NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|51102541|gb|AAT95958|]
View 

cytochrome oxidase subunit I, partial (mitochondrion) [Conus planorbis]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 2-212 3.85e-133

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


The actual alignment was detected with superfamily member MTH00153:

Pssm-ID: 469701  Cd Length: 511  Bit Score: 383.45  E-value: 3.85e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51102541    2 LFGMWSGLVGTALSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMVFPRLNNM 81
Cdd:MTH00153  19 IFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNM 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51102541   82 SFWLLPPALLLLLSSAAVESGVGTGWTVYPPLAGNLAHAGGSVDLAIFSLHLAGVSSILGAVNFITTIINMRWQGMKFER 161
Cdd:MTH00153  99 SFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDR 178

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 51102541  162 LSLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTAFFDPAGGGDPILY 212
Cdd:MTH00153 179 MPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILY 229
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 2-212 3.85e-133

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 383.45  E-value: 3.85e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51102541    2 LFGMWSGLVGTALSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMVFPRLNNM 81
Cdd:MTH00153  19 IFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNM 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51102541   82 SFWLLPPALLLLLSSAAVESGVGTGWTVYPPLAGNLAHAGGSVDLAIFSLHLAGVSSILGAVNFITTIINMRWQGMKFER 161
Cdd:MTH00153  99 SFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDR 178

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 51102541  162 LSLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTAFFDPAGGGDPILY 212
Cdd:MTH00153 179 MPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILY 229
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-212 8.04e-122

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: 353.71  E-value: 8.04e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51102541   1 ILFGMWSGLVGTALSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMVFPRLNN 80
Cdd:cd01663  11 LIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNN 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51102541  81 MSFWLLPPALLLLLSSAAVESGVGTGWTVYPPLAGNLAHAGGSVDLAIFSLHLAGVSSILGAVNFITTIINMRWQGMKFE 160
Cdd:cd01663  91 LSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLE 170

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 51102541 161 RLSLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTAFFDPAGGGDPILY 212
Cdd:cd01663 171 KMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILY 222
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-212 1.76e-64

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 208.06  E-value: 1.76e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51102541   1 ILFGMWSGLVGTALSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMmIGGFGNWLVPLMLGAPDMVFPRLNN 80
Cdd:COG0843  23 LVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPF-LAGFGNYLVPLQIGARDMAFPRLNA 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51102541  81 MSFWLLPPALLLLLSSAAVESGVGTGWTVYPPLAGNLAHAGGSVDLAIFSLHLAGVSSILGAVNFITTIINMRWQGMKFE 160
Cdd:COG0843 102 LSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLM 181

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 51102541 161 RLSLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTAFFDPAGGGDPILY 212
Cdd:COG0843 182 RMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLW 233
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-212 1.05e-38

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: 138.09  E-value: 1.05e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51102541     1 ILFGMWSGLVGTALSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMmIGGFGNWLVPLMLGAPDMVFPRLNN 80
Cdd:pfam00115   7 LVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRLNA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51102541    81 MSFWLLPPALLLLLSSAAvesGVGTGWTVYPPLAGnlahaggsVDLAIFSLHLAGVSSILGAVNFITTIINMRWQGMKFe 160
Cdd:pfam00115  86 LSFWLVVLGAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL- 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 51102541   161 RLSLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNtaffdpAGGGDPILY 212
Cdd:pfam00115 154 RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLD 199
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 11-212 6.65e-34

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: 127.28  E-value: 6.65e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51102541    11 GTALSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGgFGNWLVPLMLGAPDMVFPRLNNMSFWLLPPAL 90
Cdd:TIGR02882  68 GGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGA 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51102541    91 LLLLSSAAVESGVGTGWTVYPPLAGNLAHAGGSVDLAIFSLHLAGVSSILGAVNFITTIINMRWQGMKFERLSLFVWSVK 170
Cdd:TIGR02882 147 MLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTL 226

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 51102541   171 ITAILLLLSLPVLAGAITMLLTDRNFNTAFFDPAGGGDPILY 212
Cdd:TIGR02882 227 ITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLW 268
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 2-212 3.85e-133

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 383.45  E-value: 3.85e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51102541    2 LFGMWSGLVGTALSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMVFPRLNNM 81
Cdd:MTH00153  19 IFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNM 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51102541   82 SFWLLPPALLLLLSSAAVESGVGTGWTVYPPLAGNLAHAGGSVDLAIFSLHLAGVSSILGAVNFITTIINMRWQGMKFER 161
Cdd:MTH00153  99 SFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDR 178

