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Conserved domains on  [gi|459219180|gb|AGG41264|]
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cytochrome c oxidase subunit I, partial (mitochondrion) [Lauroia trinidadensis]

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 ...
 1-229 1.97e-146

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: 417.27  E-value: 1.97e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180   1 GGFGNWMLPLLLGAPDMSFPRLNNLSFWLLPTAMVLLMGSALVDNGCGTSWVVYPPLATSG-HPGSSVDLAIFSLHCAGI 79
Cdd:cd01663   67 GGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILaHSGPSVDLAIFSLHLAGI 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180  80 SSILGGINFMTTTKNMRSSSISLEHMSLFVWTVFVTVFLLILSLPVLAGAITMLLTDRNLNTSFFDPSSGGNPLIYQHLF 159
Cdd:cd01663  147 SSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 226

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180 160 WFFGHPEVYILILPAFGIISHSSLYLTGKKEVFGSLGMVYAILSIALIGCVVWAHHMYTVGMDLDTRAYF 229
Cdd:cd01663  227 WFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYF 296
 
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 ...
 1-229 1.97e-146

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: 417.27  E-value: 1.97e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180   1 GGFGNWMLPLLLGAPDMSFPRLNNLSFWLLPTAMVLLMGSALVDNGCGTSWVVYPPLATSG-HPGSSVDLAIFSLHCAGI 79
Cdd:cd01663   67 GGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILaHSGPSVDLAIFSLHLAGI 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180  80 SSILGGINFMTTTKNMRSSSISLEHMSLFVWTVFVTVFLLILSLPVLAGAITMLLTDRNLNTSFFDPSSGGNPLIYQHLF 159
Cdd:cd01663  147 SSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 226

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180 160 WFFGHPEVYILILPAFGIISHSSLYLTGKKEVFGSLGMVYAILSIALIGCVVWAHHMYTVGMDLDTRAYF 229
Cdd:cd01663  227 WFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYF 296
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-229 5.61e-145

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 414.08  E-value: 5.61e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180   1 GGFGNWMLPLLLGAPDMSFPRLNNLSFWLLPTAMVLLMGSALVDNGCGTSWVVYPPLATSGHPGSSVDLAIFSLHCAGIS 80
Cdd:MTH00079  77 GGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLSTLGHPGSSVDLAIFSLHCAGIS 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180  81 SILGGINFMTTTKNMRSSSISLEHMSLFVWTVFVTVFLLILSLPVLAGAITMLLTDRNLNTSFFDPSSGGNPLIYQHLFW 160
Cdd:MTH00079 157 SILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFW 236

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 459219180 161 FFGHPEVYILILPAFGIISHSSLYLTGKKEVFGSLGMVYAILSIALIGCVVWAHHMYTVGMDLDTRAYF 229
Cdd:MTH00079 237 FFGHPEVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYF 305
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-229 2.16e-91

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


Pssm-ID: 213748  Cd Length: 499  Bit Score: 277.18  E-value: 2.16e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180    1 GGFGNWMLPLLLGAPDMSFPRLNNLSFWLLPTAMVLLMGSALVDNGCGTSWVVYPPLA-TSGHPGSSVDLAIFSLHCAGI 79
Cdd:TIGR02891  69 AGFGNYLLPLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSsTSGSPGVGVDLWLLGLHLLGI 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180   80 SSILGGINFMTTTKNMRSSSISLEHMSLFVWTVFVTVFLLILSLPVLAGAITMLLTDRNLNTSFFDPSSGGNPLIYQHLF 159
Cdd:TIGR02891 149 SSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLF 228

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180  160 WFFGHPEVYILILPAFGIISHsSLYLTGKKEVFGSLGMVYAILSIALIGCVVWAHHMYTVGMDLDTRAYF 229
Cdd:TIGR02891 229 WFFGHPEVYIIFLPAFGIISE-ILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFF 297
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-229 1.56e-86

