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Conserved domains on  [gi|941488618|gb|ALK80376|]
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cytochrome oxidase subunit 3, partial (mitochondrion) [Bunodactis reynaudi]

Protein Classification

cytochrome c oxidase subunit 3 family protein( domain architecture ID 201)

cytochrome c oxidase (CcO) subunit 3 family protein is not required for catalytic activity but may play a role in the assembly of the heme-copper oxidase (such as CcO and cytochrome bo(3) ubiquinol oxidase) multimer complex

CATH:  1.20.120.80
Gene Ontology:  GO:0070069|GO:0009055
PubMed:  8083153|12907296
SCOP:  3000671

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Heme_Cu_Oxidase_III_like super family cl00211
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 1-207 7.38e-118

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.


The actual alignment was detected with superfamily member MTH00024:

Pssm-ID: 444752  Cd Length: 261  Bit Score: 335.18  E-value: 7.38e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488618   1 LFITVGSVVYFHYSQSWVLLMGAITLGLTMLVWWRDVIREATFQGLHTMVVKQGLKYGMLLFILSEVLFFFSFFWAFFHS 80
Cdd:MTH00024  25 FFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGMLLFILSEVLFFFSFFWAFFHS 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488618  81 SIAPTVELGAVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHALISGKKTEAINGLTATVILGLIFTGLQAMEYYEA 160
Cdd:MTH00024 105 SLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFLTVFLGVLFTGLQAIEYYEA 184

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 941488618 161 PFAISDSVYGSTFFVATGFHGLHVIIGTTFLAVCLVRLIYHQFTRHH 207
Cdd:MTH00024 185 PFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQ 231
 
Name Accession Description Interval E-value
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 1-207 7.38e-118

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 335.18  E-value: 7.38e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488618   1 LFITVGSVVYFHYSQSWVLLMGAITLGLTMLVWWRDVIREATFQGLHTMVVKQGLKYGMLLFILSEVLFFFSFFWAFFHS 80
Cdd:MTH00024  25 FFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGMLLFILSEVLFFFSFFWAFFHS 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488618  81 SIAPTVELGAVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHALISGKKTEAINGLTATVILGLIFTGLQAMEYYEA 160
Cdd:MTH00024 105 SLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFLTVFLGVLFTGLQAIEYYEA 184

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 941488618 161 PFAISDSVYGSTFFVATGFHGLHVIIGTTFLAVCLVRLIYHQFTRHH 207
Cdd:MTH00024 185 PFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQ 231
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-207 9.26e-96

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: 278.63  E-value: 9.26e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488618   1 LFITVGSVVYFH-YSQSWVLLMGAITLGLTMLVWWRDVIREATFQGLHTMVVKQGLKYGMLLFILSEVLFFFSFFWAFFH 79
Cdd:cd01665    8 LLLALGLVLWMHgYGGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFSFFWAFFH 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488618  80 SSIAPTVELGAVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHALISGKKTEAINGLTATVILGLIFTGLQAMEYYE 159
Cdd:cd01665   88 SSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGLQAYEYYE 167

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 941488618 160 APFAISDSVYGSTFFVATGFHGLHVIIGTTFLAVCLVRLIYHQFTRHH 207
Cdd:cd01665  168 ASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNH 215
COX3 pfam00510
Cytochrome c oxidase subunit III;
1-207 8.34e-85

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 251.56  E-value: 8.34e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488618    1 LFITVGSVVYFHYS--QSWVLLMGAITLGLTMLVWWRDVIREATFQGLHTMVVKQGLKYGMLLFILSEVLFFFSFFWAFF 78
Cdd:pfam00510  20 LLLTSGLVLWFHGYsgNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGMILFIISEVFFFLGIFWAFF 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488618   79 HSSIAPTVELGAVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHALISGKKTEAINGLTATVILGLIFTGLQAMEYY 158
Cdd:pfam00510 100 HSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGLILTILLAVYFTGLQAMEYT 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 941488618  159 EAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLAVCLVRLIYHQFTRHH 207
Cdd:pfam00510 180 EASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNH 228
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
46-207 1.36e-30

