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Conserved domains on  [gi|168487804|ref|NP_976174|]
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cytochrome c oxidase subunit III (mitochondrion) [Biomphalaria glabrata]

Protein Classification

cytochrome c oxidase subunit 3( domain architecture ID 10791091)

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 MTH00141
cytochrome c oxidase subunit III; Provisional
 1-258 7.71e-138

cytochrome c oxidase subunit III; Provisional


:

Pssm-ID: 177199  Cd Length: 259  Bit Score: 388.09  E-value: 7.71e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804   1 MRQPFHLVEFSPWPLLISFSIFSMPIGLINYIRSSNISLLILGLFTTALISFLWWRDVVRESTYQGFHNKLVMKGLKIGI 80
Cdd:MTH00141   2 TRNPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804  81 MLFILSEVCFFFAFFWAYFHSSLAPSVEIGAIWPPTGIFTLQAFQVPLLNTSVLLLSGVSITWVHHSIEEGNYKSAMQGL 160
Cdd:MTH00141  82 ILFIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 161 FITILLGLYFLMLQYGEYSETMFSISDGIYGSCLFMATGFHGTHVAVGATFLIVCFFRLKNFHFNKNHHIGFLAAAWYWH 240
Cdd:MTH00141 162 GLTIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWH 241

                        250
                 ....*....|....*...
gi 168487804 241 FVDVVWLFLYVSIYWWGS 258
Cdd:MTH00141 242 FVDVVWLFLYLSIYWWGS 259
 
Name Accession Description Interval E-value
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 1-258 7.71e-138

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 388.09  E-value: 7.71e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804   1 MRQPFHLVEFSPWPLLISFSIFSMPIGLINYIRSSNISLLILGLFTTALISFLWWRDVVRESTYQGFHNKLVMKGLKIGI 80
Cdd:MTH00141   2 TRNPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804  81 MLFILSEVCFFFAFFWAYFHSSLAPSVEIGAIWPPTGIFTLQAFQVPLLNTSVLLLSGVSITWVHHSIEEGNYKSAMQGL 160
Cdd:MTH00141  82 ILFIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 161 FITILLGLYFLMLQYGEYSETMFSISDGIYGSCLFMATGFHGTHVAVGATFLIVCFFRLKNFHFNKNHHIGFLAAAWYWH 240
Cdd:MTH00141 162 GLTIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWH 241

                        250
                 ....*....|....*...
gi 168487804 241 FVDVVWLFLYVSIYWWGS 258
Cdd:MTH00141 242 FVDVVWLFLYLSIYWWGS 259
COX3 pfam00510
Cytochrome c oxidase subunit III;
4-258 3.19e-108

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 313.19  E-value: 3.19e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804    4 PFHLVEFSPWPLLISFSIFSMPIGLINYIR--SSNISLLILGLFTTALISFLWWRDVVRESTYQGFHNKLVMKGLKIGIM 81
Cdd:pfam00510   2 PFHMVSPSPWPLFGSFALLLLTSGLVLWFHgySGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGMI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804   82 LFILSEVCFFFAFFWAYFHSSLAPSVEIGAIWPPTGIFTLQAFQVPLLNTSVLLLSGVSITWVHHSIEEGNYKSAMQGLF 161
Cdd:pfam00510  82 LFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGLI 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804  162 ITILLGLYFLMLQYGEYSETMFSISDGIYGSCLFMATGFHGTHVAVGATFLIVCFFRLKNFHFNKNHHIGFLAAAWYWHF 241
Cdd:pfam00510 162 LTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWHF 241

                         250
                  ....*....|....*..
gi 168487804  242 VDVVWLFLYVSIYWWGS 258
Cdd:pfam00510 242 VDVVWLFLYVSVYWWGS 258
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 15-256 6.33e-106

