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Conserved domains on  [gi|312604781|gb|ADQ93544|]
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cytochrome oxidase subunit 1, partial (mitochondrion) [Erythrophyllum wynnei]

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 ...
 1-221 5.99e-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: 372.20  E-value: 5.99e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781   1 TLYLIFGAFSGVLGGCMSILIRMELAQPGNhlLLGNHQVYNVLVTAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAF 80
Cdd:cd01663    8 TLYLIFGLWSGLVGTSLSLLIRLELSQPGS--QLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAF 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781  81 PRLNNISFWLLPPALCLLLLSAIVEVGAGTGWTVYPPLSSIQSHSGGAVDLAIFSLHLSGASSILGAVNFISTILNMRSP 160
Cdd:cd01663   86 PRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAP 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312604781 161 GQSMYRIPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLF 221
Cdd:cd01663  166 GMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 226
 
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 ...
 1-221 5.99e-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: 372.20  E-value: 5.99e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781   1 TLYLIFGAFSGVLGGCMSILIRMELAQPGNhlLLGNHQVYNVLVTAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAF 80
Cdd:cd01663    8 TLYLIFGLWSGLVGTSLSLLIRLELSQPGS--QLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAF 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781  81 PRLNNISFWLLPPALCLLLLSAIVEVGAGTGWTVYPPLSSIQSHSGGAVDLAIFSLHLSGASSILGAVNFISTILNMRSP 160
Cdd:cd01663   86 PRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAP 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312604781 161 GQSMYRIPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLF 221
Cdd:cd01663  166 GMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 226
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-221 3.55e-127

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 368.43  E-value: 3.55e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781   1 TLYLIFGAFSGVLGGCMSILIRMELAQPGNhlLLGNHQVYNVLVTAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00153  15 TLYFIFGAWSGMVGTSLSLLIRAELGQPGS--LIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAF 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781  81 PRLNNISFWLLPPALCLLLLSAIVEVGAGTGWTVYPPLSSIQSHSGGAVDLAIFSLHLSGASSILGAVNFISTILNMRSP 160
Cdd:MTH00153  93 PRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSK 172

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312604781 161 GQSMYRIPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLF 221
Cdd:MTH00153 173 GMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 233
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-221 1.87e-76

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 239.26  E-value: 1.87e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781   2 LYLIFGAFSGVLGGCMSILIRMELAQPGNHLLLGNHqvYNVLVTAHAFLMIFFMVMPvMIGGFGNWLVPIMIGSPDMAFP 81
Cdd:COG0843   21 MYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPET--YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFP 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781  82 RLNNISFWLLPPALCLLLLSAIVEVGAGTGWTVYPPLSSIQSHSGGAVDLAIFSLHLSGASSILGAVNFISTILNMRSPG 161
Cdd:COG0843   98 RLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPG 177

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781 162 QSMYRIPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLF 221
Cdd:COG0843  178 MTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLF 237
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 2-221 1.16e-45

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: 156.58  E-value: 1.16e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781    2 LYLIFGAFSGVLGGCMSILIRMELAQPGNHLLlgNHQVYNVLVTAHAFLMIFFMVMPvMIGGFGNWLVPIMIGSPDMAFP 81
Cdd:pfam00115   5 LYLVTALVWFLVGGLLGLLIRLQLAFPGLNFL--SPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781   82 RLNNISFWLLPPALCLLLLSAiveVGAGTGWTVYPPLssiqshsgGAVDLAIFSLHLSGASSILGAVNFISTILNMRSPG 161
Cdd:pfam00115  82 RLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPG 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781  162 QSMyRIPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNtsffdpAGGGDPVLYQHLF 221
Cdd:pfam00115 151 MTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLF 203
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 2-221 2.07e-37