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 51102541  162 LSLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTAFFDPAGGGDPILY 212
Cdd:MTH00153 179 MPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILY 229
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-212 8.04e-122

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: 353.71  E-value: 8.04e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51102541   1 ILFGMWSGLVGTALSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMVFPRLNN 80
Cdd:cd01663  11 LIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNN 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51102541  81 MSFWLLPPALLLLLSSAAVESGVGTGWTVYPPLAGNLAHAGGSVDLAIFSLHLAGVSSILGAVNFITTIINMRWQGMKFE 160
Cdd:cd01663  91 LSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLE 170

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 51102541 161 RLSLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTAFFDPAGGGDPILY 212
Cdd:cd01663 171 KMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILY 222
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-212 8.35e-122

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 354.67  E-value: 8.35e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51102541    1 ILFGMWSGLVGTALSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMVFPRLNN 80
Cdd:MTH00223  17 LIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNN 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51102541   81 MSFWLLPPALLLLLSSAAVESGVGTGWTVYPPLAGNLAHAGGSVDLAIFSLHLAGVSSILGAVNFITTIINMRWQGMKFE 160
Cdd:MTH00223  97 MSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLE 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 51102541  161 RLSLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTAFFDPAGGGDPILY 212
Cdd:MTH00223 177 RLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILY 228
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 2-212 6.10e-121

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 352.49  E-value: 6.10e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51102541    2 LFGMWSGLVGTALSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMVFPRLNNM 81
Cdd:MTH00142  19 LFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNM 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51102541   82 SFWLLPPALLLLLSSAAVESGVGTGWTVYPPLAGNLAHAGGSVDLAIFSLHLAGVSSILGAVNFITTIINMRWQGMKFER 161
Cdd:MTH00142  99 SFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFER 178

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 51102541  162 LSLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTAFFDPAGGGDPILY 212
Cdd:MTH00142 179 VPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILY 229
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 2-212 6.82e-119

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 347.05  E-value: 6.82e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51102541    2 LFGMWSGLVGTALSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMVFPRLNNM 81
Cdd:MTH00167  21 IFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNM 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51102541   82 SFWLLPPALLLLLSSAAVESGVGTGWTVYPPLAGNLAHAGGSVDLAIFSLHLAGVSSILGAVNFITTIINMRWQGMKFER 161
Cdd:MTH00167 101 SFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQ 180

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 51102541  162 LSLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTAFFDPAGGGDPILY 212
Cdd:MTH00167 181 TPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILY 231
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-212 3.78e-114

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 335.14  E-value: 3.78e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51102541    1 ILFGMWSGLVGTALSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMVFPRLNN 80
Cdd:MTH00116  20 LIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNN 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51102541   81 MSFWLLPPALLLLLSSAAVESGVGTGWTVYPPLAGNLAHAGGSVDLAIFSLHLAGVSSILGAVNFITTIINMRWQGMKFE 160
Cdd:MTH00116 100 MSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQY 179

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 51102541  161 RLSLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTAFFDPAGGGDPILY 212
Cdd:MTH00116 180 QTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILY 231
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 2-212 4.29e-106

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 314.53  E-value: 4.29e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51102541    2 LFGMWSGLVGTALSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMVFPRLNNM 81
Cdd:MTH00007  18 ILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNM 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51102541   82 SFWLLPPALLLLLSSAAVESGVGTGWTVYPPLAGNLAHAGGSVDLAIFSLHLAGVSSILGAVNFITTIINMRWQGMKFER 161
Cdd:MTH00007  98 SFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLER 177

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 51102541  162 LSLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTAFFDPAGGGDPILY 212
Cdd:MTH00007 178 IPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILY 228
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-212 4.90e-103

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 306.81  E-value: 4.90e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51102541    1 ILFGMWSGLVGTALSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMVFPRLNN 80
Cdd:MTH00103  20 LLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNN 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51102541   81 MSFWLLPPALLLLLSSAAVESGVGTGWTVYPPLAGNLAHAGGSVDLAIFSLHLAGVSSILGAVNFITTIINMRWQGMKFE 160
Cdd:MTH00103 100 MSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQY 179

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 51102541  161 RLSLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTAFFDPAGGGDPILY 212
Cdd:MTH00103 180 QTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILY 231
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-212 1.19e-102