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 110.71  E-value: 1.36e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488618  46 LHTMVVKQGLKYGMLLFILSEVLFFFSFFWAFFhssiapTVELGAVWPPQGINPLNPfSVPLLNTAVLLSSGATVTWAHH 125
Cdd:COG1845    7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYF------VLRASAPDWPAGAELLDL-PLPLINTLLLLLSSFTVALAVR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488618 126 ALISGKKTEAINGLTATVILGLIFTGLQAMEYYE---APFAISDSVYGSTFFVATGFHGLHVIIGTTFLAVCLVRLIYHQ 202
Cdd:COG1845   80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHliaEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159


                 ....*
gi 941488618 203 FTRHH 207
Cdd:COG1845  160 FTPEN 164
 
Name Accession Description Interval E-value
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 1-207 7.38e-118

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 335.18  E-value: 7.38e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488618   1 LFITVGSVVYFHYSQSWVLLMGAITLGLTMLVWWRDVIREATFQGLHTMVVKQGLKYGMLLFILSEVLFFFSFFWAFFHS 80
Cdd:MTH00024  25 FFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGMLLFILSEVLFFFSFFWAFFHS 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488618  81 SIAPTVELGAVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHALISGKKTEAINGLTATVILGLIFTGLQAMEYYEA 160
Cdd:MTH00024 105 SLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFLTVFLGVLFTGLQAIEYYEA 184

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 941488618 161 PFAISDSVYGSTFFVATGFHGLHVIIGTTFLAVCLVRLIYHQFTRHH 207
Cdd:MTH00024 185 PFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQ 231
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 1-207 3.08e-113

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 323.67  E-value: 3.08e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488618   1 LFITVGSVVYFHYSQSWVLLMGAITLGLTMLVWWRDVIREATFQGLHTMVVKQGLKYGMLLFILSEVLFFFSFFWAFFHS 80
Cdd:MTH00052  26 LFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGLKYGMILFIVSEVCLFFSFFWAFFHS 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488618  81 SIAPTVELGAVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHALISGKKTEAINGLTATVILGLIFTGLQAMEYYEA 160
Cdd:MTH00052 106 SLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEAIIGLALTVALGLLFTGLQAMEYYEA 185

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 941488618 161 PFAISDSVYGSTFFVATGFHGLHVIIGTTFLAVCLVRLIYHQFTRHH 207
Cdd:MTH00052 186 PFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHH 232
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 1-207 8.09e-103

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 297.25  E-value: 8.09e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488618   1 LFITVGSVVYFHYSQSWVLLMGAITLGLTMLVWWRDVIREATFQGLHTMVVKQGLKYGMLLFILSEVLFFFSFFWAFFHS 80
Cdd:MTH00118  25 LLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRYGMILFITSEVFFFLGFFWAFYHS 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488618  81 SIAPTVELGAVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHALISGKKTEAINGLTATVILGLIFTGLQAMEYYEA 160
Cdd:MTH00118 105 SLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQALTLTILLGLYFTALQAMEYYEA 184

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 941488618 161 PFAISDSVYGSTFFVATGFHGLHVIIGTTFLAVCLVRLIYHQFTRHH 207
Cdd:MTH00118 185 PFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNH 231
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 1-207 9.60e-97

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 282.00  E-value: 9.60e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488618   1 LFITVGSVVYFHYSQSWVLLMGAITLGLTMLVWWRDVIREATFQGLHTMVVKQGLKYGMLLFILSEVLFFFSFFWAFFHS 80
Cdd:MTH00039  24 LIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRYGMILFITSEVCFFFAFFWAFFHS 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488618  81 SIAPTVELGAVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHALISGKKTEAINGLTATVILGLIFTGLQAMEYYEA 160
Cdd:MTH00039 104 SLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQALFLTVLLGLYFTALQAWEYYDA 183