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 265.84  E-value: 1.56e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180   1 GGFGNWMLPLLLGAPDMSFPRLNNLSFWLLPTAMVLLMGSALVDNGCGTSWVVYPPLATS-GHPGSSVDLAIFSLHCAGI 79
Cdd:COG0843   78 AGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLeASPGVGVDLWLLGLALFGV 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180  80 SSILGGINFMTTTKNMRSSSISLEHMSLFVWTVFVTVFLLILSLPVLAGAITMLLTDRNLNTSFFDPSSGGNPLIYQHLF 159
Cdd:COG0843  158 GSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLF 237

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180 160 WFFGHPEVYILILPAFGIISHsSLYLTGKKEVFGSLGMVYAILSIALIGCVVWAHHMYTVGMDLDTRAYF 229
Cdd:COG0843  238 WFFGHPEVYILILPAFGIVSE-IIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFF 306
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-229 1.92e-58

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: 190.48  E-value: 1.92e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180    1 GGFGNWMLPLLLGAPDMSFPRLNNLSFWLLPTAMVLLMGSAlvdNGCGTSWVVYPPLAtsghpgsSVDLAIFSLHCAGIS 80
Cdd:pfam00115  62 FGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPLV-------GVDLWYIGLLLAGVS 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180   81 SILGGINFMTTTKNMRSSSISLeHMSLFVWTVFVTVFLLILSLPVLAGAITMLLTDRNLNTSffdpssGGNPLIYQHLFW 160
Cdd:pfam00115 132 SLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGAG------GGDPLLDQHLFW 204

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 459219180  161 FFGHPEVYILILPAFGIISHSSLYLTGKKeVFGSLGMVYAILSIALIGCVVWAHHMYTVGMDLDTRAYF 229
Cdd:pfam00115 205 WFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALF 272
 
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 ...
 1-229 1.97e-146

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: 417.27  E-value: 1.97e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180   1 GGFGNWMLPLLLGAPDMSFPRLNNLSFWLLPTAMVLLMGSALVDNGCGTSWVVYPPLATSG-HPGSSVDLAIFSLHCAGI 79
Cdd:cd01663   67 GGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILaHSGPSVDLAIFSLHLAGI 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180  80 SSILGGINFMTTTKNMRSSSISLEHMSLFVWTVFVTVFLLILSLPVLAGAITMLLTDRNLNTSFFDPSSGGNPLIYQHLF 159
Cdd:cd01663  147 SSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 226

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180 160 WFFGHPEVYILILPAFGIISHSSLYLTGKKEVFGSLGMVYAILSIALIGCVVWAHHMYTVGMDLDTRAYF 229
Cdd:cd01663  227 WFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYF 296
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-229 5.61e-145

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 414.08  E-value: 5.61e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180   1 GGFGNWMLPLLLGAPDMSFPRLNNLSFWLLPTAMVLLMGSALVDNGCGTSWVVYPPLATSGHPGSSVDLAIFSLHCAGIS 80
Cdd:MTH00079  77 GGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLSTLGHPGSSVDLAIFSLHCAGIS 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180  81 SILGGINFMTTTKNMRSSSISLEHMSLFVWTVFVTVFLLILSLPVLAGAITMLLTDRNLNTSFFDPSSGGNPLIYQHLFW 160
Cdd:MTH00079 157 SILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFW 236

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 459219180 161 FFGHPEVYILILPAFGIISHSSLYLTGKKEVFGSLGMVYAILSIALIGCVVWAHHMYTVGMDLDTRAYF 229
Cdd:MTH00079 237 FFGHPEVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYF 305
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-229 1.58e-141