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


Pssm-ID: 131928  Cd Length: 643  Bit Score: 137.29  E-value: 2.07e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781    2 LYLIFGAFSGVLGGCMSILIRMELAQPGNHLLLGNHqvYNVLVTAHAFLMIFFMVMPVMIGgFGNWLVPIMIGSPDMAFP 81
Cdd:TIGR02882  56 MYIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQH--YNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFP 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781   82 RLNNISFWLLPPALCLLLLSAIVEVGAGTGWTVYPPLSSIQSHSGGAVDLAIFSLHLSGASSILGAVNFISTILNMRSPG 161
Cdd:TIGR02882 133 VLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPG 212

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781  162 QSMYRIPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLF 221
Cdd:TIGR02882 213 MKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLF 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 ...
 1-221 5.99e-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: 372.20  E-value: 5.99e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781   1 TLYLIFGAFSGVLGGCMSILIRMELAQPGNhlLLGNHQVYNVLVTAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAF 80
Cdd:cd01663    8 TLYLIFGLWSGLVGTSLSLLIRLELSQPGS--QLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAF 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781  81 PRLNNISFWLLPPALCLLLLSAIVEVGAGTGWTVYPPLSSIQSHSGGAVDLAIFSLHLSGASSILGAVNFISTILNMRSP 160
Cdd:cd01663   86 PRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAP 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312604781 161 GQSMYRIPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLF 221
Cdd:cd01663  166 GMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 226
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-221 3.55e-127

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 368.43  E-value: 3.55e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781   1 TLYLIFGAFSGVLGGCMSILIRMELAQPGNhlLLGNHQVYNVLVTAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00153  15 TLYFIFGAWSGMVGTSLSLLIRAELGQPGS--LIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAF 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781  81 PRLNNISFWLLPPALCLLLLSAIVEVGAGTGWTVYPPLSSIQSHSGGAVDLAIFSLHLSGASSILGAVNFISTILNMRSP 160
Cdd:MTH00153  93 PRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSK 172

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312604781 161 GQSMYRIPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLF 221
Cdd:MTH00153 173 GMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 233
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-221 1.76e-114

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 336.26  E-value: 1.76e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781   1 TLYLIFGAFSGVLGGCMSILIRMELAQPGNhlLLGNHQVYNVLVTAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00167  17 TLYFIFGAWAGMVGTALSLLIRAELSQPGS--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAF 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781  81 PRLNNISFWLLPPALCLLLLSAIVEVGAGTGWTVYPPLSSIQSHSGGAVDLAIFSLHLSGASSILGAVNFISTILNMRSP 160
Cdd:MTH00167  95 PRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPP 174

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312604781 161 GQSMYRIPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLF 221
Cdd:MTH00167 175 GITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-221 4.95e-112

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 330.13  E-value: 4.95e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781   1 TLYLIFGAFSGVLGGCMSILIRMELAQPGNhlLLGNHQVYNVLVTAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00116  17 TLYLIFGAWAGMVGTALSLLIRAELGQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAF 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781  81 PRLNNISFWLLPPALCLLLLSAIVEVGAGTGWTVYPPLSSIQSHSGGAVDLAIFSLHLSGASSILGAVNFISTILNMRSP 160
Cdd:MTH00116  95 PRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPP 174

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312604781 161 GQSMYRIPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLF 221
Cdd:MTH00116 175 AMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-221 5.40e-111

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 327.32  E-value: 5.40e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781   1 TLYLIFGAFSGVLGGCMSILIRMELAQPGnhLLLGNHQVYNVLVTAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00223  14 TLYLIFGMWSGLVGTSLSLLIRAELGQPG--ALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAF 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781  81 PRLNNISFWLLPPALCLLLLSAIVEVGAGTGWTVYPPLSSIQSHSGGAVDLAIFSLHLSGASSILGAVNFISTILNMRSP 160
Cdd:MTH00223  92 PRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSP 171

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312604781 161 GQSMYRIPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLF 221
Cdd:MTH00223 172 GMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 232
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-221 1.08e-108

