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Conserved domains on  [gi|1807852394|gb|QHY93104|]
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cytochrome oxidase subunit 1, partial (mitochondrion) [Rhodymenia corallina]

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 ...
 1-189 2.03e-104

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: 308.26  E-value: 2.03e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807852394   1 SMLIRMELAQPGNHLlvGNHQLYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCL 80
Cdd:cd01663    25 SLLIRLELSQPGSQL--GNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLL 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807852394  81 LLTSAFVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHVSGASSILGAINFISTIINMRNSGQNMYRMPLFVWSIFVT 160
Cdd:cd01663   103 LLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLIT 182

                         170       180
                  ....*....|....*....|....*....
gi 1807852394 161 AFLLLLAVPVLAGAITMLLTDRNFNTSFF 189
Cdd:cd01663   183 AFLLLLSLPVLAGAITMLLTDRNFNTSFF 211
 
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 ...
 1-189 2.03e-104

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: 308.26  E-value: 2.03e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807852394   1 SMLIRMELAQPGNHLlvGNHQLYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCL 80
Cdd:cd01663    25 SLLIRLELSQPGSQL--GNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLL 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807852394  81 LLTSAFVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHVSGASSILGAINFISTIINMRNSGQNMYRMPLFVWSIFVT 160
Cdd:cd01663   103 LLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLIT 182

                         170       180
                  ....*....|....*....|....*....
gi 1807852394 161 AFLLLLAVPVLAGAITMLLTDRNFNTSFF 189
Cdd:cd01663   183 AFLLLLSLPVLAGAITMLLTDRNFNTSFF 211
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-189 2.97e-102

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 303.71  E-value: 2.97e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807852394   1 SMLIRMELAQPGNhlLVGNHQLYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCL 80
Cdd:MTH00153   32 SLLIRAELGQPGS--LIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTL 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807852394  81 LLTSAFVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHVSGASSILGAINFISTIINMRNSGQNMYRMPLFVWSIFVT 160
Cdd:MTH00153  110 LLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLIT 189

                         170       180
                  ....*....|....*....|....*....
gi 1807852394 161 AFLLLLAVPVLAGAITMLLTDRNFNTSFF 189
Cdd:MTH00153  190 AILLLLSLPVLAGAITMLLTDRNLNTSFF 218
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-189 4.69e-59

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 192.65  E-value: 4.69e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807852394   1 SMLIRMELAQPGNHLLVGNHqlYNVLITAHAFLMIFFMVMPvMIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCL 80
Cdd:COG0843    37 ALLMRLQLAGPGLGLLSPET--YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLL 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807852394  81 LLTSAFVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHVSGASSILGAINFISTIINMRNSGQNMYRMPLFVWSIFVT 160
Cdd:COG0843   114 LLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVT 193

                         170       180
                  ....*....|....*....|....*....
gi 1807852394 161 AFLLLLAVPVLAGAITMLLTDRNFNTSFF 189
Cdd:COG0843   194 SILILLAFPVLAAALLLLLLDRSLGTHFF 222
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-186 4.33e-35

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: 127.30  E-value: 4.33e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807852394   1 SMLIRMELAQPGNHLLvgNHQLYNVLITAHAFLMIFFMVMPvMIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCL 80
Cdd:pfam00115  21 GLLIRLQLAFPGLNFL--SPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807852394  81 LLTSAfveVGVGTGWTVYPPLssiqshsgAAVDLAIFSLHVSGASSILGAINFISTIINMRNSGQNMyRMPLFVWSIFVT 160
Cdd:pfam00115  98 LLASF---GGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILAT 165

                         170       180
                  ....*....|....*....|....*.
gi 1807852394 161 AFLLLLAVPVLAGAITMLLTDRNFNT 186
Cdd:pfam00115 166 AILILLAFPVLAAALLLLLLDRSLGA 191
 
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 ...
 1-189 2.03e-104

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: 308.26  E-value: 2.03e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807852394   1 SMLIRMELAQPGNHLlvGNHQLYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCL 80
Cdd:cd01663    25 SLLIRLELSQPGSQL--GNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLL 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807852394  81 LLTSAFVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHVSGASSILGAINFISTIINMRNSGQNMYRMPLFVWSIFVT 160
Cdd:cd01663   103 LLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLIT 182

                         170       180
                  ....*....|....*....|....*....
gi 1807852394 161 AFLLLLAVPVLAGAITMLLTDRNFNTSFF 189
Cdd:cd01663   183 AFLLLLSLPVLAGAITMLLTDRNFNTSFF 211
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-189 2.97e-102

