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Conserved domains on  [gi|1424745881|gb|AXC02369|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Stericta flavopuncta]

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 ...
 4-225 1.14e-155

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: 441.23  E-value: 1.14e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424745881   4 YFLDLIW--MVGTSLSLLIRAELGNPGSLIGDDQIYNTIVTGHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMN 81
Cdd:MTH00153   17 YFIFGAWsgMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMN 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424745881  82 NMSFWLLPPSLTLLISSSIVENGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMKLNGLTF 161
Cdd:MTH00153   97 NMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTL 176

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1424745881 162 DQMPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHLE 225
Cdd:MTH00153  177 DRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 240
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 4-225 1.14e-155

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 441.23  E-value: 1.14e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424745881   4 YFLDLIW--MVGTSLSLLIRAELGNPGSLIGDDQIYNTIVTGHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMN 81
Cdd:MTH00153   17 YFIFGAWsgMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMN 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424745881  82 NMSFWLLPPSLTLLISSSIVENGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMKLNGLTF 161
Cdd:MTH00153   97 NMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTL 176

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1424745881 162 DQMPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHLE 225
Cdd:MTH00153  177 DRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 240
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 2-225 5.57e-138

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: 395.70  E-value: 5.57e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424745881   2 IFYFLDLIW--MVGTSLSLLIRAELGNPGSLIGDDQIYNTIVTGHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 79
Cdd:cd01663     8 TLYLIFGLWsgLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPR 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424745881  80 MNNMSFWLLPPSLTLLISSSIVENGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMKLNGL 159
Cdd:cd01663    88 LNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGM 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1424745881 160 TFDQMPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHLE 225
Cdd:cd01663   168 TLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPE 233
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
11-223 3.94e-78

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 243.88  E-value: 3.94e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424745881  11 MVGTSLSLLIRAELGNPGSLIGDDQIYNTIVTGHAFIMIFFMVMPiMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPP 90
Cdd:COG0843    31 LIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLF 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424745881  91 SLTLLISSSIVENGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMKLNGLTFDQMPLFVWA 170
Cdd:COG0843   110 GGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWA 189

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1424745881 171 VGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 223
Cdd:COG0843   190 ALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGH 242
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 11-225 1.28e-48

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: 164.67  E-value: 1.28e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424745881  11 MVGTSLSLLIRAELGNPGSLIGDDQIYNTIVTGHAFIMIFFMVMPiMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPP 90
Cdd:pfam00115  15 LVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424745881  91 SLTLLISSSiveNGAGTGWTVYPPLssniahsgSSVDLAIFSLHLAGISSILGAINFITTIINMKLNGLTFdQMPLFVWA 170
Cdd:pfam00115  94 GAVLLLASF---GGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWA 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1424745881 171 VGITALLLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLFWFFGHLE 225
Cdd:pfam00115 162 ILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPE 210
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 8-227 8.40e-39

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


Pssm-ID: 131928  Cd Length: 643  Bit Score: 141.53  E-value: 8.40e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424745881   8 LIWMVGTSLSLLIRAELGNPGSLIGDDQIYNTIVTGHAFIMIFFMVMPIMIGgFGNWLVPLMLGAPDMAFPRMNNMSFWL 87
Cdd:TIGR02882  63 LMLFRGGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWL 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424745881  88 LPPSLTLLISSSIVENGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMKLNGLTFDQMPLF 167
Cdd:TIGR02882 142 FFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMF 221

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424745881 168 VWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHLESF 227
Cdd:TIGR02882 222 TWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVY 281
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 4-225 1.14e-155

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 441.23  E-value: 1.14e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424745881   4 YFLDLIW--MVGTSLSLLIRAELGNPGSLIGDDQIYNTIVTGHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMN 81
Cdd:MTH00153   17 YFIFGAWsgMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMN 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424745881  82 NMSFWLLPPSLTLLISSSIVENGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMKLNGLTF 161
Cdd:MTH00153   97 NMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTL 176

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1424745881 162 DQMPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHLE 225
Cdd:MTH00153  177 DRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 240
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 2-225 5.57e-138

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: 395.70  E-value: 5.57e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424745881   2 IFYFLDLIW--MVGTSLSLLIRAELGNPGSLIGDDQIYNTIVTGHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 79
Cdd:cd01663     8 TLYLIFGLWsgLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPR 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424745881  80 MNNMSFWLLPPSLTLLISSSIVENGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMKLNGL 159
Cdd:cd01663    88 LNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGM 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1424745881 160 TFDQMPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHLE 225
Cdd:cd01663   168 TLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPE 233
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 4-225 3.98e-133

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 384.03  E-value: 3.98e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424745881   4 YFLDLIW--MVGTSLSLLIRAELGNPGSLIGDDQIYNTIVTGHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMN 81
Cdd:MTH00167   19 YFIFGAWagMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMN 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424745881  82 NMSFWLLPPSLTLLISSSIVENGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMKLNGLTF 161
Cdd:MTH00167   99 NMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQ 178

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1424745881 162 DQMPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHLE 225
Cdd:MTH00167  179 YQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPE 242
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 4-225 4.99e-130

