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Conserved domains on  [gi|380469267|gb|ABN58960|]
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cytochrome oxidase subunit III, partial (mitochondrion) [Hyalotheca mucosa]

Protein Classification

cytochrome c oxidase subunit 3( domain architecture ID 10108868)

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
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 14-192 1.78e-92

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: 269.77  E-value: 1.78e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380469267  14 IVILYTMFVWWRDVVREATYLGHHTKMVQLGLRYGMILFIVSEVMFFLAFFWAFFHSSLAPTVEIGAVWPPKGIEAIGPW 93
Cdd:cd01665   32 ILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFSFFWAFFHSSLSPSVELGGTWPPVGIEPLNPF 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380469267  94 DIPFLNTLILLSSGAAVTWAHHAILAGSQRQAIYGLVATIFLAVIFTALQGMEYVEAPFTISDGIYGSTFYLATGFHGLH 173
Cdd:cd01665  112 GIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGLQAYEYYEASFTISDSVYGSTFFMLTGFHGLH 191

                        170
                 ....*....|....*....
gi 380469267 174 VIIGTIFLIICCIREYMGH 192
Cdd:cd01665  192 VIIGTIFLTVCLIRLLKGH 210
 
Name Accession Description Interval E-value
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 14-192 1.78e-92

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: 269.77  E-value: 1.78e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380469267  14 IVILYTMFVWWRDVVREATYLGHHTKMVQLGLRYGMILFIVSEVMFFLAFFWAFFHSSLAPTVEIGAVWPPKGIEAIGPW 93
Cdd:cd01665   32 ILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFSFFWAFFHSSLSPSVELGGTWPPVGIEPLNPF 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380469267  94 DIPFLNTLILLSSGAAVTWAHHAILAGSQRQAIYGLVATIFLAVIFTALQGMEYVEAPFTISDGIYGSTFYLATGFHGLH 173
Cdd:cd01665  112 GIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGLQAYEYYEASFTISDSVYGSTFFMLTGFHGLH 191

                        170
                 ....*....|....*....
gi 380469267 174 VIIGTIFLIICCIREYMGH 192
Cdd:cd01665  192 VIIGTIFLTVCLIRLLKGH 210
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 14-192 4.59e-89

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 261.65  E-value: 4.59e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380469267  14 IVILYTMFVWWRDVVREATYLGHHTKMVQLGLRYGMILFIVSEVMFFLAFFWAFFHSSLAPTVEIGAVWPPKGIEAIGPW 93
Cdd:MTH00155  46 IITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGMILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPF 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380469267  94 DIPFLNTLILLSSGAAVTWAHHAILAGSQRQAIYGLVATIFLAVIFTALQGMEYVEAPFTISDGIYGSTFYLATGFHGLH 173
Cdd:MTH00155 126 QIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSLFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLH 205

                        170
                 ....*....|....*....
gi 380469267 174 VIIGTIFLIICCIREYMGH 192
Cdd:MTH00155 206 VIIGTTFLLVCLIRHLNNH 224
COX3 pfam00510
Cytochrome c oxidase subunit III;
14-192 1.26e-81

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 242.70  E-value: 1.26e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380469267   14 IVILYTMFVWWRDVVREATYLGHHTKMVQLGLRYGMILFIVSEVMFFLAFFWAFFHSSLAPTVEIGAVWPPKGIEAIGPW 93
Cdd:pfam00510  45 FSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGMILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPF 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380469267   94 DIPFLNTLILLSSGAAVTWAHHAILAGSQRQAIYGLVATIFLAVIFTALQGMEYVEAPFTISDGIYGSTFYLATGFHGLH 173
Cdd:pfam00510 125 EVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGLILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLH 204

                         170
                  ....*....|....*....
gi 380469267  174 VIIGTIFLIICCIREYMGH 192
Cdd:pfam00510 205 VIIGTAFLAVCFLRLLKYH 223
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
36-192 1.00e-32