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 941488618 161 PFAISDSVYGSTFFVATGFHGLHVIIGTTFLAVCLVRLIYHQFTRHH 207
Cdd:MTH00039 184 PFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNH 230
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 1-207 4.15e-96

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 280.32  E-value: 4.15e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488618   1 LFITVGSVVYFHYSQSWVLLMGAITLGLTMLVWWRDVIREATFQGLHTMVVKQGLKYGMLLFILSEVLFFFSFFWAFFHS 80
Cdd:MTH00189  24 LLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRYGMILFITSEVFFFLGFFWAFFHS 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488618  81 SIAPTVELGAVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHALISGKKTEAINGLTATVILGLIFTGLQAMEYYEA 160
Cdd:MTH00189 104 SLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQALTLTVILGVYFTLLQAMEYYEA 183

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 941488618 161 PFAISDSVYGSTFFVATGFHGLHVIIGTTFLAVCLVRLIYHQFTRHH 207
Cdd:MTH00189 184 PFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSH 230
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-207 9.26e-96

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: 278.63  E-value: 9.26e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488618   1 LFITVGSVVYFH-YSQSWVLLMGAITLGLTMLVWWRDVIREATFQGLHTMVVKQGLKYGMLLFILSEVLFFFSFFWAFFH 79
Cdd:cd01665    8 LLLALGLVLWMHgYGGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFSFFWAFFH 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488618  80 SSIAPTVELGAVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHALISGKKTEAINGLTATVILGLIFTGLQAMEYYE 159
Cdd:cd01665   88 SSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGLQAYEYYE 167

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 941488618 160 APFAISDSVYGSTFFVATGFHGLHVIIGTTFLAVCLVRLIYHQFTRHH 207
Cdd:cd01665  168 ASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNH 215
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 1-207 1.32e-95

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 278.60  E-value: 1.32e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488618   1 LFITVGSVVYFHYSQSWVLLMGAITLGLTMLVWWRDVIREATFQGLHTMVVKQGLKYGMLLFILSEVLFFFSFFWAFFHS 80
Cdd:MTH00155  23 MTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGMILFIVSEVFFFISFFWAFFHS 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488618  81 SIAPTVELGAVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHALISGKKTEAINGLTATVILGLIFTGLQAMEYYEA 160
Cdd:MTH00155 103 SLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSLFFTIILGIYFTMLQAYEYYEA 182

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 941488618 161 PFAISDSVYGSTFFVATGFHGLHVIIGTTFLAVCLVRLIYHQFTRHH 207
Cdd:MTH00155 183 PFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNH 229
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 1-207 3.19e-91

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 267.91  E-value: 3.19e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488618   1 LFITVGSVVYFHYSQSWVLLMGAITLGLTMLVWWRDVIREATFQGLHTMVVKQGLKYGMLLFILSEVLFFFSFFWAFFHS 80
Cdd:MTH00141  23 LFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFILFIVSEVCFFFAFFWAYFHS 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488618  81 SIAPTVELGAVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHALISGKKTEAINGLTATVILGLIFTGLQAMEYYEA 160
Cdd:MTH00141 103 SLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGLTIILGVYFTFLQAGEYYEA 182

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 941488618 161 PFAISDSVYGSTFFVATGFHGLHVIIGTTFLAVCLVRLIYHQF-TRHH 207
Cdd:MTH00141 183 SFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFsTNHH 230
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 1-207 8.91e-90

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 264.32  E-value: 8.91e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488618   1 LFITVGSVVYFHYSQSWVLLMGAITLGLTMLVWWRDVIREATFQGLHTMVVKQGLKYGMLLFILSEVLFFFSFFWAFFHS 80
Cdd:MTH00130  25 LLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRYGMILFITSEVFFFLGFFWAFYHS 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488618  81 SIAPTVELGAVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHALISGKKTEAINGLTATVILGLIFTGLQAMEYYEA 160
Cdd:MTH00130 105 SLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQSLTLTILLGFYFTFLQAMEYYEA 184