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 376.37  E-value: 4.99e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424745881   4 YFLDLIW--MVGTSLSLLIRAELGNPGSLIGDDQIYNTIVTGHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMN 81
Cdd:MTH00142   17 YFLFGAWagMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMN 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424745881  82 NMSFWLLPPSLTLLISSSIVENGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMKLNGLTF 161
Cdd:MTH00142   97 NMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKF 176

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1424745881 162 DQMPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHLE 225
Cdd:MTH00142  177 ERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPE 240
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 4-225 1.03e-129

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 375.58  E-value: 1.03e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424745881   4 YFLDLIW--MVGTSLSLLIRAELGNPGSLIGDDQIYNTIVTGHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMN 81
Cdd:MTH00116   19 YLIFGAWagMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMN 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424745881  82 NMSFWLLPPSLTLLISSSIVENGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMKLNGLTF 161
Cdd:MTH00116   99 NMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQ 178

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1424745881 162 DQMPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHLE 225
Cdd:MTH00116  179 YQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPE 242
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 3-225 9.81e-128

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 370.46  E-value: 9.81e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424745881   3 FYFLDLIW--MVGTSLSLLIRAELGNPGSLIGDDQIYNTIVTGHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRM 80
Cdd:MTH00223   15 LYLIFGMWsgLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRL 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424745881  81 NNMSFWLLPPSLTLLISSSIVENGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMKLNGLT 160
Cdd:MTH00223   95 NNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQ 174

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1424745881 161 FDQMPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHLE 225
Cdd:MTH00223  175 LERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPE 239
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 3-227 1.52e-117

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 344.58  E-value: 1.52e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424745881   3 FYFLDLIW--MVGTSLSLLIRAELGNPGSLIGDDQIYNTIVTGHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRM 80
Cdd:MTH00007   15 LYFILGVWggLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRL 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424745881  81 NNMSFWLLPPSLTLLISSSIVENGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMKLNGLT 160
Cdd:MTH00007   95 NNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLR 174

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1424745881 161 FDQMPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHLESF 227
Cdd:MTH00007  175 LERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 241
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 11-227 5.81e-116

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 340.36  E-value: 5.81e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424745881  11 MVGTSLSLLIRAELGNPGSLIGDDQIYNTIVTGHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPP 90
Cdd:MTH00183   28 MVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPP 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424745881  91 SLTLLISSSIVENGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMKLNGLTFDQMPLFVWA 170
Cdd:MTH00183  108 SFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWA 187

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1424745881 171 VGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHLESF 227
Cdd:MTH00183  188 VLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVY 244
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 11-227 1.41e-115

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 339.55  E-value: 1.41e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424745881  11 MVGTSLSLLIRAELGNPGSLIGDDQIYNTIVTGHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPP 90
Cdd:MTH00103   28 MVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPP 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424745881  91 SLTLLISSSIVENGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMKLNGLTFDQMPLFVWA 170
Cdd:MTH00103  108 SFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWS 187

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1424745881 171 VGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHLESF 227
Cdd:MTH00103  188 VLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVY 244
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 11-227 1.22e-114

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 337.30  E-value: 1.22e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424745881  11 MVGTSLSLLIRAELGNPGSLIGDDQIYNTIVTGHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPP 90
Cdd:MTH00077   28 MVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPP 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424745881  91 SLTLLISSSIVENGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMKLNGLTFDQMPLFVWA 170
Cdd:MTH00077  108 SFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWS 187

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1424745881 171 VGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHLESF 227
Cdd:MTH00077  188 VLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVY 244
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 4-227 5.78e-112

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 330.25  E-value: 5.78e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424745881   4 YFLDLIW--MVGTSLSLLIRAELGNPGSLIGDDQIYNTIVTGHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMN 81
Cdd:MTH00037   19 YLIFGAWagMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMN 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424745881  82 NMSFWLLPPSLTLLISSSIVENGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMKLNGLTF 161
Cdd:MTH00037   99 NMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTF 178

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1424745881 162 DQMPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHLESF 227
Cdd:MTH00037  179 DRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVY 244
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 11-227 7.59e-107

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 317.15  E-value: 7.59e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424745881  11 MVGTSLSLLIRAELGNPGSLIGDDQIYNTIVTGHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPP 90
Cdd:MTH00184   30 MIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPP 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424745881  91 SLTLLISSSIVENGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMKLNGLTFDQMPLFVWA 170
Cdd:MTH00184  110 ALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWS 189

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1424745881 171 VGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHLESF 227
Cdd:MTH00184  190 ILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVY 246
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 11-227 1.52e-106

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 316.76  E-value: 1.52e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424745881  11 MVGTSLSLLIRAELGNPGSLIGDDQIYNTIVTGHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPP 90
Cdd:MTH00182   30 MIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPP 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424745881  91 SLTLLISSSIVENGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMKLNGLTFDQMPLFVWA 170
Cdd:MTH00182  110 ALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWS 189

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1424745881 171 VGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHLESF 227
Cdd:MTH00182  190 ILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVY 246
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 3-225 1.79e-101

