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Conserved domains on  [gi|1732629961|gb|QEK23339|]
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cytochrome c oxidase, subunit III, partial (mitochondrion) [Saccharomyces kudriavzevii]

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 ...
 1-164 3.50e-89

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 pfam00510:

Pssm-ID: 444752  Cd Length: 258  Bit Score: 260.81  E-value: 3.50e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629961   1 AVRKGINLGFLMFVVSEVLIFAGLFWAYFHSAMSPDVTLGACWPPVGIQAVQPTELPLLNTIILLSSGATVTYSHHALIA 80
Cdd:pfam00510  71 AVQKGLNLGMILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIE 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629961  81 GNRNKALSGLLITFWLIVIFVSCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMIMLAAMLGVNYWRMKNYHLTAGHHV 160
Cdd:pfam00510 151 GNRKQALQGLILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHF 230


                  ....
gi 1732629961 161 GYET 164
Cdd:pfam00510 231 GFEA 234
 
Name Accession Description Interval E-value
COX3 pfam00510
Cytochrome c oxidase subunit III;
1-164 3.50e-89

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 260.81  E-value: 3.50e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629961   1 AVRKGINLGFLMFVVSEVLIFAGLFWAYFHSAMSPDVTLGACWPPVGIQAVQPTELPLLNTIILLSSGATVTYSHHALIA 80
Cdd:pfam00510  71 AVQKGLNLGMILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIE 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629961  81 GNRNKALSGLLITFWLIVIFVSCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMIMLAAMLGVNYWRMKNYHLTAGHHV 160
Cdd:pfam00510 151 GNRKQALQGLILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHF 230


                  ....
gi 1732629961 161 GYET 164
Cdd:pfam00510 231 GFEA 234
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-164 3.40e-78

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: 232.41  E-value: 3.40e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629961   1 AVRKGINLGFLMFVVSEVLIFAGLFWAYFHSAMSPDVTLGACWPPVGIQAVQPTELPLLNTIILLSSGATVTYSHHALIA 80
Cdd:cd01665    58 KVQKGLRLGMILFILSEVMFFFSFFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLL 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629961  81 GNRNKALSGLLITFWLIVIFVSCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMIMLAAMLGVNYWRMKNYHLTAGHHV 160
Cdd:cd01665   138 GNRKKAILGLILTILLGVYFTGLQAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHL 217


                  ....
gi 1732629961 161 GYET 164
Cdd:cd01665   218 GFEA 221
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 2-163 8.99e-61

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 188.47  E-value: 8.99e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629961   2 VRKGINLGFLMFVVSEVLIFAGLFWAYFHSAMSPDVTLGACWPPVGIQAVQPTELPLLNTIILLSSGATVTYSHHALIAG 81
Cdd:MTH00155   73 VTKGLRWGMILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMEN 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629961  82 NRNKALSGLLITFWLIVIFVSCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMIMLAAMLGVNYWRMKNYHLTAGHHVG 161
Cdd:MTH00155  153 NYKQATQSLFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFG 232


                  ..
gi 1732629961 162 YE 163
Cdd:MTH00155  233 FE 234
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
8-164 8.11e-33

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 114.95  E-value: 8.11e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629961   8 LGFLMFVVSEVLIFAGLFWAYF-HSAMSPDvtlgacWPPvGIQAVQPTeLPLLNTIILLSSGATVTYSHHALIAGNRNKA 86
Cdd:COG1845    18 LGMWLFLASEVMLFAALFAAYFvLRASAPD------WPA-GAELLDLP-LPLINTLLLLLSSFTVALAVRAARRGDRKGL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629961  87 LSGLLITFWLIVIFVSCQYIEYTNAA---FTISDGVYGSVFYAGTGLHFLHMIMLAAMLGVNYWRMKNYHLTAGHHVGYE 163
Cdd:COG1845    90 RLWLLLTLLLGLAFLGLQAYEYSHLIaegLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGFTPENHTGVE 169


                  .
gi 1732629961 164 T 164
Cdd:COG1845   170 A 170
 
Name Accession Description Interval E-value
COX3 pfam00510
Cytochrome c oxidase subunit III;
1-164 3.50e-89

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 260.81  E-value: 3.50e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629961   1 AVRKGINLGFLMFVVSEVLIFAGLFWAYFHSAMSPDVTLGACWPPVGIQAVQPTELPLLNTIILLSSGATVTYSHHALIA 80
Cdd:pfam00510  71 AVQKGLNLGMILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIE 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629961  81 GNRNKALSGLLITFWLIVIFVSCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMIMLAAMLGVNYWRMKNYHLTAGHHV 160
Cdd:pfam00510 151 GNRKQALQGLILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHF 230