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: 306.75  E-value: 6.33e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804  15 LLISFSIFSMPIGLINYIR-SSNISLLILGLFTTALISFLWWRDVVRESTYQGFHNKLVMKGLKIGIMLFILSEVCFFFA 93
Cdd:cd01665    1 ILGSFGLLLLALGLVLWMHgYGGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804  94 FFWAYFHSSLAPSVEIGAIWPPTGIFTLQAFQVPLLNTSVLLLSGVSITWVHHSIEEGNYKSAMQGLFITILLGLYFLML 173
Cdd:cd01665   81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 174 QYGEYSETMFSISDGIYGSCLFMATGFHGTHVAVGATFLIVCFFRLKNFHFNKNHHIGFLAAAWYWHFVDVVWLFLYVSI 253
Cdd:cd01665  161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240


                 ...
gi 168487804 254 YWW 256
Cdd:cd01665  241 YWW 243
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
127-256 4.91e-41

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 139.60  E-value: 4.91e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 127 PLLNTSVLLLSGVSITWVHHSIEEGNYKSAMQGLFITILLGLYFLMLQYGEYSETM---FSISDGIYGSCLFMATGFHGT 203
Cdd:COG1845   60 PLINTLLLLLSSFTVALAVRAARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHLIaegLTPTSNAFGSFFFLLTGFHGL 139

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 168487804 204 HVAVGATFLIVCFFRLKNFHFNKNHHIGFLAAAWYWHFVDVVWLFLYVSIYWW 256
Cdd:COG1845  140 HVIIGLIWLLVVLVRALRGGFTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 114-257 1.16e-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: 56.40  E-value: 1.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804  114 PPTGIFTLQAFqvpLLNTSVLLLSGVSITWVHHSIEEGNYKSAMQGLFITILLGLYFL---MLQYGEYSETMFSISDGIY 190
Cdd:TIGR02897  45 MPAELFELPLV---LIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVgfeIYEFAHYASEGVTPQIGSY 121

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 168487804  191 GSCLFMATGFHGTHVAVGATFLIVCFFRLKNFHFNKNHHIGFLAAAWYWHFVDVVWLFLYVSIYWWG 257
Cdd:TIGR02897 122 WSSFFVLLGTHGCHVTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
 
Name Accession Description Interval E-value
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 1-258 7.71e-138

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 388.09  E-value: 7.71e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804   1 MRQPFHLVEFSPWPLLISFSIFSMPIGLINYIRSSNISLLILGLFTTALISFLWWRDVVRESTYQGFHNKLVMKGLKIGI 80
Cdd:MTH00141   2 TRNPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804  81 MLFILSEVCFFFAFFWAYFHSSLAPSVEIGAIWPPTGIFTLQAFQVPLLNTSVLLLSGVSITWVHHSIEEGNYKSAMQGL 160
Cdd:MTH00141  82 ILFIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 161 FITILLGLYFLMLQYGEYSETMFSISDGIYGSCLFMATGFHGTHVAVGATFLIVCFFRLKNFHFNKNHHIGFLAAAWYWH 240
Cdd:MTH00141 162 GLTIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWH 241

                        250
                 ....*....|....*...
gi 168487804 241 FVDVVWLFLYVSIYWWGS 258
Cdd:MTH00141 242 FVDVVWLFLYLSIYWWGS 259
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 1-254 3.82e-122

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 347.94  E-value: 3.82e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804   1 MRQPFHLVEFSPWPLLISFSIFSMPIGLINYIRSSNISLLILGLFTTALISFLWWRDVVRESTYQGFHNKLVMKGLKIGI 80
Cdd:MTH00155   2 KNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804  81 MLFILSEVCFFFAFFWAYFHSSLAPSVEIGAIWPPTGIFTLQAFQVPLLNTSVLLLSGVSITWVHHSIEEGNYKSAMQGL 160
Cdd:MTH00155  82 ILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 161 FITILLGLYFLMLQYGEYSETMFSISDGIYGSCLFMATGFHGTHVAVGATFLIVCFFRLKNFHFNKNHHIGFLAAAWYWH 240
Cdd:MTH00155 162 FFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYWH 241