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 115.72  E-value: 1.00e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380469267  36 HHTKMVQLGLRYGMILFIVSEVMFFLAFFWAFFHSSLAptveiGAVWPPkGIEAIGPWdIPFLNTLILLSSGAAVTWAHH 115
Cdd:COG1845    7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS-----APDWPA-GAELLDLP-LPLINTLLLLLSSFTVALAVR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380469267 116 AILAGSQRQAIYGLVATIFLAVIFTALQGMEY---VEAPFTISDGIYGSTFYLATGFHGLHVIIGTIFLIICCIREYMGH 192
Cdd:COG1845   80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159
 
Name Accession Description Interval E-value
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 14-192 1.78e-92

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: 269.77  E-value: 1.78e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380469267  14 IVILYTMFVWWRDVVREATYLGHHTKMVQLGLRYGMILFIVSEVMFFLAFFWAFFHSSLAPTVEIGAVWPPKGIEAIGPW 93
Cdd:cd01665   32 ILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFSFFWAFFHSSLSPSVELGGTWPPVGIEPLNPF 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380469267  94 DIPFLNTLILLSSGAAVTWAHHAILAGSQRQAIYGLVATIFLAVIFTALQGMEYVEAPFTISDGIYGSTFYLATGFHGLH 173
Cdd:cd01665  112 GIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGLQAYEYYEASFTISDSVYGSTFFMLTGFHGLH 191

                        170
                 ....*....|....*....
gi 380469267 174 VIIGTIFLIICCIREYMGH 192
Cdd:cd01665  192 VIIGTIFLTVCLIRLLKGH 210
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 14-192 4.59e-89

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 261.65  E-value: 4.59e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380469267  14 IVILYTMFVWWRDVVREATYLGHHTKMVQLGLRYGMILFIVSEVMFFLAFFWAFFHSSLAPTVEIGAVWPPKGIEAIGPW 93
Cdd:MTH00155  46 IITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGMILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPF 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380469267  94 DIPFLNTLILLSSGAAVTWAHHAILAGSQRQAIYGLVATIFLAVIFTALQGMEYVEAPFTISDGIYGSTFYLATGFHGLH 173
Cdd:MTH00155 126 QIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSLFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLH 205

                        170
                 ....*....|....*....
gi 380469267 174 VIIGTIFLIICCIREYMGH 192
Cdd:MTH00155 206 VIIGTTFLLVCLIRHLNNH 224
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 14-192 2.19e-88

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 259.88  E-value: 2.19e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380469267  14 IVILYTMFVWWRDVVREATYLGHHTKMVQLGLRYGMILFIVSEVMFFLAFFWAFFHSSLAPTVEIGAVWPPKGIEAIGPW 93
Cdd:MTH00118  48 LSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRYGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPF 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380469267  94 DIPFLNTLILLSSGAAVTWAHHAILAGSQRQAIYGLVATIFLAVIFTALQGMEYVEAPFTISDGIYGSTFYLATGFHGLH 173
Cdd:MTH00118 128 EVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLH 207

                        170
                 ....*....|....*....
gi 380469267 174 VIIGTIFLIICCIREYMGH 192
Cdd:MTH00118 208 VIIGSTFLIVCLLRLIKFH 226
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 14-192 3.19e-86

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 254.51  E-value: 3.19e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380469267  14 IVILYTMFVWWRDVVREATYLGHHTKMVQLGLRYGMILFIVSEVMFFLAFFWAFFHSSLAPTVEIGAVWPPKGIEAIGPW 93
Cdd:MTH00189  47 ILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRYGMILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPF 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380469267  94 DIPFLNTLILLSSGAAVTWAHHAILAGSQRQAIYGLVATIFLAVIFTALQGMEYVEAPFTISDGIYGSTFYLATGFHGLH 173
Cdd:MTH00189 127 EVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQALTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLH 206

                        170
                 ....*....|....*....
gi 380469267 174 VIIGTIFLIICCIREYMGH 192
Cdd:MTH00189 207 VIIGSTFLLVCLLRQIQGH 225
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 14-192 7.80e-83

