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Conserved domains on  [gi|767808744|gb|AJT57027|]
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cytochrome oxidase subunit 1, partial (mitochondrion) [Arthropoda sp. FLFIV287-14]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Heme_Cu_Oxidase_I super family cl00275
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
1-104 1.71e-52

Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. Membership in the superfamily is defined by subunit I, which contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons to the binuclear center. Only subunit I is common to the entire superfamily. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from the electron donor on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I of cytochrome c oxidase (CcO) and ubiquinol oxidase. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electron transfer occurs in two segments: from the electron donor to the low-spin heme, and from the low-spin heme to the binuclear center. The first segment can be a multi-step process and varies among the different families, while the second segment, a direct transfer, is consistent throughout the superfamily.


The actual alignment was detected with superfamily member MTH00153:

Pssm-ID: 412277  Cd Length: 511  Bit Score: 171.20  E-value: 1.71e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767808744   1 LSGKLSYSGCSVDFSIFSLHLAGVSSILGSINFISTIFNSTPNFNFFMEISLYTISVFVTTILLLASLPVLAGAITMLLA 80
Cdd:MTH00153 130 LSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLT 209
                         90       100
                 ....*....|....*....|....
gi 767808744  81 DRNFNTSFFDPTGGGDPVLYQHLF 104
Cdd:MTH00153 210 DRNLNTSFFDPAGGGDPILYQHLF 233
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
1-104 1.71e-52

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 171.20  E-value: 1.71e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767808744   1 LSGKLSYSGCSVDFSIFSLHLAGVSSILGSINFISTIFNSTPNFNFFMEISLYTISVFVTTILLLASLPVLAGAITMLLA 80
Cdd:MTH00153 130 LSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLT 209
                         90       100
                 ....*....|....*....|....
gi 767808744  81 DRNFNTSFFDPTGGGDPVLYQHLF 104
Cdd:MTH00153 210 DRNLNTSFFDPAGGGDPILYQHLF 233
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
1-104 6.60e-52

Cytochrome C oxidase subunit I. 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. It 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, may play a role in assembly or oxygen delivery to the active site. 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 I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme (heme a3) and a copper ion (CuB). It also contains a low-spin heme (heme a), believed to participate in the transfer of electrons to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from cytochrome c on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are transferred from cytochrome c (the electron donor) to heme a via the CuA binuclear site in subunit II, and directly from heme a to the binuclear center.


Pssm-ID: 238833  Cd Length: 488  Bit Score: 169.20  E-value: 6.60e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767808744   1 LSGKLSYSGCSVDFSIFSLHLAGVSSILGSINFISTIFNSTPNFNFFMEISLYTISVFVTTILLLASLPVLAGAITMLLA 80
Cdd:cd01663  123 LSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLT 202
                         90       100
                 ....*....|....*....|....
gi 767808744  81 DRNFNTSFFDPTGGGDPVLYQHLF 104
Cdd:cd01663  203 DRNFNTSFFDPAGGGDPILYQHLF 226
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
5-104 3.42e-32

Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];


Pssm-ID: 223913  Cd Length: 566  Bit Score: 117.40  E-value: 3.42e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767808744   5 LSYSGCSVDFSIFSLHLAGVSSILGSINFISTIFNSTPNFNFFMEISLYTISVFVTTILLLASLPVLAGAITMLLADRNF 84
Cdd:COG0843  140 ISYSGPGVDLFILGLHLLGIGSLLGAINFIVTILNMRAPGMTMMKMPLFTWSILITAILILLAFPVLAAALTMLLLDRNF 219
                         90       100
                 ....*....|....*....|
gi 767808744  85 NTSFFDPTGGGDPVLYQHLF 104
Cdd:COG0843  220 GTSFFTPAGGGDPLLYQHLF 239
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I;
12-104 1.64e-17

Cytochrome C and Quinol oxidase polypeptide I;


Pssm-ID: 395065  Cd Length: 434  Bit Score: 75.68  E-value: 1.64e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767808744   12 VDFSIFSLHLAGVSSILGSINFISTIFNSTPNFNFFMEISLYTISVFVTTILLLASLPVLAGAITMLLADRNFNTSFFDP 91
Cdd:pfam00115 115 VDLWYLGLLLAGVGSLLGAINFIVTILKRRAPGMYLSRMPLFVWAILATAILILLAFPVLAAALLLLLLDRSFGTHFFDP 194
                          90
                  ....*....|...
gi 767808744   92 tggGDPVLYQHLF 104
Cdd:pfam00115 195 ---GDPLLDQHLF 204
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
1-104 1.71e-52

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 171.20  E-value: 1.71e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767808744   1 LSGKLSYSGCSVDFSIFSLHLAGVSSILGSINFISTIFNSTPNFNFFMEISLYTISVFVTTILLLASLPVLAGAITMLLA 80
Cdd:MTH00153 130 LSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLT 209
                         90       100
                 ....*....|....*....|....
gi 767808744  81 DRNFNTSFFDPTGGGDPVLYQHLF 104
Cdd:MTH00153 210 DRNLNTSFFDPAGGGDPILYQHLF 233
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
1-104 6.60e-52

Cytochrome C oxidase subunit I. 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. It 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, may play a role in assembly or oxygen delivery to the active site. 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 I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme (heme a3) and a copper ion (CuB). It also contains a low-spin heme (heme a), believed to participate in the transfer of electrons to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from cytochrome c on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are transferred from cytochrome c (the electron donor) to heme a via the CuA binuclear site in subunit II, and directly from heme a to the binuclear center.


Pssm-ID: 238833  Cd Length: 488  Bit Score: 169.20  E-value: 6.60e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767808744   1 LSGKLSYSGCSVDFSIFSLHLAGVSSILGSINFISTIFNSTPNFNFFMEISLYTISVFVTTILLLASLPVLAGAITMLLA 80
Cdd:cd01663  123 LSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLT 202
                         90       100
                 ....*....|....*....|....
gi 767808744  81 DRNFNTSFFDPTGGGDPVLYQHLF 104
Cdd:cd01663  203 DRNFNTSFFDPAGGGDPILYQHLF 226
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
1-104 2.47e-46

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 154.83  E-value: 2.47e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767808744   1 LSGKLSYSGCSVDFSIFSLHLAGVSSILGSINFISTIFNSTPNFNFFMEISLYTISVFVTTILLLASLPVLAGAITMLLA 80
Cdd:MTH00167 132 LAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLT 211
                         90       100
                 ....*....|....*....|....
gi 767808744  81 DRNFNTSFFDPTGGGDPVLYQHLF 104
Cdd:MTH00167 212 DRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
1-104 1.63e-45

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 152.82  E-value: 1.63e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767808744   1 LSGKLSYSGCSVDFSIFSLHLAGVSSILGSINFISTIFNSTPNFNFFMEISLYTISVFVTTILLLASLPVLAGAITMLLA 80
Cdd:MTH00223 129 LSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLT 208
                         90       100
                 ....*....|....*....|....
gi 767808744  81 DRNFNTSFFDPTGGGDPVLYQHLF 104
Cdd:MTH00223 209 DRNFNTSFFDPAGGGDPILYQHLF 232
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
1-104 7.50e-44

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 148.32  E-value: 7.50e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767808744   1 LSGKLSYSGCSVDFSIFSLHLAGVSSILGSINFISTIFNSTPNFNFFMEISLYTISVFVTTILLLASLPVLAGAITMLLA 80
Cdd:MTH00116 132 LAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLT 211
                         90       100
                 ....*....|....*....|....
gi 767808744  81 DRNFNTSFFDPTGGGDPVLYQHLF 104
Cdd:MTH00116 212 DRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
1-104 1.95e-43

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 147.18  E-value: 1.95e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767808744   1 LSGKLSYSGCSVDFSIFSLHLAGVSSILGSINFISTIFNSTPNFNFFMEISLYTISVFVTTILLLASLPVLAGAITMLLA 80
Cdd:MTH00142 130 LSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLT 209
                         90       100
                 ....*....|....*....|....
gi 767808744  81 DRNFNTSFFDPTGGGDPVLYQHLF 104
Cdd:MTH00142 210 DRNFNTSFFDPAGGGDPILYQHLF 233
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
1-104 3.64e-38

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 133.12  E-value: 3.64e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767808744   1 LSGKLSYSGCSVDFSIFSLHLAGVSSILGSINFISTIFNSTPNFNFFMEISLYTISVFVTTILLLASLPVLAGAITMLLA 80
Cdd:MTH00183 132 LAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLT 211
                         90       100
                 ....*....|....*....|....
gi 767808744  81 DRNFNTSFFDPTGGGDPVLYQHLF 104
Cdd:MTH00183 212 DRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
1-104 2.36e-37

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 131.22  E-value: 2.36e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767808744   1 LSGKLSYSGCSVDFSIFSLHLAGVSSILGSINFISTIFNSTPNFNFFMEISLYTISVFVTTILLLASLPVLAGAITMLLA 80
Cdd:MTH00077 132 LAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLT 211
                         90       100
                 ....*....|....*....|....
gi 767808744  81 DRNFNTSFFDPTGGGDPVLYQHLF 104
Cdd:MTH00077 212 DRNLNTTFFDPAGGGDPVLYQHLF 235
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
1-104 2.58e-37

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 130.77  E-value: 2.58e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767808744   1 LSGKLSYSGCSVDFSIFSLHLAGVSSILGSINFISTIFNSTPNFNFFMEISLYTISVFVTTILLLASLPVLAGAITMLLA 80
Cdd:MTH00103 132 LAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLT 211
                         90       100
                 ....*....|....*....|....
gi 767808744  81 DRNFNTSFFDPTGGGDPVLYQHLF 104
Cdd:MTH00103 212 DRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
1-104 1.57e-36

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 128.79  E-value: 1.57e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767808744   1 LSGKLSYSGCSVDFSIFSLHLAGVSSILGSINFISTIFNSTPNFNFFMEISLYTISVFVTTILLLASLPVLAGAITMLLA 80
Cdd:MTH00184 134 LSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLT 213
                         90       100
                 ....*....|....*....|....
gi 767808744  81 DRNFNTSFFDPTGGGDPVLYQHLF 104
Cdd:MTH00184 214 DRNFNTTFFDPAGGGDPILYQHLF 237
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
1-104 2.90e-36

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 128.10  E-value: 2.90e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767808744   1 LSGKLSYSGCSVDFSIFSLHLAGVSSILGSINFISTIFNSTPNFNFFMEISLYTISVFVTTILLLASLPVLAGAITMLLA 80
Cdd:MTH00007 129 LASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLT 208
                         90       100
                 ....*....|....*....|....
gi 767808744  81 DRNFNTSFFDPTGGGDPVLYQHLF 104
Cdd:MTH00007 209 DRNLNTSFFDPAGGGDPILYQHLF 232
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
1-104 3.46e-36

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 128.02  E-value: 3.46e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767808744   1 LSGKLSYSGCSVDFSIFSLHLAGVSSILGSINFISTIFNSTPNFNFFMEISLYTISVFVTTILLLASLPVLAGAITMLLA 80
Cdd:MTH00037 132 LSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLT 211
                         90       100
                 ....*....|....*....|....
gi 767808744  81 DRNFNTSFFDPTGGGDPVLYQHLF 104
Cdd:MTH00037 212 DRNINTTFFDPAGGGDPILFQHLF 235
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
1-104 6.97e-36

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 127.24  E-value: 6.97e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767808744   1 LSGKLSYSGCSVDFSIFSLHLAGVSSILGSINFISTIFNSTPNFNFFMEISLYTISVFVTTILLLASLPVLAGAITMLLA 80
Cdd:MTH00182 134 LSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLT 213
                         90       100
                 ....*....|....*....|....
gi 767808744  81 DRNFNTSFFDPTGGGDPVLYQHLF 104
Cdd:MTH00182 214 DRNFNTTFFDPAGGGDPILFQHLF 237
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
1-104 5.99e-35

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 124.40  E-value: 5.99e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767808744   1 LSGKLSYSGCSVDFSIFSLHLAGVSSILGSINFISTIFnSTPNFNFFMEISLYTISVFVTTILLLASLPVLAGAITMLLA 80
Cdd:MTH00048 131 LSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIY-SAFMTNVFSRTSIILWSYLFTSILLLLSLPVLAAAITMLLF 209
                         90       100
                 ....*....|....*....|....
gi 767808744  81 DRNFNTSFFDPTGGGDPVLYQHLF 104
Cdd:MTH00048 210 DRNFGSAFFDPLGGGDPVLFQHMF 233
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
5-104 1.29e-34

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 123.64  E-value: 1.29e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767808744   5 LSYSGCSVDFSIFSLHLAGVSSILGSINFISTIFNSTPNFNFFMEISLYTISVFVTTILLLASLPVLAGAITMLLADRNF 84
Cdd:MTH00079 136 LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNL 215
                         90       100
                 ....*....|....*....|
gi 767808744  85 NTSFFDPTGGGDPVLYQHLF 104
Cdd:MTH00079 216 NTSFFDPSTGGNPLLYQHLF 235
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
1-104 2.80e-33

Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. Membership in the superfamily is defined by subunit I, which contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons to the binuclear center. Only subunit I is common to the entire superfamily. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from the electron donor on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I of cytochrome c oxidase (CcO) and ubiquinol oxidase. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electron transfer occurs in two segments: from the electron donor to the low-spin heme, and from the low-spin heme to the binuclear center. The first segment can be a multi-step process and varies among the different families, while the second segment, a direct transfer, is consistent throughout the superfamily.


Pssm-ID: 238461  Cd Length: 463  Bit Score: 119.56  E-value: 2.80e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767808744   1 LSGKLSYSGCSVDFSIFSLHLAGVSSILGSINFISTIFNSTPNFNFFMEISLYTISVFVTTILLLASLPVLAGAITMLLA 80
Cdd:cd00919  120 LSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLL 199
                         90       100
                 ....*....|....*....|....
gi 767808744  81 DRNFNTSFFDPTGGGDPVLYQHLF 104
Cdd:cd00919  200 DRNFGTSFFDPAGGGDPVLYQHLF 223
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
5-104 3.42e-32

Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];


Pssm-ID: 223913  Cd Length: 566  Bit Score: 117.40  E-value: 3.42e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767808744   5 LSYSGCSVDFSIFSLHLAGVSSILGSINFISTIFNSTPNFNFFMEISLYTISVFVTTILLLASLPVLAGAITMLLADRNF 84
Cdd:COG0843  140 ISYSGPGVDLFILGLHLLGIGSLLGAINFIVTILNMRAPGMTMMKMPLFTWSILITAILILLAFPVLAAALTMLLLDRNF 219
                         90       100
                 ....*....|....*....|
gi 767808744  85 NTSFFDPTGGGDPVLYQHLF 104
Cdd:COG0843  220 GTSFFTPAGGGDPLLYQHLF 239
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
6-104 6.67e-31

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 113.57  E-value: 6.67e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767808744   6 SYSGCSVDFSIFSLHLAGVSSILGSINFISTIFNSTPNFNFFMEISLYTISVFVTTILLLASLPVLAGAITMLLADRNFN 85
Cdd:MTH00026 138 AHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFN 217
                         90
                 ....*....|....*....
gi 767808744  86 TSFFDPTGGGDPVLYQHLF 104
Cdd:MTH00026 218 TTFFDPAGGGDPILYQHLF 236
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
1-104 3.44e-22

Ubiquinol oxidase subunit I. 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. The number of subunits in ubiquinol oxidase varies from two to five. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons from ubiquinol to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from ubiquinol on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. It is generally believed that the channels contain water molecules that act as 'proton wires' to transfer the protons. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are believed to be transferred directly from ubiquinol (the electron donor) to the low-spin heme, and directly from the low-spin heme to the binuclear center.


Pssm-ID: 238832  Cd Length: 501  Bit Score: 89.18  E-value: 3.44e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767808744   1 LSGKLSYSGCSVDFSIFSLHLAGVSSILGSINFISTIFNSTPNFNFFMEISLYTISVFVTTILLLASLPVLAGAITMLLA 80
Cdd:cd01662  126 LSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLEL 205
                         90       100
                 ....*....|....*....|....
gi 767808744  81 DRNFNTSFFDPTGGGDPVLYQHLF 104
Cdd:cd01662  206 DRYFGTHFFTNALGGNPMLWQHLF 229
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I;
12-104 1.64e-17

Cytochrome C and Quinol oxidase polypeptide I;


Pssm-ID: 395065  Cd Length: 434  Bit Score: 75.68  E-value: 1.64e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767808744   12 VDFSIFSLHLAGVSSILGSINFISTIFNSTPNFNFFMEISLYTISVFVTTILLLASLPVLAGAITMLLADRNFNTSFFDP 91
Cdd:pfam00115 115 VDLWYLGLLLAGVGSLLGAINFIVTILKRRAPGMYLSRMPLFVWAILATAILILLAFPVLAAALLLLLLDRSFGTHFFDP 194
                          90
                  ....*....|...
gi 767808744   92 tggGDPVLYQHLF 104
Cdd:pfam00115 195 ---GDPLLDQHLF 204
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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