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Conserved domains on  [gi|1111818327|gb|API70779|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Cinara contortae]

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 1.14e-131

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: 379.98  E-value: 1.14e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111818327   1 GTLYFIFGIWSGMMGSSLSMLIRLELSQINSIINNNQLYNVIVTIHAFIMIFFMTMPIVIGGFGNWLIPLMMGSPDMAFP 80
Cdd:MTH00153   14 GTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFP 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111818327  81 RLNNISFWLLPPSLMMMICSFMINNGTGTGWTIYPPLSNNIAHNNISVDLTIFSLHLAGISSILGAINFICTILNMMPNN 160
Cdd:MTH00153   94 RMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKG 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1111818327 161 LKLNQIPLFPWSILITALLLILSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFW 221
Cdd:MTH00153  174 MTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFW 234
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-221 1.14e-131

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 379.98  E-value: 1.14e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111818327   1 GTLYFIFGIWSGMMGSSLSMLIRLELSQINSIINNNQLYNVIVTIHAFIMIFFMTMPIVIGGFGNWLIPLMMGSPDMAFP 80
Cdd:MTH00153   14 GTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFP 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111818327  81 RLNNISFWLLPPSLMMMICSFMINNGTGTGWTIYPPLSNNIAHNNISVDLTIFSLHLAGISSILGAINFICTILNMMPNN 160
Cdd:MTH00153   94 RMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKG 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1111818327 161 LKLNQIPLFPWSILITALLLILSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFW 221
Cdd:MTH00153  174 MTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFW 234
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-221 4.49e-125

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: 362.57  E-value: 4.49e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111818327   1 GTLYFIFGIWSGMMGSSLSMLIRLELSQINSIINNNQLYNVIVTIHAFIMIFFMTMPIVIGGFGNWLIPLMMGSPDMAFP 80
Cdd:cd01663     7 GTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111818327  81 RLNNISFWLLPPSLMMMICSFMINNGTGTGWTIYPPLSNNIAHNNISVDLTIFSLHLAGISSILGAINFICTILNMMPNN 160
Cdd:cd01663    87 RLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPG 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1111818327 161 LKLNQIPLFPWSILITALLLILSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFW 221
Cdd:cd01663   167 MTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFW 227
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-221 1.43e-69

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 221.54  E-value: 1.43e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111818327   1 GTLYFIFGIWSGMMGSSLSMLIRLELSQINSIINNNQLYNVIVTIHAFIMIFFMTMPIvIGGFGNWLIPLMMGSPDMAFP 80
Cdd:COG0843    19 GIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPF-LAGFGNYLVPLQIGARDMAFP 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111818327  81 RLNNISFWLLPPSLMMMICSFMINNGTGTGWTIYPPLSNNIAHNNISVDLTIFSLHLAGISSILGAINFICTILNMMPNN 160
Cdd:COG0843    98 RLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPG 177

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1111818327 161 LKLNQIPLFPWSILITALLLILSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFW 221
Cdd:COG0843   178 MTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFW 238
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-221 3.56e-43

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: 150.03  E-value: 3.56e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111818327   1 GTLYFIFGIWSGMMGSSLSMLIRLELSQINSIINNNQLYNVIVTIHAFIMIFFMTMPIvIGGFGNWLIPLMMGSPDMAFP 80
Cdd:pfam00115   3 GLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111818327  81 RLNNISFWLLPPSLMMMICSFMinnGTGTGWTIYPPLsnniahnnISVDLTIFSLHLAGISSILGAINFICTILNMMPNN 160
Cdd:pfam00115  82 RLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPG 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1111818327 161 LKLnQIPLFPWSILITALLLILSLPVLAGAITMLLTDRNLNTsffdpsGGGDPILYQHLFW 221
Cdd:pfam00115 151 MTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFW 204
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 1-221 1.06e-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: 129.97  E-value: 1.06e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111818327   1 GTLYFIFGIWSGMMGSSLSMLIRLELSQINSIINNNQLYNVIVTIHAFIMIFFMTMPIVIGgFGNWLIPLMMGSPDMAFP 80
Cdd:TIGR02882  54 GVMYIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFP 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111818327  81 RLNNISFWLLPPSLMMMICSFMINNGTGTGWTIYPPLSNNIAHNNISVDLTIFSLHLAGISSILGAINFICTILNMMPNN 160
Cdd:TIGR02882 133 VLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPG 212