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 245.96  E-value: 7.80e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380469267  14 IVILYTMFVWWRDVVREATYLGHHTKMVQLGLRYGMILFIVSEVMFFLAFFWAFFHSSLAPTVEIGAVWPPKGIEAIGPW 93
Cdd:MTH00141  46 VLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFILFIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPF 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380469267  94 DIPFLNTLILLSSGAAVTWAHHAILAGSQRQAIYGLVATIFLAVIFTALQGMEYVEAPFTISDGIYGSTFYLATGFHGLH 173
Cdd:MTH00141 126 QVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGLTIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLH 205

                        170
                 ....*....|....*....
gi 380469267 174 VIIGTIFLIICCIREYMGH 192
Cdd:MTH00141 206 VIIGTTFLLVCLVRLLLGH 224
COX3 pfam00510
Cytochrome c oxidase subunit III;
14-192 1.26e-81

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 242.70  E-value: 1.26e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380469267   14 IVILYTMFVWWRDVVREATYLGHHTKMVQLGLRYGMILFIVSEVMFFLAFFWAFFHSSLAPTVEIGAVWPPKGIEAIGPW 93
Cdd:pfam00510  45 FSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGMILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPF 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380469267   94 DIPFLNTLILLSSGAAVTWAHHAILAGSQRQAIYGLVATIFLAVIFTALQGMEYVEAPFTISDGIYGSTFYLATGFHGLH 173
Cdd:pfam00510 125 EVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGLILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLH 204

                         170
                  ....*....|....*....
gi 380469267  174 VIIGTIFLIICCIREYMGH 192
Cdd:pfam00510 205 VIIGTAFLAVCFLRLLKYH 223
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 14-192 8.19e-81

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 240.81  E-value: 8.19e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380469267  14 IVILYTMFVWWRDVVREATYLGHHTKMVQLGLRYGMILFIVSEVMFFLAFFWAFFHSSLAPTVEIGAVWPPKGIEAIGPW 93
Cdd:MTH00024  48 LVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPF 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380469267  94 DIPFLNTLILLSSGAAVTWAHHAILAGSQRQAIYGLVATIFLAVIFTALQGMEYVEAPFTISDGIYGSTFYLATGFHGLH 173
Cdd:MTH00024 128 SVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFLTVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLH 207

                        170
                 ....*....|....*....
gi 380469267 174 VIIGTIFLIICCIREYMGH 192
Cdd:MTH00024 208 VIIGTTFLFVCLLRLLSNQ 226
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 14-187 1.75e-80

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 240.08  E-value: 1.75e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380469267  14 IVILYTMFVWWRDVVREATYLGHHTKMVQLGLRYGMILFIVSEVMFFLAFFWAFFHSSLAPTVEIGAVWPPKGIEAIGPW 93
Cdd:MTH00052  49 ITIIFTMVVWWRDVIRESTYQGHHTLIVKQGLKYGMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPF 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380469267  94 DIPFLNTLILLSSGAAVTWAHHAILAGSQRQAIYGLVATIFLAVIFTALQGMEYVEAPFTISDGIYGSTFYLATGFHGLH 173
Cdd:MTH00052 129 SVPLLNTAVLLSSGATVTWAHHGIISGKRKEAIIGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGH 208

                        170
                 ....*....|....
gi 380469267 174 VIIGTIFLIICCIR 187
Cdd:MTH00052 209 VLIGSSFLLVCLFR 222
PLN02194 PLN02194
cytochrome-c oxidase
 14-192 2.26e-79

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 237.25  E-value: 2.26e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380469267  14 IVILYTMFVWWRDVVREATYLGHHTKMVQLGLRYGMILFIVSEVMFFLAFFWAFFHSSLAPTVEIGAVWPPKGIEAIGPW 93
Cdd:PLN02194  51 IFILYTMFVWWRDVLRESTLEGHHTKVVQLGPRYGSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPW 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380469267  94 DIPFLNTLILLSSGAAVTWAHHAILAGSQRQAIYGLVATIFLAVIFTALQGMEYVEAPFTISDGIYGSTFYLATGFHGLH 173
Cdd:PLN02194 131 EIPFLNTPILPSSGAAVTWAHHAILAGKEKRAVYALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFH 210