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 303.71  E-value: 2.97e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807852394   1 SMLIRMELAQPGNhlLVGNHQLYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCL 80
Cdd:MTH00153   32 SLLIRAELGQPGS--LIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTL 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807852394  81 LLTSAFVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHVSGASSILGAINFISTIINMRNSGQNMYRMPLFVWSIFVT 160
Cdd:MTH00153  110 LLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLIT 189

                         170       180
                  ....*....|....*....|....*....
gi 1807852394 161 AFLLLLAVPVLAGAITMLLTDRNFNTSFF 189
Cdd:MTH00153  190 AILLLLSLPVLAGAITMLLTDRNLNTSFF 218
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-189 1.44e-91

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 276.17  E-value: 1.44e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807852394   1 SMLIRMELAQPGNhlLVGNHQLYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCL 80
Cdd:MTH00167   34 SLLIRAELSQPGS--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLL 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807852394  81 LLTSAFVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHVSGASSILGAINFISTIINMRNSGQNMYRMPLFVWSIFVT 160
Cdd:MTH00167  112 LLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVT 191

                         170       180
                  ....*....|....*....|....*....
gi 1807852394 161 AFLLLLAVPVLAGAITMLLTDRNFNTSFF 189
Cdd:MTH00167  192 TILLLLSLPVLAAAITMLLTDRNLNTTFF 220
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-189 8.68e-90

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 271.85  E-value: 8.68e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807852394   1 SMLIRMELAQPGnhLLVGNHQLYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCL 80
Cdd:MTH00223   31 SLLIRAELGQPG--ALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLYL 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807852394  81 LLTSAFVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHVSGASSILGAINFISTIINMRNSGQNMYRMPLFVWSIFVT 160
Cdd:MTH00223  109 LLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVT 188

                         170       180
                  ....*....|....*....|....*....
gi 1807852394 161 AFLLLLAVPVLAGAITMLLTDRNFNTSFF 189
Cdd:MTH00223  189 AFLLLLSLPVLAGAITMLLTDRNFNTSFF 217
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-189 1.09e-88

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 268.88  E-value: 1.09e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807852394   1 SMLIRMELAQPGNhlLVGNHQLYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCL 80
Cdd:MTH00116   34 SLLIRAELGQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLL 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807852394  81 LLTSAFVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHVSGASSILGAINFISTIINMRNSGQNMYRMPLFVWSIFVT 160
Cdd:MTH00116  112 LLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLIT 191

                         170       180
                  ....*....|....*....|....*....
gi 1807852394 161 AFLLLLAVPVLAGAITMLLTDRNFNTSFF 189
Cdd:MTH00116  192 AVLLLLSLPVLAAGITMLLTDRNLNTTFF 220
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-189 6.71e-87

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 264.28  E-value: 6.71e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807852394   1 SMLIRMELAQPGNhlLVGNHQLYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCL 80
Cdd:MTH00142   32 SLLIRAELGQPGS--LLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALLL 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807852394  81 LLTSAFVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHVSGASSILGAINFISTIINMRNSGQNMYRMPLFVWSIFVT 160
Cdd:MTH00142  110 LLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKIT 189

                         170       180
                  ....*....|....*....|....*....
gi 1807852394 161 AFLLLLAVPVLAGAITMLLTDRNFNTSFF 189
Cdd:MTH00142  190 AILLLLSLPVLAGAITMLLTDRNFNTSFF 218
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-189 5.42e-83

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 254.75  E-value: 5.42e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807852394   1 SMLIRMELAQPGNhlLVGNHQLYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCL 80
Cdd:MTH00182   36 SMLIRLELSAPGA--MLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALIL 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807852394  81 LLTSAFVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHVSGASSILGAINFISTIINMRNSGQNMYRMPLFVWSIFVT 160
Cdd:MTH00182  114 LLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILIT 193

                         170       180
                  ....*....|....*....|....*....
gi 1807852394 161 AFLLLLAVPVLAGAITMLLTDRNFNTSFF 189
Cdd:MTH00182  194 AFLLLLSLPVLAGAITMLLTDRNFNTTFF 222
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-189 5.71e-81

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 249.36  E-value: 5.71e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807852394   1 SMLIRMELAQPGNhlLVGNHQLYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCL 80
Cdd:MTH00184   36 SMLIRLELSAPGS--MLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPALTL 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807852394  81 LLTSAFVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHVSGASSILGAINFISTIINMRNSGQNMYRMPLFVWSIFVT 160
Cdd:MTH00184  114 LLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVT 193

                         170       180
                  ....*....|....*....|....*....
gi 1807852394 161 AFLLLLAVPVLAGAITMLLTDRNFNTSFF 189
Cdd:MTH00184  194 TFLLLLSLPVLAGAITMLLTDRNFNTTFF 222
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-189 2.38e-78