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1111818327 161 LKLNQIPLFPWSILITALLLILSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFW 221
Cdd:TIGR02882 213 MKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFW 273
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-221 1.14e-131

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 379.98  E-value: 1.14e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111818327   1 GTLYFIFGIWSGMMGSSLSMLIRLELSQINSIINNNQLYNVIVTIHAFIMIFFMTMPIVIGGFGNWLIPLMMGSPDMAFP 80
Cdd:MTH00153   14 GTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFP 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111818327  81 RLNNISFWLLPPSLMMMICSFMINNGTGTGWTIYPPLSNNIAHNNISVDLTIFSLHLAGISSILGAINFICTILNMMPNN 160
Cdd:MTH00153   94 RMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKG 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1111818327 161 LKLNQIPLFPWSILITALLLILSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFW 221
Cdd:MTH00153  174 MTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFW 234
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-221 4.49e-125

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: 362.57  E-value: 4.49e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111818327   1 GTLYFIFGIWSGMMGSSLSMLIRLELSQINSIINNNQLYNVIVTIHAFIMIFFMTMPIVIGGFGNWLIPLMMGSPDMAFP 80
Cdd:cd01663     7 GTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111818327  81 RLNNISFWLLPPSLMMMICSFMINNGTGTGWTIYPPLSNNIAHNNISVDLTIFSLHLAGISSILGAINFICTILNMMPNN 160
Cdd:cd01663    87 RLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPG 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1111818327 161 LKLNQIPLFPWSILITALLLILSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFW 221
Cdd:cd01663   167 MTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFW 227
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-221 4.15e-116

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 340.50  E-value: 4.15e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111818327   1 GTLYFIFGIWSGMMGSSLSMLIRLELSQINSIINNNQLYNVIVTIHAFIMIFFMTMPIVIGGFGNWLIPLMMGSPDMAFP 80
Cdd:MTH00167   16 GTLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFP 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111818327  81 RLNNISFWLLPPSLMMMICSFMINNGTGTGWTIYPPLSNNIAHNNISVDLTIFSLHLAGISSILGAINFICTILNMMPNN 160
Cdd:MTH00167   96 RMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPG 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1111818327 161 LKLNQIPLFPWSILITALLLILSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFW 221
Cdd:MTH00167  176 ITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFW 236
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-221 4.12e-112

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 330.40  E-value: 4.12e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111818327   1 GTLYFIFGIWSGMMGSSLSMLIRLELSQINSIINNNQLYNVIVTIHAFIMIFFMTMPIVIGGFGNWLIPLMMGSPDMAFP 80
Cdd:MTH00223   13 GTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFP 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111818327  81 RLNNISFWLLPPSLMMMICSFMINNGTGTGWTIYPPLSNNIAHNNISVDLTIFSLHLAGISSILGAINFICTILNMMPNN 160
Cdd:MTH00223   93 RLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPG 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1111818327 161 LKLNQIPLFPWSILITALLLILSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFW 221
Cdd:MTH00223  173 MQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFW 233
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-221 3.17e-111

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 328.20  E-value: 3.17e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111818327   1 GTLYFIFGIWSGMMGSSLSMLIRLELSQINSIINNNQLYNVIVTIHAFIMIFFMTMPIVIGGFGNWLIPLMMGSPDMAFP 80
Cdd:MTH00116   16 GTLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFP 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111818327  81 RLNNISFWLLPPSLMMMICSFMINNGTGTGWTIYPPLSNNIAHNNISVDLTIFSLHLAGISSILGAINFICTILNMMPNN 160
Cdd:MTH00116   96 RMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPA 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1111818327 161 LKLNQIPLFPWSILITALLLILSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFW 221
Cdd:MTH00116  176 MSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFW 236
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-221 2.38e-109