                        250
                 ....*....|....
gi 168487804 241 FVDVVWLFLYVSIY 254
Cdd:MTH00155 242 FVDVVWLFLYISIY 255
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 4-258 3.64e-117

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 335.79  E-value: 3.64e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804   4 PFHLVEFSPWPLLISFSIFSMPIGLINYIRSSNISLLILGLFTTALISFLWWRDVVRESTYQGFHNKLVMKGLKIGIMLF 83
Cdd:MTH00189   6 PFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRYGMILF 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804  84 ILSEVCFFFAFFWAYFHSSLAPSVEIGAIWPPTGIFTLQAFQVPLLNTSVLLLSGVSITWVHHSIEEGNYKSAMQGLFIT 163
Cdd:MTH00189  86 ITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQALTLT 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 164 ILLGLYFLMLQYGEYSETMFSISDGIYGSCLFMATGFHGTHVAVGATFLIVCFFRLKNFHFNKNHHIGFLAAAWYWHFVD 243
Cdd:MTH00189 166 VILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWYWHFVD 245

                        250
                 ....*....|....*
gi 168487804 244 VVWLFLYVSIYWWGS 258
Cdd:MTH00189 246 VVWLFLYVSIYWWGS 260
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 4-258 1.12e-116

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 334.61  E-value: 1.12e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804   4 PFHLVEFSPWPLLISFSIFSMPIGLINYIRSSNISLLILGLFTTALISFLWWRDVVRESTYQGFHNKLVMKGLKIGIMLF 83
Cdd:MTH00118   7 PYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRYGMILF 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804  84 ILSEVCFFFAFFWAYFHSSLAPSVEIGAIWPPTGIFTLQAFQVPLLNTSVLLLSGVSITWVHHSIEEGNYKSAMQGLFIT 163
Cdd:MTH00118  87 ITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQALTLT 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 164 ILLGLYFLMLQYGEYSETMFSISDGIYGSCLFMATGFHGTHVAVGATFLIVCFFRLKNFHFNKNHHIGFLAAAWYWHFVD 243
Cdd:MTH00118 167 ILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWYWHFVD 246

                        250
                 ....*....|....*
gi 168487804 244 VVWLFLYVSIYWWGS 258
Cdd:MTH00118 247 VVWLFLYISIYWWGS 261
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 4-258 8.25e-112

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 322.06  E-value: 8.25e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804   4 PFHLVEFSPWPLLISFSIFSMPIGLINYIRSSNISLLILGLFTTALISFLWWRDVVRESTYQGFHNKLVMKGLKIGIMLF 83
Cdd:MTH00039   6 PYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRYGMILF 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804  84 ILSEVCFFFAFFWAYFHSSLAPSVEIGAIWPPTGIFTLQAFQVPLLNTSVLLLSGVSITWVHHSIEEGNYKSAMQGLFIT 163
Cdd:MTH00039  86 ITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQALFLT 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 164 ILLGLYFLMLQYGEYSETMFSISDGIYGSCLFMATGFHGTHVAVGATFLIVCFFRLKNFHFNKNHHIGFLAAAWYWHFVD 243
Cdd:MTH00039 166 VLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWYWHFVD 245

                        250
                 ....*....|....*
gi 168487804 244 VVWLFLYVSIYWWGS 258
Cdd:MTH00039 246 VVWLFLYVCIYWWGS 260
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 4-258 9.53e-112

