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Conserved domains on  [gi|155675166|gb|ABU24918|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Hymeniacidon heliophila]

Protein Classification

heme-copper oxidase family protein( domain architecture ID 14)

heme-copper oxidase family protein may catalyze the transfer of electrons from an electron donor onto molecular oxygen

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 ...
 1-195 2.20e-111

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 cd01663:

Pssm-ID: 469701  Cd Length: 488  Bit Score: 326.36  E-value: 2.20e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155675166   1 MIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVLIGGFGNWFVPLYIGAPDMAFPRLNNLSFWLLPP 80
Cdd:cd01663   19 LVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPP 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155675166  81 ALTLLLSSAFVEQGAGTGWTVYPPLSSIQFHSGGSVDMAIFSLHLAGISSILGAMNFITTIINMRAPGITMDRMPLFVWS 160
Cdd:cd01663   99 SLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWS 178

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 155675166 161 VLVTAVLLLLSLPVFAGAITMLLTDRNFNTAFFDP 195
Cdd:cd01663  179 VLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDP 213
 
Name Accession Description Interval E-value
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-195 2.20e-111

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: 326.36  E-value: 2.20e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155675166   1 MIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVLIGGFGNWFVPLYIGAPDMAFPRLNNLSFWLLPP 80
Cdd:cd01663   19 LVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPP 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155675166  81 ALTLLLSSAFVEQGAGTGWTVYPPLSSIQFHSGGSVDMAIFSLHLAGISSILGAMNFITTIINMRAPGITMDRMPLFVWS 160
Cdd:cd01663   99 SLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWS 178

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 155675166 161 VLVTAVLLLLSLPVFAGAITMLLTDRNFNTAFFDP 195
Cdd:cd01663  179 VLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDP 213
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-195 2.37e-111

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 327.21  E-value: 2.37e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155675166   1 MIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVLIGGFGNWFVPLYIGAPDMAFPRLNNLSFWLLPP 80
Cdd:MTH00153  26 MVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPP 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155675166  81 ALTLLLSSAFVEQGAGTGWTVYPPLSSIQFHSGGSVDMAIFSLHLAGISSILGAMNFITTIINMRAPGITMDRMPLFVWS 160
Cdd:MTH00153 106 SLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWS 185

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 155675166 161 VLVTAVLLLLSLPVFAGAITMLLTDRNFNTAFFDP 195
Cdd:MTH00153 186 VLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDP 220
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-195 6.45e-63

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 203.05  E-value: 6.45e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155675166   1 MIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPvLIGGFGNWFVPLYIGAPDMAFPRLNNLSFWLLPP 80
Cdd:COG0843   31 LIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLF 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155675166  81 ALTLLLSSAFVEQGAGTGWTVYPPLSSIQFHSGGSVDMAIFSLHLAGISSILGAMNFITTIINMRAPGITMDRMPLFVWS 160
Cdd:COG0843  110 GGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWA 189

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 155675166 161 VLVTAVLLLLSLPVFAGAITMLLTDRNFNTAFFDP 195
Cdd:COG0843  190 ALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDP 224
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-195 3.47e-39

Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key enzyme in aerobic metabolism. Proton pumping haem-copper oxidases represent the terminal, energy-transfer enzymes of respiratory chains in prokaryotes and eukaryotes. The CuB-haem a3 (or haem o) binuclear centre, associated with the largest subunit I of cytochrome c and ubiquinol oxidases (E.C:1.10.3.11), is directly involved in the coupling between dioxygen reduction and proton pumping. Some terminal oxidases generate a transmembrane proton gradient across the plasma membrane (prokaryotes) or the mitochondrial inner membrane (eukaryotes). The enzyme complex consists of 3-4 subunits (prokaryotes) up to 13 polypeptides (mammals) of which only the catalytic subunit (equivalent to mammalian subunit I (COXI) is found in all haem-copper respiratory oxidases. The presence of a bimetallic centre (formed by a high-spin haem and copper B) as well as a low-spin haem, both ligated to six conserved histidine residues near the outer side of four transmembrane spans within CO I is common to all family members.