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 242.43  E-value: 2.38e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807852394   1 SMLIRMELAQPGNhlLVGNHQLYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCL 80
Cdd:MTH00037   34 SVIIRTELAQPGS--LLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLL 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807852394  81 LLTSAFVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHVSGASSILGAINFISTIINMRNSGQNMYRMPLFVWSIFVT 160
Cdd:MTH00037  112 LLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFIT 191

                         170       180
                  ....*....|....*....|....*....
gi 1807852394 161 AFLLLLAVPVLAGAITMLLTDRNFNTSFF 189
Cdd:MTH00037  192 AFLLLLSLPVLAGAITMLLTDRNINTTFF 220
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-189 5.56e-78

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 241.34  E-value: 5.56e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807852394   1 SMLIRMELAQPGNHLlvGNHQLYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCL 80
Cdd:MTH00007   31 SLLIRIELGQPGAFL--GSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPALIL 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807852394  81 LLTSAFVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHVSGASSILGAINFISTIINMRNSGQNMYRMPLFVWSIFVT 160
Cdd:MTH00007  109 LVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVIT 188

                         170       180
                  ....*....|....*....|....*....
gi 1807852394 161 AFLLLLAVPVLAGAITMLLTDRNFNTSFF 189
Cdd:MTH00007  189 VVLLLLSLPVLAGAITMLLTDRNLNTSFF 217
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-189 4.18e-77

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 239.01  E-value: 4.18e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807852394   1 SMLIRMELAQPGNhlLVGNHQLYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCL 80
Cdd:MTH00103   34 SLLIRAELGQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLL 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807852394  81 LLTSAFVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHVSGASSILGAINFISTIINMRNSGQNMYRMPLFVWSIFVT 160
Cdd:MTH00103  112 LLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLIT 191

                         170       180
                  ....*....|....*....|....*....
gi 1807852394 161 AFLLLLAVPVLAGAITMLLTDRNFNTSFF 189
Cdd:MTH00103  192 AVLLLLSLPVLAAGITMLLTDRNLNTTFF 220
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-189 2.74e-76

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 237.13  E-value: 2.74e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807852394   1 SMLIRMELAQPGNhlLVGNHQLYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCL 80
Cdd:MTH00183   34 SLLIRAELSQPGA--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLL 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807852394  81 LLTSAFVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHVSGASSILGAINFISTIINMRNSGQNMYRMPLFVWSIFVT 160
Cdd:MTH00183  112 LLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLIT 191

                         170       180
                  ....*....|....*....|....*....
gi 1807852394 161 AFLLLLAVPVLAGAITMLLTDRNFNTSFF 189
Cdd:MTH00183  192 AVLLLLSLPVLAAGITMLLTDRNLNTTFF 220
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-189 1.10e-75

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 235.61  E-value: 1.10e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807852394   1 SMLIRMELAQPGNhlLVGNHQLYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCL 80
Cdd:MTH00077   34 SLLIRAELSQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLL 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807852394  81 LLTSAFVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHVSGASSILGAINFISTIINMRNSGQNMYRMPLFVWSIFVT 160
Cdd:MTH00077  112 LLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLIT 191

                         170       180
                  ....*....|....*....|....*....
gi 1807852394 161 AFLLLLAVPVLAGAITMLLTDRNFNTSFF 189
Cdd:MTH00077  192 AVLLLLSLPVLAAGITMLLTDRNLNTTFF 220
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-189 5.73e-74

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 230.72  E-value: 5.73e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807852394   1 SMLIRMELAQPGnhLLVGNHQLYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCL 80
Cdd:MTH00079   35 SLIIRLELSKPG--LLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFL 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807852394  81 LLTSAFVEVGVGTGWTVYPPLSSiQSHSGAAVDLAIFSLHVSGASSILGAINFISTIINMRNSGQNMYRMPLFVWSIFVT 160
Cdd:MTH00079  113 ILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVT 191

                         170       180
                  ....*....|....*....|....*....
gi 1807852394 161 AFLLLLAVPVLAGAITMLLTDRNFNTSFF 189
Cdd:MTH00079  192 VFLLVLSLPVLAGAITMLLTDRNLNTSFF 220
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-189 2.55e-71

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 224.89  E-value: 2.55e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807852394   1 SMLIRMELAQPGNhlLVGNHQLYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCL 80
Cdd:MTH00026   35 SMLIRLELSSPGS--MLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPALFL 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807852394  81 LLTSAFVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHVSGASSILGAINFISTIINMRNSGQNMYRMPLFVWSIFVT 160
Cdd:MTH00026  113 LLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFIT 192