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 322.06  E-value: 9.53e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804   4 PFHLVEFSPWPLLISFSIFSMPIGLINYIRSSNISLLILGLFTTALISFLWWRDVVRESTYQGFHNKLVMKGLKIGIMLF 83
Cdd:MTH00099   7 AYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRYGMILF 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804  84 ILSEVCFFFAFFWAYFHSSLAPSVEIGAIWPPTGIFTLQAFQVPLLNTSVLLLSGVSITWVHHSIEEGNYKSAMQGLFIT 163
Cdd:MTH00099  87 IISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQALFIT 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 164 ILLGLYFLMLQYGEYSETMFSISDGIYGSCLFMATGFHGTHVAVGATFLIVCFFRLKNFHFNKNHHIGFLAAAWYWHFVD 243
Cdd:MTH00099 167 ILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWYWHFVD 246

                        250
                 ....*....|....*
gi 168487804 244 VVWLFLYVSIYWWGS 258
Cdd:MTH00099 247 VVWLFLYVSIYWWGS 261
COX3 pfam00510
Cytochrome c oxidase subunit III;
4-258 3.19e-108

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 313.19  E-value: 3.19e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804    4 PFHLVEFSPWPLLISFSIFSMPIGLINYIR--SSNISLLILGLFTTALISFLWWRDVVRESTYQGFHNKLVMKGLKIGIM 81
Cdd:pfam00510   2 PFHMVSPSPWPLFGSFALLLLTSGLVLWFHgySGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGMI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804   82 LFILSEVCFFFAFFWAYFHSSLAPSVEIGAIWPPTGIFTLQAFQVPLLNTSVLLLSGVSITWVHHSIEEGNYKSAMQGLF 161
Cdd:pfam00510  82 LFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGLI 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804  162 ITILLGLYFLMLQYGEYSETMFSISDGIYGSCLFMATGFHGTHVAVGATFLIVCFFRLKNFHFNKNHHIGFLAAAWYWHF 241
Cdd:pfam00510 162 LTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWHF 241

                         250
                  ....*....|....*..
gi 168487804  242 VDVVWLFLYVSIYWWGS 258
Cdd:pfam00510 242 VDVVWLFLYVSVYWWGS 258
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 15-256 6.33e-106

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: 306.75  E-value: 6.33e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804  15 LLISFSIFSMPIGLINYIR-SSNISLLILGLFTTALISFLWWRDVVRESTYQGFHNKLVMKGLKIGIMLFILSEVCFFFA 93
Cdd:cd01665    1 ILGSFGLLLLALGLVLWMHgYGGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804  94 FFWAYFHSSLAPSVEIGAIWPPTGIFTLQAFQVPLLNTSVLLLSGVSITWVHHSIEEGNYKSAMQGLFITILLGLYFLML 173
Cdd:cd01665   81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 174 QYGEYSETMFSISDGIYGSCLFMATGFHGTHVAVGATFLIVCFFRLKNFHFNKNHHIGFLAAAWYWHFVDVVWLFLYVSI 253
Cdd:cd01665  161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240


                 ...
gi 168487804 254 YWW 256
Cdd:cd01665  241 YWW 243
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 2-258 1.51e-105

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 306.33  E-value: 1.51e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804   2 RQPFHLVEFSPWPLLISFSIFSMPIGLINYIRSSNISLLILGLFTTALISFLWWRDVVRESTYQGFHNKLVMKGLKIGIM 81
Cdd:MTH00219   6 TNPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLRIGMI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804  82 LFILSEVCFFFAFFWAYFHSSLAPSVEIGAIWPPTGIFTLQAFQVPLLNTSVLLLSGVSITWVHHSIEEGNYKSAMQGLF 161
Cdd:MTH00219  86 LFIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQQGLL 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 162 ITILLGLYFLMLQYGEYSETMFSISDGIYGSCLFMATGFHGTHVAVGATFLIVCFFRLKNFHFNKNHHIGFLAAAWYWHF 241
Cdd:MTH00219 166 FTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAAWYWHF 245

                        250
                 ....*....|....*..
gi 168487804 242 VDVVWLFLYVSIYWWGS 258
Cdd:MTH00219 246 VDVVWLFLYVSIYWWGS 262
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 4-258 7.34e-103