Pssm-ID: 459678  Cd Length: 432  Bit Score: 138.47  E-value: 3.47e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155675166    1 MIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVlIGGFGNWFVPLYIGAPDMAFPRLNNLSFWLLPP 80
Cdd:pfam00115  15 LVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRLNALSFWLVVL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155675166   81 ALTLLLSSAfveQGAGTGWTVYPPLssiqfhsgGSVDMAIFSLHLAGISSILGAMNFITTIINMRAPGITMdRMPLFVWS 160
Cdd:pfam00115  94 GAVLLLASF---GGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWA 161

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 155675166  161 VLVTAVLLLLSLPVFAGAITMLLTDRNFNTAFFDP 195
Cdd:pfam00115 162 ILATAILILLAFPVLAAALLLLLLDRSLGAGGGDP 196
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 3-193 1.52e-34

cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]


Pssm-ID: 131928  Cd Length: 643  Bit Score: 128.43  E-value: 1.52e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155675166    3 GTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVLIGgFGNWFVPLYIGAPDMAFPRLNNLSFWLLPPAL 82
Cdd:TIGR02882  68 GGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGA 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155675166   83 TLLLSSAFVEQGAGTGWTVYPPLSSIQFHSGGSVDMAIFSLHLAGISSILGAMNFITTIINMRAPGITMDRMPLFVWSVL 162
Cdd:TIGR02882 147 MLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTL 226

                         170       180       190
                  ....*....|....*....|....*....|.
gi 155675166  163 VTAVLLLLSLPVFAGAITMLLTDRNFNTAFF 193
Cdd:TIGR02882 227 ITTLIIIFAFPVLTVALALMTTDRIFDTAFF 257
 
Name Accession Description Interval E-value
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-195 2.20e-111

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: 326.36  E-value: 2.20e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155675166   1 MIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVLIGGFGNWFVPLYIGAPDMAFPRLNNLSFWLLPP 80
Cdd:cd01663   19 LVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPP 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155675166  81 ALTLLLSSAFVEQGAGTGWTVYPPLSSIQFHSGGSVDMAIFSLHLAGISSILGAMNFITTIINMRAPGITMDRMPLFVWS 160
Cdd:cd01663   99 SLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWS 178

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 155675166 161 VLVTAVLLLLSLPVFAGAITMLLTDRNFNTAFFDP 195
Cdd:cd01663  179 VLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDP 213
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-195 2.37e-111

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 327.21  E-value: 2.37e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155675166   1 MIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVLIGGFGNWFVPLYIGAPDMAFPRLNNLSFWLLPP 80
Cdd:MTH00153  26 MVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPP 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155675166  81 ALTLLLSSAFVEQGAGTGWTVYPPLSSIQFHSGGSVDMAIFSLHLAGISSILGAMNFITTIINMRAPGITMDRMPLFVWS 160
Cdd:MTH00153 106 SLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWS 185

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 155675166 161 VLVTAVLLLLSLPVFAGAITMLLTDRNFNTAFFDP 195
Cdd:MTH00153 186 VLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDP 220
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-195 1.16e-104

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 310.22  E-value: 1.16e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155675166   1 MIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVLIGGFGNWFVPLYIGAPDMAFPRLNNLSFWLLPP 80
Cdd:MTH00184  30 MIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPP 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155675166  81 ALTLLLSSAFVEQGAGTGWTVYPPLSSIQFHSGGSVDMAIFSLHLAGISSILGAMNFITTIINMRAPGITMDRMPLFVWS 160
Cdd:MTH00184 110 ALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWS 189

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 155675166 161 VLVTAVLLLLSLPVFAGAITMLLTDRNFNTAFFDP 195
Cdd:MTH00184 190 ILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDP 224
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-195 3.11e-103

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 306.75  E-value: 3.11e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155675166   1 MIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVLIGGFGNWFVPLYIGAPDMAFPRLNNLSFWLLPP 80
Cdd:MTH00182  30 MIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPP 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155675166  81 ALTLLLSSAFVEQGAGTGWTVYPPLSSIQFHSGGSVDMAIFSLHLAGISSILGAMNFITTIINMRAPGITMDRMPLFVWS 160
Cdd:MTH00182 110 ALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWS 189

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 155675166 161 VLVTAVLLLLSLPVFAGAITMLLTDRNFNTAFFDP 195
Cdd:MTH00182 190 ILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDP 224
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-195 2.77e-100

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 298.82  E-value: 2.77e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155675166   1 MIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVLIGGFGNWFVPLYIGAPDMAFPRLNNLSFWLLPP 80
Cdd:MTH00223  25 LVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPP 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155675166  81 ALTLLLSSAFVEQGAGTGWTVYPPLSSIQFHSGGSVDMAIFSLHLAGISSILGAMNFITTIINMRAPGITMDRMPLFVWS 160
Cdd:MTH00223 105 SLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWS 184

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 155675166 161 VLVTAVLLLLSLPVFAGAITMLLTDRNFNTAFFDP 195
Cdd:MTH00223 185 VKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDP 219
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-195 8.71e-100

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 297.74  E-value: 8.71e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155675166   1 MIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVLIGGFGNWFVPLYIGAPDMAFPRLNNLSFWLLPP 80
Cdd:MTH00167  28 MVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPP 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155675166  81 ALTLLLSSAFVEQGAGTGWTVYPPLSSIQFHSGGSVDMAIFSLHLAGISSILGAMNFITTIINMRAPGITMDRMPLFVWS 160
Cdd:MTH00167 108 SLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWS 187

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 155675166 161 VLVTAVLLLLSLPVFAGAITMLLTDRNFNTAFFDP 195
Cdd:MTH00167 188 ILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDP 222
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-195 5.04e-97

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 290.47  E-value: 5.04e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155675166   1 MIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVLIGGFGNWFVPLYIGAPDMAFPRLNNLSFWLLPP 80
Cdd:MTH00142  26 MVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPP 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155675166  81 ALTLLLSSAFVEQGAGTGWTVYPPLSSIQFHSGGSVDMAIFSLHLAGISSILGAMNFITTIINMRAPGITMDRMPLFVWS 160
Cdd:MTH00142 106 ALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWS 185

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 155675166 161 VLVTAVLLLLSLPVFAGAITMLLTDRNFNTAFFDP 195
Cdd:MTH00142 186 VKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDP 220
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-195 8.07e-93

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 280.05  E-value: 8.07e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155675166   1 MIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVLIGGFGNWFVPLYIGAPDMAFPRLNNLSFWLLPP 80
Cdd:MTH00116  28 MVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPP 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155675166  81 ALTLLLSSAFVEQGAGTGWTVYPPLSSIQFHSGGSVDMAIFSLHLAGISSILGAMNFITTIINMRAPGITMDRMPLFVWS 160
Cdd:MTH00116 108 SFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWS 187

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 155675166 161 VLVTAVLLLLSLPVFAGAITMLLTDRNFNTAFFDP 195
Cdd:MTH00116 188 VLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDP 222
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 2-195 5.80e-89

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 270.73  E-value: 5.80e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155675166   2 IGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVLIGGFGNWFVPLYIGAPDMAFPRLNNLSFWLLPPA 81
Cdd:MTH00026  30 IGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPA 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155675166  82 LTLLLSSAFVEQGAGTGWTVYPPLSSIQFHSGGSVDMAIFSLHLAGISSILGAMNFITTIINMRAPGITMDRMPLFVWSV 161
Cdd:MTH00026 110 LFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSV 189

                        170       180       190
                 ....*....|....*....|....*....|....
gi 155675166 162 LVTAVLLLLSLPVFAGAITMLLTDRNFNTAFFDP 195
Cdd:MTH00026 190 FITAILLLLSLPVLAGAITMLLTDRNFNTTFFDP 223
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-195 2.62e-86

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 263.23  E-value: 2.62e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155675166   1 MIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVLIGGFGNWFVPLYIGAPDMAFPRLNNLSFWLLPP 80
Cdd:MTH00037  28 MVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPP 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155675166  81 ALTLLLSSAFVEQGAGTGWTVYPPLSSIQFHSGGSVDMAIFSLHLAGISSILGAMNFITTIINMRAPGITMDRMPLFVWS 160
Cdd:MTH00037 108 SFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWS 187

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 155675166 161 VLVTAVLLLLSLPVFAGAITMLLTDRNFNTAFFDP 195
Cdd:MTH00037 188 VFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDP 222
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-195 1.37e-85

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 261.37  E-value: 1.37e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155675166   1 MIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVLIGGFGNWFVPLYIGAPDMAFPRLNNLSFWLLPP 80
Cdd:MTH00007  25 LLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPP 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155675166  81 ALTLLLSSAFVEQGAGTGWTVYPPLSSIQFHSGGSVDMAIFSLHLAGISSILGAMNFITTIINMRAPGITMDRMPLFVWS 160
Cdd:MTH00007 105 ALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWA 184

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 155675166 161 VLVTAVLLLLSLPVFAGAITMLLTDRNFNTAFFDP 195
Cdd:MTH00007 185 VVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDP 219
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-195 2.96e-84

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 257.93  E-value: 2.96e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155675166   1 MIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVLIGGFGNWFVPLYIGAPDMAFPRLNNLSFWLLPP 80
Cdd:MTH00183  28 MVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPP 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155675166  81 ALTLLLSSAFVEQGAGTGWTVYPPLSSIQFHSGGSVDMAIFSLHLAGISSILGAMNFITTIINMRAPGITMDRMPLFVWS 160
Cdd:MTH00183 108 SFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWA 187

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 155675166 161 VLVTAVLLLLSLPVFAGAITMLLTDRNFNTAFFDP 195
Cdd:MTH00183 188 VLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDP 222
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-195 1.58e-83

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 256.02  E-value: 1.58e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155675166   1 MIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVLIGGFGNWFVPLYIGAPDMAFPRLNNLSFWLLPP 80
Cdd:MTH00077  28 MVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPP 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155675166  81 ALTLLLSSAFVEQGAGTGWTVYPPLSSIQFHSGGSVDMAIFSLHLAGISSILGAMNFITTIINMRAPGITMDRMPLFVWS 160
Cdd:MTH00077 108 SFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWS 187

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 155675166 161 VLVTAVLLLLSLPVFAGAITMLLTDRNFNTAFFDP 195
Cdd:MTH00077 188 VLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDP 222
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-195 2.26e-83

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 255.58  E-value: 2.26e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155675166   1 MIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVLIGGFGNWFVPLYIGAPDMAFPRLNNLSFWLLPP 80
Cdd:MTH00103  28 MVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPP 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155675166  81 ALTLLLSSAFVEQGAGTGWTVYPPLSSIQFHSGGSVDMAIFSLHLAGISSILGAMNFITTIINMRAPGITMDRMPLFVWS 160
Cdd:MTH00103 108 SFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWS 187

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 155675166 161 VLVTAVLLLLSLPVFAGAITMLLTDRNFNTAFFDP 195
Cdd:MTH00103 188 VLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDP 222
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-195 3.28e-80

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 247.29  E-value: 3.28e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155675166   1 MIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVLIGGFGNWFVPLYIGAPDMAFPRLNNLSFWLLPP 80
Cdd:MTH00079  29 MVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPT 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155675166  81 ALTLLLSSAFVEQGAGTGWTVYPPLSSIQfHSGGSVDMAIFSLHLAGISSILGAMNFITTIINMRAPGITMDRMPLFVWS 160
Cdd:MTH00079 109 SLFLILDSCFVDMGPGTSWTVYPPLSTLG-HPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWT 187

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 155675166 161 VLVTAVLLLLSLPVFAGAITMLLTDRNFNTAFFDP 195
Cdd:MTH00079 188 VFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDP 222
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-195 5.22e-70

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: 219.71  E-value: 5.22e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155675166   1 MIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVLIGGFGNWFVPLyIGAPDMAFPRLNNLSFWLLPP 80
Cdd:cd00919   17 LLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPPL-IGARDLAFPRLNNLSFWLFPP 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155675166  81 ALTLLLSSAFVEQGAGTGWTVYPPLSSIQFHSGGSVDMAIFSLHLAGISSILGAMNFITTIINMRAPGITMDRMPLFVWS 160
Cdd:cd00919   96 GLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWS 175

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 155675166 161 VLVTAVLLLLSLPVFAGAITMLLTDRNFNTAFFDP 195
Cdd:cd00919  176 VLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDP 210
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-195 6.45e-63

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 203.05  E-value: 6.45e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155675166   1 MIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPvLIGGFGNWFVPLYIGAPDMAFPRLNNLSFWLLPP 80
Cdd:COG0843   31 LIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLF 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155675166  81 ALTLLLSSAFVEQGAGTGWTVYPPLSSIQFHSGGSVDMAIFSLHLAGISSILGAMNFITTIINMRAPGITMDRMPLFVWS 160
Cdd:COG0843  110 GGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWA 189

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 155675166 161 VLVTAVLLLLSLPVFAGAITMLLTDRNFNTAFFDP 195
Cdd:COG0843  190 ALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDP 224
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 2-195 1.17e-53

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: 178.16  E-value: 1.17e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155675166   2 IGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVLIGgFGNWFVPLYIGAPDMAFPRLNNLSFWLLPPA 81
Cdd:cd01662   24 RGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFG 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155675166  82 LTLLLSSAFVEQGAGTGWTVYPPLSSIQFHSGGSVDMAIFSLHLAGISSILGAMNFITTIINMRAPGITMDRMPLFVWSV 161
Cdd:cd01662  103 GLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTT 182

                        170       180       190
                 ....*....|....*....|....*....|....
gi 155675166 162 LVTAVLLLLSLPVFAGAITMLLTDRNFNTAFFDP 195
Cdd:cd01662  183 LVTSILILFAFPVLTAALALLELDRYFGTHFFTN 216
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 2-195 2.84e-53

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 177.18  E-value: 2.84e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155675166   2 IGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVLIGGFGNWFVPLYIGAPDMAFPRLNNLSFWLLPPA 81
Cdd:MTH00048  30 VGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPS 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155675166  82 LTLLLSSAFVeqGAGTGWTVYPPLSSIQFHSGGSVDMAIFSLHLAGISSILGAMNFITTIINMRAPGITMdRMPLFVWSV 161
Cdd:MTH00048 110 IVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFS-RTSIILWSY 186

                        170       180       190
                 ....*....|....*....|....*....|....
gi 155675166 162 LVTAVLLLLSLPVFAGAITMLLTDRNFNTAFFDP 195
Cdd:MTH00048 187 LFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDP 220
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-195 3.47e-39

Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key enzyme in aerobic metabolism. Proton pumping haem-copper oxidases represent the terminal, energy-transfer enzymes of respiratory chains in prokaryotes and eukaryotes. The CuB-haem a3 (or haem o) binuclear centre, associated with the largest subunit I of cytochrome c and ubiquinol oxidases (E.C:1.10.3.11), is directly involved in the coupling between dioxygen reduction and proton pumping. Some terminal oxidases generate a transmembrane proton gradient across the plasma membrane (prokaryotes) or the mitochondrial inner membrane (eukaryotes). The enzyme complex consists of 3-4 subunits (prokaryotes) up to 13 polypeptides (mammals) of which only the catalytic subunit (equivalent to mammalian subunit I (COXI) is found in all haem-copper respiratory oxidases. The presence of a bimetallic centre (formed by a high-spin haem and copper B) as well as a low-spin haem, both ligated to six conserved histidine residues near the outer side of four transmembrane spans within CO I is common to all family members.


Pssm-ID: 459678  Cd Length: 432  Bit Score: 138.47  E-value: 3.47e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155675166    1 MIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVlIGGFGNWFVPLYIGAPDMAFPRLNNLSFWLLPP 80
Cdd:pfam00115  15 LVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRLNALSFWLVVL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155675166   81 ALTLLLSSAfveQGAGTGWTVYPPLssiqfhsgGSVDMAIFSLHLAGISSILGAMNFITTIINMRAPGITMdRMPLFVWS 160
Cdd:pfam00115  94 GAVLLLASF---GGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWA 161

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 155675166  161 VLVTAVLLLLSLPVFAGAITMLLTDRNFNTAFFDP 195
Cdd:pfam00115 162 ILATAILILLAFPVLAAALLLLLLDRSLGAGGGDP 196
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 25-193 1.74e-37

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 136.60  E-value: 1.74e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155675166  25 HLYNVIVTAHAFVMIFFLVMPVLIGgFGNWFVPLYIGAPDMAFPRLNNLSFWLLPPALTLLLSSAFVEQGAGTGWTVYPP 104
Cdd:PRK15017  97 HHYDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPP 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155675166 105 LSSIQFHSGGSVDMAIFSLHLAGISSILGAMNFITTIINMRAPGITMDRMPLFVWSVLVTAVLLLLSLPVFAGAITMLLT 184
Cdd:PRK15017 176 LSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTL 255


                 ....*....
gi 155675166 185 DRNFNTAFF 193
Cdd:PRK15017 256 DRYLGTHFF 264
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 3-193 1.52e-34

cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]


Pssm-ID: 131928  Cd Length: 643  Bit Score: 128.43  E-value: 1.52e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155675166    3 GTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVLIGgFGNWFVPLYIGAPDMAFPRLNNLSFWLLPPAL 82
Cdd:TIGR02882  68 GGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGA 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155675166   83 TLLLSSAFVEQGAGTGWTVYPPLSSIQFHSGGSVDMAIFSLHLAGISSILGAMNFITTIINMRAPGITMDRMPLFVWSVL 162
Cdd:TIGR02882 147 MLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTL 226

                         170       180       190
                  ....*....|....*....|....*....|.
gi 155675166  163 VTAVLLLLSLPVFAGAITMLLTDRNFNTAFF 193
Cdd:TIGR02882 227 ITTLIIIFAFPVLTVALALMTTDRIFDTAFF 257
 
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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