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 941488618 161 PFAISDSVYGSTFFVATGFHGLHVIIGTTFLAVCLVRLIYHQFTRHH 207
Cdd:MTH00130 185 PFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEH 231
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 1-207 9.02e-90

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 264.30  E-value: 9.02e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488618   1 LFITVGSVVYFHYSQSWVLLMGAITLGLTMLVWWRDVIREATFQGLHTMVVKQGLKYGMLLFILSEVLFFFSFFWAFFHS 80
Cdd:MTH00075  25 LLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRYGMILFITSEVFFFLGFFWAFYNS 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488618  81 SIAPTVELGAVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHALISGKKTEAINGLTATVILGLIFTGLQAMEYYEA 160
Cdd:MTH00075 105 SLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQSLALTIILGLYFTLLQAMEYYEA 184

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 941488618 161 PFAISDSVYGSTFFVATGFHGLHVIIGTTFLAVCLVRLIYHQFTRHH 207
Cdd:MTH00075 185 PFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQH 231
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 1-207 4.33e-87

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 257.35  E-value: 4.33e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488618   1 LFITVGSVVYFHYSQSWVLLMGAITLGLTMLVWWRDVIREATFQGLHTMVVKQGLKYGMLLFILSEVLFFFSFFWAFFHS 80
Cdd:MTH00099  25 LLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRYGMILFIISEVFFFAGFFWAFYHS 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488618  81 SIAPTVELGAVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHALISGKKTEAINGLTATVILGLIFTGLQAMEYYEA 160
Cdd:MTH00099 105 SLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQALFITILLGLYFTLLQASEYYEA 184

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 941488618 161 PFAISDSVYGSTFFVATGFHGLHVIIGTTFLAVCLVRLIYHQFTRHH 207
Cdd:MTH00099 185 PFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNH 231
COX3 pfam00510
Cytochrome c oxidase subunit III;
1-207 8.34e-85

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 251.56  E-value: 8.34e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488618    1 LFITVGSVVYFHYS--QSWVLLMGAITLGLTMLVWWRDVIREATFQGLHTMVVKQGLKYGMLLFILSEVLFFFSFFWAFF 78
Cdd:pfam00510  20 LLLTSGLVLWFHGYsgNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGMILFIISEVFFFLGIFWAFF 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488618   79 HSSIAPTVELGAVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHALISGKKTEAINGLTATVILGLIFTGLQAMEYY 158
Cdd:pfam00510 100 HSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGLILTILLAVYFTGLQAMEYT 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 941488618  159 EAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLAVCLVRLIYHQFTRHH 207
Cdd:pfam00510 180 EASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNH 228
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 1-207 3.44e-82

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 245.08  E-value: 3.44e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488618   1 LFITVGSVVYFHYSQSWVLLMGAITLGLTMLVWWRDVIREATFQGLHTMVVKQGLKYGMLLFILSEVLFFFSFFWAFFHS 80
Cdd:MTH00219  26 LMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLRIGMILFIVSEILFFFAFFWAFFHS 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488618  81 SIAPTVELGAVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHALISGKKTEAINGLTATVILGLIFTGLQAMEYYEA 160
Cdd:MTH00219 106 SLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQQGLLFTILLGLYFTMLQGMEYLEA 185

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 941488618 161 PFAISDSVYGSTFFVATGFHGLHVIIGTTFLAVCLVRLIYHQFTRHH 207
Cdd:MTH00219 186 SFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNH 232
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 3-207 1.02e-78

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 236.27  E-value: 1.02e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488618   3 ITVGSVVYFHYSQSWVLLMGAITLGLTMLVWWRDVIREATFQGLHTMVVKQGLKYGMLLFILSEVLFFFSFFWAFFHSSI 82
Cdd:MTH00009  25 LTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMILFIASEVMFFFAFFWAFFHSSL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488618  83 APTVELGAVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHALISGKKTEAINGLTATVILGLIFTGLQAMEYYEAPF 162
Cdd:MTH00009 105 APTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALILTVLLGAYFTFLQAGEYIEAPF 184