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 321.67  E-value: 1.08e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781   1 TLYLIFGAFSGVLGGCMSILIRMELAQPGNhlLLGNHQVYNVLVTAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00142  15 TLYFLFGAWAGMVGTGLSLLIRAELGQPGS--LLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAF 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781  81 PRLNNISFWLLPPALCLLLLSAIVEVGAGTGWTVYPPLSSIQSHSGGAVDLAIFSLHLSGASSILGAVNFISTILNMRSP 160
Cdd:MTH00142  93 PRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAG 172

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312604781 161 GQSMYRIPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLF 221
Cdd:MTH00142 173 GMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 233
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-221 7.08e-102

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 304.44  E-value: 7.08e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781   1 TLYLIFGAFSGVLGGCMSILIRMELAQPGNhlLLGNHQVYNVLVTAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00182  19 TLYLVFGAGAGMIGTAFSMLIRLELSAPGA--MLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAF 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781  81 PRLNNISFWLLPPALCLLLLSAIVEVGAGTGWTVYPPLSSIQSHSGGAVDLAIFSLHLSGASSILGAVNFISTILNMRSP 160
Cdd:MTH00182  97 PRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAP 176

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312604781 161 GQSMYRIPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLF 221
Cdd:MTH00182 177 GVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLF 237
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-221 8.17e-101

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 301.75  E-value: 8.17e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781   1 TLYLIFGAFSGVLGGCMSILIRMELAQPGNhlLLGNHQVYNVLVTAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00037  17 TLYLIFGAWAGMVGTAMSVIIRTELAQPGS--LLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAF 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781  81 PRLNNISFWLLPPALCLLLLSAIVEVGAGTGWTVYPPLSSIQSHSGGAVDLAIFSLHLSGASSILGAVNFISTILNMRSP 160
Cdd:MTH00037  95 PRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTP 174

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312604781 161 GQSMYRIPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLF 221
Cdd:MTH00037 175 GMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLF 235
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-221 1.49e-100

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 300.98  E-value: 1.49e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781   1 TLYLIFGAFSGVLGGCMSILIRMELAQPGNhlLLGNHQVYNVLVTAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00184  19 TLYLLFGAFAGMIGTAFSMLIRLELSAPGS--MLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAF 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781  81 PRLNNISFWLLPPALCLLLLSAIVEVGAGTGWTVYPPLSSIQSHSGGAVDLAIFSLHLSGASSILGAVNFISTILNMRSP 160
Cdd:MTH00184  97 PRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAP 176

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312604781 161 GQSMYRIPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLF 221
Cdd:MTH00184 177 GITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLF 237
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-221 1.27e-98

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 296.02  E-value: 1.27e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781   1 TLYLIFGAFSGVLGGCMSILIRMELAQPGNhlLLGNHQVYNVLVTAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00103  17 TLYLLFGAWAGMVGTALSLLIRAELGQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAF 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781  81 PRLNNISFWLLPPALCLLLLSAIVEVGAGTGWTVYPPLSSIQSHSGGAVDLAIFSLHLSGASSILGAVNFISTILNMRSP 160
Cdd:MTH00103  95 PRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPP 174

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312604781 161 GQSMYRIPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLF 221
Cdd:MTH00103 175 AMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-221 6.29e-98

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 294.16  E-value: 6.29e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781   1 TLYLIFGAFSGVLGGCMSILIRMELAQPGNhlLLGNHQVYNVLVTAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00077  17 TLYLVFGAWAGMVGTALSLLIRAELSQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAF 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781  81 PRLNNISFWLLPPALCLLLLSAIVEVGAGTGWTVYPPLSSIQSHSGGAVDLAIFSLHLSGASSILGAVNFISTILNMRSP 160
Cdd:MTH00077  95 PRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPP 174

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312604781 161 GQSMYRIPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLF 221
Cdd:MTH00077 175 SMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLF 235
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-221 2.55e-97