                         170       180
                  ....*....|....*....|....*....
gi 1807852394 161 AFLLLLAVPVLAGAITMLLTDRNFNTSFF 189
Cdd:MTH00026  193 AILLLLSLPVLAGAITMLLTDRNFNTTFF 221
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-189 8.75e-64

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: 203.53  E-value: 8.75e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807852394   1 SMLIRMELAQPGNHLLvgNHQLYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPiMIGSPDMAFPRLNNISFWLLPPSLCL 80
Cdd:cd00919    23 ALLIRLELATPGSLFL--DPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWLFPPGLLL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807852394  81 LLTSAFVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHVSGASSILGAINFISTIINMRNSGQNMYRMPLFVWSIFVT 160
Cdd:cd00919   100 LLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVT 179

                         170       180
                  ....*....|....*....|....*....
gi 1807852394 161 AFLLLLAVPVLAGAITMLLTDRNFNTSFF 189
Cdd:cd00919   180 AILLLLALPVLAAALVMLLLDRNFGTSFF 208
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-189 4.69e-59

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 192.65  E-value: 4.69e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807852394   1 SMLIRMELAQPGNHLLVGNHqlYNVLITAHAFLMIFFMVMPvMIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCL 80
Cdd:COG0843    37 ALLMRLQLAGPGLGLLSPET--YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLL 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807852394  81 LLTSAFVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHVSGASSILGAINFISTIINMRNSGQNMYRMPLFVWSIFVT 160
Cdd:COG0843   114 LLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVT 193

                         170       180
                  ....*....|....*....|....*....
gi 1807852394 161 AFLLLLAVPVLAGAITMLLTDRNFNTSFF 189
Cdd:COG0843   194 SILILLAFPVLAAALLLLLLDRSLGTHFF 222
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 2-189 3.16e-49

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: 166.22  E-value: 3.16e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807852394   2 MLIRMELAQPGNHLLVGNHqlYNVLITAHAFLMIFFMVMPVMIGgFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCLL 81
Cdd:cd01662    30 LLMRTQLALPGNDFLSPEH--YNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGGLLL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807852394  82 LTSAFVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHVSGASSILGAINFISTIINMRNSGQNMYRMPLFVWSIFVTA 161
Cdd:cd01662   107 NASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTS 186

                         170       180
                  ....*....|....*....|....*...
gi 1807852394 162 FLLLLAVPVLAGAITMLLTDRNFNTSFF 189
Cdd:cd01662   187 ILILFAFPVLTAALALLELDRYFGTHFF 214
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-189 3.67e-44

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 152.91  E-value: 3.67e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807852394   1 SMLIRMELAQPGNHLLvgNHQLYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCL 80
Cdd:MTH00048   35 SLLIRLNFLDPYYNVI--SLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVF 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807852394  81 LLTSAFveVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHVSGASSILGAINFISTIINMRNSGQNmYRMPLFVWSIFVT 160
Cdd:MTH00048  113 LLLSMC--LGAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVF-SRTSIILWSYLFT 189

                         170       180
                  ....*....|....*....|....*....
gi 1807852394 161 AFLLLLAVPVLAGAITMLLTDRNFNTSFF 189
Cdd:MTH00048  190 SILLLLSLPVLAAAITMLLFDRNFGSAFF 218
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-186 4.33e-35

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: 127.30  E-value: 4.33e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807852394   1 SMLIRMELAQPGNHLLvgNHQLYNVLITAHAFLMIFFMVMPvMIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCL 80
Cdd:pfam00115  21 GLLIRLQLAFPGLNFL--SPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807852394  81 LLTSAfveVGVGTGWTVYPPLssiqshsgAAVDLAIFSLHVSGASSILGAINFISTIINMRNSGQNMyRMPLFVWSIFVT 160
Cdd:pfam00115  98 LLASF---GGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILAT 165

                         170       180
                  ....*....|....*....|....*.
gi 1807852394 161 AFLLLLAVPVLAGAITMLLTDRNFNT 186
Cdd:pfam00115 166 AILILLAFPVLAAALLLLLLDRSLGA 191
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 23-189 2.67e-31

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 118.88  E-value: 2.67e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807852394  23 YNVLITAHAFLMIFFMVMPVMIGgFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCLLLTSAFVEVGVGTGWTVYPPLS 102
Cdd:PRK15017   99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807852394 103 SIQSHSGAAVDLAIFSLHVSGASSILGAINFISTIINMRNSGQNMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDR 182
Cdd:PRK15017  178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257


                  ....*..
gi 1807852394 183 NFNTSFF 189
Cdd:PRK15017  258 YLGTHFF 264
 
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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