NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1896069809|gb|QNJ47060|]
View 

cytochrome c oxidase subunit III, partial (mitochondrion) [Dictyophorus spumans]

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 3.04e-144

cytochrome c oxidase subunit III; Provisional


:

Pssm-ID: 214439  Cd Length: 255  Bit Score: 404.18  E-value: 3.04e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809   5 KSNQPFHLVDFSPWPIMSAMSAMILTSGLTKWFHTFNMNLLIMSIMIMIMIMIQWWRDVIRESTYQGLHTKSVSMGLRWG 84
Cdd:MTH00155    1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809  85 MMLFISSEVLFFISFFWAFFSSSITPTIEIGMTWPPMGIKPFNPMQIPLLNTAILLSSGVTVTWAHHSLMESNHSQTMQG 164
Cdd:MTH00155   81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809 165 LFFTSIMGMYFTMLQAYEYYEAPFTIADAIYGSTFFMATGFHGLHVIIGTMFLMTCLIRHSMNQFSSSHHFGFEAAAWYW 244
Cdd:MTH00155  161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240

                         250
                  ....*....|....*
gi 1896069809 245 HFVDVVWLLLYISIY 259
Cdd:MTH00155  241 HFVDVVWLFLYISIY 255
 
Name Accession Description Interval E-value
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 5-259 3.04e-144

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 404.18  E-value: 3.04e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809   5 KSNQPFHLVDFSPWPIMSAMSAMILTSGLTKWFHTFNMNLLIMSIMIMIMIMIQWWRDVIRESTYQGLHTKSVSMGLRWG 84
Cdd:MTH00155    1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809  85 MMLFISSEVLFFISFFWAFFSSSITPTIEIGMTWPPMGIKPFNPMQIPLLNTAILLSSGVTVTWAHHSLMESNHSQTMQG 164
Cdd:MTH00155   81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809 165 LFFTSIMGMYFTMLQAYEYYEAPFTIADAIYGSTFFMATGFHGLHVIIGTMFLMTCLIRHSMNQFSSSHHFGFEAAAWYW 244
Cdd:MTH00155  161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240

                         250
                  ....*....|....*
gi 1896069809 245 HFVDVVWLLLYISIY 259
Cdd:MTH00155  241 HFVDVVWLFLYISIY 255
COX3 pfam00510
Cytochrome c oxidase subunit III;
9-263 2.03e-112

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 323.98  E-value: 2.03e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809   9 PFHLVDFSPWPIMSAMSAMILTSGLTKWFHTF--NMNLLIMSIMIMIMIMIQWWRDVIRESTYQGLHTKSVSMGLRWGMM 86
Cdd:pfam00510   2 PFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYsgNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGMI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809  87 LFISSEVLFFISFFWAFFSSSITPTIEIGMTWPPMGIKPFNPMQIPLLNTAILLSSGVTVTWAHHSLMESNHSQTMQGLF 166
Cdd:pfam00510  82 LFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGLI 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809 167 FTSIMGMYFTMLQAYEYYEAPFTIADAIYGSTFFMATGFHGLHVIIGTMFLMTCLIRHSMNQFSSSHHFGFEAAAWYWHF 246
Cdd:pfam00510 162 LTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWHF 241

                         250
                  ....*....|....*..
gi 1896069809 247 VDVVWLLLYISIYWWGS 263
Cdd:pfam00510 242 VDVVWLFLYVSVYWWGS 258
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 20-261 2.98e-111

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: 320.23  E-value: 2.98e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809  20 IMSAMSAMILTSGLTKWFHTF-NMNLLIMSIMIMIMIMIQWWRDVIRESTYQGLHTKSVSMGLRWGMMLFISSEVLFFIS 98
Cdd:cd01665     1 ILGSFGLLLLALGLVLWMHGYgGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809  99 FFWAFFSSSITPTIEIGMTWPPMGIKPFNPMQIPLLNTAILLSSGVTVTWAHHSLMESNHSQTMQGLFFTSIMGMYFTML 178
Cdd:cd01665    81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809 179 QAYEYYEAPFTIADAIYGSTFFMATGFHGLHVIIGTMFLMTCLIRHSMNQFSSSHHFGFEAAAWYWHFVDVVWLLLYISI 258
Cdd:cd01665   161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240


                  ...
gi 1896069809 259 YWW 261
Cdd:cd01665   241 YWW 243
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
72-261 3.27e-46

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 153.08  E-value: 3.27e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809  72 LHTKSVSMGLRWGMMLFISSEVLFFISFFWAFFSSSITptieigMTWPPMGIKPFNPmQIPLLNTAILLSSGVTVTWAHH 151
Cdd:COG1845     7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS------APDWPAGAELLDL-PLPLINTLLLLLSSFTVALAVR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809 152 SLMESNHSQTMQGLFFTSIMGMYFTMLQAYEYYE---APFTIADAIYGSTFFMATGFHGLHVIIGTMFLMTCLIRHSMNQ 228
Cdd:COG1845    80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHliaEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1896069809 229 FSSSHHFGFEAAAWYWHFVDVVWLLLYISIYWW 261
Cdd:COG1845   160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 133-262 3.09e-08

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: 52.16  E-value: 3.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809 133 LLNTAILLSSGVTVTWAHHSLMESNHSQTMQGLFFTSIMGMYFTMLQAYE---YYEAPFTIADAIYGSTFFMATGFHGLH 209
Cdd:TIGR02897  56 LIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCH 135

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1896069809 210 VIIGTMFLMTCLI---RHSMNQFSSSHHFgfeAAAWYWHFVDVVWLLLYISIYWWG 262
Cdd:TIGR02897 136 VTLGIVWAICLLIqiqRRGLTPYTAPKVF---IVSLYWHFLDVVWVFIFTAVYLIG 188
 
Name Accession Description Interval E-value
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 5-259 3.04e-144

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 404.18  E-value: 3.04e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809   5 KSNQPFHLVDFSPWPIMSAMSAMILTSGLTKWFHTFNMNLLIMSIMIMIMIMIQWWRDVIRESTYQGLHTKSVSMGLRWG 84
Cdd:MTH00155    1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809  85 MMLFISSEVLFFISFFWAFFSSSITPTIEIGMTWPPMGIKPFNPMQIPLLNTAILLSSGVTVTWAHHSLMESNHSQTMQG 164
Cdd:MTH00155   81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809 165 LFFTSIMGMYFTMLQAYEYYEAPFTIADAIYGSTFFMATGFHGLHVIIGTMFLMTCLIRHSMNQFSSSHHFGFEAAAWYW 244
Cdd:MTH00155  161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240

                         250
                  ....*....|....*
gi 1896069809 245 HFVDVVWLLLYISIY 259
Cdd:MTH00155  241 HFVDVVWLFLYISIY 255
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 9-263 3.56e-130

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 368.90  E-value: 3.56e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809   9 PFHLVDFSPWPIMSAMSAMILTSGLTKWFHTFNMNLLIMSIMIMIMIMIQWWRDVIRESTYQGLHTKSVSMGLRWGMMLF 88
Cdd:MTH00118    7 PYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRYGMILF 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809  89 ISSEVLFFISFFWAFFSSSITPTIEIGMTWPPMGIKPFNPMQIPLLNTAILLSSGVTVTWAHHSLMESNHSQTMQGLFFT 168
Cdd:MTH00118   87 ITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQALTLT 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809 169 SIMGMYFTMLQAYEYYEAPFTIADAIYGSTFFMATGFHGLHVIIGTMFLMTCLIRHSMNQFSSSHHFGFEAAAWYWHFVD 248
Cdd:MTH00118  167 ILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWYWHFVD 246

                         250
                  ....*....|....*
gi 1896069809 249 VVWLLLYISIYWWGS 263
Cdd:MTH00118  247 VVWLFLYISIYWWGS 261
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 9-263 2.78e-127

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 361.60  E-value: 2.78e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809   9 PFHLVDFSPWPIMSAMSAMILTSGLTKWFHTFNMNLLIMSIMIMIMIMIQWWRDVIRESTYQGLHTKSVSMGLRWGMMLF 88
Cdd:MTH00189    6 PFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRYGMILF 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809  89 ISSEVLFFISFFWAFFSSSITPTIEIGMTWPPMGIKPFNPMQIPLLNTAILLSSGVTVTWAHHSLMESNHSQTMQGLFFT 168
Cdd:MTH00189   86 ITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQALTLT 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809 169 SIMGMYFTMLQAYEYYEAPFTIADAIYGSTFFMATGFHGLHVIIGTMFLMTCLIRHSMNQFSSSHHFGFEAAAWYWHFVD 248
Cdd:MTH00189  166 VILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWYWHFVD 245

                         250
                  ....*....|....*
gi 1896069809 249 VVWLLLYISIYWWGS 263
Cdd:MTH00189  246 VVWLFLYVSIYWWGS 260
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 9-263 7.97e-124

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 352.88  E-value: 7.97e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809   9 PFHLVDFSPWPIMSAMSAMILTSGLTKWFHTFNMNLLIMSIMIMIMIMIQWWRDVIRESTYQGLHTKSVSMGLRWGMMLF 88
Cdd:MTH00039    6 PYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRYGMILF 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809  89 ISSEVLFFISFFWAFFSSSITPTIEIGMTWPPMGIKPFNPMQIPLLNTAILLSSGVTVTWAHHSLMESNHSQTMQGLFFT 168
Cdd:MTH00039   86 ITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQALFLT 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809 169 SIMGMYFTMLQAYEYYEAPFTIADAIYGSTFFMATGFHGLHVIIGTMFLMTCLIRHSMNQFSSSHHFGFEAAAWYWHFVD 248
Cdd:MTH00039  166 VLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWYWHFVD 245

                         250
                  ....*....|....*
gi 1896069809 249 VVWLLLYISIYWWGS 263
Cdd:MTH00039  246 VVWLFLYVCIYWWGS 260
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 8-263 1.58e-122

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 349.57  E-value: 1.58e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809   8 QPFHLVDFSPWPIMSAMSAMILTSGLTKWFHTFNMNLLIMSIMIMIMIMIQWWRDVIRESTYQGLHTKSVSMGLRWGMML 87
Cdd:MTH00141    4 NPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFIL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809  88 FISSEVLFFISFFWAFFSSSITPTIEIGMTWPPMGIKPFNPMQIPLLNTAILLSSGVTVTWAHHSLMESNHSQTMQGLFF 167
Cdd:MTH00141   84 FIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809 168 TSIMGMYFTMLQAYEYYEAPFTIADAIYGSTFFMATGFHGLHVIIGTMFLMTCLIRHSMNQFSSSHHFGFEAAAWYWHFV 247
Cdd:MTH00141  164 TIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFV 243

                         250
                  ....*....|....*.
gi 1896069809 248 DVVWLLLYISIYWWGS 263
Cdd:MTH00141  244 DVVWLFLYLSIYWWGS 259
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 1-263 9.88e-119

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 339.84  E-value: 9.88e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809   1 MMTKKSNqPFHLVDFSPWPIMSAMSAMILTSGLTKWFHTFNMNLLIMSIMIMIMIMIQWWRDVIRESTYQGLHTKSVSMG 80
Cdd:MTH00219    1 MMFFQTN-PYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809  81 LRWGMMLFISSEVLFFISFFWAFFSSSITPTIEIGMTWPPMGIKPFNPMQIPLLNTAILLSSGVTVTWAHHSLMESNHSQ 160
Cdd:MTH00219   80 LRIGMILFIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809 161 TMQGLFFTSIMGMYFTMLQAYEYYEAPFTIADAIYGSTFFMATGFHGLHVIIGTMFLMTCLIRHSMNQFSSSHHFGFEAA 240
Cdd:MTH00219  160 AQQGLLFTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAA 239

                         250       260
                  ....*....|....*....|...
gi 1896069809 241 AWYWHFVDVVWLLLYISIYWWGS 263
Cdd:MTH00219  240 AWYWHFVDVVWLFLYVSIYWWGS 262
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 10-263 1.12e-116

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 334.79  E-value: 1.12e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809  10 FHLVDFSPWPIMSAMSAMILTSGLTKWFHTFNMNLLIMSIMIMIMIMIQWWRDVIRESTYQGLHTKSVSMGLRWGMMLFI 89
Cdd:MTH00075    8 FHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRYGMILFI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809  90 SSEVLFFISFFWAFFSSSITPTIEIGMTWPPMGIKPFNPMQIPLLNTAILLSSGVTVTWAHHSLMESNHSQTMQGLFFTS 169
Cdd:MTH00075   88 TSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQSLALTI 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809 170 IMGMYFTMLQAYEYYEAPFTIADAIYGSTFFMATGFHGLHVIIGTMFLMTCLIRHSMNQFSSSHHFGFEAAAWYWHFVDV 249
Cdd:MTH00075  168 ILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWYWHFVDV 247

                         250
                  ....*....|....
gi 1896069809 250 VWLLLYISIYWWGS 263
Cdd:MTH00075  248 VWLFLYVSIYWWGS 261
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 9-263 2.44e-116

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 334.00  E-value: 2.44e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809   9 PFHLVDFSPWPIMSAMSAMILTSGLTKWFHTFNMNLLIMSIMIMIMIMIQWWRDVIRESTYQGLHTKSVSMGLRWGMMLF 88
Cdd:MTH00099    7 AYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRYGMILF 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809  89 ISSEVLFFISFFWAFFSSSITPTIEIGMTWPPMGIKPFNPMQIPLLNTAILLSSGVTVTWAHHSLMESNHSQTMQGLFFT 168
Cdd:MTH00099   87 IISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQALFIT 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809 169 SIMGMYFTMLQAYEYYEAPFTIADAIYGSTFFMATGFHGLHVIIGTMFLMTCLIRHSMNQFSSSHHFGFEAAAWYWHFVD 248
Cdd:MTH00099  167 ILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWYWHFVD 246

                         250
                  ....*....|....*
gi 1896069809 249 VVWLLLYISIYWWGS 263
Cdd:MTH00099  247 VVWLFLYVSIYWWGS 261
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 9-263 3.75e-115

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 330.96  E-value: 3.75e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809   9 PFHLVDFSPWPIMSAMSAMILTSGLTKWFHTFNMNLLIMSIMIMIMIMIQWWRDVIRESTYQGLHTKSVSMGLRWGMMLF 88
Cdd:MTH00130    7 AYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRYGMILF 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809  89 ISSEVLFFISFFWAFFSSSITPTIEIGMTWPPMGIKPFNPMQIPLLNTAILLSSGVTVTWAHHSLMESNHSQTMQGLFFT 168
Cdd:MTH00130   87 ITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQSLTLT 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809 169 SIMGMYFTMLQAYEYYEAPFTIADAIYGSTFFMATGFHGLHVIIGTMFLMTCLIRHSMNQFSSSHHFGFEAAAWYWHFVD 248
Cdd:MTH00130  167 ILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWYWHFVD 246

                         250
                  ....*....|....*
gi 1896069809 249 VVWLLLYISIYWWGS 263
Cdd:MTH00130  247 VVWLFLYISIYWWGS 261
COX3 pfam00510
Cytochrome c oxidase subunit III;
9-263 2.03e-112

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 323.98  E-value: 2.03e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809   9 PFHLVDFSPWPIMSAMSAMILTSGLTKWFHTF--NMNLLIMSIMIMIMIMIQWWRDVIRESTYQGLHTKSVSMGLRWGMM 86
Cdd:pfam00510   2 PFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYsgNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGMI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809  87 LFISSEVLFFISFFWAFFSSSITPTIEIGMTWPPMGIKPFNPMQIPLLNTAILLSSGVTVTWAHHSLMESNHSQTMQGLF 166
Cdd:pfam00510  82 LFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGLI 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809 167 FTSIMGMYFTMLQAYEYYEAPFTIADAIYGSTFFMATGFHGLHVIIGTMFLMTCLIRHSMNQFSSSHHFGFEAAAWYWHF 246
Cdd:pfam00510 162 LTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWHF 241

                         250
                  ....*....|....*..
gi 1896069809 247 VDVVWLLLYISIYWWGS 263
Cdd:pfam00510 242 VDVVWLFLYVSVYWWGS 258
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 20-261 2.98e-111

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: 320.23  E-value: 2.98e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809  20 IMSAMSAMILTSGLTKWFHTF-NMNLLIMSIMIMIMIMIQWWRDVIRESTYQGLHTKSVSMGLRWGMMLFISSEVLFFIS 98
Cdd:cd01665     1 ILGSFGLLLLALGLVLWMHGYgGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809  99 FFWAFFSSSITPTIEIGMTWPPMGIKPFNPMQIPLLNTAILLSSGVTVTWAHHSLMESNHSQTMQGLFFTSIMGMYFTML 178
Cdd:cd01665    81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809 179 QAYEYYEAPFTIADAIYGSTFFMATGFHGLHVIIGTMFLMTCLIRHSMNQFSSSHHFGFEAAAWYWHFVDVVWLLLYISI 258
Cdd:cd01665   161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240


                  ...
gi 1896069809 259 YWW 261
Cdd:cd01665   241 YWW 243
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 8-263 1.17e-107

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 311.77  E-value: 1.17e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809   8 QPFHLVDFSPWPIMSAMSAMILTSGLTKWFHTFNMNLLIMSIMIMIMIMIQWWRDVIRESTYQGLHTKSVSMGLRWGMML 87
Cdd:MTH00009    4 QPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMIL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809  88 FISSEVLFFISFFWAFFSSSITPTIEIGMTWPPMGIKPFNPMQIPLLNTAILLSSGVTVTWAHHSLMESNHSQTMQGLFF 167
Cdd:MTH00009   84 FIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALIL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809 168 TSIMGMYFTMLQAYEYYEAPFTIADAIYGSTFFMATGFHGLHVIIGTMFLMTCLIRHSMNQFSSSHHFGFEAAAWYWHFV 247
Cdd:MTH00009  164 TVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFV 243

                         250
                  ....*....|....*.
gi 1896069809 248 DVVWLLLYISIYWWGS 263
Cdd:MTH00009  244 DVVWIFLYLCIYWWGS 259
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 9-263 4.85e-106

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 307.83  E-value: 4.85e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809   9 PFHLVDFSPWPIMSAMSAMILTSGLTKWFHTFNMNLLIMSIMIMIMIMIQWWRDVIRESTYQGLHTKSVSMGLRWGMMLF 88
Cdd:MTH00024    7 PYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGMLLF 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809  89 ISSEVLFFISFFWAFFSSSITPTIEIGMTWPPMGIKPFNPMQIPLLNTAILLSSGVTVTWAHHSLMESNHSQTMQGLFFT 168
Cdd:MTH00024   87 ILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFLT 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809 169 SIMGMYFTMLQAYEYYEAPFTIADAIYGSTFFMATGFHGLHVIIGTMFLMTCLIRHSMNQFSSSHHFGFEAAAWYWHFVD 248
Cdd:MTH00024  167 VFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASWYWHFVD 246

