVTVTWAHH 151
Cdd:COG1845     7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYF------VLRASAPDWPAGAELLDL-PLPLINTLLLLLSSFTVALAVR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853 152 SLMESNHTQALQGLFFTVMLGFYFTLLQAYEY---WEAPFTIADAVYGSTFFIATGFHGLHVIIGTMFLLTCLMRHSKNQ 228
Cdd:COG1845    80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1331215853 229 FSPSHHFGFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:COG1845   160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 133-262 2.08e-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: 55.63  E-value: 2.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853 133 LLNTAILLASGVTVTWAHHSLMESNHTQALQGLFFTVMLGFYFTLLQAYE---YWEAPFTIADAVYGSTFFIATGFHGLH 209
Cdd:TIGR02897  56 LIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCH 135

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1331215853 210 VIIGTMFLLTCLMRHSKNQFSPSHHFGFEAAAWYWHFVDVVWLFLYISIYWWG 262
Cdd:TIGR02897 136 VTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
 
Name Accession Description Interval E-value
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 5-259 1.15e-156

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 435.76  E-value: 1.15e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853   5 HSNHPFHLVDYSPWPLTGAIGAMVLVSGLAKWFHLFNINLFTIGISITLLTMIQWWRDIIREGTYQGLHTGFVSIGLRWG 84
Cdd:MTH00155    1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853  85 MILFIASEVLFFLSFFWAFFSSSLAPTIELGMLWPPMGIQPFNPMQIPLLNTAILLASGVTVTWAHHSLMESNHTQALQG 164
Cdd:MTH00155   81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853 165 LFFTVMLGFYFTLLQAYEYWEAPFTIADAVYGSTFFIATGFHGLHVIIGTMFLLTCLMRHSKNQFSPSHHFGFEAAAWYW 244
Cdd:MTH00155  161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240

                         250
                  ....*....|....*
gi 1331215853 245 HFVDVVWLFLYISIY 259
Cdd:MTH00155  241 HFVDVVWLFLYISIY 255
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 5-263 4.08e-140

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 393.93  E-value: 4.08e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853   5 HSNHPFHLVDYSPWPLTGAIGAMVLVSGLAKWFHLFNINLFTIGISITLLTMIQWWRDIIREGTYQGLHTGFVSIGLRWG 84
Cdd:MTH00118    3 HQAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRYG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853  85 MILFIASEVLFFLSFFWAFFSSSLAPTIELGMLWPPMGIQPFNPMQIPLLNTAILLASGVTVTWAHHSLMESNHTQALQG 164
Cdd:MTH00118   83 MILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853 165 LFFTVMLGFYFTLLQAYEYWEAPFTIADAVYGSTFFIATGFHGLHVIIGTMFLLTCLMRHSKNQFSPSHHFGFEAAAWYW 244
Cdd:MTH00118  163 LTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWYW 242

                         250
                  ....*....|....*....
gi 1331215853 245 HFVDVVWLFLYISIYWWGS 263
Cdd:MTH00118  243 HFVDVVWLFLYISIYWWGS 261
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 5-263 2.82e-135

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 381.63  E-value: 2.82e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853   5 HSNHPFHLVDYSPWPLTGAIGAMVLVSGLAKWFHLFNINLFTIGISITLLTMIQWWRDIIREGTYQGLHTGFVSIGLRWG 84
Cdd:MTH00189    2 HQAHPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRYG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853  85 MILFIASEVLFFLSFFWAFFSSSLAPTIELGMLWPPMGIQPFNPMQIPLLNTAILLASGVTVTWAHHSLMESNHTQALQG 164
Cdd:MTH00189   82 MILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853 165 LFFTVMLGFYFTLLQAYEYWEAPFTIADAVYGSTFFIATGFHGLHVIIGTMFLLTCLMRHSKNQFSPSHHFGFEAAAWYW 244
Cdd:MTH00189  162 LTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWYW 241

                         250
                  ....*....|....*....
gi 1331215853 245 HFVDVVWLFLYISIYWWGS 263
Cdd:MTH00189  242 HFVDVVWLFLYVSIYWWGS 260
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 8-263 1.54e-129

