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Conserved domains on  [gi|2021353306|gb|QTK16337|]
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cytochrome c oxidase subunit I, partial (mitochondrion) [Pseudolynchia canariensis]

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 ...
 1-234 4.39e-167

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: 469701  Cd Length: 511  Bit Score: 470.50  E-value: 4.39e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021353306   1 MVMPTVIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALTFLLMSSMTENGSGTGWTVYPPLSSTIAHSGASVDMAIF 80
Cdd:MTH00153   67 MVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIF 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021353306  81 SLHLAGISSILGAVNFITTVINMRSTGISFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDP 160
Cdd:MTH00153  147 SLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDP 226

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2021353306 161 ILYQHLFWFFSLPEVYILILTGIGMISHMISQESGKKETFGSLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTR 234
Cdd:MTH00153  227 ILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTR 300
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-234 4.39e-167

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 470.50  E-value: 4.39e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021353306   1 MVMPTVIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALTFLLMSSMTENGSGTGWTVYPPLSSTIAHSGASVDMAIF 80
Cdd:MTH00153   67 MVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIF 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021353306  81 SLHLAGISSILGAVNFITTVINMRSTGISFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDP 160
Cdd:MTH00153  147 SLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDP 226

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2021353306 161 ILYQHLFWFFSLPEVYILILTGIGMISHMISQESGKKETFGSLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTR 234
Cdd:MTH00153  227 ILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTR 300
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-234 2.40e-151

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: 429.98  E-value: 2.40e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021353306   1 MVMPTVIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALTFLLMSSMTENGSGTGWTVYPPLSSTIAHSGASVDMAIF 80
Cdd:cd01663    60 MVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIF 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021353306  81 SLHLAGISSILGAVNFITTVINMRSTGISFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDP 160
Cdd:cd01663   140 SLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDP 219

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2021353306 161 ILYQHLFWFFSLPEVYILILTGIGMISHMISQESGKKETFGSLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTR 234
Cdd:cd01663   220 ILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTR 293
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-230 2.82e-92

cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) of cytochrome c oxidases of bacterial origin. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits I-III form the functional core of the enzyme complex. Subunit I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit II and heme a of subunit I to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. In the bacilli an apparent split (paralogism) has created a sister clade (TIGR02882) encoding subunits (QoxA) of the aa3-type quinone oxidase complex which reacts directly with quinones, bypassing the interaction with soluble cytochrome c. This model attempts to exclude these sequences, placing them between the trusted and noise cutoffs. These families, as well as archaeal and eukaryotic cytochrome c subunit I's are included within the superfamily model, pfam00115. [Energy metabolism, Electron transport]


Pssm-ID: 213748  Cd Length: 499  Bit Score: 279.49  E-value: 2.82e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021353306   1 MVMPtVIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALTFLLMSSMTENGSGTGWTVYPPLSSTIAHSGASVDMAIF 80
Cdd:TIGR02891  63 FAIP-ILAGFGNYLLPLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLL 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021353306  81 SLHLAGISSILGAVNFITTVINMRSTGISFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDP 160
Cdd:TIGR02891 142 GLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDP 221

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021353306 161 ILYQHLFWFFSLPEVYILILTGIGMISHMISQESGKKeTFGSLGMIYAMLSIGLLGFIVWAHHMFTVGMD 230
Cdd:TIGR02891 222 LLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMP 290
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-229 1.20e-87

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 268.92  E-value: 1.20e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021353306   1 MVMPtVIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALTFLLMSSMTENGSGTGWTVYPPLSSTIAHSGASVDMAIF 80
Cdd:COG0843    72 FATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLL 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021353306  81 SLHLAGISSILGAVNFITTVINMRSTGISFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDP 160
Cdd:COG0843   151 GLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDP 230

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2021353306 161 ILYQHLFWFFSLPEVYILILTGIGMISHMISQESGKKeTFGSLGMIYAMLSIGLLGFIVWAHHMFTVGM 229
Cdd:COG0843   231 LLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGI 298
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-234 5.10e-54

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: 178.92  E-value: 5.10e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021353306   1 MVMPtVIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALTFLLMSSMtenGSGTGWTVYPPLsstiahsgASVDMAIF 80
Cdd:pfam00115  56 FATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYI 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021353306  81 SLHLAGISSILGAVNFITTVINMRSTGISFdRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNFNtsffdpAGGGDP 160
Cdd:pfam00115 124 GLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDP 196

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2021353306 161 ILYQHLFWFFSLPEVYILILTGIGMISHMISQESGKKeTFGSLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTR 234
Cdd:pfam00115 197 LLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQ 269
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-234 4.39e-167

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 470.50  E-value: 4.39e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021353306   1 MVMPTVIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALTFLLMSSMTENGSGTGWTVYPPLSSTIAHSGASVDMAIF 80
Cdd:MTH00153   67 MVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIF 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021353306  81 SLHLAGISSILGAVNFITTVINMRSTGISFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDP 160
Cdd:MTH00153  147 SLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDP 226

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2021353306 161 ILYQHLFWFFSLPEVYILILTGIGMISHMISQESGKKETFGSLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTR 234
Cdd:MTH00153  227 ILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTR 300
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-234 2.40e-151

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: 429.98  E-value: 2.40e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021353306   1 MVMPTVIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALTFLLMSSMTENGSGTGWTVYPPLSSTIAHSGASVDMAIF 80
Cdd:cd01663    60 MVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIF 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021353306  81 SLHLAGISSILGAVNFITTVINMRSTGISFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDP 160
Cdd:cd01663   140 SLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDP 219

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2021353306 161 ILYQHLFWFFSLPEVYILILTGIGMISHMISQESGKKETFGSLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTR 234
Cdd:cd01663   220 ILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTR 293
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-234 2.59e-141

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 405.13  E-value: 2.59e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021353306   1 MVMPTVIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALTFLLMSSMTENGSGTGWTVYPPLSSTIAHSGASVDMAIF 80
Cdd:MTH00223   66 LVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIF 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021353306  81 SLHLAGISSILGAVNFITTVINMRSTGISFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDP 160
Cdd:MTH00223  146 SLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDP 225

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2021353306 161 ILYQHLFWFFSLPEVYILILTGIGMISHMISQESGKKETFGSLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTR 234
Cdd:MTH00223  226 ILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTR 299
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-234 8.91e-140

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 401.36  E-value: 8.91e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021353306   1 MVMPTVIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALTFLLMSSMTENGSGTGWTVYPPLSSTIAHSGASVDMAIF 80
Cdd:MTH00167   69 MVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIF 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021353306  81 SLHLAGISSILGAVNFITTVINMRSTGISFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDP 160
Cdd:MTH00167  149 SLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDP 228

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2021353306 161 ILYQHLFWFFSLPEVYILILTGIGMISHMISQESGKKETFGSLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTR 234
Cdd:MTH00167  229 ILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTR 302
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-234 6.83e-138

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 396.40  E-value: 6.83e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021353306   1 MVMPTVIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALTFLLMSSMTENGSGTGWTVYPPLSSTIAHSGASVDMAIF 80
Cdd:MTH00142   67 MVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIF 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021353306  81 SLHLAGISSILGAVNFITTVINMRSTGISFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDP 160
Cdd:MTH00142  147 SLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDP 226

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2021353306 161 ILYQHLFWFFSLPEVYILILTGIGMISHMISQESGKKETFGSLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTR 234
Cdd:MTH00142  227 ILYQHLFWFFGHPEVYILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTR 300
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-234 3.94e-135

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 389.45  E-value: 3.94e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021353306   1 MVMPTVIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALTFLLMSSMTENGSGTGWTVYPPLSSTIAHSGASVDMAIF 80
Cdd:MTH00116   69 MVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIF 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021353306  81 SLHLAGISSILGAVNFITTVINMRSTGISFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDP 160
Cdd:MTH00116  149 SLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDP 228

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2021353306 161 ILYQHLFWFFSLPEVYILILTGIGMISHMISQESGKKETFGSLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTR 234
Cdd:MTH00116  229 ILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTR 302
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-234 3.55e-124

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 361.53  E-value: 3.55e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021353306   1 MVMPTVIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALTFLLMSSMTENGSGTGWTVYPPLSSTIAHSGASVDMAIF 80
Cdd:MTH00007   66 LVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIF 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021353306  81 SLHLAGISSILGAVNFITTVINMRSTGISFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDP 160
Cdd:MTH00007  146 SLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDP 225

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2021353306 161 ILYQHLFWFFSLPEVYILILTGIGMISHMISQESGKKETFGSLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTR 234
Cdd:MTH00007  226 ILYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTR 299
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-234 1.77e-121

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 354.91  E-value: 1.77e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021353306   1 MVMPTVIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALTFLLMSSMTENGSGTGWTVYPPLSSTIAHSGASVDMAIF 80
Cdd:MTH00037   69 MVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIF 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021353306  81 SLHLAGISSILGAVNFITTVINMRSTGISFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDP 160
Cdd:MTH00037  149 SLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDP 228

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2021353306 161 ILYQHLFWFFSLPEVYILILTGIGMISHMISQESGKKETFGSLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTR 234
Cdd:MTH00037  229 ILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTR 302
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-234 1.83e-120

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 352.59  E-value: 1.83e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021353306   1 MVMPTVIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALTFLLMSSMTENGSGTGWTVYPPLSSTIAHSGASVDMAIF 80
Cdd:MTH00182   71 LVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIF 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021353306  81 SLHLAGISSILGAVNFITTVINMRSTGISFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDP 160
Cdd:MTH00182  151 SLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDP 230

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2021353306 161 ILYQHLFWFFSLPEVYILILTGIGMISHMISQESGKKETFGSLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTR 234
Cdd:MTH00182  231 ILFQHLFWFFGHPEVYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTR 304
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-234 3.42e-119

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 349.22  E-value: 3.42e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021353306   1 MVMPTVIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALTFLLMSSMTENGSGTGWTVYPPLSSTIAHSGASVDMAIF 80
Cdd:MTH00183   69 MVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIF 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021353306  81 SLHLAGISSILGAVNFITTVINMRSTGISFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDP 160
Cdd:MTH00183  149 SLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDP 228

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2021353306 161 ILYQHLFWFFSLPEVYILILTGIGMISHMISQESGKKETFGSLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTR 234
Cdd:MTH00183  229 ILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTR 302
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-234 1.16e-118

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 347.64  E-value: 1.16e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021353306   1 MVMPTVIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALTFLLMSSMTENGSGTGWTVYPPLSSTIAHSGASVDMAIF 80
Cdd:MTH00103   69 MVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIF 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021353306  81 SLHLAGISSILGAVNFITTVINMRSTGISFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDP 160
Cdd:MTH00103  149 SLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDP 228

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2021353306 161 ILYQHLFWFFSLPEVYILILTGIGMISHMISQESGKKETFGSLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTR 234
Cdd:MTH00103  229 ILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTR 302
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-234 3.63e-118

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 346.43  E-value: 3.63e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021353306   1 MVMPTVIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALTFLLMSSMTENGSGTGWTVYPPLSSTIAHSGASVDMAIF 80
Cdd:MTH00184   71 LVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIF 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021353306  81 SLHLAGISSILGAVNFITTVINMRSTGISFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDP 160
Cdd:MTH00184  151 SLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDP 230

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2021353306 161 ILYQHLFWFFSLPEVYILILTGIGMISHMISQESGKKETFGSLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTR 234
Cdd:MTH00184  231 ILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTR 304
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-234 1.34e-116

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 342.31  E-value: 1.34e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021353306   1 MVMPTVIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALTFLLMSSMTENGSGTGWTVYPPLSSTIAHSGASVDMAIF 80
Cdd:MTH00077   69 MVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIF 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021353306  81 SLHLAGISSILGAVNFITTVINMRSTGISFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDP 160
Cdd:MTH00077  149 SLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDP 228

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2021353306 161 ILYQHLFWFFSLPEVYILILTGIGMISHMISQESGKKETFGSLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTR 234
Cdd:MTH00077  229 VLYQHLFWFFGHPEVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTR 302
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-234 7.71e-115

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 337.81  E-value: 7.71e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021353306   1 MVMPTVIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALTFLLMSSMTENGSGTGWTVYPPLSsTIAHSGASVDMAIF 80
Cdd:MTH00079   70 MVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLS-TLGHPGSSVDLAIF 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021353306  81 SLHLAGISSILGAVNFITTVINMRSTGISFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDP 160
Cdd:MTH00079  149 SLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNP 228

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2021353306 161 ILYQHLFWFFSLPEVYILILTGIGMISHMISQESGKKETFGSLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTR 234
Cdd:MTH00079  229 LLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSR 302
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-234 1.77e-107

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 319.65  E-value: 1.77e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021353306   1 MVMPTVIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALTFLLMSSMTENGSGTGWTVYPPLSSTIAHSGASVDMAIF 80
Cdd:MTH00026   70 LVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIF 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021353306  81 SLHLAGISSILGAVNFITTVINMRSTGISFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDP 160
Cdd:MTH00026  150 SLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDP 229

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2021353306 161 ILYQHLFWFFSLPEVYILILTGIGMISHMISQESGKKETFGSLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTR 234
Cdd:MTH00026  230 ILYQHLFWFFGHPEVYILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTR 303
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-234 4.52e-94

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: 283.27  E-value: 4.52e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021353306   1 MVMPTVIGGFGNWLVPlMLGAPDMAFPRMNNMSFWLLPPALTFLLMSSMTENGSGTGWTVYPPLSSTIAHSGASVDMAIF 80
Cdd:cd00919    58 FVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAIL 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021353306  81 SLHLAGISSILGAVNFITTVINMRSTGISFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDP 160
Cdd:cd00919   137 GLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDP 216