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 299.37  E-value: 7.34e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804   4 PFHLVEFSPWPLLISFSIFSMPIGLINYIRSSNISLLILGLFTTALISFLWWRDVVRESTYQGFHNKLVMKGLKIGIMLF 83
Cdd:MTH00130   7 AYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRYGMILF 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804  84 ILSEVCFFFAFFWAYFHSSLAPSVEIGAIWPPTGIFTLQAFQVPLLNTSVLLLSGVSITWVHHSIEEGNYKSAMQGLFIT 163
Cdd:MTH00130  87 ITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQSLTLT 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 164 ILLGLYFLMLQYGEYSETMFSISDGIYGSCLFMATGFHGTHVAVGATFLIVCFFRLKNFHFNKNHHIGFLAAAWYWHFVD 243
Cdd:MTH00130 167 ILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWYWHFVD 246

                        250
                 ....*....|....*
gi 168487804 244 VVWLFLYVSIYWWGS 258
Cdd:MTH00130 247 VVWLFLYISIYWWGS 261
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 5-258 7.80e-102

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 297.04  E-value: 7.80e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804   5 FHLVEFSPWPLLISFSIFSMPIGLINYIRSSNISLLILGLFTTALISFLWWRDVVRESTYQGFHNKLVMKGLKIGIMLFI 84
Cdd:MTH00075   8 FHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRYGMILFI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804  85 LSEVCFFFAFFWAYFHSSLAPSVEIGAIWPPTGIFTLQAFQVPLLNTSVLLLSGVSITWVHHSIEEGNYKSAMQGLFITI 164
Cdd:MTH00075  88 TSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQSLALTI 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 165 LLGLYFLMLQYGEYSETMFSISDGIYGSCLFMATGFHGTHVAVGATFLIVCFFRLKNFHFNKNHHIGFLAAAWYWHFVDV 244
Cdd:MTH00075 168 ILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWYWHFVDV 247

                        250
                 ....*....|....
gi 168487804 245 VWLFLYVSIYWWGS 258
Cdd:MTH00075 248 VWLFLYVSIYWWGS 261
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 4-258 6.69e-100

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 292.04  E-value: 6.69e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804   4 PFHLVEFSPWPLLISFSIFSMPIGLINYIRSSNISLLILGLFTTALISFLWWRDVVRESTYQGFHNKLVMKGLKIGIMLF 83
Cdd:MTH00024   7 PYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGMLLF 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804  84 ILSEVCFFFAFFWAYFHSSLAPSVEIGAIWPPTGIFTLQAFQVPLLNTSVLLLSGVSITWVHHSIEEGNYKSAMQGLFIT 163
Cdd:MTH00024  87 ILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFLT 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 164 ILLGLYFLMLQYGEYSETMFSISDGIYGSCLFMATGFHGTHVAVGATFLIVCFFRLKNFHFNKNHHIGFLAAAWYWHFVD 243
Cdd:MTH00024 167 VFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASWYWHFVD 246

                        250
                 ....*....|....*
gi 168487804 244 VVWLFLYVSIYWWGS 258
Cdd:MTH00024 247 VVWLFLYLCIYWWGS 261
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 3-258 2.74e-97

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 285.53  E-value: 2.74e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804   3 QPFHLVEFSPWPLLISFSIFSMPIGLINYIRSSNISLLILGLFTTALISFLWWRDVVRESTYQGFHNKLVMKGLKIGIML 82
Cdd:MTH00052   7 HPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGLKYGMIL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804  83 FILSEVCFFFAFFWAYFHSSLAPSVEIGAIWPPTGIFTLQAFQVPLLNTSVLLLSGVSITWVHHSIEEGNYKSAMQGLFI 162
Cdd:MTH00052  87 FIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEAIIGLAL 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 163 TILLGLYFLMLQYGEYSETMFSISDGIYGSCLFMATGFHGTHVAVGATFLIVCFFRLKNFHFNKNHHIGFLAAAWYWHFV 242
Cdd:MTH00052 167 TVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAAWYWHFV 246