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 367.13  E-value: 1.54e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853   8 HPFHLVDYSPWPLTGAIGAMVLVSGLAKWFHLFNINLFTIGISITLLTMIQWWRDIIREGTYQGLHTGFVSIGLRWGMIL 87
Cdd:MTH00039    5 HPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRYGMIL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853  88 FIASEVLFFLSFFWAFFSSSLAPTIELGMLWPPMGIQPFNPMQIPLLNTAILLASGVTVTWAHHSLMESNHTQALQGLFF 167
Cdd:MTH00039   85 FITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQALFL 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853 168 TVMLGFYFTLLQAYEYWEAPFTIADAVYGSTFFIATGFHGLHVIIGTMFLLTCLMRHSKNQFSPSHHFGFEAAAWYWHFV 247
Cdd:MTH00039  165 TVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWYWHFV 244

                         250
                  ....*....|....*.
gi 1331215853 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00039  245 DVVWLFLYVCIYWWGS 260
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 5-263 4.15e-128

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 363.70  E-value: 4.15e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853   5 HSNHPFHLVDYSPWPLTGAIGAMVLVSGLAKWFHLFNINLFTIGISITLLTMIQWWRDIIREGTYQGLHTGFVSIGLRWG 84
Cdd:MTH00130    3 HQAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRYG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853  85 MILFIASEVLFFLSFFWAFFSSSLAPTIELGMLWPPMGIQPFNPMQIPLLNTAILLASGVTVTWAHHSLMESNHTQALQG 164
Cdd:MTH00130   83 MILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQS 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853 165 LFFTVMLGFYFTLLQAYEYWEAPFTIADAVYGSTFFIATGFHGLHVIIGTMFLLTCLMRHSKNQFSPSHHFGFEAAAWYW 244
Cdd:MTH00130  163 LTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWYW 242

                         250
                  ....*....|....*....
gi 1331215853 245 HFVDVVWLFLYISIYWWGS 263
Cdd:MTH00130  243 HFVDVVWLFLYISIYWWGS 261
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 8-263 4.52e-128

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 363.44  E-value: 4.52e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853   8 HPFHLVDYSPWPLTGAIGAMVLVSGLAKWFHLFNINLFTIGISITLLTMIQWWRDIIREGTYQGLHTGFVSIGLRWGMIL 87
Cdd:MTH00141    4 NPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFIL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853  88 FIASEVLFFLSFFWAFFSSSLAPTIELGMLWPPMGIQPFNPMQIPLLNTAILLASGVTVTWAHHSLMESNHTQALQGLFF 167
Cdd:MTH00141   84 FIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853 168 TVMLGFYFTLLQAYEYWEAPFTIADAVYGSTFFIATGFHGLHVIIGTMFLLTCLMRHSKNQFSPSHHFGFEAAAWYWHFV 247
Cdd:MTH00141  164 TIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFV 243

                         250
                  ....*....|....*.
gi 1331215853 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00141  244 DVVWLFLYLSIYWWGS 259
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 5-263 4.55e-126

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 358.67  E-value: 4.55e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853   5 HSNHPFHLVDYSPWPLTGAIGAMVLVSGLAKWFHLFNINLFTIGISITLLTMIQWWRDIIREGTYQGLHTGFVSIGLRWG 84
Cdd:MTH00075    3 HQAHAFHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRYG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853  85 MILFIASEVLFFLSFFWAFFSSSLAPTIELGMLWPPMGIQPFNPMQIPLLNTAILLASGVTVTWAHHSLMESNHTQALQG 164
Cdd:MTH00075   83 MILFITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQS 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853 165 LFFTVMLGFYFTLLQAYEYWEAPFTIADAVYGSTFFIATGFHGLHVIIGTMFLLTCLMRHSKNQFSPSHHFGFEAAAWYW 244
Cdd:MTH00075  163 LALTIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWYW 242

                         250
                  ....*....|....*....
gi 1331215853 245 HFVDVVWLFLYISIYWWGS 263
Cdd:MTH00075  243 HFVDVVWLFLYVSIYWWGS 261
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 8-263 1.02e-125

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 357.56  E-value: 1.02e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853   8 HPFHLVDYSPWPLTGAIGAMVLVSGLAKWFHLFNINLFTIGISITLLTMIQWWRDIIREGTYQGLHTGFVSIGLRWGMIL 87
Cdd:MTH00219    7 NPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLRIGMIL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853  88 FIASEVLFFLSFFWAFFSSSLAPTIELGMLWPPMGIQPFNPMQIPLLNTAILLASGVTVTWAHHSLMESNHTQALQGLFF 167
Cdd:MTH00219   87 FIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQQGLLF 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853 168 TVMLGFYFTLLQAYEYWEAPFTIADAVYGSTFFIATGFHGLHVIIGTMFLLTCLMRHSKNQFSPSHHFGFEAAAWYWHFV 247
Cdd:MTH00219  167 TILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAAWYWHFV 246

                         250
                  ....*....|....*.
gi 1331215853 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00219  247 DVVWLFLYVSIYWWGS 262
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 5-263 1.64e-125

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 357.11  E-value: 1.64e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853   5 HSNHPFHLVDYSPWPLTGAIGAMVLVSGLAKWFHLFNINLFTIGISITLLTMIQWWRDIIREGTYQGLHTGFVSIGLRWG 84
Cdd:MTH00099    3 HQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRYG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853  85 MILFIASEVLFFLSFFWAFFSSSLAPTIELGMLWPPMGIQPFNPMQIPLLNTAILLASGVTVTWAHHSLMESNHTQALQG 164
Cdd:MTH00099   83 MILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853 165 LFFTVMLGFYFTLLQAYEYWEAPFTIADAVYGSTFFIATGFHGLHVIIGTMFLLTCLMRHSKNQFSPSHHFGFEAAAWYW 244
Cdd:MTH00099  163 LFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWYW 242

                         250
                  ....*....|....*....
gi 1331215853 245 HFVDVVWLFLYISIYWWGS 263
Cdd:MTH00099  243 HFVDVVWLFLYVSIYWWGS 261
COX3 pfam00510
Cytochrome c oxidase subunit III;
8-263 2.64e-121

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 346.32  E-value: 2.64e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853   8 HPFHLVDYSPWPLTGAIGAMVLVSGLAKWFHLF--NINLFTIGISITLLTMIQWWRDIIREGTYQGLHTGFVSIGLRWGM 85
Cdd:pfam00510   1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYsgNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853  86 ILFIASEVLFFLSFFWAFFSSSLAPTIELGMLWPPMGIQPFNPMQIPLLNTAILLASGVTVTWAHHSLMESNHTQALQGL 165
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853 166 FFTVMLGFYFTLLQAYEYWEAPFTIADAVYGSTFFIATGFHGLHVIIGTMFLLTCLMRHSKNQFSPSHHFGFEAAAWYWH 245
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240

                         250
                  ....*....|....*...
gi 1331215853 246 FVDVVWLFLYISIYWWGS 263
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWGS 258
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 8-263 1.04e-117

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 337.19  E-value: 1.04e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853   8 HPFHLVDYSPWPLTGAIGAMVLVSGLAKWFHLFNINLFTIGISITLLTMIQWWRDIIREGTYQGLHTGFVSIGLRWGMIL 87
Cdd:MTH00009    4 QPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMIL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853  88 FIASEVLFFLSFFWAFFSSSLAPTIELGMLWPPMGIQPFNPMQIPLLNTAILLASGVTVTWAHHSLMESNHTQALQGLFF 167
Cdd:MTH00009   84 FIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALIL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853 168 TVMLGFYFTLLQAYEYWEAPFTIADAVYGSTFFIATGFHGLHVIIGTMFLLTCLMRHSKNQFSPSHHFGFEAAAWYWHFV 247
Cdd:MTH00009  164 TVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFV 243

                         250
                  ....*....|....*.
gi 1331215853 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00009  244 DVVWIFLYLCIYWWGS 259
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 20-261 3.24e-115

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: 330.25  E-value: 3.24e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853  20 LTGAIGAMVLVSGLAKWFHLF-NINLFTIGISITLLTMIQWWRDIIREGTYQGLHTGFVSIGLRWGMILFIASEVLFFLS 98
Cdd:cd01665     1 ILGSFGLLLLALGLVLWMHGYgGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853  99 FFWAFFSSSLAPTIELGMLWPPMGIQPFNPMQIPLLNTAILLASGVTVTWAHHSLMESNHTQALQGLFFTVMLGFYFTLL 178
Cdd:cd01665    81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853 179 QAYEYWEAPFTIADAVYGSTFFIATGFHGLHVIIGTMFLLTCLMRHSKNQFSPSHHFGFEAAAWYWHFVDVVWLFLYISI 258
Cdd:cd01665   161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240


                  ...
gi 1331215853 259 YWW 261
Cdd:cd01665   241 YWW 243
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 8-263 9.68e-108

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 312.07  E-value: 9.68e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853   8 HPFHLVDYSPWPLTGAIGAMVLVSGLAKWFHLFNINLFTIGISITLLTMIQWWRDIIREGTYQGLHTGFVSIGLRWGMIL 87
Cdd:MTH00024    6 HPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGMLL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853  88 FIASEVLFFLSFFWAFFSSSLAPTIELGMLWPPMGIQPFNPMQIPLLNTAILLASGVTVTWAHHSLMESNHTQALQGLFF 167
Cdd:MTH00024   86 FILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853 168 TVMLGFYFTLLQAYEYWEAPFTIADAVYGSTFFIATGFHGLHVIIGTMFLLTCLMRHSKNQFSPSHHFGFEAAAWYWHFV 247
Cdd:MTH00024  166 TVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASWYWHFV 245

                         250
                  ....*....|....*.
gi 1331215853 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00024  246 DVVWLFLYLCIYWWGS 261
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 2-263 1.97e-103

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 301.33  E-value: 1.97e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853   2 LTKHSNHPFHLVDYSPWPLTGAIGAMVLVSGLAKWFHLFNINLFTIGISITLLTMIQWWRDIIREGTYQGLHTGFVSIGL 81
Cdd:MTH00052    1 MMQQYYHPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853  82 RWGMILFIASEVLFFLSFFWAFFSSSLAPTIELGMLWPPMGIQPFNPMQIPLLNTAILLASGVTVTWAHHSLMESNHTQA 161
Cdd:MTH00052   81 KYGMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853 162 LQGLFFTVMLGFYFTLLQAYEYWEAPFTIADAVYGSTFFIATGFHGLHVIIGTMFLLTCLMRHSKNQFSPSHHFGFEAAA 241
Cdd:MTH00052  161 IIGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAA 240

                         250       260
                  ....*....|....*....|..
gi 1331215853 242 WYWHFVDVVWLFLYISIYWWGS 263
Cdd:MTH00052  241 WYWHFVDVVWLFLFIFMYWWGS 262
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 8-263 4.97e-90

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 268.47  E-value: 4.97e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853   8 HPFHLVDYSPWPLTGAIGAMVLVSGLAKWFHLFNINLFTIGISITLLTMIQWWRDIIREGTYQGLHTGFVSIGLRWGMIL 87
Cdd:MTH00028    6 HPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853  88 FIASEVLFFLSFFWAFFSSSLAPTIELGMLWPPMGIQPFNPMQIPLLNTAILLASGVTVTWAHHSLMESNH--------- 158
Cdd:MTH00028   86 FILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTGNpaslekgtq 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853 159 ---------------------------TQALQGLFFTVMLGFYFTLLQAYEYWEAPFTIADAVYGSTFFIATGFHGLHVI 211
Cdd:MTH00028  166 giegpnpsngappdpqkgptfllsdfrTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVL 245

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1331215853 212 IGTMFLLTCLMRHSKNQFSPSHHFGFEAAAWYWHFVDVVWLFLYISIYWWGS 263
Cdd:MTH00028  246 VGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWGS 297
PLN02194 PLN02194
cytochrome-c oxidase
 2-262 9.60e-79