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 323.21  E-value: 2.38e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111818327   1 GTLYFIFGIWSGMMGSSLSMLIRLELSQINSIINNNQLYNVIVTIHAFIMIFFMTMPIVIGGFGNWLIPLMMGSPDMAFP 80
Cdd:MTH00142   14 GTLYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFP 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111818327  81 RLNNISFWLLPPSLMMMICSFMINNGTGTGWTIYPPLSNNIAHNNISVDLTIFSLHLAGISSILGAINFICTILNMMPNN 160
Cdd:MTH00142   94 RMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGG 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1111818327 161 LKLNQIPLFPWSILITALLLILSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFW 221
Cdd:MTH00142  174 MKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFW 234
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-221 3.95e-101

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 302.21  E-value: 3.95e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111818327   1 GTLYFIFGIWSGMMGSSLSMLIRLELSQINSIINNNQLYNVIVTIHAFIMIFFMTMPIVIGGFGNWLIPLMMGSPDMAFP 80
Cdd:MTH00007   13 GTLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFP 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111818327  81 RLNNISFWLLPPSLMMMICSFMINNGTGTGWTIYPPLSNNIAHNNISVDLTIFSLHLAGISSILGAINFICTILNMMPNN 160
Cdd:MTH00007   93 RLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKG 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1111818327 161 LKLNQIPLFPWSILITALLLILSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFW 221
Cdd:MTH00007  173 LRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFW 233
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-221 1.39e-100

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 301.07  E-value: 1.39e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111818327   1 GTLYFIFGIWSGMMGSSLSMLIRLELSQINSIINNNQLYNVIVTIHAFIMIFFMTMPIVIGGFGNWLIPLMMGSPDMAFP 80
Cdd:MTH00183   16 GTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFP 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111818327  81 RLNNISFWLLPPSLMMMICSFMINNGTGTGWTIYPPLSNNIAHNNISVDLTIFSLHLAGISSILGAINFICTILNMMPNN 160
Cdd:MTH00183   96 RMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPA 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1111818327 161 LKLNQIPLFPWSILITALLLILSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFW 221
Cdd:MTH00183  176 ISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFW 236
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-221 1.90e-100

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 300.70  E-value: 1.90e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111818327   1 GTLYFIFGIWSGMMGSSLSMLIRLELSQINSIINNNQLYNVIVTIHAFIMIFFMTMPIVIGGFGNWLIPLMMGSPDMAFP 80
Cdd:MTH00077   16 GTLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFP 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111818327  81 RLNNISFWLLPPSLMMMICSFMINNGTGTGWTIYPPLSNNIAHNNISVDLTIFSLHLAGISSILGAINFICTILNMMPNN 160
Cdd:MTH00077   96 RMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPS 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1111818327 161 LKLNQIPLFPWSILITALLLILSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFW 221
Cdd:MTH00077  176 MSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFW 236
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-221 6.22e-99

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 296.79  E-value: 6.22e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111818327   1 GTLYFIFGIWSGMMGSSLSMLIRLELSQINSIINNNQLYNVIVTIHAFIMIFFMTMPIVIGGFGNWLIPLMMGSPDMAFP 80
Cdd:MTH00103   16 GTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFP 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111818327  81 RLNNISFWLLPPSLMMMICSFMINNGTGTGWTIYPPLSNNIAHNNISVDLTIFSLHLAGISSILGAINFICTILNMMPNN 160
Cdd:MTH00103   96 RMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPA 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1111818327 161 LKLNQIPLFPWSILITALLLILSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFW 221
Cdd:MTH00103  176 MSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFW 236
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-221 7.62e-96

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 288.50  E-value: 7.62e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111818327   1 GTLYFIFGIWSGMMGSSLSMLIRLELSQINSIINNNQLYNVIVTIHAFIMIFFMTMPIVIGGFGNWLIPLMMGSPDMAFP 80
Cdd:MTH00079   17 GTLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFP 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111818327  81 RLNNISFWLLPPSLMMMICSFMINNGTGTGWTIYPPLSnNIAHNNISVDLTIFSLHLAGISSILGAINFICTILNMMPNN 160
Cdd:MTH00079   97 RLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLS-TLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSS 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1111818327 161 LKLNQIPLFPWSILITALLLILSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFW 221
Cdd:MTH00079  176 ISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFW 236
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-221 1.13e-94