                        250
                 ....*....|....*.
gi 168487804 243 DVVWLFLYVSIYWWGS 258
Cdd:MTH00052 247 DVVWLFLFIFMYWWGS 262
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 1-258 1.85e-95

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 280.57  E-value: 1.85e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804   1 MRQPFHLVEFSPWPLLISFSIFSMPIGLINYIRSSNISLLILGLFTTALISFLWWRDVVRESTYQGFHNKLVMKGLKIGI 80
Cdd:MTH00009   2 IRQPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804  81 MLFILSEVCFFFAFFWAYFHSSLAPSVEIGAIWPPTGIFTLQAFQVPLLNTSVLLLSGVSITWVHHSIEEGNYKSAMQGL 160
Cdd:MTH00009  82 ILFIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQAL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 161 FITILLGLYFLMLQYGEYSETMFSISDGIYGSCLFMATGFHGTHVAVGATFLIVCFFRLKNFHFNKNHHIGFLAAAWYWH 240
Cdd:MTH00009 162 ILTVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWH 241

                        250
                 ....*....|....*...
gi 168487804 241 FVDVVWLFLYVSIYWWGS 258
Cdd:MTH00009 242 FVDVVWIFLYLCIYWWGS 259
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 3-258 3.11e-87

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 261.15  E-value: 3.11e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804   3 QPFHLVEFSPWPLLISFSIFSMPIGLINYIRSSNISLLILGLFTTALISFLWWRDVVRESTYQGFHNKLVMKGLKIGIML 82
Cdd:MTH00028   6 HPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804  83 FILSEVCFFFAFFWAYFHSSLAPSVEIGAIWPPTGIFTLQAFQVPLLNTSVLLLSGVSITWVHHSI-------------- 148
Cdd:MTH00028  86 FILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIigtgnpaslekgtq 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 149 -EEGNYKS---------------------AMQGLFITILLGLYFLMLQYGEYSETMFSISDGIYGSCLFMATGFHGTHVA 206
Cdd:MTH00028 166 gIEGPNPSngappdpqkgptfllsdfrtnAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVL 245

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 168487804 207 VGATFLIVCFFRLKNFHFNKNHHIGFLAAAWYWHFVDVVWLFLYVSIYWWGS 258
Cdd:MTH00028 246 VGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWGS 297
PLN02194 PLN02194
cytochrome-c oxidase
 2-257 1.88e-73

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 224.93  E-value: 1.88e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804   2 RQPFHLVEFSPWPLLISFSIFSMPIGLINYIR--SSNISLLILGLFTTALISFLWWRDVVRESTYQGFHNKLVMKGLKIG 79
Cdd:PLN02194   6 RHSYHLVDPSPWPISGSLGALATTVGGVMYMHpfQGGARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGPRYG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804  80 IMLFILSEVCFFFAFFWAYFHSSLAPSVEIGAIWPPTGIFTLQAFQVPLLNTSVLLLSGVSITWVHHSIEEGNYKSAMQG 159
Cdd:PLN02194  86 SILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEKRAVYA 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 160 LFITILLGLYFLMLQYGEYSETMFSISDGIYGSCLFMATGFHGTHVAVGATFLIVCFFRLKNFHFNKNHHIGFLAAAWYW 239
Cdd:PLN02194 166 LVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWYW 245

                        250
                 ....*....|....*...
gi 168487804 240 HFVDVVWLFLYVSIYWWG 257
Cdd:PLN02194 246 HFVDVVWLFLFVSIYWWG 263
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
 5-258 1.36e-66

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 207.12  E-value: 1.36e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804   5 FHLVEFSPWPLLISFSIFSMPIGLINYIRSSNISLLILGLFTTALISFLWWRDVVREStYQGFHNKLVMKGLKIGIMLFI 84
Cdd:MTH00083   5 FHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMILFI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804  85 LSEVCFFFAFFWAYFHSSLAPSVEIGAIWPPTGIFTLQAFQVPLLNTSVLLLSGVSITWVHHSIEEGNyKSAMQGLFITI 164
Cdd:MTH00083  84 FSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSN-KSCTNSLLLTC 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 165 LLGLYFLMLQYGEYSETMFSISDGIYGSCLFMATGFHGTHVAVGATFLIVCFFRLKNFHFNKNHHIGFLAAAWYWHFVDV 244
Cdd:MTH00083 163 FLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFVDV 242

                        250
                 ....*....|....
gi 168487804 245 VWLFLYVSIYWWGS 258
Cdd:MTH00083 243 VWLFLFVFVYWWSY 256
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 68-256 3.54e-56

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: 178.17  E-value: 3.54e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804  68 HNKLVMKGLKIGIMLFILSEVCFFFAFFWAYFHSSLAPSVEIGAiwpptgifTLQAFQVPLLNTSVLLLSGVSITWVHHS 147
Cdd:cd00386    1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFGA--------GLDPLDLPLLNTNTLLLSGSSVTWAHAS 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 148 I--EEGNYKSAMQGLFITILLGLYFLMLQYGEYSETMFSISDGIYGSCLFMATGFHGTHVAVGATFLIVCFFRLKNFHFN 225
Cdd:cd00386   73 LaaRRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152

                        170       180       190
                 ....*....|....*....|....*....|.
gi 168487804 226 KNHHIGFLAAAWYWHFVDVVWLFLYVSIYWW 256
Cdd:cd00386  153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
127-256 4.91e-41

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 139.60  E-value: 4.91e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 127 PLLNTSVLLLSGVSITWVHHSIEEGNYKSAMQGLFITILLGLYFLMLQYGEYSETM---FSISDGIYGSCLFMATGFHGT 203
Cdd:COG1845   60 PLINTLLLLLSSFTVALAVRAARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHLIaegLTPTSNAFGSFFFLLTGFHGL 139

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 168487804 204 HVAVGATFLIVCFFRLKNFHFNKNHHIGFLAAAWYWHFVDVVWLFLYVSIYWW 256
Cdd:COG1845  140 HVIIGLIWLLVVLVRALRGGFTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
NorE_like cd02862
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ...
 128-254 2.20e-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: 88.06  E-value: 2.20e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 128 LLNTSVLLLSGVSITWVHHSIEEGNYKSAMQGLFITILLGLYFLMLQYGEYSE---TMFSISDGIYGSCLFMATGFHGTH 204
Cdd:cd02862   55 ALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYAHkiaAGIDPDAGLFFTLYFLLTGFHLLH 134

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 168487804 205 VAVGATFLIVCFFRLKNFHFNKNHHIGFLAAAWYWHFVDVVWLFLYVSIY 254
Cdd:cd02862  135 VLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVLFPLLY 184
Ubiquinol_oxidase_III cd02863
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ...
 124-254 6.89e-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: 70.73  E-value: 6.89e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 124 FQVPL--LNTSVLLLSGVSITWVHHSIEEGNYKSAMQGLFITILLGLYFLMLQYGEYSETM---FSISDGIYGSCLFMAT 198
Cdd:cd02863   48 FELPLvfIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEFHHLIaegAGPDRSAFLSAFFTLV 127

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 168487804 199 GFHGTHVAVGATFLIVCFFRLKNFHFNKNHHIGFLAAAWYWHFVDVVWLFLYVSIY 254
Cdd:cd02863  128 GTHGLHVTFGLIWILVMIIQLKKRGLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
Heme_Cu_Oxidase_III_2 cd02865
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 126-256 1.22e-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: 67.39  E-value: 1.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 126 VPLLNTSVLLLSGVSITWVHHSIEEGNYKSAMQGLFITILLGLYFLMLQYGEY---SETMFSISDGIYGSCLFMATGFHG 202
Cdd:cd02865   51 LLSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWhalNDAGYGPTSNPAGSFFYLLTGLHG 130