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 303.14  E-value: 1.79e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424745881   3 FYFLDLIW--MVGTSLSLLIRAELGNPGSLIGDDQIYNTIVTGHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRM 80
Cdd:MTH00079   19 LYFLFGLWsgMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424745881  81 NNMSFWLLPPSLTLLISSSIVENGAGTGWTVYPPLSSnIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMKLNGLT 160
Cdd:MTH00079   99 NNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSIS 177

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1424745881 161 FDQMPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHLE 225
Cdd:MTH00079  178 LEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPE 242
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 12-227 4.61e-96

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 290.38  E-value: 4.61e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424745881  12 VGTSLSLLIRAELGNPGSLIGDDQIYNTIVTGHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPS 91
Cdd:MTH00026   30 IGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPA 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424745881  92 LTLLISSSIVENGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMKLNGLTFDQMPLFVWAV 171
Cdd:MTH00026  110 LFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSV 189

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1424745881 172 GITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHLESF 227
Cdd:MTH00026  190 FITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVY 245
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 2-223 1.40e-87

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: 266.32  E-value: 1.40e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424745881   2 IFYFLDLIWM--VGTSLSLLIRAELGNPGSLIGDDQIYNTIVTGHAFIMIFFMVMPIMIGGFGNWLVPlMLGAPDMAFPR 79
Cdd:cd00919     6 LLYLIFAFVAllLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424745881  80 MNNMSFWLLPPSLTLLISSSIVENGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMKLNGL 159
Cdd:cd00919    85 LNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGM 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1424745881 160 TFDQMPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 223
Cdd:cd00919   165 TLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGH 228
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
11-223 3.94e-78

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 243.88  E-value: 3.94e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424745881  11 MVGTSLSLLIRAELGNPGSLIGDDQIYNTIVTGHAFIMIFFMVMPiMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPP 90
Cdd:COG0843    31 LIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLF 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424745881  91 SLTLLISSSIVENGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMKLNGLTFDQMPLFVWA 170
Cdd:COG0843   110 GGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWA 189

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1424745881 171 VGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 223
Cdd:COG0843   190 ALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGH 242
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 2-225 2.30e-69

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 220.70  E-value: 2.30e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424745881   2 IFYFLDLIW--MVGTSLSLLIRAELGNPGSLIGDDQIYNTIVTGHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 79
Cdd:MTH00048   18 VIYTLLGVWsgFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPR 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424745881  80 MNNMSFWLLPPSLTLLISSSIVenGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMKLNGL 159
Cdd:MTH00048   98 LNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNV 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1424745881 160 TFdQMPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHLE 225
Cdd:MTH00048  176 FS-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPE 240
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 13-225 1.28e-61

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: 200.11  E-value: 1.28e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424745881  13 GTSLSLLIRAELGNPGSLIGDDQIYNTIVTGHAFIMIFFMVMPIMIGgFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSL 92
Cdd:cd01662    25 GGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGG 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424745881  93 TLLISSSIVENGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMKLNGLTFDQMPLFVWAVG 172
Cdd:cd01662   104 LLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTL 183

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1424745881 173 ITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHLE 225
Cdd:cd01662   184 VTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPE 236
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 11-225 1.28e-48

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: 164.67  E-value: 1.28e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424745881  11 MVGTSLSLLIRAELGNPGSLIGDDQIYNTIVTGHAFIMIFFMVMPiMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPP 90
Cdd:pfam00115  15 LVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424745881  91 SLTLLISSSiveNGAGTGWTVYPPLssniahsgSSVDLAIFSLHLAGISSILGAINFITTIINMKLNGLTFdQMPLFVWA 170
Cdd:pfam00115  94 GAVLLLASF---GGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWA 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1424745881 171 VGITALLLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLFWFFGHLE 225
Cdd:pfam00115 162 ILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPE 210
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 8-227 8.40e-39

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


Pssm-ID: 131928  Cd Length: 643  Bit Score: 141.53  E-value: 8.40e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424745881   8 LIWMVGTSLSLLIRAELGNPGSLIGDDQIYNTIVTGHAFIMIFFMVMPIMIGgFGNWLVPLMLGAPDMAFPRMNNMSFWL 87
Cdd:TIGR02882  63 LMLFRGGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWL 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424745881  88 LPPSLTLLISSSIVENGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMKLNGLTFDQMPLF 167
Cdd:TIGR02882 142 FFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMF 221

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424745881 168 VWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHLESF 227
Cdd:TIGR02882 222 TWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVY 281
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 37-227 3.47e-36

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 134.29  E-value: 3.47e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424745881  37 YNTIVTGHAFIMIFFMVMPIMIGgFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLISSSIVENGAGTGWTVYPPLS 116
Cdd:PRK15017   99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424745881 117 SNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMKLNGLTFDQMPLFVWAVGITALLLLLSLPVLAGAITMLLTDR 196
Cdd:PRK15017  178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1424745881 197 NLNTSFFDPAGGGDPILYQHLFWFFGHLESF 227
Cdd:PRK15017  258 YLGTHFFTNDMGGNMMMYINLIWAWGHPEVY 288
 
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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