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 285.96  E-value: 1.13e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111818327   1 GTLYFIFGIWSGMMGSSLSMLIRLELSQINSIINNNQLYNVIVTIHAFIMIFFMTMPIVIGGFGNWLIPLMMGSPDMAFP 80
Cdd:MTH00037   16 GTLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFP 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111818327  81 RLNNISFWLLPPSLMMMICSFMINNGTGTGWTIYPPLSNNIAHNNISVDLTIFSLHLAGISSILGAINFICTILNMMPNN 160
Cdd:MTH00037   96 RMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPG 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1111818327 161 LKLNQIPLFPWSILITALLLILSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFW 221
Cdd:MTH00037  176 MTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFW 236
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-221 6.73e-93

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 281.71  E-value: 6.73e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111818327   1 GTLYFIFGIWSGMMGSSLSMLIRLELSQINSIINNNQLYNVIVTIHAFIMIFFMTMPIVIGGFGNWLIPLMMGSPDMAFP 80
Cdd:MTH00182   18 GTLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFP 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111818327  81 RLNNISFWLLPPSLMMMICSFMINNGTGTGWTIYPPLSNNIAHNNISVDLTIFSLHLAGISSILGAINFICTILNMMPNN 160
Cdd:MTH00182   98 RLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPG 177

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1111818327 161 LKLNQIPLFPWSILITALLLILSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFW 221
Cdd:MTH00182  178 VTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFW 238
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-221 1.23e-92

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 280.56  E-value: 1.23e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111818327   1 GTLYFIFGIWSGMMGSSLSMLIRLELSQINSIINNNQLYNVIVTIHAFIMIFFMTMPIVIGGFGNWLIPLMMGSPDMAFP 80
Cdd:MTH00184   18 GTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFP 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111818327  81 RLNNISFWLLPPSLMMMICSFMINNGTGTGWTIYPPLSNNIAHNNISVDLTIFSLHLAGISSILGAINFICTILNMMPNN 160
Cdd:MTH00184   98 RLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPG 177

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1111818327 161 LKLNQIPLFPWSILITALLLILSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFW 221
Cdd:MTH00184  178 ITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFW 238
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-221 1.54e-83

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 257.63  E-value: 1.54e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111818327   1 GTLYFIFGIWSGMMGSSLSMLIRLELSQINSIINNNQLYNVIVTIHAFIMIFFMTMPIVIGGFGNWLIPLMMGSPDMAFP 80
Cdd:MTH00026   17 GSLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFP 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111818327  81 RLNNISFWLLPPSLMMMICSFMINNGTGTGWTIYPPLSNNIAHNNISVDLTIFSLHLAGISSILGAINFICTILNMMPNN 160
Cdd:MTH00026   97 RLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPG 176

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1111818327 161 LKLNQIPLFPWSILITALLLILSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFW 221
Cdd:MTH00026  177 MTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFW 237
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-221 1.32e-79

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: 245.52  E-value: 1.32e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111818327   1 GTLYFIFGIWSGMMGSSLSMLIRLELSQINSIINNNQLYNVIVTIHAFIMIFFMTMPIVIGGFGNWLIPlMMGSPDMAFP 80
Cdd:cd00919     5 GLLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111818327  81 RLNNISFWLLPPSLMMMICSFMINNGTGTGWTIYPPLSNNIAHNNISVDLTIFSLHLAGISSILGAINFICTILNMMPNN 160
Cdd:cd00919    84 RLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPG 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1111818327 161 LKLNQIPLFPWSILITALLLILSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFW 221
Cdd:cd00919   164 MTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFW 224
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-221 1.43e-69

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 221.54  E-value: 1.43e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111818327   1 GTLYFIFGIWSGMMGSSLSMLIRLELSQINSIINNNQLYNVIVTIHAFIMIFFMTMPIvIGGFGNWLIPLMMGSPDMAFP 80
Cdd:COG0843    19 GIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPF-LAGFGNYLVPLQIGARDMAFP 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111818327  81 RLNNISFWLLPPSLMMMICSFMINNGTGTGWTIYPPLSNNIAHNNISVDLTIFSLHLAGISSILGAINFICTILNMMPNN 160
Cdd:COG0843    98 RLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPG 177