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 168487804 203 THVAVGATFLIVCFFRLKNFHFNKNHHIGFLAAAWYWHFVDVVWLFLYVSIYWW 256
Cdd:cd02865  131 LHVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVLLALLYGT 184
Heme_Cu_Oxidase_III_1 cd02864
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 113-256 2.46e-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: 2.46e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 113 WPPTGIF---TLQAFQVPL----LNTSVLLLSGVSITWVHHSIEEGNYKSAMQGLFITILLGLYFLMLQYGEYSETMFSI 185
Cdd:cd02864   42 WPLPSDVfalRIGHFNIPLvliaIMTFILITSSGTMAMAVNFGYRGNRKAAARLMLATALLGATFVGMQAFEWTKLIVEE 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 186 SDG---------IYGSCLFMATGFHGTHVAVGATFLIVCFFRLKNFHFN-KNHHIGFLAAAWYWHFVDVVWLFLYVSIYW 255
Cdd:cd02864  122 GVRpwgnpwgaaQFGASFFMITGFHGTHVTIGVIYLIIIARKVWRGKYQrIGRYEIVEIAGLYWHFVDLVWVFIFAFFYL 201


                 .
gi 168487804 256 W 256
Cdd:cd02864  202 W 202
COX3 MTH00049
cytochrome c oxidase subunit III; Validated
 123-254 4.48e-12

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177124  Cd Length: 215  Bit Score: 63.40  E-value: 4.48e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 123 AFQVPLLNTSVLLLSGVSITWVHHSIeegNYKSAMQGLFITILLGLYFLMLQYGEYSETMFSISDGIYGSCLFMATGFHG 202
Cdd:MTH00049  89 SLEIPFVGCFLLLGSSITVTAYHHLL---GWKYCDLFLYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHF 165

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 168487804 203 THVAVGATFLI-VCFFRLKNFHFNKNHHIgflaaAWYWHFVDVVWLFLYVSIY 254
Cdd:MTH00049 166 SHVVLGVVGLStLLLVGSSSFGVYRSTVL-----TWYWHFVDYIWLLVYLIVY 213
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 114-257 1.16e-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: 56.40  E-value: 1.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804  114 PPTGIFTLQAFqvpLLNTSVLLLSGVSITWVHHSIEEGNYKSAMQGLFITILLGLYFL---MLQYGEYSETMFSISDGIY 190
Cdd:TIGR02897  45 MPAELFELPLV---LIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVgfeIYEFAHYASEGVTPQIGSY 121

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 168487804  191 GSCLFMATGFHGTHVAVGATFLIVCFFRLKNFHFNKNHHIGFLAAAWYWHFVDVVWLFLYVSIYWWG 257
Cdd:TIGR02897 122 WSSFFVLLGTHGCHVTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
PRK10663 PRK10663
cytochrome o ubiquinol oxidase subunit III; Provisional
 124-258 2.29e-06

cytochrome o ubiquinol oxidase subunit III; Provisional


Pssm-ID: 182628  Cd Length: 204  Bit Score: 47.08  E-value: 2.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 124 FQVP--LLNTSVLLLSGVSITWVHHSIEEGNYKSAMQGLFITILLGLYFLMLQYGEYSETM---FSISDGIYGSCLFMAT 198
Cdd:PRK10663  64 FELPfvLVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFHHLIvegMGPDRSGFLSAFFALV 143

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 199 GFHGTHVAVGATFLIVCFFRLKNFHFNKNHHIGFLAAAWYWHFVDVVWLFLYVSIYWWGS 258
Cdd:PRK10663 144 GTHGLHVTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGA 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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