                  ....
gi 1732629961 161 GYET 164
Cdd:pfam00510 231 GFEA 234
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-164 3.40e-78

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: 232.41  E-value: 3.40e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629961   1 AVRKGINLGFLMFVVSEVLIFAGLFWAYFHSAMSPDVTLGACWPPVGIQAVQPTELPLLNTIILLSSGATVTYSHHALIA 80
Cdd:cd01665    58 KVQKGLRLGMILFILSEVMFFFSFFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLL 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629961  81 GNRNKALSGLLITFWLIVIFVSCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMIMLAAMLGVNYWRMKNYHLTAGHHV 160
Cdd:cd01665   138 GNRKKAILGLILTILLGVYFTGLQAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHL 217


                  ....
gi 1732629961 161 GYET 164
Cdd:cd01665   218 GFEA 221
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 2-163 8.99e-61

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 188.47  E-value: 8.99e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629961   2 VRKGINLGFLMFVVSEVLIFAGLFWAYFHSAMSPDVTLGACWPPVGIQAVQPTELPLLNTIILLSSGATVTYSHHALIAG 81
Cdd:MTH00155   73 VTKGLRWGMILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMEN 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629961  82 NRNKALSGLLITFWLIVIFVSCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMIMLAAMLGVNYWRMKNYHLTAGHHVG 161
Cdd:MTH00155  153 NYKQATQSLFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFG 232


                  ..
gi 1732629961 162 YE 163
Cdd:MTH00155  233 FE 234
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 2-163 3.02e-60

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 187.10  E-value: 3.02e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629961   2 VRKGINLGFLMFVVSEVLIFAGLFWAYFHSAMSPDVTLGACWPPVGIQAVQPTELPLLNTIILLSSGATVTYSHHALIAG 81
Cdd:MTH00189   74 VQKGLRYGMILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEG 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629961  82 NRNKALSGLLITFWLIVIFVSCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMIMLAAMLGVNYWRMKNYHLTAGHHVG 161
Cdd:MTH00189  154 NRKEAIQALTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFG 233


                  ..
gi 1732629961 162 YE 163
Cdd:MTH00189  234 FE 235
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 2-163 5.11e-57

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 178.93  E-value: 5.11e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629961   2 VRKGINLGFLMFVVSEVLIFAGLFWAYFHSAMSPDVTLGACWPPVGIQAVQPTELPLLNTIILLSSGATVTYSHHALIAG 81
Cdd:MTH00141   73 VQRGLRWGFILFIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEG 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629961  82 NRNKALSGLLITFWLIVIFVSCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMIMLAAMLGVNYWRMKNYHLTAGHHVG 161
Cdd:MTH00141  153 DYKSALQGLGLTIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFG 232


                  ..
gi 1732629961 162 YE 163
Cdd:MTH00141  233 FE 234
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 2-163 1.61e-56

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 177.84  E-value: 1.61e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629961   2 VRKGINLGFLMFVVSEVLIFAGLFWAYFHSAMSPDVTLGACWPPVGIQAVQPTELPLLNTIILLSSGATVTYSHHALIAG 81
Cdd:MTH00118   75 VQKGLRYGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEG 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629961  82 NRNKALSGLLITFWLIVIFVSCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMIMLAAMLGVNYWRMKNYHLTAGHHVG 161
Cdd:MTH00118  155 NRKQAIQALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFG 234


                  ..
gi 1732629961 162 YE 163
Cdd:MTH00118  235 FE 236
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 2-163 6.55e-56

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 176.48  E-value: 6.55e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629961   2 VRKGINLGFLMFVVSEVLIFAGLFWAYFHSAMSPDVTLGACWPPVGIQAVQPTELPLLNTIILLSSGATVTYSHHALIAG 81
Cdd:MTH00024   75 VKQGLKYGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISG 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629961  82 NRNKALSGLLITFWLIVIFVSCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMIMLAAMLGVNYWRMKNYHLTAGHHVG 161
Cdd:MTH00024  155 KRKEAILGLFLTVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVG 234


                  ..
gi 1732629961 162 YE 163
Cdd:MTH00024  235 FE 236
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 2-163 3.23e-55

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 174.53  E-value: 3.23e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629961   2 VRKGINLGFLMFVVSEVLIFAGLFWAYFHSAMSPDVTLGACWPPVGIQAVQPTELPLLNTIILLSSGATVTYSHHALIAG 81
Cdd:MTH00039   74 VINGLRYGMILFITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEG 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629961  82 NRNKALSGLLITFWLIVIFVSCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMIMLAAMLGVNYWRMKNYHLTAGHHVG 161
Cdd:MTH00039  154 NRTEAIQALFLTVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFG 233


                  ..
gi 1732629961 162 YE 163
Cdd:MTH00039  234 FE 235
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 2-163 3.55e-53

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 169.14  E-value: 3.55e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629961   2 VRKGINLGFLMFVVSEVLIFAGLFWAYFHSAMSPDVTLGACWPPVGIQAVQPTELPLLNTIILLSSGATVTYSHHALIAG 81
Cdd:MTH00099   75 VQKGLRYGMILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEG 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629961  82 NRNKALSGLLITFWLIVIFVSCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMIMLAAMLGVNYWRMKNYHLTAGHHVG 161
Cdd:MTH00099  155 NRKHMLQALFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFG 234


                  ..
gi 1732629961 162 YE 163
Cdd:MTH00099  235 FE 236
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 2-163 3.16e-52

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 166.89  E-value: 3.16e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629961   2 VRKGINLGFLMFVVSEVLIFAGLFWAYFHSAMSPDVTLGACWPPVGIQAVQPTELPLLNTIILLSSGATVTYSHHALIAG 81
Cdd:MTH00052   76 VKQGLKYGMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISG 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629961  82 NRNKALSGLLITFWLIVIFVSCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMIMLAAMLGVNYWRMKNYHLTAGHHVG 161
Cdd:MTH00052  156 KRKEAIIGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFG 235


                  ..
gi 1732629961 162 YE 163
Cdd:MTH00052  236 FE 237
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 2-163 4.20e-52

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 166.48  E-value: 4.20e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629961   2 VRKGINLGFLMFVVSEVLIFAGLFWAYFHSAMSPDVTLGACWPPVGIQAVQPTELPLLNTIILLSSGATVTYSHHALIAG 81
Cdd:MTH00130   75 VQKGLRYGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEG 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629961  82 NRNKALSGLLITFWLIVIFVSCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMIMLAAMLGVNYWRMKNYHLTAGHHVG 161
Cdd:MTH00130  155 ERKQAIQSLTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFG 234


                  ..
gi 1732629961 162 YE 163
Cdd:MTH00130  235 FE 236
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 2-163 1.71e-49

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 159.91  E-value: 1.71e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629961   2 VRKGINLGFLMFVVSEVLIFAGLFWAYFHSAMSPDVTLGACWPPVGIQAVQPTELPLLNTIILLSSGATVTYSHHALIAG 81
Cdd:MTH00075   75 VQKGLRYGMILFITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQG 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629961  82 NRNKALSGLLITFWLIVIFVSCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMIMLAAMLGVNYWRMKNYHLTAGHHVG 161
Cdd:MTH00075  155 NRKEAIQSLALTIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFG 234


                  ..
gi 1732629961 162 YE 163
Cdd:MTH00075  235 FE 236
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 2-163 1.86e-49

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 159.95  E-value: 1.86e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629961   2 VRKGINLGFLMFVVSEVLIFAGLFWAYFHSAMSPDVTLGACWPPVGIQAVQPTELPLLNTIILLSSGATVTYSHHALIAG 81
Cdd:MTH00219   76 VSTGLRIGMILFIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMES 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629961  82 NRNKALSGLLITFWLIVIFVSCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMIMLAAMLGVNYWRMKNYHLTAGHHVG 161
Cdd:MTH00219  156 NHKEAQQGLLFTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFG 235


                  ..
gi 1732629961 162 YE 163
Cdd:MTH00219  236 FE 237
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 2-164 5.96e-49

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: 155.82  E-value: 5.96e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629961   2 VRKGINLGFLMFVVSEVLIFAGLFWAYFHSAMSPDVTLGAcwppvgiqAVQPTELPLLNTIILLSSGATVTYSHHALIA- 80
Cdd:cd00386     5 VRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFGA--------GLDPLDLPLLNTNTLLLSGSSVTWAHASLAAr 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629961  81 -GNRNKALSGLLITFWLIVIFVSCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMIMLAAMLGVNYWRMKNYHLTAGHH 159
Cdd:cd00386    77 rGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFTPRHH 156


                  ....*
gi 1732629961 160 VGYET 164
Cdd:cd00386   157 LGLEA 161
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
 2-163 5.72e-47

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 153.19  E-value: 5.72e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629961   2 VRKGINLGFLMFVVSEVLIFAGLFWAYFHSAMSPDVTLGACWPPVGIQAVQPTELPLLNTIILLSSGATVTYSHHALIAG 81
Cdd:MTH00083   71 VMDGFKFGMILFIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLS 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629961  82 NrNKALSGLLITFWLIVIFVSCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMIMLAAMLGVNYWRMKNYHLTAGHHVG 161
Cdd:MTH00083  151 N-KSCTNSLLLTCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLG 229


                  ..
gi 1732629961 162 YE 163
Cdd:MTH00083  230 LE 231
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 2-163 4.55e-44

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 146.13  E-value: 4.55e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629961   2 VRKGINLGFLMFVVSEVLIFAGLFWAYFHSAMSPDVTLGACWPPVGIQAVQPTELPLLNTIILLSSGATVTYSHHALIAG 81
Cdd:MTH00009   73 VTKGLRWGMILFIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEG 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629961  82 NRNKALSGLLITFWLIVIFVSCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMIMLAAMLGVNYWRMKNYHLTAGHHVG 161
Cdd:MTH00009  153 DRPEATQALILTVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFG 232


                  ..
gi 1732629961 162 YE 163
Cdd:MTH00009  233 FE 234
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 2-163 7.30e-44

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 146.75  E-value: 7.30e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629961   2 VRKGINLGFLMFVVSEVLIFAGLFWAYFHSAMSPDVTLGACWPPVGIQAVQPTELPLLNTIILLSSGATVTYSHHALIAG 81
Cdd:MTH00028   75 VVRGLKLGMLLFILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGT 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629961  82 N------------------------------------RNKALSGLLITFWLIVIFVSCQYIEYTNAAFTISDGVYGSVFY 125
Cdd:MTH00028  155 GnpaslekgtqgiegpnpsngappdpqkgptfllsdfRTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFF 234

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1732629961 126 AGTGLHFLHMIMLAAMLGVNYWRMKNYHLTAGHHVGYE 163
Cdd:MTH00028  235 MLTGTHGLHVLVGTTFLIVCFIRLLSNQFTNSHHLGLE 272
PLN02194 PLN02194
cytochrome-c oxidase
 2-163 1.21e-37

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 129.78  E-value: 1.21e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629961   2 VRKGINLGFLMFVVSEVLIFAGLFWAYFHSAMSPDVTLGACWPPVGIQAVQPTELPLLNTIILLSSGATVTYSHHALIAG 81
Cdd:PLN02194   78 VQLGPRYGSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAG 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629961  82 NRNKALSGLLITFWLIVIFVSCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMIMLAAMLGVNYWRMKNYHLTAGHHVG 161
Cdd:PLN02194  158 KEKRAVYALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVG 237


                  ..
gi 1732629961 162 YE 163
Cdd:PLN02194  238 FE 239
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
8-164 8.11e-33

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 114.95  E-value: 8.11e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629961   8 LGFLMFVVSEVLIFAGLFWAYF-HSAMSPDvtlgacWPPvGIQAVQPTeLPLLNTIILLSSGATVTYSHHALIAGNRNKA 86
Cdd:COG1845    18 LGMWLFLASEVMLFAALFAAYFvLRASAPD------WPA-GAELLDLP-LPLINTLLLLLSSFTVALAVRAARRGDRKGL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629961  87 LSGLLITFWLIVIFVSCQYIEYTNAA---FTISDGVYGSVFYAGTGLHFLHMIMLAAMLGVNYWRMKNYHLTAGHHVGYE 163
Cdd:COG1845    90 RLWLLLTLLLGLAFLGLQAYEYSHLIaegLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGFTPENHTGVE 169


                  .
gi 1732629961 164 T 164
Cdd:COG1845   170 A 170
COX3 MTH00049
cytochrome c oxidase subunit III; Validated
 9-136 2.09e-06

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177124  Cd Length: 215  Bit Score: 45.68  E-value: 2.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629961   9 GFLMFVVSEVLIFAGLFWAYFHSAMSPDVTLGAcwppvgiqavqPTELPLLNTIILLSSGATVTYSHHaLIAGNRNKALs 88
Cdd:MTH00049   56 AFWLFILSEVIIFGSLLVCCLWFDDWSYISLSS-----------SLEIPFVGCFLLLGSSITVTAYHH-LLGWKYCDLF- 122

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1732629961  89 gLLITFWLIVIFVSCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMI 136
Cdd:MTH00049  123 -LYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHFSHVV 169
Heme_Cu_Oxidase_III_2 cd02865
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 13-152 1.04e-04

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: 40.82  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629961  13 FVVSEVLIFAGLFWAYFHSAMSPDVtlgacWPPVGIQAVQpteLPLLNTIILLSSGATVTYSHHALIAGNRNKALSGLLI 92
Cdd:cd02865    16 FMAVEGTLFALLISAYFMRMTSGDW-----QPGAPLPLPN---LLSLNTAVLAASSVAMQWARRAARRNRRVLARLGLAL 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1732629961  93 TFWLIVIFVSCQYIEY---TNAAFTISDGVYGSVFYAGTGLHFLHMIM-LAAMLGVNYWRMKNY 152
Cdd:cd02865    88 AGALALAFLAGQLLAWhalNDAGYGPTSNPAGSFFYLLTGLHGLHVIGgLVALAIVLAGLIRGH 151
 
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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