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1111818327 161 LKLNQIPLFPWSILITALLLILSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFW 221
Cdd:COG0843   178 MTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFW 238
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-221 1.40e-65

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 210.69  E-value: 1.40e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111818327   1 GTLYFIFGIWSGMMGSSLSMLIRLELSQINSIINNNQLYNVIVTIHAFIMIFFMTMPIVIGGFGNWLIPLMMGSPDMAFP 80
Cdd:MTH00048   17 GVIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLP 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111818327  81 RLNNISFWLLPPSLMMMICSFMInnGTGTGWTIYPPLSNNIAHNNISVDLTIFSLHLAGISSILGAINFICTILNMMPNN 160
Cdd:MTH00048   97 RLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTN 174

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1111818327 161 LKLNqIPLFPWSILITALLLILSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFW 221
Cdd:MTH00048  175 VFSR-TSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFW 234
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-221 2.15e-52

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: 175.85  E-value: 2.15e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111818327   1 GTLYFIFGIWSGMMGSSLSMLIRLELSQINSIINNNQLYNVIVTIHAFIMIFFMTMPIVIGgFGNWLIPLMMGSPDMAFP 80
Cdd:cd01662    11 GIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFP 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111818327  81 RLNNISFWLLPPSLMMMICSFMINNGTGTGWTIYPPLSNNIAHNNISVDLTIFSLHLAGISSILGAINFICTILNMMPNN 160
Cdd:cd01662    90 RLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPG 169

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1111818327 161 LKLNQIPLFPWSILITALLLILSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFW 221
Cdd:cd01662   170 MTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFW 230
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-221 3.56e-43

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: 150.03  E-value: 3.56e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111818327   1 GTLYFIFGIWSGMMGSSLSMLIRLELSQINSIINNNQLYNVIVTIHAFIMIFFMTMPIvIGGFGNWLIPLMMGSPDMAFP 80
Cdd:pfam00115   3 GLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111818327  81 RLNNISFWLLPPSLMMMICSFMinnGTGTGWTIYPPLsnniahnnISVDLTIFSLHLAGISSILGAINFICTILNMMPNN 160
Cdd:pfam00115  82 RLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPG 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1111818327 161 LKLnQIPLFPWSILITALLLILSLPVLAGAITMLLTDRNLNTsffdpsGGGDPILYQHLFW 221
Cdd:pfam00115 151 MTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFW 204
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 1-221 1.06e-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: 129.97  E-value: 1.06e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111818327   1 GTLYFIFGIWSGMMGSSLSMLIRLELSQINSIINNNQLYNVIVTIHAFIMIFFMTMPIVIGgFGNWLIPLMMGSPDMAFP 80
Cdd:TIGR02882  54 GVMYIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFP 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111818327  81 RLNNISFWLLPPSLMMMICSFMINNGTGTGWTIYPPLSNNIAHNNISVDLTIFSLHLAGISSILGAINFICTILNMMPNN 160
Cdd:TIGR02882 133 VLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPG 212

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1111818327 161 LKLNQIPLFPWSILITALLLILSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFW 221
Cdd:TIGR02882 213 MKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFW 273
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 39-221 1.17e-30

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 118.50  E-value: 1.17e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111818327  39 YNVIVTIHAFIMIFFMTMPIVIGgFGNWLIPLMMGSPDMAFPRLNNISFWLLPPSLMMMICSFMINNGTGTGWTIYPPLS 118
Cdd:PRK15017   99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111818327 119 NNIAHNNISVDLTIFSLHLAGISSILGAINFICTILNMMPNNLKLNQIPLFPWSILITALLLILSLPVLAGAITMLLTDR 198
Cdd:PRK15017  178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257

                         170       180
                  ....*....|....*....|...
gi 1111818327 199 NLNTSFFDPSGGGDPILYQHLFW 221
Cdd:PRK15017  258 YLGTHFFTNDMGGNMMMYINLIW 280
 
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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