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 405.41  E-value: 1.58e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180   1 GGFGNWMLPLLLGAPDMSFPRLNNLSFWLLPTAMVLLMGSALVDNGCGTSWVVYPPLATS-GHPGSSVDLAIFSLHCAGI 79
Cdd:MTH00153  74 GGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNiAHSGASVDLAIFSLHLAGI 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180  80 SSILGGINFMTTTKNMRSSSISLEHMSLFVWTVFVTVFLLILSLPVLAGAITMLLTDRNLNTSFFDPSSGGNPLIYQHLF 159
Cdd:MTH00153 154 SSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 233

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180 160 WFFGHPEVYILILPAFGIISHSSLYLTGKKEVFGSLGMVYAILSIALIGCVVWAHHMYTVGMDLDTRAYF 229
Cdd:MTH00153 234 WFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYF 303
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-229 5.59e-130

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 376.24  E-value: 5.59e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180   1 GGFGNWMLPLLLGAPDMSFPRLNNLSFWLLPTAMVLLMGSALVDNGCGTSWVVYPPLATS-GHPGSSVDLAIFSLHCAGI 79
Cdd:MTH00223  73 GGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNlAHAGPSVDLAIFSLHLAGV 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180  80 SSILGGINFMTTTKNMRSSSISLEHMSLFVWTVFVTVFLLILSLPVLAGAITMLLTDRNLNTSFFDPSSGGNPLIYQHLF 159
Cdd:MTH00223 153 SSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 232

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180 160 WFFGHPEVYILILPAFGIISHSSLYLTGKKEVFGSLGMVYAILSIALIGCVVWAHHMYTVGMDLDTRAYF 229
Cdd:MTH00223 233 WFFGHPEVYILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYF 302
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-229 3.23e-128

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 371.70  E-value: 3.23e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180   1 GGFGNWMLPLLLGAPDMSFPRLNNLSFWLLPTAMVLLMGSALVDNGCGTSWVVYPPLATS-GHPGSSVDLAIFSLHCAGI 79
Cdd:MTH00167  76 GGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNlAHAGASVDLAIFSLHLAGV 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180  80 SSILGGINFMTTTKNMRSSSISLEHMSLFVWTVFVTVFLLILSLPVLAGAITMLLTDRNLNTSFFDPSSGGNPLIYQHLF 159
Cdd:MTH00167 156 SSILGSINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180 160 WFFGHPEVYILILPAFGIISHSSLYLTGKKEVFGSLGMVYAILSIALIGCVVWAHHMYTVGMDLDTRAYF 229
Cdd:MTH00167 236 WFFGHPEVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYF 305
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-229 9.16e-124

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 360.19  E-value: 9.16e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180   1 GGFGNWMLPLLLGAPDMSFPRLNNLSFWLLPTAMVLLMGSALVDNGCGTSWVVYPPLATSG-HPGSSVDLAIFSLHCAGI 79
Cdd:MTH00142  74 GGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLaHSGGSVDLAIFSLHLAGV 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180  80 SSILGGINFMTTTKNMRSSSISLEHMSLFVWTVFVTVFLLILSLPVLAGAITMLLTDRNLNTSFFDPSSGGNPLIYQHLF 159
Cdd:MTH00142 154 SSILGAINFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 233

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180 160 WFFGHPEVYILILPAFGIISHSSLYLTGKKEVFGSLGMVYAILSIALIGCVVWAHHMYTVGMDLDTRAYF 229
Cdd:MTH00142 234 WFFGHPEVYILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYF 303
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-229 3.62e-123

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 359.02  E-value: 3.62e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180   1 GGFGNWMLPLLLGAPDMSFPRLNNLSFWLLPTAMVLLMGSALVDNGCGTSWVVYPPLATS-GHPGSSVDLAIFSLHCAGI 79
Cdd:MTH00116  76 GGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNlAHAGASVDLAIFSLHLAGV 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180  80 SSILGGINFMTTTKNMRSSSISLEHMSLFVWTVFVTVFLLILSLPVLAGAITMLLTDRNLNTSFFDPSSGGNPLIYQHLF 159
Cdd:MTH00116 156 SSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180 160 WFFGHPEVYILILPAFGIISHSSLYLTGKKEVFGSLGMVYAILSIALIGCVVWAHHMYTVGMDLDTRAYF 229
Cdd:MTH00116 236 WFFGHPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYF 305
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-229 5.33e-113

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 333.02  E-value: 5.33e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180   1 GGFGNWMLPLLLGAPDMSFPRLNNLSFWLLPTAMVLLMGSALVDNGCGTSWVVYPPLATS-GHPGSSVDLAIFSLHCAGI 79
Cdd:MTH00007  73 GGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNlAHAGPSVDLAIFSLHLAGV 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180  80 SSILGGINFMTTTKNMRSSSISLEHMSLFVWTVFVTVFLLILSLPVLAGAITMLLTDRNLNTSFFDPSSGGNPLIYQHLF 159
Cdd:MTH00007 153 SSILGAINFITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 232

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180 160 WFFGHPEVYILILPAFGIISHSSLYLTGKKEVFGSLGMVYAILSIALIGCVVWAHHMYTVGMDLDTRAYF 229
Cdd:MTH00007 233 WFFGHPEVYILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYF 302
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-229 2.26e-109

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 323.76  E-value: 2.26e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180   1 GGFGNWMLPLLLGAPDMSFPRLNNLSFWLLPTAMVLLMGSALVDNGCGTSWVVYPPLATS-GHPGSSVDLAIFSLHCAGI 79
Cdd:MTH00103  76 GGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNlAHAGASVDLTIFSLHLAGV 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180  80 SSILGGINFMTTTKNMRSSSISLEHMSLFVWTVFVTVFLLILSLPVLAGAITMLLTDRNLNTSFFDPSSGGNPLIYQHLF 159
Cdd:MTH00103 156 SSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180 160 WFFGHPEVYILILPAFGIISHSSLYLTGKKEVFGSLGMVYAILSIALIGCVVWAHHMYTVGMDLDTRAYF 229
Cdd:MTH00103 236 WFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYF 305
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-229 2.15e-108

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 321.39  E-value: 2.15e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180   1 GGFGNWMLPLLLGAPDMSFPRLNNLSFWLLPTAMVLLMGSALVDNGCGTSWVVYPPLAT-SGHPGSSVDLAIFSLHCAGI 79
Cdd:MTH00182  78 GGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSiQAHSGGAVDMAIFSLHLAGV 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180  80 SSILGGINFMTTTKNMRSSSISLEHMSLFVWTVFVTVFLLILSLPVLAGAITMLLTDRNLNTSFFDPSSGGNPLIYQHLF 159
Cdd:MTH00182 158 SSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLF 237

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180 160 WFFGHPEVYILILPAFGIISHSSLYLTGKKEVFGSLGMVYAILSIALIGCVVWAHHMYTVGMDLDTRAYF 229
Cdd:MTH00182 238 WFFGHPEVYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYF 307
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-229 2.74e-108

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 321.01  E-value: 2.74e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180   1 GGFGNWMLPLLLGAPDMSFPRLNNLSFWLLPTAMVLLMGSALVDNGCGTSWVVYPPLATS-GHPGSSVDLAIFSLHCAGI 79
Cdd:MTH00037  76 GGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNiAHAGGSVDLAIFSLHLAGA 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180  80 SSILGGINFMTTTKNMRSSSISLEHMSLFVWTVFVTVFLLILSLPVLAGAITMLLTDRNLNTSFFDPSSGGNPLIYQHLF 159
Cdd:MTH00037 156 SSILASINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLF 235

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180 160 WFFGHPEVYILILPAFGIISHSSLYLTGKKEVFGSLGMVYAILSIALIGCVVWAHHMYTVGMDLDTRAYF 229
Cdd:MTH00037 236 WFFGHPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYF 305
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-229 4.74e-108

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 320.62  E-value: 4.74e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180   1 GGFGNWMLPLLLGAPDMSFPRLNNLSFWLLPTAMVLLMGSALVDNGCGTSWVVYPPLAT-SGHPGSSVDLAIFSLHCAGI 79
Cdd:MTH00184  78 GGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSiQAHSGGSVDMAIFSLHLAGI 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180  80 SSILGGINFMTTTKNMRSSSISLEHMSLFVWTVFVTVFLLILSLPVLAGAITMLLTDRNLNTSFFDPSSGGNPLIYQHLF 159
Cdd:MTH00184 158 SSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLF 237

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180 160 WFFGHPEVYILILPAFGIISHSSLYLTGKKEVFGSLGMVYAILSIALIGCVVWAHHMYTVGMDLDTRAYF 229
Cdd:MTH00184 238 WFFGHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYF 307
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-229 9.47e-108

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 319.56  E-value: 9.47e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180   1 GGFGNWMLPLLLGAPDMSFPRLNNLSFWLLPTAMVLLMGSALVDNGCGTSWVVYPPLATS-GHPGSSVDLAIFSLHCAGI 79
Cdd:MTH00183  76 GGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNlAHAGASVDLTIFSLHLAGV 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180  80 SSILGGINFMTTTKNMRSSSISLEHMSLFVWTVFVTVFLLILSLPVLAGAITMLLTDRNLNTSFFDPSSGGNPLIYQHLF 159
Cdd:MTH00183 156 SSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180 160 WFFGHPEVYILILPAFGIISHSSLYLTGKKEVFGSLGMVYAILSIALIGCVVWAHHMYTVGMDLDTRAYF 229
Cdd:MTH00183 236 WFFGHPEVYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYF 305
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-229 2.85e-107

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 318.42  E-value: 2.85e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180   1 GGFGNWMLPLLLGAPDMSFPRLNNLSFWLLPTAMVLLMGSALVDNGCGTSWVVYPPLATS-GHPGSSVDLAIFSLHCAGI 79
Cdd:MTH00077  76 GGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNlAHAGASVDLTIFSLHLAGV 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180  80 SSILGGINFMTTTKNMRSSSISLEHMSLFVWTVFVTVFLLILSLPVLAGAITMLLTDRNLNTSFFDPSSGGNPLIYQHLF 159
Cdd:MTH00077 156 SSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLF 235

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180 160 WFFGHPEVYILILPAFGIISHSSLYLTGKKEVFGSLGMVYAILSIALIGCVVWAHHMYTVGMDLDTRAYF 229
Cdd:MTH00077 236 WFFGHPEVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYF 305
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-229 3.21e-98

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 295.77  E-value: 3.21e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180   1 GGFGNWMLPLLLGAPDMSFPRLNNLSFWLLPTAMVLLMGSALVDNGCGTSWVVYPPLAT-SGHPGSSVDLAIFSLHCAGI 79
Cdd:MTH00026  77 GGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASiQAHSGGSVDMAIFSLHLAGL 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180  80 SSILGGINFMTTTKNMRSSSISLEHMSLFVWTVFVTVFLLILSLPVLAGAITMLLTDRNLNTSFFDPSSGGNPLIYQHLF 159
Cdd:MTH00026 157 SSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLF 236

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180 160 WFFGHPEVYILILPAFGIISHSSLYLTGKKEVFGSLGMVYAILSIALIGCVVWAHHMYTVGMDLDTRAYF 229
Cdd:MTH00026 237 WFFGHPEVYILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYF 306
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-229 8.23e-94

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


Pssm-ID: 238461  Cd Length: 463  Bit Score: 282.11  E-value: 8.23e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180   1 GGFGNWMlPLLLGAPDMSFPRLNNLSFWLLPTAMVLLMGSALVDNGCGTSWVVYPPLAT-SGHPGSSVDLAIFSLHCAGI 79
Cdd:cd00919   65 GGFGNLL-PPLIGARDLAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTlSYSSGVGVDLAILGLHLAGV 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180  80 SSILGGINFMTTTKNMRSSSISLEHMSLFVWTVFVTVFLLILSLPVLAGAITMLLTDRNLNTSFFDPSSGGNPLIYQHLF 159
Cdd:cd00919  144 SSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLF 223

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180 160 WFFGHPEVYILILPAFGIISHSSLYLTGKKeVFGSLGMVYAILSIALIGCVVWAHHMYTVGMDLDTRAYF 229
Cdd:cd00919  224 WFFGHPEVYILILPAFGAISEIIPTFSGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYF 292
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-229 2.16e-91

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


Pssm-ID: 213748  Cd Length: 499  Bit Score: 277.18  E-value: 2.16e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180    1 GGFGNWMLPLLLGAPDMSFPRLNNLSFWLLPTAMVLLMGSALVDNGCGTSWVVYPPLA-TSGHPGSSVDLAIFSLHCAGI 79
Cdd:TIGR02891  69 AGFGNYLLPLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSsTSGSPGVGVDLWLLGLHLLGI 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180   80 SSILGGINFMTTTKNMRSSSISLEHMSLFVWTVFVTVFLLILSLPVLAGAITMLLTDRNLNTSFFDPSSGGNPLIYQHLF 159
Cdd:TIGR02891 149 SSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLF 228

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180  160 WFFGHPEVYILILPAFGIISHsSLYLTGKKEVFGSLGMVYAILSIALIGCVVWAHHMYTVGMDLDTRAYF 229
Cdd:TIGR02891 229 WFFGHPEVYIIFLPAFGIISE-ILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFF 297
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-229 1.56e-86

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 265.84  E-value: 1.56e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180   1 GGFGNWMLPLLLGAPDMSFPRLNNLSFWLLPTAMVLLMGSALVDNGCGTSWVVYPPLATS-GHPGSSVDLAIFSLHCAGI 79
Cdd:COG0843   78 AGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLeASPGVGVDLWLLGLALFGV 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180  80 SSILGGINFMTTTKNMRSSSISLEHMSLFVWTVFVTVFLLILSLPVLAGAITMLLTDRNLNTSFFDPSSGGNPLIYQHLF 159
Cdd:COG0843  158 GSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLF 237

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180 160 WFFGHPEVYILILPAFGIISHsSLYLTGKKEVFGSLGMVYAILSIALIGCVVWAHHMYTVGMDLDTRAYF 229
Cdd:COG0843  238 WFFGHPEVYILILPAFGIVSE-IIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFF 306
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-229 2.96e-81

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 251.52  E-value: 2.96e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180   1 GGFGNWMLPLLLGAPDMSFPRLNNLSFWLLPTAMVLLMGSALVdnGCGTSWVVYPPLATS-GHPGSSVDLAIFSLHCAGI 79
Cdd:MTH00048  77 GGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSlFSSSWGVDFLMFSLHLAGV 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180  80 SSILGGINFMTTTKNMRSSSISLEHmSLFVWTVFVTVFLLILSLPVLAGAITMLLTDRNLNTSFFDPSSGGNPLIYQHLF 159
Cdd:MTH00048 155 SSLFGSINFICTIYSAFMTNVFSRT-SIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMF 233

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180 160 WFFGHPEVYILILPAFGIISHSSLYLTGKKEVFGSLGMVYAILSIALIGCVVWAHHMYTVGMDLDTRAYF 229
Cdd:MTH00048 234 WFFGHPEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFF 303
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 2-229 9.96e-76

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: 237.09  E-value: 9.96e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180   2 GFGNWMLPLLLGAPDMSFPRLNNLSFWLLPTAMVLLMGSALVDNGCGTSWVVYPPLATSGH-PGSSVDLAIFSLHCAGIS 80
Cdd:cd01662   71 GLMNYLVPLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYsPGVGVDYWILGLQFSGIG 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180  81 SILGGINFMTTTKNMRSSSISLEHMSLFVWTVFVTVFLLILSLPVLAGAITMLLTDRNLNTSFFDPSSGGNPLIYQHLFW 160
Cdd:cd01662  151 TLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFW 230