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2021353306 161 ILYQHLFWFFSLPEVYILILTGIGMISHMISQESGKKeTFGSLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTR 234
Cdd:cd00919   217 VLYQHLFWFFGHPEVYILILPAFGAISEIIPTFSGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTR 289
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-230 2.82e-92

cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) of cytochrome c oxidases of bacterial origin. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits I-III form the functional core of the enzyme complex. Subunit I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit II and heme a of subunit I to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. In the bacilli an apparent split (paralogism) has created a sister clade (TIGR02882) encoding subunits (QoxA) of the aa3-type quinone oxidase complex which reacts directly with quinones, bypassing the interaction with soluble cytochrome c. This model attempts to exclude these sequences, placing them between the trusted and noise cutoffs. These families, as well as archaeal and eukaryotic cytochrome c subunit I's are included within the superfamily model, pfam00115. [Energy metabolism, Electron transport]


Pssm-ID: 213748  Cd Length: 499  Bit Score: 279.49  E-value: 2.82e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021353306   1 MVMPtVIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALTFLLMSSMTENGSGTGWTVYPPLSSTIAHSGASVDMAIF 80
Cdd:TIGR02891  63 FAIP-ILAGFGNYLLPLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLL 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021353306  81 SLHLAGISSILGAVNFITTVINMRSTGISFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDP 160
Cdd:TIGR02891 142 GLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDP 221

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021353306 161 ILYQHLFWFFSLPEVYILILTGIGMISHMISQESGKKeTFGSLGMIYAMLSIGLLGFIVWAHHMFTVGMD 230
Cdd:TIGR02891 222 LLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMP 290
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-229 1.20e-87

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 268.92  E-value: 1.20e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021353306   1 MVMPtVIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALTFLLMSSMTENGSGTGWTVYPPLSSTIAHSGASVDMAIF 80
Cdd:COG0843    72 FATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLL 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021353306  81 SLHLAGISSILGAVNFITTVINMRSTGISFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDP 160
Cdd:COG0843   151 GLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDP 230

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2021353306 161 ILYQHLFWFFSLPEVYILILTGIGMISHMISQESGKKeTFGSLGMIYAMLSIGLLGFIVWAHHMFTVGM 229
Cdd:COG0843   231 LLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGI 298
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 3-233 6.05e-84

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 258.45  E-value: 6.05e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021353306   3 MPTVIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALTFLLMSSMTenGSGTGWTVYPPLSSTIAHSGASVDMAIFSL 82
Cdd:MTH00048   72 MPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSL 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021353306  83 HLAGISSILGAVNFITTVINMRSTGISFdRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPIL 162
Cdd:MTH00048  150 HLAGVSSLFGSINFICTIYSAFMTNVFS-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVL 228

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2021353306 163 YQHLFWFFSLPEVYILILTGIGMISHMISQESGKKETFGSLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDT 233
Cdd:MTH00048  229 FQHMFWFFGHPEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKT 299
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-229 2.53e-72

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: 228.23  E-value: 2.53e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021353306   1 MVMPTVIGgFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALTFLLMSSMTENGSGTGWTVYPPLSSTIAHSGASVDMAIF 80
Cdd:cd01662    64 FAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWIL 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021353306  81 SLHLAGISSILGAVNFITTVINMRSTGISFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDP 160
Cdd:cd01662   143 GLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNP 222

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2021353306 161 ILYQHLFWFFSLPEVYILILTGIGMISHMISQESGKKeTFGSLGMIYAMLSIGLLGFIVWAHHMFTVGM 229
Cdd:cd01662   223 MLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFSRKP-LFGYRSMVYATVAIGFLSFGVWVHHMFTTGA 290
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-234 5.10e-54

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: 178.92  E-value: 5.10e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021353306   1 MVMPtVIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALTFLLMSSMtenGSGTGWTVYPPLsstiahsgASVDMAIF 80
Cdd:pfam00115  56 FATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYI 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021353306  81 SLHLAGISSILGAVNFITTVINMRSTGISFdRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNFNtsffdpAGGGDP 160
Cdd:pfam00115 124 GLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDP 196

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2021353306 161 ILYQHLFWFFSLPEVYILILTGIGMISHMISQESGKKeTFGSLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTR 234
Cdd:pfam00115 197 LLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQ 269
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 1-228 1.29e-42

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 152.40  E-value: 1.29e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021353306   1 MVMPTVIGgFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALTFLLMSSMTENGSGTGWTVYPPLSSTIAHSGASVDMAIF 80
Cdd:PRK15017  114 VAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIW 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021353306  81 SLHLAGISSILGAVNFITTVINMRSTGISFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDP 160
Cdd:PRK15017  193 SLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNM 272

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2021353306 161 ILYQHLFWFFSLPEVYILILTGIGMISHMISQESgKKETFGSLGMIYAMLSIGLLGFIVWAHHMFTVG 228
Cdd:PRK15017  273 MMYINLIWAWGHPEVYILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFFTMG 339
 
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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