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Conserved domains on  [gi|732450203|gb|AIZ68438|]
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cytochrome c oxidase subunit III, partial (mitochondrion) [Hippidion sp.]

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 ...
 1-74 1.08e-13

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 MTH00099:

Pssm-ID: 444752  Cd Length: 261  Bit Score: 68.21  E-value: 1.08e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 732450203   1 MV*PSPWPLTGALSALLMTSGLA*******************************ESTFQGHHTSI*QKGLRY*M 74
Cdd:MTH00099  10 MVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRYGM 83
Heme_Cu_Oxidase_III_like super family cl00211
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 197-224 3.31e-08

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: 52.65  E-value: 3.31e-08
                         10        20
                 ....*....|....*....|....*...
gi 732450203 197 L*VIIGSTFLIVCFLRQLKFHFTS*HHF 224
Cdd:MTH00118 206 LHVIIGSTFLIVCLLRLIKFHFTTNHHF 233
 
Name Accession Description Interval E-value
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 1-74 1.08e-13

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 68.21  E-value: 1.08e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 732450203   1 MV*PSPWPLTGALSALLMTSGLA*******************************ESTFQGHHTSI*QKGLRY*M 74
Cdd:MTH00099  10 MVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRYGM 83
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 197-224 3.31e-08

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 52.65  E-value: 3.31e-08
                         10        20
                 ....*....|....*....|....*...
gi 732450203 197 L*VIIGSTFLIVCFLRQLKFHFTS*HHF 224
Cdd:MTH00118 206 LHVIIGSTFLIVCLLRLIKFHFTTNHHF 233
COX3 pfam00510
Cytochrome c oxidase subunit III;
1-74 5.34e-06

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 45.86  E-value: 5.34e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 732450203    1 MV*PSPWPLTGALSALLMTSGLA****************************--***ESTFQGHHTSI*QKGLRY*M 74
Cdd:pfam00510   5 MVSPSPWPLFGSFALLLLTSGLVLWFHGYSGNMTLFIIALFSLLLTMYLWFrdIIREGTFLGDHTFAVQKGLNLGM 80
COX3 pfam00510
Cytochrome c oxidase subunit III;
197-224 3.75e-05

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 43.55  E-value: 3.75e-05
                          10        20
                  ....*....|....*....|....*...
gi 732450203  197 L*VIIGSTFLIVCFLRQLKFHFTS*HHF 224
Cdd:pfam00510 203 LHVIIGTAFLAVCFLRLLKYHLTDNHHF 230
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 199-224 4.13e-05

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: 43.27  E-value: 4.13e-05
                         10        20
                 ....*....|....*....|....*.
gi 732450203 199 VIIGSTFLIVCFLRQLKFHFTS*HHF 224
Cdd:cd01665  192 VIIGTIFLTVCLIRLLKGHFSSNHHL 217
 
Name Accession Description Interval E-value
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 1-74 1.08e-13

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 68.21  E-value: 1.08e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 732450203   1 MV*PSPWPLTGALSALLMTSGLA*******************************ESTFQGHHTSI*QKGLRY*M 74
Cdd:MTH00099  10 MVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRYGM 83
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 1-74 2.44e-12

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 64.20  E-value: 2.44e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 732450203   1 MV*PSPWPLTGALSALLMTSGLA*******************************ESTFQGHHTSI*QKGLRY*M 74
Cdd:MTH00118  10 MVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRYGM 83
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 1-74 4.64e-12

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 63.63  E-value: 4.64e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 732450203   1 MV*PSPWPLTGALSALLMTSGLA*******************************ESTFQGHHTSI*QKGLRY*M 74
Cdd:MTH00130  10 MVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRYGM 83
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 1-74 8.99e-12

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 62.84  E-value: 8.99e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 732450203   1 MV*PSPWPLTGALSALLMTSGLA*******************************ESTFQGHHTSI*QKGLRY*M 74
Cdd:MTH00075  10 MVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRYGM 83
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 1-74 2.69e-09

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 55.75  E-value: 2.69e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 732450203   1 MV*PSPWPLTGALSALLMTSGLA*******************************ESTFQGHHTSI*QKGLRY*M 74
Cdd:MTH00189   9 LVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRYGM 82
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 197-224 3.31e-08

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 52.65  E-value: 3.31e-08
                         10        20
                 ....*....|....*....|....*...
gi 732450203 197 L*VIIGSTFLIVCFLRQLKFHFTS*HHF 224
Cdd:MTH00118 206 LHVIIGSTFLIVCLLRLIKFHFTTNHHF 233
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 1-74 4.83e-08

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 52.04  E-value: 4.83e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 732450203   1 MV*PSPWPLTGALSALLMTSGLA*******************************ESTFQGHHTSI*QKGLRY*M 74
Cdd:MTH00039   9 LVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRYGM 82
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 197-224 5.03e-07

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 48.82  E-value: 5.03e-07
                         10        20
                 ....*....|....*....|....*...
gi 732450203 197 L*VIIGSTFLIVCFLRQLKFHFTS*HHF 224
Cdd:MTH00189 205 LHVIIGSTFLLVCLLRQIQGHFTSSHHF 232
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 1-74 1.75e-06

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 47.58  E-value: 1.75e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 732450203   1 MV*PSPWPLTGALSALLMTSGLA*******************************ESTFQGHHTSI*QKGLRY*M 74
Cdd:MTH00141   8 LVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGF 81
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 1-74 2.59e-06

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 47.09  E-value: 2.59e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 732450203   1 MV*PSPWPLTGALSALLMTSGLA*******************************ESTFQGHHTSI*QKGLRY*M 74
Cdd:MTH00219  11 LVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLRIGM 84
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 1-74 4.88e-06

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 45.94  E-value: 4.88e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 732450203   1 MV*PSPWPLTGALSALLMTSGLA*******************************ESTFQGHHTSI*QKGLRY*M 74
Cdd:MTH00155   8 LVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGM 81
COX3 pfam00510
Cytochrome c oxidase subunit III;
1-74 5.34e-06

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 45.86  E-value: 5.34e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 732450203    1 MV*PSPWPLTGALSALLMTSGLA****************************--***ESTFQGHHTSI*QKGLRY*M 74
Cdd:pfam00510   5 MVSPSPWPLFGSFALLLLTSGLVLWFHGYSGNMTLFIIALFSLLLTMYLWFrdIIREGTFLGDHTFAVQKGLNLGM 80
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 197-224 9.94e-06

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 45.17  E-value: 9.94e-06
                         10        20
                 ....*....|....*....|....*...
gi 732450203 197 L*VIIGSTFLIVCFLRQLKFHFTS*HHF 224
Cdd:MTH00155 204 LHVIIGTTFLLVCLIRHLNNHFSSNHHF 231
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 197-224 2.45e-05

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 44.11  E-value: 2.45e-05
                         10        20
                 ....*....|....*....|....*...
gi 732450203 197 L*VIIGSTFLIVCFLRQLKFHFTS*HHF 224
Cdd:MTH00141 204 LHVIIGTTFLLVCLVRLLLGHFSTNHHF 231
COX3 pfam00510
Cytochrome c oxidase subunit III;
197-224 3.75e-05

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 43.55  E-value: 3.75e-05
                          10        20
                  ....*....|....*....|....*...
gi 732450203  197 L*VIIGSTFLIVCFLRQLKFHFTS*HHF 224
Cdd:pfam00510 203 LHVIIGTAFLAVCFLRLLKYHLTDNHHF 230
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 199-224 4.13e-05

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: 43.27  E-value: 4.13e-05
                         10        20
                 ....*....|....*....|....*.
gi 732450203 199 VIIGSTFLIVCFLRQLKFHFTS*HHF 224
Cdd:cd01665  192 VIIGTIFLTVCLIRLLKGHFSSNHHL 217
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 1-74 5.47e-05

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 42.90  E-value: 5.47e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 732450203   1 MV*PSPWPLTGALSALLMTSGLA*******************************ESTFQGHHTSI*QKGLRY*M 74
Cdd:MTH00009   8 LVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGM 81
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 197-224 6.00e-05

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 42.85  E-value: 6.00e-05
                         10        20
                 ....*....|....*....|....*...
gi 732450203 197 L*VIIGSTFLIVCFLRQLKFHFTS*HHF 224
Cdd:MTH00219 207 LHVIIGTIFLFVCFMRGLMLHFSKNHHF 234
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 1-74 6.59e-05

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 42.82  E-value: 6.59e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 732450203   1 MV*PSPWPLTGALSALLMTSGLA*******************************ESTFQGHHTSI*QKGLRY*M 74
Cdd:MTH00024  10 LVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGM 83
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 197-224 8.35e-05

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 42.41  E-value: 8.35e-05
                         10        20
                 ....*....|....*....|....*...
gi 732450203 197 L*VIIGSTFLIVCFLRQLKFHFTS*HHF 224
Cdd:MTH00039 205 LHVIIGTTFLAVCLFRLINHHFSNNHHF 232
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 1-74 8.49e-05

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 42.47  E-value: 8.49e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 732450203   1 MV*PSPWPLTGALSALLMTSGLA*******************************ESTFQGHHTSI*QKGLRY*M 74
Cdd:MTH00052  11 LVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGLKYGM 84
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 1-74 6.48e-04

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 40.05  E-value: 6.48e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 732450203   1 MV*PSPWPLTGALSALLMTSGLA*******************************ESTFQGHHTSI*QKGLRY*M 74
Cdd:MTH00028  10 LVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGM 83
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 197-224 3.96e-03

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 37.42  E-value: 3.96e-03
                         10        20
                 ....*....|....*....|....*...
gi 732450203 197 L*VIIGSTFLIVCFLRQLKFHFTS*HHF 224
Cdd:MTH00024 206 LHVIIGTTFLFVCLLRLLSNQFTRRQHV 233
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 197-224 4.16e-03

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 37.46  E-value: 4.16e-03
                         10        20
                 ....*....|....*....|....*...
gi 732450203 197 L*VIIGSTFLIVCFLRQLKFHFTS*HHF 224
Cdd:MTH00052 207 GHVLIGSSFLLVCLFRLINHQFTRHHHF 234
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 197-224 5.77e-03

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 36.97  E-value: 5.77e-03
                         10        20
                 ....*....|....*....|....*...
gi 732450203 197 L*VIIGSTFLIVCFLRQLKFHFTS*HHF 224
Cdd:MTH00028 242 LHVLVGTTFLIVCFIRLLSNQFTNSHHL 269
 
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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