                        170
                 ....*....|....*....
gi 380469267 174 VIIGTIFLIICCIREYMGH 192
Cdd:PLN02194 211 VIIGTLFLIICGIRQYLGH 229
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 14-192 3.93e-77

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 231.54  E-value: 3.93e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380469267  14 IVILYTMFVWWRDVVREATYLGHHTKMVQLGLRYGMILFIVSEVMFFLAFFWAFFHSSLAPTVEIGAVWPPKGIEAIGPW 93
Cdd:MTH00039  47 LLLILTSINWWRDVIREATFQGMHTLIVINGLRYGMILFITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPF 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380469267  94 DIPFLNTLILLSSGAAVTWAHHAILAGSQRQAIYGLVATIFLAVIFTALQGMEYVEAPFTISDGIYGSTFYLATGFHGLH 173
Cdd:MTH00039 127 LVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQALFLTVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLH 206

                        170
                 ....*....|....*....
gi 380469267 174 VIIGTIFLIICCIREYMGH 192
Cdd:MTH00039 207 VIIGTTFLAVCLFRLINHH 225
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 14-192 6.19e-77

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 230.81  E-value: 6.19e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380469267  14 IVILYTMFVWWRDVVREATYLGHHTKMVQLGLRYGMILFIVSEVMFFLAFFWAFFHSSLAPTVEIGAVWPPKGIEAIGPW 93
Cdd:MTH00130  48 ILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRYGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPF 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380469267  94 DIPFLNTLILLSSGAAVTWAHHAILAGSQRQAIYGLVATIFLAVIFTALQGMEYVEAPFTISDGIYGSTFYLATGFHGLH 173
Cdd:MTH00130 128 EVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQSLTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLH 207

                        170
                 ....*....|....*....
gi 380469267 174 VIIGTIFLIICCIREYMGH 192
Cdd:MTH00130 208 VIIGSTFLAVCLLRQIQYH 226
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 17-192 2.28e-76

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 229.61  E-value: 2.28e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380469267  17 LYTMFVWWRDVVREATYLGHHTKMVQLGLRYGMILFIVSEVMFFLAFFWAFFHSSLAPTVEIGAVWPPKGIEAIGPWDIP 96
Cdd:MTH00099  51 MLTMYQWWRDIIRESTFQGHHTPIVQKGLRYGMILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVP 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380469267  97 FLNTLILLSSGAAVTWAHHAILAGSQRQAIYGLVATIFLAVIFTALQGMEYVEAPFTISDGIYGSTFYLATGFHGLHVII 176
Cdd:MTH00099 131 LLNTSVLLASGVSITWAHHSLMEGNRKHMLQALFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVII 210

                        170
                 ....*....|....*.
gi 380469267 177 GTIFLIICCIREYMGH 192
Cdd:MTH00099 211 GSTFLIVCFLRQLKFH 226
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 14-192 4.23e-75

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 226.16  E-value: 4.23e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380469267  14 IVILYTMFVWWRDVVREATYLGHHTKMVQLGLRYGMILFIVSEVMFFLAFFWAFFHSSLAPTVEIGAVWPPKGIEAIGPW 93
Cdd:MTH00075  48 IIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRYGMILFITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPF 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380469267  94 DIPFLNTLILLSSGAAVTWAHHAILAGSQRQAIYGLVATIFLAVIFTALQGMEYVEAPFTISDGIYGSTFYLATGFHGLH 173
Cdd:MTH00075 128 EVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQSLALTIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLH 207

                        170
                 ....*....|....*....
gi 380469267 174 VIIGTIFLIICCIREYMGH 192
Cdd:MTH00075 208 VIIGSLFLLVCLLRQINFH 226
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 14-192 1.91e-74