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 238.79  E-value: 9.60e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853   2 LTKHSNHPFHLVDYSPWPLTGAIGAMVLVSGLAKWFHLFN--INLFTIGISITLLTMIQWWRDIIREGTYQGLHTGFVSI 79
Cdd:PLN02194    1 MIESQRHSYHLVDPSPWPISGSLGALATTVGGVMYMHPFQggARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853  80 GLRWGMILFIASEVLFFLSFFWAFFSSSLAPTIELGMLWPPMGIQPFNPMQIPLLNTAILLASGVTVTWAHHSLMESNHT 159
Cdd:PLN02194   81 GPRYGSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853 160 QALQGLFFTVMLGFYFTLLQAYEYWEAPFTIADAVYGSTFFIATGFHGLHVIIGTMFLLTCLMRHSKNQFSPSHHFGFEA 239
Cdd:PLN02194  161 RAVYALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEA 240

                         250       260
                  ....*....|....*....|...
gi 1331215853 240 AAWYWHFVDVVWLFLYISIYWWG 262
Cdd:PLN02194  241 AAWYWHFVDVVWLFLFVSIYWWG 263
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
 8-263 1.43e-62

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 197.10  E-value: 1.43e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853   8 HPFHLVDYSPWPLTGAIGAMVLVSGLAKWFHLFNINLFTIGISITLLTMIQWWRDIIREGtYQGLHTGFVSIGLRWGMIL 87
Cdd:MTH00083    3 HNFHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMIL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853  88 FIASEVLFFLSFFWAFFSSSLAPTIELGMLWPPMGIQPFNPMQIPLLNTAILLASGVTVTWAHHSLMESNhTQALQGLFF 167
Cdd:MTH00083   82 FIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSN-KSCTNSLLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853 168 TVMLGFYFTLLQAYEYWEAPFTIADAVYGSTFFIATGFHGLHVIIGTMFLLTCLMRHSKNQFSPSHHFGFEAAAWYWHFV 247
Cdd:MTH00083  161 TCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFV 240

                         250
                  ....*....|....*.
gi 1331215853 248 DVVWLFLYISIYWWGS 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 5.46e-59

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: 185.48  E-value: 5.46e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853  73 HTGFVSIGLRWGMILFIASEVLFFLSFFWAFFSSSLAPTIELGMlwppmgiqPFNPMQIPLLNTAILLASGVTVTWAHHS 152
Cdd:cd00386     1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFGA--------GLDPLDLPLLNTNTLLLSGSSVTWAHAS 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853 153 LM--ESNHTQALQGLFFTVMLGFYFTLLQAYEYWEAPFTIADAVYGSTFFIATGFHGLHVIIGTMFLLTCLMRHSKNQFS 230
Cdd:cd00386    73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1331215853 231 PSHHFGFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:cd00386   153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
72-261 9.84e-46

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 151.93  E-value: 9.84e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853  72 LHTGFVSIGLRWGMILFIASEVLFFLSFFWAFFssslapTIELGMLWPPMGIQPFNPmQIPLLNTAILLASGVTVTWAHH 151
Cdd:COG1845     7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYF------VLRASAPDWPAGAELLDL-PLPLINTLLLLLSSFTVALAVR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853 152 SLMESNHTQALQGLFFTVMLGFYFTLLQAYEY---WEAPFTIADAVYGSTFFIATGFHGLHVIIGTMFLLTCLMRHSKNQ 228
Cdd:COG1845    80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1331215853 229 FSPSHHFGFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:COG1845   160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
NorE_like cd02862
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ...
 133-259 4.24e-21

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: 87.68  E-value: 4.24e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853 133 LLNTAILLASGVTVTWAHHSLMESNHTQALQGLFFTVMLGFYFTLLQAYEYWE---APFTIADAVYGSTFFIATGFHGLH 209
Cdd:cd02862    55 ALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYAHkiaAGIDPDAGLFFTLYFLLTGFHLLH 134

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1331215853 210 VIIGTMFLLTCLMRHSKNQFSPSHHFGFEAAAWYWHFVDVVWLFLYISIY 259
Cdd:cd02862   135 VLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVLFPLLY 184
Heme_Cu_Oxidase_III_2 cd02865
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 132-261 2.03e-16

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


Pssm-ID: 239216  Cd Length: 184  Bit Score: 75.10  E-value: 2.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853 132 PLLNTAILLASGVTVTWAHHSLMESNHTQALQGLFFTVMLGFYFTLLQAYEYWEAPF---TIADAVYGSTFFIATGFHGL 208
Cdd:cd02865    52 LSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWHALNDagyGPTSNPAGSFFYLLTGLHGL 131

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1331215853 209 HVIIGTMFLLTCLMRHSKNQFSPSHHFGFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:cd02865   132 HVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVLLALLYGT 184
Ubiquinol_oxidase_III cd02863
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ...
 133-259 4.57e-15

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


Pssm-ID: 239214  Cd Length: 186  Bit Score: 71.12  E-value: 4.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853 133 LLNTAILLASGVTVTWAHHSLMESNHTQALQGLFFTVMLGFYFTLLQAYE---YWEAPFTIADAVYGSTFFIATGFHGLH 209
Cdd:cd02863    54 FIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLVGTHGLH 133

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1331215853 210 VIIGTMFLLTCLMRHSKNQFSPSHHFGFEAAAWYWHFVDVVWLFLYISIY 259
Cdd:cd02863   134 VTFGLIWILVMIIQLKKRGLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
COX3 MTH00049
cytochrome c oxidase subunit III; Validated
 128-259 1.65e-14

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177124  Cd Length: 215  Bit Score: 70.33  E-value: 1.65e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853 128 PMQIPLLNTAILLASGVTVTwAHHSLMESNHTQALqgLFFTVMLGFYFTLLQAYEYWEAPFTIADAVYGSTFFIATGFHG 207
Cdd:MTH00049   89 SLEIPFVGCFLLLGSSITVT-AYHHLLGWKYCDLF--LYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHF 165

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1331215853 208 LHVIIGTMFLLTCLMRHSKNqFSPSHHfgfEAAAWYWHFVDVVWLFLYISIY 259
Cdd:MTH00049  166 SHVVLGVVGLSTLLLVGSSS-FGVYRS---TVLTWYWHFVDYIWLLVYLIVY 213
Heme_Cu_Oxidase_III_1 cd02864
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 136-261 1.31e-13

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: 67.53  E-value: 1.31e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853 136 TAILLASGVTVTWAHHSLMESNHTQALQGLFFTVMLGFYFTLLQAYEY-----------WEAPFTIAdaVYGSTFFIATG 204
Cdd:cd02864    67 TFILITSSGTMAMAVNFGYRGNRKAAARLMLATALLGATFVGMQAFEWtkliveegvrpWGNPWGAA--QFGASFFMITG 144

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1331215853 205 FHGLHVIIGTMFLLTCLMRHSKNQFSPSHHF-GFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:cd02864   145 FHGTHVTIGVIYLIIIARKVWRGKYQRIGRYeIVEIAGLYWHFVDLVWVFIFAFFYLW 202
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 133-262 2.08e-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: 55.63  E-value: 2.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853 133 LLNTAILLASGVTVTWAHHSLMESNHTQALQGLFFTVMLGFYFTLLQAYE---YWEAPFTIADAVYGSTFFIATGFHGLH 209
Cdd:TIGR02897  56 LIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCH 135

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1331215853 210 VIIGTMFLLTCLMRHSKNQFSPSHHFGFEAAAWYWHFVDVVWLFLYISIYWWG 262
Cdd:TIGR02897 136 VTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
PRK10663 PRK10663
cytochrome o ubiquinol oxidase subunit III; Provisional
 133-263 3.09e-07

cytochrome o ubiquinol oxidase subunit III; Provisional


Pssm-ID: 182628  Cd Length: 204  Bit Score: 49.78  E-value: 3.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215853 133 LLNTAILLASGVTVTWAHHSLMESNHTQALQGLFFTVMLGFYFTLLQAYEYW---EAPFTIADAVYGSTFFIATGFHGLH 209
Cdd:PRK10663   70 LVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFHhliVEGMGPDRSGFLSAFFALVGTHGLH 149

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1331215853 210 VIIGTMFLLTCLMRHSKNQFSPSHHFGFEAAAWYWHFVDVVWLFLYISIYWWGS 263
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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