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 292.60  E-value: 2.55e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781   1 TLYLIFGAFSGVLGGCMSILIRMELAQPGNhlLLGNHQVYNVLVTAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00183  17 TLYLVFGAWAGMVGTALSLLIRAELSQPGA--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAF 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781  81 PRLNNISFWLLPPALCLLLLSAIVEVGAGTGWTVYPPLSSIQSHSGGAVDLAIFSLHLSGASSILGAVNFISTILNMRSP 160
Cdd:MTH00183  95 PRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPP 174

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312604781 161 GQSMYRIPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLF 221
Cdd:MTH00183 175 AISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-221 1.61e-95

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 287.95  E-value: 1.61e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781   1 TLYLIFGAFSGVLGGCMSILIRMELAQPGNhlLLGNHQVYNVLVTAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00007  14 TLYFILGVWGGLLGTSMSLLIRIELGQPGA--FLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAF 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781  81 PRLNNISFWLLPPALCLLLLSAIVEVGAGTGWTVYPPLSSIQSHSGGAVDLAIFSLHLSGASSILGAVNFISTILNMRSP 160
Cdd:MTH00007  92 PRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWK 171

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312604781 161 GQSMYRIPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLF 221
Cdd:MTH00007 172 GLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 232
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-221 2.49e-91

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 277.66  E-value: 2.49e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781   1 TLYLIFGAFSGVLGGCMSILIRMELAQPGNhlLLGNHQVYNVLVTAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00026  18 SLYLVFGALSGAIGTAFSMLIRLELSSPGS--MLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAF 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781  81 PRLNNISFWLLPPALCLLLLSAIVEVGAGTGWTVYPPLSSIQSHSGGAVDLAIFSLHLSGASSILGAVNFISTILNMRSP 160
Cdd:MTH00026  96 PRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTP 175

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312604781 161 GQSMYRIPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLF 221
Cdd:MTH00026 176 GMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLF 236
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-221 6.83e-91

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 275.79  E-value: 6.83e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781   1 TLYLIFGAFSGVLGGCMSILIRMELAQPGnhLLLGNHQVYNVLVTAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00079  18 TLYFLFGLWSGMVGTSLSLIIRLELSKPG--LLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSF 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781  81 PRLNNISFWLLPPALCLLLLSAIVEVGAGTGWTVYPPLSSiQSHSGGAVDLAIFSLHLSGASSILGAVNFISTILNMRSP 160
Cdd:MTH00079  96 PRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSS 174

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312604781 161 GQSMYRIPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLF 221
Cdd:MTH00079 175 SISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLF 235
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-221 2.87e-81

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: 249.76  E-value: 2.87e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781   1 TLYLIFGAFSGVLGGCMSILIRMELAQPGNhlLLGNHQVYNVLVTAHAFLMIFFMVMPVMIGGFGNWLVPiMIGSPDMAF 80
Cdd:cd00919    6 LLYLIFAFVALLLGGLLALLIRLELATPGS--LFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781  81 PRLNNISFWLLPPALCLLLLSAIVEVGAGTGWTVYPPLSSIQSHSGGAVDLAIFSLHLSGASSILGAVNFISTILNMRSP 160
Cdd:cd00919   83 PRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAP 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312604781 161 GQSMYRIPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLF 221
Cdd:cd00919  163 GMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLF 223
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-221 1.87e-76

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 239.26  E-value: 1.87e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781   2 LYLIFGAFSGVLGGCMSILIRMELAQPGNHLLLGNHqvYNVLVTAHAFLMIFFMVMPvMIGGFGNWLVPIMIGSPDMAFP 81
Cdd:COG0843   21 MYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPET--YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFP 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781  82 RLNNISFWLLPPALCLLLLSAIVEVGAGTGWTVYPPLSSIQSHSGGAVDLAIFSLHLSGASSILGAVNFISTILNMRSPG 161
Cdd:COG0843   98 RLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPG 177