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 305.69  E-value: 1.19e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51102541    1 ILFGMWSGLVGTALSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMVFPRLNN 80
Cdd:MTH00183  20 LVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNN 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51102541   81 MSFWLLPPALLLLLSSAAVESGVGTGWTVYPPLAGNLAHAGGSVDLAIFSLHLAGVSSILGAVNFITTIINMRWQGMKFE 160
Cdd:MTH00183 100 MSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQY 179

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 51102541  161 RLSLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTAFFDPAGGGDPILY 212
Cdd:MTH00183 180 QTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILY 231
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-212 3.44e-102

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 304.83  E-value: 3.44e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51102541    1 ILFGMWSGLVGTALSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMVFPRLNN 80
Cdd:MTH00037  20 LIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNN 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51102541   81 MSFWLLPPALLLLLSSAAVESGVGTGWTVYPPLAGNLAHAGGSVDLAIFSLHLAGVSSILGAVNFITTIINMRWQGMKFE 160
Cdd:MTH00037 100 MSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFD 179

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 51102541  161 RLSLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTAFFDPAGGGDPILY 212
Cdd:MTH00037 180 RLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILF 231
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-212 4.01e-102

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 304.56  E-value: 4.01e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51102541    1 ILFGMWSGLVGTALSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMVFPRLNN 80
Cdd:MTH00077  20 LVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNN 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51102541   81 MSFWLLPPALLLLLSSAAVESGVGTGWTVYPPLAGNLAHAGGSVDLAIFSLHLAGVSSILGAVNFITTIINMRWQGMKFE 160
Cdd:MTH00077 100 MSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQY 179

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 51102541  161 RLSLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTAFFDPAGGGDPILY 212
Cdd:MTH00077 180 QTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLY 231
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-212 4.23e-97

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 292.11  E-value: 4.23e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51102541    1 ILFGMWSGLVGTALSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMVFPRLNN 80
Cdd:MTH00182  22 LVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNN 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51102541   81 MSFWLLPPALLLLLSSAAVESGVGTGWTVYPPLAGNLAHAGGSVDLAIFSLHLAGVSSILGAVNFITTIINMRWQGMKFE 160
Cdd:MTH00182 102 ISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFN 181

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 51102541  161 RLSLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTAFFDPAGGGDPILY 212
Cdd:MTH00182 182 RLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILF 233
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-212 1.83e-95

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 287.49  E-value: 1.83e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51102541    1 ILFGMWSGLVGTALSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMVFPRLNN 80
Cdd:MTH00184  22 LLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNN 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51102541   81 MSFWLLPPALLLLLSSAAVESGVGTGWTVYPPLAGNLAHAGGSVDLAIFSLHLAGVSSILGAVNFITTIINMRWQGMKFE 160
Cdd:MTH00184 102 ISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMD 181

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 51102541  161 RLSLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTAFFDPAGGGDPILY 212
Cdd:MTH00184 182 RMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILY 233
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-212 3.10e-91

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 276.18  E-value: 3.10e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51102541    1 ILFGMWSGLVGTALSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMVFPRLNN 80
Cdd:MTH00079  21 FLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNN 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51102541   81 MSFWLLPPALLLLLSSAAVESGVGTGWTVYPPLAgNLAHAGGSVDLAIFSLHLAGVSSILGAVNFITTIINMRWQGMKFE 160
Cdd:MTH00079 101 LSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLS-TLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLE 179

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 51102541  161 RLSLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTAFFDPAGGGDPILY 212
Cdd:MTH00079 180 HMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLY 231
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-212 2.81e-87

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 266.88  E-value: 2.81e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51102541    1 ILFGMWSGLVGTALSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMVFPRLNN 80
Cdd:MTH00026  21 LVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNN 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51102541   81 MSFWLLPPALLLLLSSAAVESGVGTGWTVYPPLAGNLAHAGGSVDLAIFSLHLAGVSSILGAVNFITTIINMRWQGMKFE 160
Cdd:MTH00026 101 ISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMS 180

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 51102541  161 RLSLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTAFFDPAGGGDPILY 212
Cdd:MTH00026 181 RIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILY 232
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-212 9.61e-75

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: 232.42  E-value: 9.61e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51102541   1 ILFGMWSGLVGTALSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPlMLGAPDMVFPRLNN 80
Cdd:cd00919   9 LIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNN 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51102541  81 MSFWLLPPALLLLLSSAAVESGVGTGWTVYPPLAGNLAHAGGSVDLAIFSLHLAGVSSILGAVNFITTIINMRWQGMKFE 160
Cdd:cd00919  88 LSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLD 167