                         250
                  ....*....|....*
gi 1896069809 249 VVWLLLYISIYWWGS 263
Cdd:MTH00024  247 VVWLFLYLCIYWWGS 261
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 2-263 1.79e-98

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 288.61  E-value: 1.79e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809   2 MTKKSNQPFHLVDFSPWPIMSAMSAMILTSGLTKWFHTFNMNLLIMSIMIMIMIMIQWWRDVIRESTYQGLHTKSVSMGL 81
Cdd:MTH00052    1 MMQQYYHPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809  82 RWGMMLFISSEVLFFISFFWAFFSSSITPTIEIGMTWPPMGIKPFNPMQIPLLNTAILLSSGVTVTWAHHSLMESNHSQT 161
Cdd:MTH00052   81 KYGMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809 162 MQGLFFTSIMGMYFTMLQAYEYYEAPFTIADAIYGSTFFMATGFHGLHVIIGTMFLMTCLIRHSMNQFSSSHHFGFEAAA 241
Cdd:MTH00052  161 IIGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAA 240

                         250       260
                  ....*....|....*....|..
gi 1896069809 242 WYWHFVDVVWLLLYISIYWWGS 263
Cdd:MTH00052  241 WYWHFVDVVWLFLFIFMYWWGS 262
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 8-263 1.19e-85

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 257.30  E-value: 1.19e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809   8 QPFHLVDFSPWPIMSAMSAMILTSGLTKWFHTFNMNLLIMSIMIMIMIMIQWWRDVIRESTYQGLHTKSVSMGLRWGMML 87
Cdd:MTH00028    6 HPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809  88 FISSEVLFFISFFWAFFSSSITPTIEIGMTWPPMGIKPFNPMQIPLLNTAILLSSGVTVTWAHHSLM------------- 154
Cdd:MTH00028   86 FILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIgtgnpaslekgtq 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809 155 ------ESNHSQTMQ-----------------GLFFTSIMGMYFTMLQAYEYYEAPFTIADAIYGSTFFMATGFHGLHVI 211
Cdd:MTH00028  166 giegpnPSNGAPPDPqkgptfllsdfrtnaviGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVL 245

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1896069809 212 IGTMFLMTCLIRHSMNQFSSSHHFGFEAAAWYWHFVDVVWLLLYISIYWWGS 263
Cdd:MTH00028  246 VGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWGS 297
PLN02194 PLN02194
cytochrome-c oxidase
 2-262 5.98e-78

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 236.48  E-value: 5.98e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809   2 MTKKSNQPFHLVDFSPWPIMSAMSAMILTSGLTKWFHTFN--MNLLIMSIMIMIMIMIQWWRDVIRESTYQGLHTKSVSM 79
Cdd:PLN02194    1 MIESQRHSYHLVDPSPWPISGSLGALATTVGGVMYMHPFQggARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809  80 GLRWGMMLFISSEVLFFISFFWAFFSSSITPTIEIGMTWPPMGIKPFNPMQIPLLNTAILLSSGVTVTWAHHSLMESNHS 159
Cdd:PLN02194   81 GPRYGSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809 160 QTMQGLFFTSIMGMYFTMLQAYEYYEAPFTIADAIYGSTFFMATGFHGLHVIIGTMFLMTCLIRHSMNQFSSSHHFGFEA 239
Cdd:PLN02194  161 RAVYALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEA 240

                         250       260
                  ....*....|....*....|...
gi 1896069809 240 AAWYWHFVDVVWLLLYISIYWWG 262
Cdd:PLN02194  241 AAWYWHFVDVVWLFLFVSIYWWG 263
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
 10-263 2.86e-60

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 191.32  E-value: 2.86e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809  10 FHLVDFSPWPIMSAMSAMILTSGLTKWFHTFNMNLLIMSIMIMIMIMIQWWRDVIREStYQGLHTKSVSMGLRWGMMLFI 89
Cdd:MTH00083    5 FHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMILFI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809  90 SSEVLFFISFFWAFFSSSITPTIEIGMTWPPMGIKPFNPMQIPLLNTAILLSSGVTVTWAHHSLMESNHSQTMqGLFFTS 169
Cdd:MTH00083   84 FSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSNKSCTN-SLLLTC 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809 170 IMGMYFTMLQAYEYYEAPFTIADAIYGSTFFMATGFHGLHVIIGTMFLMTCLIRHSMNQFSSSHHFGFEAAAWYWHFVDV 249
Cdd:MTH00083  163 FLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFVDV 242

                         250
                  ....*....|....
gi 1896069809 250 VWLLLYISIYWWGS 263
Cdd:MTH00083  243 VWLFLFVFVYWWSY 256
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 73-261 1.45e-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: 186.64  E-value: 1.45e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809  73 HTKSVSMGLRWGMMLFISSEVLFFISFFWAFFSSSITPTIEIGMtwppmgikPFNPMQIPLLNTAILLSSGVTVTWAHHS 152
Cdd:cd00386     1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFGA--------GLDPLDLPLLNTNTLLLSGSSVTWAHAS 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809 153 LM--ESNHSQTMQGLFFTSIMGMYFTMLQAYEYYEAPFTIADAIYGSTFFMATGFHGLHVIIGTMFLMTCLIRHSMNQFS 230
Cdd:cd00386    73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1896069809 231 SSHHFGFEAAAWYWHFVDVVWLLLYISIYWW 261
Cdd:cd00386   153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
72-261 3.27e-46

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 153.08  E-value: 3.27e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809  72 LHTKSVSMGLRWGMMLFISSEVLFFISFFWAFFSSSITptieigMTWPPMGIKPFNPmQIPLLNTAILLSSGVTVTWAHH 151
Cdd:COG1845     7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS------APDWPAGAELLDL-PLPLINTLLLLLSSFTVALAVR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809 152 SLMESNHSQTMQGLFFTSIMGMYFTMLQAYEYYE---APFTIADAIYGSTFFMATGFHGLHVIIGTMFLMTCLIRHSMNQ 228
Cdd:COG1845    80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHliaEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1896069809 229 FSSSHHFGFEAAAWYWHFVDVVWLLLYISIYWW 261
Cdd:COG1845   160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
NorE_like cd02862
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ...
 133-259 7.06e-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: 86.91  E-value: 7.06e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809 133 LLNTAILLSSGVTVTWAHHSLMESNHSQTMQGLFFTSIMGMYFTMLQAYEYYEApFTIADAIYGSTFFMA----TGFHGL 208
Cdd:cd02862    55 ALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYAHK-IAAGIDPDAGLFFTLyfllTGFHLL 133

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1896069809 209 HVIIGTMFLMTCLIRHSMNQFSSSHHFGFEAAAWYWHFVDVVWLLLYISIY 259
Cdd:cd02862   134 HVLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVLFPLLY 184
COX3 MTH00049
cytochrome c oxidase subunit III; Validated
 128-259 7.48e-17

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177124  Cd Length: 215  Bit Score: 76.88  E-value: 7.48e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809 128 PMQIPLLNTAILLSSGVTVTwAHHSLMESNHSQTMqgLFFTSIMGMYFTMLQAYEYYEAPFTIADAIYGSTFFMATGFHG 207
Cdd:MTH00049   89 SLEIPFVGCFLLLGSSITVT-AYHHLLGWKYCDLF--LYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHF 165

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1896069809 208 LHVIIGTMFLMTCLIRHSMNqFSSSHHfgfEAAAWYWHFVDVVWLLLYISIY 259
Cdd:MTH00049  166 SHVVLGVVGLSTLLLVGSSS-FGVYRS---TVLTWYWHFVDYIWLLVYLIVY 213
Ubiquinol_oxidase_III cd02863
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ...
 133-259 3.54e-14

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


Pssm-ID: 239214  Cd Length: 186  Bit Score: 68.81  E-value: 3.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809 133 LLNTAILLSSGVTVTWAHHSLMESNHSQTMQGLFFTSIMGMYFTMLQAYE---YYEAPFTIADAIYGSTFFMATGFHGLH 209
Cdd:cd02863    54 FIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLVGTHGLH 133

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1896069809 210 VIIGTMFLMTCLIRHSMNQFSSSHHFGFEAAAWYWHFVDVVWLLLYISIY 259
Cdd:cd02863   134 VTFGLIWILVMIIQLKKRGLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
Heme_Cu_Oxidase_III_2 cd02865
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 132-261 2.06e-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: 239216  Cd Length: 184  Bit Score: 66.62  E-value: 2.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809 132 PLLNTAILLSSGVTVTWAHHSLMESNHSQTMQGLFFTSIMGMYFTMLQAYEYYEAPF---TIADAIYGSTFFMATGFHGL 208
Cdd:cd02865    52 LSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWHALNDagyGPTSNPAGSFFYLLTGLHGL 131

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1896069809 209 HVIIGTMFLMTCLIRHSMNQFSSSHHFGFEAAAWYWHFVDVVWLLLYISIYWW 261
Cdd:cd02865   132 HVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVLLALLYGT 184
Heme_Cu_Oxidase_III_1 cd02864
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 84-261 2.42e-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: 66.76  E-value: 2.42e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809  84 GMMLFISSEVLFFISFFWAFFSSSITPTIEIGMTWPPMGIkPFNPMQIPL----LNTAILLSSGVTVTWAHHSLMESNHS 159
Cdd:cd02864    12 MMWFFLLSDAFIFSSFLIAYMTARISTTEPWPLPSDVFAL-RIGHFNIPLvliaIMTFILITSSGTMAMAVNFGYRGNRK 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809 160 QTMQGLFFTSIMGMYFTMLQAYEYYE---------APFTIADAIYGSTFFMATGFHGLHVIIGTMFLMTCLIRHSMNQFS 230
Cdd:cd02864    91 AAARLMLATALLGATFVGMQAFEWTKliveegvrpWGNPWGAAQFGASFFMITGFHGTHVTIGVIYLIIIARKVWRGKYQ 170

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1896069809 231 SSHHF-GFEAAAWYWHFVDVVWLLLYISIYWW 261
Cdd:cd02864   171 RIGRYeIVEIAGLYWHFVDLVWVFIFAFFYLW 202
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 133-262 3.09e-08

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: 52.16  E-value: 3.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809 133 LLNTAILLSSGVTVTWAHHSLMESNHSQTMQGLFFTSIMGMYFTMLQAYE---YYEAPFTIADAIYGSTFFMATGFHGLH 209
Cdd:TIGR02897  56 LIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCH 135

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1896069809 210 VIIGTMFLMTCLI---RHSMNQFSSSHHFgfeAAAWYWHFVDVVWLLLYISIYWWG 262
Cdd:TIGR02897 136 VTLGIVWAICLLIqiqRRGLTPYTAPKVF---IVSLYWHFLDVVWVFIFTAVYLIG 188
PRK10663 PRK10663
cytochrome o ubiquinol oxidase subunit III; Provisional
 133-263 3.18e-08

cytochrome o ubiquinol oxidase subunit III; Provisional


Pssm-ID: 182628  Cd Length: 204  Bit Score: 52.48  E-value: 3.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069809 133 LLNTAILLSSGVTVTWAHHSLMESNHSQTMQGLFFTSIMGMYFTMLQAYEYY---EAPFTIADAIYGSTFFMATGFHGLH 209
Cdd:PRK10663   70 LVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFHhliVEGMGPDRSGFLSAFFALVGTHGLH 149

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1896069809 210 VIIGTMFLMTCLIRHSMNQFSSSHHFGFEAAAWYWHFVDVVWLLLYISIYWWGS 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH