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Conserved domains on  [gi|1798176458|gb|QHI43072|]
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cytochrome c oxidase subunit I, partial (mitochondrion) [Pterocladiella capillacea]

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 ...
 1-218 3.75e-129

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: 372.59  E-value: 3.75e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176458   1 SGIFGGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFW 80
Cdd:cd01663    17 SGLVGTSLSLLIRLELSQPGS--QLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFW 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176458  81 LLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPL 160
Cdd:cd01663    95 LLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPL 174

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1798176458 161 FVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHP 218
Cdd:cd01663   175 FVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHP 232
 
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 ...
 1-218 3.75e-129

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: 372.59  E-value: 3.75e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176458   1 SGIFGGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFW 80
Cdd:cd01663    17 SGLVGTSLSLLIRLELSQPGS--QLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFW 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176458  81 LLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPL 160
Cdd:cd01663    95 LLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPL 174

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1798176458 161 FVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHP 218
Cdd:cd01663   175 FVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHP 232
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-218 2.17e-125

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 363.80  E-value: 2.17e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176458   1 SGIFGGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFW 80
Cdd:MTH00153   24 SGMVGTSLSLLIRAELGQPGS--LIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176458  81 LLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPL 160
Cdd:MTH00153  102 LLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPL 181

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1798176458 161 FVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHP 218
Cdd:MTH00153  182 FVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHP 239
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 2-218 1.95e-83

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: 256.38  E-value: 1.95e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176458   2 GIFGGCMSILIRMELAQPGNHLLlgNHQVYNVLITAHAFLMIFFMVMPVLiGGFGNWLVPIMIGSPDMAFPRLNNISFWL 81
Cdd:TIGR02891  21 FLVGGVLALLMRAQLATPGNTFM--DAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPRLNAFSYWL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176458  82 LPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLF 161
Cdd:TIGR02891  98 YLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLF 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1798176458 162 VWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHP 218
Cdd:TIGR02891 178 VWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHP 234
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
3-218 6.29e-80

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 248.12  E-value: 6.29e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176458   3 IFGGCMSILIRMELAQPGNHLLLGNHqvYNVLITAHAFLMIFFMVMPvLIGGFGNWLVPIMIGSPDMAFPRLNNISFWLL 82
Cdd:COG0843    31 LIGGLLALLMRLQLAGPGLGLLSPET--YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLY 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176458  83 PPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFV 162
Cdd:COG0843   108 LFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFT 187

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1798176458 163 WSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHP 218
Cdd:COG0843   188 WAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHP 243
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 2-218 3.16e-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: 163.13  E-value: 3.16e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176458   2 GIFGGCMSILIRMELAQPGNHLLlgNHQVYNVLITAHAFLMIFFMVMPVlIGGFGNWLVPIMIGSPDMAFPRLNNISFWL 81
Cdd:pfam00115  14 FLVGGLLGLLIRLQLAFPGLNFL--SPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRLNALSFWL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176458  82 LPPSLCLLLTSALvevGVGTGWTVYPPLssiqshsgGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMyRMPLF 161
Cdd:pfam00115  91 VVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLF 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1798176458 162 VWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNtsffdpAGGGDPVLYQHLFWFFGHP 218
Cdd:pfam00115 159 VWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHP 209
 
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 ...
 1-218 3.75e-129

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: 372.59  E-value: 3.75e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176458   1 SGIFGGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFW 80
Cdd:cd01663    17 SGLVGTSLSLLIRLELSQPGS--QLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFW 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176458  81 LLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPL 160
Cdd:cd01663    95 LLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPL 174

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1798176458 161 FVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHP 218
Cdd:cd01663   175 FVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHP 232
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-218 2.17e-125

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 363.80  E-value: 2.17e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176458   1 SGIFGGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFW 80
Cdd:MTH00153   24 SGMVGTSLSLLIRAELGQPGS--LIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176458  81 LLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPL 160
Cdd:MTH00153  102 LLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPL 181

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1798176458 161 FVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHP 218
Cdd:MTH00153  182 FVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHP 239
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-218 2.72e-113

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 333.18  E-value: 2.72e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176458   1 SGIFGGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFW 80
Cdd:MTH00167   26 AGMVGTALSLLIRAELSQPGS--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFW 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176458  81 LLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPL 160
Cdd:MTH00167  104 LLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPL 183

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1798176458 161 FVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHP 218
Cdd:MTH00167  184 FVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 241
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-218 7.17e-111

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 326.93  E-value: 7.17e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176458   1 SGIFGGCMSILIRMELAQPGnhLLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFW 80
Cdd:MTH00223   23 SGLVGTSLSLLIRAELGQPG--ALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFW 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176458  81 LLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPL 160
Cdd:MTH00223  101 LLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPL 180

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1798176458 161 FVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHP 218
Cdd:MTH00223  181 FVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHP 238
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-218 3.56e-110

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 325.12  E-value: 3.56e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176458   1 SGIFGGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFW 80
Cdd:MTH00116   26 AGMVGTALSLLIRAELGQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFW 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176458  81 LLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPL 160
Cdd:MTH00116  104 LLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPL 183

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1798176458 161 FVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHP 218
Cdd:MTH00116  184 FVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 241
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-218 2.92e-107

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 317.82  E-value: 2.92e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176458   1 SGIFGGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFW 80
Cdd:MTH00142   24 AGMVGTGLSLLIRAELGQPGS--LLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176458  81 LLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPL 160
Cdd:MTH00142  102 LLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPL 181

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1798176458 161 FVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHP 218
Cdd:MTH00142  182 FVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHP 239
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-218 1.34e-101

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 303.67  E-value: 1.34e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176458   1 SGIFGGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFW 80
Cdd:MTH00182   28 AGMIGTAFSMLIRLELSAPGA--MLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFW 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176458  81 LLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPL 160
Cdd:MTH00182  106 LLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPL 185

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1798176458 161 FVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHP 218
Cdd:MTH00182  186 FVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHP 243
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-218 1.71e-99

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 297.90  E-value: 1.71e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176458   1 SGIFGGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFW 80
Cdd:MTH00037   26 AGMVGTAMSVIIRTELAQPGS--LLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFW 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176458  81 LLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPL 160
Cdd:MTH00037  104 LIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPL 183

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1798176458 161 FVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHP 218
Cdd:MTH00037  184 FVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHP 241
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-218 1.90e-99

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 297.89  E-value: 1.90e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176458   1 SGIFGGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFW 80
Cdd:MTH00184   28 AGMIGTAFSMLIRLELSAPGS--MLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFW 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176458  81 LLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPL 160
Cdd:MTH00184  106 LLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPL 185

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1798176458 161 FVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHP 218
Cdd:MTH00184  186 FVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHP 243
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-218 3.07e-97

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 292.17  E-value: 3.07e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176458   1 SGIFGGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFW 80
Cdd:MTH00103   26 AGMVGTALSLLIRAELGQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFW 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176458  81 LLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPL 160
Cdd:MTH00103  104 LLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPL 183

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1798176458 161 FVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHP 218
Cdd:MTH00103  184 FVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 241
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-218 4.98e-97

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 291.84  E-value: 4.98e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176458   1 SGIFGGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFW 80
Cdd:MTH00077   26 AGMVGTALSLLIRAELSQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFW 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176458  81 LLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPL 160
Cdd:MTH00077  104 LLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPL 183

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1798176458 161 FVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHP 218
Cdd:MTH00077  184 FVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHP 241
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 2-218 1.14e-96

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 290.65  E-value: 1.14e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176458   2 GIFGGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFWL 81
Cdd:MTH00007   24 GLLGTSMSLLIRIELGQPGA--FLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWL 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176458  82 LPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLF 161
Cdd:MTH00007  102 LPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLF 181

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1798176458 162 VWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHP 218
Cdd:MTH00007  182 VWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHP 238
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-218 1.31e-95

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 287.98  E-value: 1.31e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176458   1 SGIFGGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFW 80
Cdd:MTH00183   26 AGMVGTALSLLIRAELSQPGA--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFW 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176458  81 LLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPL 160
Cdd:MTH00183  104 LLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPL 183

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1798176458 161 FVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHP 218
Cdd:MTH00183  184 FVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 241
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-218 2.96e-92

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 279.26  E-value: 2.96e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176458   1 SGIFGGCMSILIRMELAQPGnhLLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFW 80
Cdd:MTH00079   27 SGMVGTSLSLIIRLELSKPG--LLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFW 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176458  81 LLPPSLCLLLTSALVEVGVGTGWTVYPPLSSiQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPL 160
Cdd:MTH00079  105 LLPTSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSL 183

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1798176458 161 FVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHP 218
Cdd:MTH00079  184 FVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHP 241
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-218 9.62e-91

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 276.12  E-value: 9.62e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176458   1 SGIFGGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFW 80
Cdd:MTH00026   27 SGAIGTAFSMLIRLELSSPGS--MLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFW 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176458  81 LLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPL 160
Cdd:MTH00026  105 LLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPL 184

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1798176458 161 FVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHP 218
Cdd:MTH00026  185 FVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHP 242
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 2-218 1.95e-83

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: 256.38  E-value: 1.95e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176458   2 GIFGGCMSILIRMELAQPGNHLLlgNHQVYNVLITAHAFLMIFFMVMPVLiGGFGNWLVPIMIGSPDMAFPRLNNISFWL 81
Cdd:TIGR02891  21 FLVGGVLALLMRAQLATPGNTFM--DAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPRLNAFSYWL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176458  82 LPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLF 161
Cdd:TIGR02891  98 YLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLF 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1798176458 162 VWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHP 218
Cdd:TIGR02891 178 VWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHP 234
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-218 3.67e-83

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: 254.38  E-value: 3.67e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176458   1 SGIFGGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPiMIGSPDMAFPRLNNISFW 80
Cdd:cd00919    15 ALLLGGLLALLIRLELATPGS--LFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFW 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176458  81 LLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPL 160
Cdd:cd00919    92 LFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPL 171

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1798176458 161 FVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHP 218
Cdd:cd00919   172 FVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHP 229
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
3-218 6.29e-80

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 248.12  E-value: 6.29e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176458   3 IFGGCMSILIRMELAQPGNHLLLGNHqvYNVLITAHAFLMIFFMVMPvLIGGFGNWLVPIMIGSPDMAFPRLNNISFWLL 82
Cdd:COG0843    31 LIGGLLALLMRLQLAGPGLGLLSPET--YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLY 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176458  83 PPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFV 162
Cdd:COG0843   108 LFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFT 187

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1798176458 163 WSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHP 218
Cdd:COG0843   188 WAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHP 243
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 3-218 9.81e-68

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: 215.91  E-value: 9.81e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176458   3 IFGGCMSILIRMELAQPGNHLLLGNHqvYNVLITAHAFLMIFFMVMPVLIGgFGNWLVPIMIGSPDMAFPRLNNISFWLL 82
Cdd:cd01662    23 LRGGVDALLMRTQLALPGNDFLSPEH--YNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLF 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176458  83 PPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFV 162
Cdd:cd01662   100 LFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFT 179

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1798176458 163 WSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHP 218
Cdd:cd01662   180 WTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHP 235
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-218 1.05e-62

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 202.99  E-value: 1.05e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176458   1 SGIFGGCMSILIRMELAQPGNHLLlgNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFW 80
Cdd:MTH00048   27 SGFVGLSLSLLIRLNFLDPYYNVI--SLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAW 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176458  81 LLPPSLCLLLTSALVevGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPgQTMYRMPL 160
Cdd:MTH00048  105 LLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMT-NVFSRTSI 181

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1798176458 161 FVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHP 218
Cdd:MTH00048  182 ILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHP 239
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 2-218 3.16e-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: 163.13  E-value: 3.16e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176458   2 GIFGGCMSILIRMELAQPGNHLLlgNHQVYNVLITAHAFLMIFFMVMPVlIGGFGNWLVPIMIGSPDMAFPRLNNISFWL 81
Cdd:pfam00115  14 FLVGGLLGLLIRLQLAFPGLNFL--SPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRLNALSFWL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176458  82 LPPSLCLLLTSALvevGVGTGWTVYPPLssiqshsgGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMyRMPLF 161
Cdd:pfam00115  91 VVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLF 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1798176458 162 VWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNtsffdpAGGGDPVLYQHLFWFFGHP 218
Cdd:pfam00115 159 VWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHP 209
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 9-218 2.62e-38

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 140.07  E-value: 2.62e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176458   9 SILIRME--LAQPGNHLLLGNHQvYNVLITAHAFLMIFFMVMPVLIGgFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSL 86
Cdd:PRK15017   76 AIMMRSQqaLASAGEAGFLPPHH-YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGV 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176458  87 CLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFVWSIF 166
Cdd:PRK15017  154 ILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASL 233

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1798176458 167 VTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHP 218
Cdd:PRK15017  234 CANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHP 285
 
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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