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781 162 QSMYRIPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLF 221
Cdd:COG0843  178 MTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLF 237
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 2-221 3.11e-63

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: 204.35  E-value: 3.11e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781   2 LYLIFGAFSGVLGGCMSILIRMELAQPGNHLLLGNHqvYNVLVTAHAFLMIFFMVMPVMIGgFGNWLVPIMIGSPDMAFP 81
Cdd:cd01662   13 MYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEH--YNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFP 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781  82 RLNNISFWLLPPALCLLLLSAIVEVGAGTGWTVYPPLSSIQSHSGGAVDLAIFSLHLSGASSILGAVNFISTILNMRSPG 161
Cdd:cd01662   90 RLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPG 169

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781 162 QSMYRIPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLF 221
Cdd:cd01662  170 MTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLF 229
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 2-221 2.88e-59

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 194.13  E-value: 2.88e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781   2 LYLIFGAFSGVLGGCMSILIRMELAQPGNHLLlgNHQVYNVLVTAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAFP 81
Cdd:MTH00048  19 IYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVI--SLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLP 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781  82 RLNNISFWLLPPALCLLLLSAIVevGAGTGWTVYPPLSSIQSHSGGAVDLAIFSLHLSGASSILGAVNFISTILNMRSPG 161
Cdd:MTH00048  97 RLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTN 174

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781 162 QSmYRIPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLF 221
Cdd:MTH00048 175 VF-SRTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMF 233
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 2-221 1.16e-45

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: 156.58  E-value: 1.16e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781    2 LYLIFGAFSGVLGGCMSILIRMELAQPGNHLLlgNHQVYNVLVTAHAFLMIFFMVMPvMIGGFGNWLVPIMIGSPDMAFP 81
Cdd:pfam00115   5 LYLVTALVWFLVGGLLGLLIRLQLAFPGLNFL--SPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781   82 RLNNISFWLLPPALCLLLLSAiveVGAGTGWTVYPPLssiqshsgGAVDLAIFSLHLSGASSILGAVNFISTILNMRSPG 161
Cdd:pfam00115  82 RLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPG 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781  162 QSMyRIPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNtsffdpAGGGDPVLYQHLF 221
Cdd:pfam00115 151 MTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLF 203
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 2-221 2.07e-37

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


Pssm-ID: 131928  Cd Length: 643  Bit Score: 137.29  E-value: 2.07e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781    2 LYLIFGAFSGVLGGCMSILIRMELAQPGNHLLLGNHqvYNVLVTAHAFLMIFFMVMPVMIGgFGNWLVPIMIGSPDMAFP 81
Cdd:TIGR02882  56 MYIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQH--YNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFP 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781   82 RLNNISFWLLPPALCLLLLSAIVEVGAGTGWTVYPPLSSIQSHSGGAVDLAIFSLHLSGASSILGAVNFISTILNMRSPG 161
Cdd:TIGR02882 133 VLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPG 212

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781  162 QSMYRIPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLF 221
Cdd:TIGR02882 213 MKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLF 272
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 2-220 3.40e-35

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 131.21  E-value: 3.40e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781   2 LYLIFGAFSGVLGGCMSILIRME--LAQPGNHLLLGNHQvYNVLVTAHAFLMIFFMVMPVMIGgFGNWLVPIMIGSPDMA 79
Cdd:PRK15017  60 MYIIVAIVMLLRGFADAIMMRSQqaLASAGEAGFLPPHH-YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVA 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312604781  80 FPRLNNISFWLLPPALCLLLLSAIVEVGAGTGWTVYPPLSSIQSHSGGAVDLAIFSLHLSGASSILGAVNFISTILNMRS 159
Cdd:PRK15017 138 FPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRA 217

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312604781 160 PGQSMYRIPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHL 220
Cdd:PRK15017 218 PGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINL 278
 
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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