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 941488618 163 AISDSVYGSTFFVATGFHGLHVIIGTTFLAVCLVRLIYHQFTRHH 207
Cdd:MTH00009 185 TIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGH 229
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 1-207 2.19e-75

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 228.80  E-value: 2.19e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488618   1 LFITVGSVVYFHYSQSWVLLMGAITLGLTMLVWWRDVIREATFQGLHTMVVKQGLKYGMLLFILSEVLFFFSFFWAFFHS 80
Cdd:MTH00028  25 FLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLLFILSEVCLFFAFFWAFFHS 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488618  81 SIAPTVELGAVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHALISGK----------------------------- 131
Cdd:MTH00028 105 SLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTGnpaslekgtqgiegpnpsngappdpqkgp 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488618 132 -------KTEAINGLTATVILGLIFTGLQAMEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLAVCLVRLIYHQFT 204
Cdd:MTH00028 185 tfllsdfRTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVLVGTTFLIVCFIRLLSNQFT 264


                 ...
gi 941488618 205 RHH 207
Cdd:MTH00028 265 NSH 267
PLN02194 PLN02194
cytochrome-c oxidase
 1-207 2.61e-65

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 202.20  E-value: 2.61e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488618   1 LFITVGSVVYFHYSQ--SWVLLMGAITLGLTMLVWWRDVIREATFQGLHTMVVKQGLKYGMLLFILSEVLFFFSFFWAFF 78
Cdd:PLN02194  26 LATTVGGVMYMHPFQggARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGPRYGSILFIVSEVMFFFAFFWASS 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488618  79 HSSIAPTVELGAVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHALISGKKTEAINGLTATVILGLIFTGLQAMEYY 158
Cdd:PLN02194 106 HSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEKRAVYALVATVLLALVFTGFQGMEYY 185

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 941488618 159 EAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLAVCLVRLIYHQFTRHH 207
Cdd:PLN02194 186 QAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEH 234
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
 1-207 1.79e-51

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 166.67  E-value: 1.79e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488618   1 LFITVGSVVYFHYSQSWVLLMGAITLGLTMLVWWRDVIREAtFQGLHTMVVKQGLKYGMLLFILSEVLFFFSFFWAFFHS 80
Cdd:MTH00083  22 LGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMILFIFSEFMFFFSIFWTFFDA 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488618  81 SIAPTVELGAVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAL-ISGKKTEaiNGLTATVILGLIFTGLQAMEYYE 159
Cdd:MTH00083 101 ALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLcLSNKSCT--NSLLLTCFLGLYFTSFQLMEYKE 178

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 941488618 160 APFAISDSVYGSTFFVATGFHGLHVIIGTTFLAVCLVRLIYHQFTRHH 207
Cdd:MTH00083 179 ASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNH 226
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 47-207 6.84e-44

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: 144.65  E-value: 6.84e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488618  47 HTMVVKQGLKYGMLLFILSEVLFFFSFFWAFFHSSIAPTVELGAvwppqginPLNPFSVPLLNTAVLLSSGATVTWAHHA 126
Cdd:cd00386    1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFGA--------GLDPLDLPLLNTNTLLLSGSSVTWAHAS 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488618 127 LI--SGKKTEAINGLTATVILGLIFTGLQAMEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLAVCLVRLIYHQFT 204
Cdd:cd00386   73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152


                 ...
gi 941488618 205 RHH 207
Cdd:cd00386  153 PRH 155
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
46-207 1.36e-30

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 110.71  E-value: 1.36e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488618  46 LHTMVVKQGLKYGMLLFILSEVLFFFSFFWAFFhssiapTVELGAVWPPQGINPLNPfSVPLLNTAVLLSSGATVTWAHH 125
Cdd:COG1845    7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYF------VLRASAPDWPAGAELLDL-PLPLINTLLLLLSSFTVALAVR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488618 126 ALISGKKTEAINGLTATVILGLIFTGLQAMEYYE---APFAISDSVYGSTFFVATGFHGLHVIIGTTFLAVCLVRLIYHQ 202
Cdd:COG1845   80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHliaEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159


                 ....*
gi 941488618 203 FTRHH 207
Cdd:COG1845  160 FTPEN 164
Ubiquinol_oxidase_III cd02863
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ...
 107-204 1.53e-13

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: 66.11  E-value: 1.53e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488618 107 LLNTAVLLSSGATVTWAHHALISGKKTEAINGLTATVILGLIFTGLQAME---YYEAPFAISDSVYGSTFFVATGFHGLH 183
Cdd:cd02863   54 FIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLVGTHGLH 133

                         90       100
                 ....*....|....*....|.
gi 941488618 184 VIIGTTFLAVCLVRLIYHQFT 204
Cdd:cd02863  134 VTFGLIWILVMIIQLKKRGLT 154
NorE_like cd02862
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ...
 107-197 2.37e-13

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: 65.33  E-value: 2.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488618 107 LLNTAVLLSSGATVTWAHHALISGKKTEAINGLTATVILGLIFTGLQAMEYYE---APFAISDSVYGSTFFVATGFHGLH 183
Cdd:cd02862   55 ALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYAHkiaAGIDPDAGLFFTLYFLLTGFHLLH 134

                         90
                 ....*....|....
gi 941488618 184 VIIGTTFLAVCLVR 197
Cdd:cd02862  135 VLIGLGILLWVAWR 148
Heme_Cu_Oxidase_III_2 cd02865
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 89-204 2.41e-11

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: 60.08  E-value: 2.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488618  89 GAVWPPQGINPLNpfsVPLLNTAVLLSSGATVTWAHHALISGKKTEAINGLTATVILGLIFTGLQAMEYYEAPFAI---S 165
Cdd:cd02865   38 GDWQPGAPLPLPN---LLSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWHALNDAGygpT 114

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 941488618 166 DSVYGSTFFVATGFHGLHVIIGTTFLAVCLVRLIYHQFT 204
Cdd:cd02865  115 SNPAGSFFYLLTGLHGLHVIGGLVALAIVLAGLIRGHYG 153
Heme_Cu_Oxidase_III_1 cd02864
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 56-206 5.32e-09

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: 53.66  E-value: 5.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488618  56 KYGMLLFILSEVLFFFSFFWAFFHSSIAPTVELGAVWPPQGInPLNPFSVPL----LNTAVLLSSGATVTWAHHALISGK 131
Cdd:cd02864   10 KAMMWFFLLSDAFIFSSFLIAYMTARISTTEPWPLPSDVFAL-RIGHFNIPLvliaIMTFILITSSGTMAMAVNFGYRGN 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488618 132 KTEAINGLTATVILGLIFTGLQAMEYYE---------APFAISDSVYGSTFFVATGFHGLHVIIGTTFLAVCLVRLIYHQ 202
Cdd:cd02864   89 RKAAARLMLATALLGATFVGMQAFEWTKliveegvrpWGNPWGAAQFGASFFMITGFHGTHVTIGVIYLIIIARKVWRGK 168


                 ....
gi 941488618 203 FTRH 206
Cdd:cd02864  169 YQRI 172
COX3 MTH00049
cytochrome c oxidase subunit III; Validated
 61-188 1.09e-05

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177124  Cd Length: 215  Bit Score: 44.52  E-value: 1.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488618  61 LFILSEVLfffsffwaffhssIAPTVELGAVW--PPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHALisGKKTEAINg 138
Cdd:MTH00049  59 LFILSEVI-------------IFGSLLVCCLWfdDWSYISLSSSLEIPFVGCFLLLGSSITVTAYHHLL--GWKYCDLF- 122

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 941488618 139 LTATVILGLIFTGLQAMEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGT 188
Cdd:MTH00049 123 LYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHFSHVVLGV 172
 
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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