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 51102541 161 RLSLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTAFFDPAGGGDPILY 212
Cdd:cd00919 168 KMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLY 219
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-212 1.76e-64

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 208.06  E-value: 1.76e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51102541   1 ILFGMWSGLVGTALSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMmIGGFGNWLVPLMLGAPDMVFPRLNN 80
Cdd:COG0843  23 LVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPF-LAGFGNYLVPLQIGARDMAFPRLNA 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51102541  81 MSFWLLPPALLLLLSSAAVESGVGTGWTVYPPLAGNLAHAGGSVDLAIFSLHLAGVSSILGAVNFITTIINMRWQGMKFE 160
Cdd:COG0843 102 LSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLM 181

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 51102541 161 RLSLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTAFFDPAGGGDPILY 212
Cdd:COG0843 182 RMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLW 233
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-212 5.58e-60

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 195.67  E-value: 5.58e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51102541    1 ILFGMWSGLVGTALSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMVFPRLNN 80
Cdd:MTH00048  21 TLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNA 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51102541   81 MSFWLLPPALLLLLSSAAVesGVGTGWTVYPPLAGNLAHAGGSVDLAIFSLHLAGVSSILGAVNFITTIINMrWQGMKFE 160
Cdd:MTH00048 101 LSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSA-FMTNVFS 177

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 51102541  161 RLSLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTAFFDPAGGGDPILY 212
Cdd:MTH00048 178 RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLF 229
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 9-212 3.08e-51

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: 172.38  E-value: 3.08e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51102541   9 LVGTALSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGgFGNWLVPLMLGAPDMVFPRLNNMSFWLLPP 88
Cdd:cd01662  23 LRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLF 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51102541  89 ALLLLLSSAAVESGVGTGWTVYPPLAGNLAHAGGSVDLAIFSLHLAGVSSILGAVNFITTIINMRWQGMKFERLSLFVWS 168
Cdd:cd01662 102 GGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWT 181

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 51102541 169 VKITAILLLLSLPVLAGAITMLLTDRNFNTAFFDPAGGGDPILY 212
Cdd:cd01662 182 TLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLW 225
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-212 1.05e-38

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: 138.09  E-value: 1.05e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51102541     1 ILFGMWSGLVGTALSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMmIGGFGNWLVPLMLGAPDMVFPRLNN 80
Cdd:pfam00115   7 LVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRLNA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51102541    81 MSFWLLPPALLLLLSSAAvesGVGTGWTVYPPLAGnlahaggsVDLAIFSLHLAGVSSILGAVNFITTIINMRWQGMKFe 160
Cdd:pfam00115  86 LSFWLVVLGAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL- 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 51102541   161 RLSLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNtaffdpAGGGDPILY 212
Cdd:pfam00115 154 RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLD 199
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 11-212 6.65e-34

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: 127.28  E-value: 6.65e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51102541    11 GTALSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGgFGNWLVPLMLGAPDMVFPRLNNMSFWLLPPAL 90
Cdd:TIGR02882  68 GGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGA 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51102541    91 LLLLSSAAVESGVGTGWTVYPPLAGNLAHAGGSVDLAIFSLHLAGVSSILGAVNFITTIINMRWQGMKFERLSLFVWSVK 170
Cdd:TIGR02882 147 MLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTL 226

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 51102541   171 ITAILLLLSLPVLAGAITMLLTDRNFNTAFFDPAGGGDPILY 212
Cdd:TIGR02882 227 ITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLW 268
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 35-212 2.06e-29

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 114.65  E-value: 2.06e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51102541   35 YNVIVTAHAFVMIFFLVMPMMIGgFGNWLVPLMLGAPDMVFPRLNNMSFWLLPPALLLLLSSAAVESGVGTGWTVYPPLA 114
Cdd:PRK15017  99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51102541  115 GNLAHAGGSVDLAIFSLHLAGVSSILGAVNFITTIINMRWQGMKFERLSLFVWSVKITAILLLLSLPVLAGAITMLLTDR 194
Cdd:PRK15017 178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257

                        170
                 ....*....|....*...
gi 51102541  195 NFNTAFFDPAGGGDPILY 212
Cdd:PRK15017 258 YLGTHFFTNDMGGNMMMY 275
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH