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Conserved domains on  [gi|1294136453|gb|AUB13411|]
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cytochrome c oxidase subunit III, partial (mitochondrion) [Drosophila melanogaster]

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 ...
 4-64 1.13e-31

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 MTH00155:

Pssm-ID: 444752  Cd Length: 255  Bit Score: 109.50  E-value: 1.13e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1294136453   4 HSNHPFHLVDYSPWPLTGAIGAMTTVSGMVKWFHQYDISLFVLGNIITILTVYQWWRDVSR 64
Cdd:MTH00155    1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIR 61
 
Name Accession Description Interval E-value
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 4-64 1.13e-31

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 109.50  E-value: 1.13e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1294136453   4 HSNHPFHLVDYSPWPLTGAIGAMTTVSGMVKWFHQYDISLFVLGNIITILTVYQWWRDVSR 64
Cdd:MTH00155    1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIR 61
COX3 pfam00510
Cytochrome c oxidase subunit III;
7-64 1.60e-17

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 72.83  E-value: 1.60e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1294136453   7 HPFHLVDYSPWPLTGAIGAMTTVSGMVKWFHQYDIS--LFVLGNIITILTVYQWWRDVSR 64
Cdd:pfam00510   1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYSGNmtLFIIALFSLLLTMYLWFRDIIR 60
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 19-64 6.24e-09

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: 49.44  E-value: 6.24e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1294136453  19 LTGAIGAMTTVSGMVKWFHQYDIS-LFVLGNIITILTVYQWWRDVSR 64
Cdd:cd01665     1 ILGSFGLLLLALGLVLWMHGYGGPlLLFLGLILLILTMFLWWRDVIR 47
 
Name Accession Description Interval E-value
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 4-64 1.13e-31

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 109.50  E-value: 1.13e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1294136453   4 HSNHPFHLVDYSPWPLTGAIGAMTTVSGMVKWFHQYDISLFVLGNIITILTVYQWWRDVSR 64
Cdd:MTH00155    1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIR 61
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 3-64 5.18e-24

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 90.03  E-value: 5.18e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1294136453   3 THSNHPFHLVDYSPWPLTGAIGAMTTVSGMVKWFHQYDISLFVLGNIITILTVYQWWRDVSR 64
Cdd:MTH00189    1 MHQAHPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVR 62
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 3-64 1.75e-22

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 85.77  E-value: 1.75e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1294136453   3 THSNHPFHLVDYSPWPLTGAIGAMTTVSGMVKWFHQYDISLFVLGNIITILTVYQWWRDVSR 64
Cdd:MTH00118    2 THQAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVR 63
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 1-64 9.10e-22

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 84.07  E-value: 9.10e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1294136453   1 MSTHSNHPFHLVDYSPWPLTGAIGAMTTVSGMVKWFHQYDISLFVLGNIITILTVYQWWRDVSR 64
Cdd:MTH00219    1 MMFFQTNPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIR 64
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 7-64 1.98e-20

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 80.32  E-value: 1.98e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1294136453   7 HPFHLVDYSPWPLTGAIGAMTTVSGMVKWFHQYDISLFVLGNIITILTVYQWWRDVSR 64
Cdd:MTH00141    4 NPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVR 61
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 3-64 7.51e-20

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 79.04  E-value: 7.51e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1294136453   3 THSNHPFHLVDYSPWPLTGAIGAMTTVSGMVKWFHQYDISLFVLGNIITILTVYQWWRDVSR 64
Cdd:MTH00130    2 AHQAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVR 63
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 7-64 1.32e-19

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 78.23  E-value: 1.32e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1294136453   7 HPFHLVDYSPWPLTGAIGAMTTVSGMVKWFHQYDISLFVLGNIITILTVYQWWRDVSR 64
Cdd:MTH00039    5 HPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIR 62
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 3-64 4.99e-19

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 76.69  E-value: 4.99e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1294136453   3 THSNHPFHLVDYSPWPLTGAIGAMTTVSGMVKWFHQYDISLFVLGNIITILTVYQWWRDVSR 64
Cdd:MTH00099    2 THQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIR 63
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 3-64 3.56e-18

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 74.40  E-value: 3.56e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1294136453   3 THSNHPFHLVDYSPWPLTGAIGAMTTVSGMVKWFHQYDISLFVLGNIITILTVYQWWRDVSR 64
Cdd:MTH00075    2 AHQAHAFHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVR 63
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 7-64 6.10e-18

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 74.10  E-value: 6.10e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1294136453   7 HPFHLVDYSPWPLTGAIGAMTTVSGMVKWFHQYDISLFVLGNIITILTVYQWWRDVSR 64
Cdd:MTH00009    4 QPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIR 61
COX3 pfam00510
Cytochrome c oxidase subunit III;
7-64 1.60e-17

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 72.83  E-value: 1.60e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1294136453   7 HPFHLVDYSPWPLTGAIGAMTTVSGMVKWFHQYDIS--LFVLGNIITILTVYQWWRDVSR 64
Cdd:pfam00510   1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYSGNmtLFIIALFSLLLTMYLWFRDIIR 60
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 1-64 8.39e-14

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 62.89  E-value: 8.39e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1294136453   1 MSTHSNHPFHLVDYSPWPLTGAIGAMTTVSGMVKWFHQYDISLFVLGNIITILTVYQWWRDVSR 64
Cdd:MTH00052    1 MMQQYYHPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIR 64
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 7-64 5.96e-13

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 60.85  E-value: 5.96e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1294136453   7 HPFHLVDYSPWPLTGAIGAMTTVSGMVKWFHQYDISLFVLGNIITILTVYQWWRDVSR 64
Cdd:MTH00028    6 HPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIR 63
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 7-64 2.81e-11

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 55.91  E-value: 2.81e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1294136453   7 HPFHLVDYSPWPLTGAIGAMTTVSGMVKWFHQYDISLFVLGNIITILTVYQWWRDVSR 64
Cdd:MTH00024    6 HPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIR 63
PLN02194 PLN02194
cytochrome-c oxidase
 1-64 1.86e-09

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 51.20  E-value: 1.86e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1294136453   1 MSTHSNHPFHLVDYSPWPLTGAIGAMTTVSGMVKWFHQYD--ISLFVLGNIITILTVYQWWRDVSR 64
Cdd:PLN02194    1 MIESQRHSYHLVDPSPWPISGSLGALATTVGGVMYMHPFQggARLLSLGLIFILYTMFVWWRDVLR 66
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 19-64 6.24e-09

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: 49.44  E-value: 6.24e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1294136453  19 LTGAIGAMTTVSGMVKWFHQYDIS-LFVLGNIITILTVYQWWRDVSR 64
Cdd:cd01665     1 ILGSFGLLLLALGLVLWMHGYGGPlLLFLGLILLILTMFLWWRDVIR 47
 
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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