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 224.67  E-value: 1.91e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380469267  14 IVILYTMFVWWRDVVREATYLGHHTKMVQLGLRYGMILFIVSEVMFFLAFFWAFFHSSLAPTVEIGAVWPPKGIEAIGPW 93
Cdd:MTH00219  49 LIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLRIGMILFIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPF 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380469267  94 DIPFLNTLILLSSGAAVTWAHHAILAGSQRQAIYGLVATIFLAVIFTALQGMEYVEAPFTISDGIYGSTFYLATGFHGLH 173
Cdd:MTH00219 129 QVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQQGLLFTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLH 208

                        170
                 ....*....|....*....
gi 380469267 174 VIIGTIFLIICCIREYMGH 192
Cdd:MTH00219 209 VIIGTIFLFVCFMRGLMLH 227
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 14-192 2.18e-66

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 204.30  E-value: 2.18e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380469267  14 IVILYTMFVWWRDVVREATYLGHHTKMVQLGLRYGMILFIVSEVMFFLAFFWAFFHSSLAPTVEIGAVWPPKGIEAIGPW 93
Cdd:MTH00009  46 IIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMILFIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPF 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380469267  94 DIPFLNTLILLSSGAAVTWAHHAILAGSQRQAIYGLVATIFLAVIFTALQGMEYVEAPFTISDGIYGSTFYLATGFHGLH 173
Cdd:MTH00009 126 SVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALILTVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLH 205

                        170
                 ....*....|....*....
gi 380469267 174 VIIGTIFLIICCIREYMGH 192
Cdd:MTH00009 206 VLIGSSFLFVCLLRTWSHH 224
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 14-187 1.99e-62

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 195.29  E-value: 1.99e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380469267  14 IVILYTMFVWWRDVVREATYLGHHTKMVQLGLRYGMILFIVSEVMFFLAFFWAFFHSSLAPTVEIGAVWPPKGIEAIGPW 93
Cdd:MTH00028  48 FLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLLFILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPF 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380469267  94 DIPFLNTLILLSSGAAVTWAHHAILAGS------------------------------------QRQAIYGLVATIFLAV 137
Cdd:MTH00028 128 AVPLLNTTILLSSGATVTWAHHAIIGTGnpaslekgtqgiegpnpsngappdpqkgptfllsdfRTNAVIGLLMTILLGI 207

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 380469267 138 IFTALQGMEYVEAPFTISDGIYGSTFYLATGFHGLHVIIGTIFLIICCIR 187
Cdd:MTH00028 208 IFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVLVGTTFLIVCFIR 257
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
 14-192 1.73e-51

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 165.90  E-value: 1.73e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380469267  14 IVILYTMFVWWRDVVREAtYLGHHTKMVQLGLRYGMILFIVSEVMFFLAFFWAFFHSSLAPTVEIGAVWPPKGIEAIGPW 93
Cdd:MTH00083  45 LYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMILFIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYL 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380469267  94 DIPFLNTLILLSSGAAVTWAHHAILAGSQRQAIYgLVATIFLAVIFTALQGMEYVEAPFTISDGIYGSTFYLATGFHGLH 173
Cdd:MTH00083 124 GVPLLNTIILLSSGVSVTWSHHSLCLSNKSCTNS-LLLTCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIH 202

                        170
                 ....*....|....*....
gi 380469267 174 VIIGTIFLIICCIREYMGH 192
Cdd:MTH00083 203 VLCGGLFLLFNLLRLLKSH 221
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 37-192 1.76e-45

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: 148.12  E-value: 1.76e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380469267  37 HTKMVQLGLRYGMILFIVSEVMFFLAFFWAFFHSSLAPTVEIGAvwppkgieAIGPWDIPFLNTLILLSSGAAVTWAHHA 116
Cdd:cd00386    1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFGA--------GLDPLDLPLLNTNTLLLSGSSVTWAHAS 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 380469267 117 ILA--GSQRQAIYGLVATIFLAVIFTALQGMEYVEAPFTISDGIYGSTFYLATGFHGLHVIIGTIFLIICCIREYMGH 192
Cdd:cd00386   73 LAArrGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGH 150
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
36-192 1.00e-32