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 459219180 161 FFGHPEVYILILPAFGIIShSSLYLTGKKEVFGSLGMVYAILSIALIGCVVWAHHMYTVGMDLDTRAYF 229
Cdd:cd01662  231 IFGHPEVYILILPAFGIFS-EIVPTFSRKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFF 298
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-229 1.92e-58

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: 190.48  E-value: 1.92e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180    1 GGFGNWMLPLLLGAPDMSFPRLNNLSFWLLPTAMVLLMGSAlvdNGCGTSWVVYPPLAtsghpgsSVDLAIFSLHCAGIS 80
Cdd:pfam00115  62 FGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPLV-------GVDLWYIGLLLAGVS 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180   81 SILGGINFMTTTKNMRSSSISLeHMSLFVWTVFVTVFLLILSLPVLAGAITMLLTDRNLNTSffdpssGGNPLIYQHLFW 160
Cdd:pfam00115 132 SLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGAG------GGDPLLDQHLFW 204

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 459219180  161 FFGHPEVYILILPAFGIISHSSLYLTGKKeVFGSLGMVYAILSIALIGCVVWAHHMYTVGMDLDTRAYF 229
Cdd:pfam00115 205 WFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALF 272
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 2-229 6.85e-50

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 172.43  E-value: 6.85e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180   2 GFGNWMLPLLLGAPDMSFPRLNNLSFWLLPTAMVLLMGSALVDNGCGTSWVVYPPLATSGH-PGSSVDLAIFSLHCAGIS 80
Cdd:PRK15017 121 GLMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYsPGVGVDYWIWSLQLSGIG 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180  81 SILGGINFMTTTKNMRSSSISLEHMSLFVWTVFVTVFLLILSLPVLAGAITMLLTDRNLNTSFFDPSSGGNPLIYQHLFW 160
Cdd:PRK15017 201 TTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIW 280

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 459219180 161 FFGHPEVYILILPAFGIISHSSLYLTgKKEVFGSLGMVYAILSIALIGCVVWAHHMYTVGMDLDTRAYF 229
Cdd:PRK15017 281 AWGHPEVYILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFF 348
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 2-175 2.26e-03

ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and some archaea which catalyze the reduction of O2 and simultaneously pump protons across the membrane. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. The ba3 family contains oxidases that lack the conserved residues that form the D- and K-pathways in CcO and ubiquinol oxidase. Instead they contain a potential alternative K-pathway. Additional proton channels have been proposed for this family of oxidases but none have been identified definitively. For general information on the heme-copper oxidase superfamily, please see cd00919.


Pssm-ID: 238830  Cd Length: 473  Bit Score: 38.42  E-value: 2.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180   2 GFGNWMLPLLLGAPDMSfPRLNNLSFWLLpTAMVLLMGSALVDNGCGTSWVVYPPLatSGHPGSSVDLAIFSLHcagiSS 81
Cdd:cd01660   66 GFFYAIVARALLRSLFN-RRLAWAGFWLM-VIGTVMAAVPILLGQASVLYTFYPPL--QAHPLFYIGAALVVVG----SW 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459219180  82 ILGGINFMTTTKNMRSssISLEHMSLFVWTVFVTVFL-LILSLPVlagAITMLLtdrnlntsFFDPSSGG-----NPLIY 155
Cdd:cd01660  138 ISGFAMFVTLWRWKKA--NPGKKVPLATFMVVTTMILwLVASLGV---ALEVLF--------QLLPWSLGlvdtvDVLLS 204

                        170       180
                 ....*....|....*....|
gi 459219180 156 QHLFWFFGHPEVYILILPAF 175
Cdd:cd01660  205 RTLFWWFGHPLVYFWLLPAY 224
 
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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