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Conserved domains on  [gi|28268832|gb|AAO37914|]
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cytochrome oxidase subunit III, partial (mitochondrion) [Hapalemur griseus alaotrensis]

Protein Classification

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 ...
 1-17 7.17e-07

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 MTH00118:

Pssm-ID: 444752  Cd Length: 261  Bit Score: 41.09  E-value: 7.17e-07
                         10
                 ....*....|....*..
gi 28268832    1 VDVVWLFLYVSIYWWGS 17
Cdd:MTH00118 245 VDVVWLFLYISIYWWGS 261
 
Name Accession Description Interval E-value
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 1-17 7.17e-07

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 41.09  E-value: 7.17e-07
                         10
                 ....*....|....*..
gi 28268832    1 VDVVWLFLYVSIYWWGS 17
Cdd:MTH00118 245 VDVVWLFLYISIYWWGS 261
COX3 pfam00510
Cytochrome c oxidase subunit III;
1-17 8.80e-05

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 35.46  E-value: 8.80e-05
                          10
                  ....*....|....*..
gi 28268832     1 VDVVWLFLYVSIYWWGS 17
Cdd:pfam00510 242 VDVVWLFLYVSVYWWGS 258
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-15 1.75e-03

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: 31.72  E-value: 1.75e-03
                        10
                ....*....|....*
gi 28268832   1 VDVVWLFLYVSIYWW 15
Cdd:cd01665 229 VDVVWLFLFVFVYWW 243
 
Name Accession Description Interval E-value
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 1-17 7.17e-07

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 41.09  E-value: 7.17e-07
                         10
                 ....*....|....*..
gi 28268832    1 VDVVWLFLYVSIYWWGS 17
Cdd:MTH00118 245 VDVVWLFLYISIYWWGS 261
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 1-17 6.03e-06

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 38.55  E-value: 6.03e-06
                         10
                 ....*....|....*..
gi 28268832    1 VDVVWLFLYVSIYWWGS 17
Cdd:MTH00099 245 VDVVWLFLYVSIYWWGS 261
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 1-17 1.04e-05

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 37.82  E-value: 1.04e-05
                         10
                 ....*....|....*..
gi 28268832    1 VDVVWLFLYVSIYWWGS 17
Cdd:MTH00130 245 VDVVWLFLYISIYWWGS 261
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 1-17 1.11e-05

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 37.80  E-value: 1.11e-05
                         10
                 ....*....|....*..
gi 28268832    1 VDVVWLFLYVSIYWWGS 17
Cdd:MTH00075 245 VDVVWLFLYVSIYWWGS 261
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 1-17 3.61e-05

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 36.49  E-value: 3.61e-05
                         10
                 ....*....|....*..
gi 28268832    1 VDVVWLFLYVSIYWWGS 17
Cdd:MTH00189 244 VDVVWLFLYVSIYWWGS 260
COX3 pfam00510
Cytochrome c oxidase subunit III;
1-17 8.80e-05

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 35.46  E-value: 8.80e-05
                          10
                  ....*....|....*..
gi 28268832     1 VDVVWLFLYVSIYWWGS 17
Cdd:pfam00510 242 VDVVWLFLYVSVYWWGS 258
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 1-17 1.79e-04

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 34.32  E-value: 1.79e-04
                         10
                 ....*....|....*..
gi 28268832    1 VDVVWLFLYVSIYWWGS 17
Cdd:MTH00039 244 VDVVWLFLYVCIYWWGS 260
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 1-17 2.19e-04

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 34.38  E-value: 2.19e-04
                         10
                 ....*....|....*..
gi 28268832    1 VDVVWLFLYVSIYWWGS 17
Cdd:MTH00219 246 VDVVWLFLYVSIYWWGS 262
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 1-17 3.80e-04

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 33.50  E-value: 3.80e-04
                         10
                 ....*....|....*..
gi 28268832    1 VDVVWLFLYVSIYWWGS 17
Cdd:MTH00028 281 VDVVWLFLYVFVYWWGS 297
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 1-17 4.18e-04

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 33.33  E-value: 4.18e-04
                         10
                 ....*....|....*..
gi 28268832    1 VDVVWLFLYVSIYWWGS 17
Cdd:MTH00141 243 VDVVWLFLYLSIYWWGS 259
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 1-17 8.32e-04

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 32.42  E-value: 8.32e-04
                         10
                 ....*....|....*..
gi 28268832    1 VDVVWLFLYVSIYWWGS 17
Cdd:MTH00024 245 VDVVWLFLYLCIYWWGS 261
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-15 1.75e-03

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: 31.72  E-value: 1.75e-03
                        10
                ....*....|....*
gi 28268832   1 VDVVWLFLYVSIYWW 15
Cdd:cd01665 229 VDVVWLFLFVFVYWW 243
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 1-17 3.44e-03

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 30.96  E-value: 3.44e-03
                         10
                 ....*....|....*..
gi 28268832    1 VDVVWLFLYVSIYWWGS 17
Cdd:MTH00009 243 VDVVWIFLYLCIYWWGS 259
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 1-17 5.51e-03

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 30.15  E-value: 5.51e-03
                         10
                 ....*....|....*..
gi 28268832    1 VDVVWLFLYVSIYWWGS 17
Cdd:MTH00052 246 VDVVWLFLFIFMYWWGS 262
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 1-13 5.69e-03

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 30.15  E-value: 5.69e-03
                         10
                 ....*....|...
gi 28268832    1 VDVVWLFLYVSIY 13
Cdd:MTH00155 243 VDVVWLFLYISIY 255
 
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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