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 115.72  E-value: 1.00e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380469267  36 HHTKMVQLGLRYGMILFIVSEVMFFLAFFWAFFHSSLAptveiGAVWPPkGIEAIGPWdIPFLNTLILLSSGAAVTWAHH 115
Cdd:COG1845    7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS-----APDWPA-GAELLDLP-LPLINTLLLLLSSFTVALAVR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380469267 116 AILAGSQRQAIYGLVATIFLAVIFTALQGMEY---VEAPFTISDGIYGSTFYLATGFHGLHVIIGTIFLIICCIREYMGH 192
Cdd:COG1845   80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159
NorE_like cd02862
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ...
 98-187 6.02e-14

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: 66.87  E-value: 6.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380469267  98 LNTLILLSSGAAVTWAHHAILAGSQRQAIYGLVATIFLAVIFTALQGMEY---VEAPFTISDGIYGSTFYLATGFHGLHV 174
Cdd:cd02862   56 LNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYahkIAAGIDPDAGLFFTLYFLLTGFHLLHV 135

                         90
                 ....*....|...
gi 380469267 175 IIGTIFLIICCIR 187
Cdd:cd02862  136 LIGLGILLWVAWR 148
Heme_Cu_Oxidase_III_2 cd02865
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 96-192 1.79e-08

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: 51.60  E-value: 1.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380469267  96 PFLNTLILLSSGAAVTWAHHAILAGSQRQAIYGLVATIFLAVIFTALQGMEY---VEAPFTISDGIYGSTFYLATGFHGL 172
Cdd:cd02865   52 LSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWhalNDAGYGPTSNPAGSFFYLLTGLHGL 131

                         90       100
                 ....*....|....*....|
gi 380469267 173 HVIIGTIFLIICCIREYMGH 192
Cdd:cd02865  132 HVIGGLVALAIVLAGLIRGH 151
Ubiquinol_oxidase_III cd02863
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ...
 97-183 2.07e-08

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: 51.47  E-value: 2.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380469267  97 FLNTLILLSSGAAVTWAHHAILAGSQRQAIYGLVATIFLAVIFTALQGME---YVEAPFTISDGIYGSTFYLATGFHGLH 173
Cdd:cd02863   54 FIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLVGTHGLH 133

                         90
                 ....*....|
gi 380469267 174 VIIGTIFLII 183
Cdd:cd02863  134 VTFGLIWILV 143
Heme_Cu_Oxidase_III_1 cd02864
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 46-185 1.21e-06

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: 46.73  E-value: 1.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380469267  46 RYGMILFIVSEVMFFLAFFWAFFHSSLAPTVEIGAVWPPKGIEaIGPWDIPF----LNTLILLSSGAAVTWAHHAILAGS 121
Cdd:cd02864   10 KAMMWFFLLSDAFIFSSFLIAYMTARISTTEPWPLPSDVFALR-IGHFNIPLvliaIMTFILITSSGTMAMAVNFGYRGN 88

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 380469267 122 QRQAIYGLVATIFLAVIFTALQGMEYVEAPFTISDG---------IYGSTFYLATGFHGLHVIIGTIFLIICC 185
Cdd:cd02864   89 RKAAARLMLATALLGATFVGMQAFEWTKLIVEEGVRpwgnpwgaaQFGASFFMITGFHGTHVTIGVIYLIIIA 161
COX3 MTH00049
cytochrome c oxidase subunit III; Validated
 51-183 6.09e-06

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177124  Cd Length: 215  Bit Score: 44.91  E-value: 6.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380469267  51 LFIVSEVMFFLaffwaffhsSLAPTVEIGAVWPPKGIEAigPWDIPFLNTLILLSSGAAVTWAHHaiLAGSQRQAIYgLV 130
Cdd:MTH00049  59 LFILSEVIIFG---------SLLVCCLWFDDWSYISLSS--SLEIPFVGCFLLLGSSITVTAYHH--LLGWKYCDLF-LY 124

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 380469267 131 ATIFLAVIFTALQGMEYVEAPFTISDGIYGSTFYLATGFHGLHVIIGTIFLII 183
Cdd:MTH00049 125 LTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHFSHVVLGVVGLST 177
 
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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