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Conserved domains on  [gi|301350664|gb|ADK74711|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Crucella hystrix]

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 ...
 1-217 3.17e-157

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: 444.70  E-value: 3.17e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301350664   1 NWLIPLMIGAPDMAFPRMNNMSFWLVPPSFVLLLTSASIENGAGTGWTIYPPLSSNIAHAGSSVDLAIFSLHLAGASSIL 80
Cdd:MTH00153  78 NWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSIL 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301350664  81 ASINFITTIINMRTPGVSFDRLPLFVWSVFITAFLLILSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFG 160
Cdd:MTH00153 158 GAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFG 237

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 301350664 161 HPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMAAIGILGFLVWAHHMFTVG 217
Cdd:MTH00153 238 HPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVG 294
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-217 3.17e-157

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 444.70  E-value: 3.17e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301350664   1 NWLIPLMIGAPDMAFPRMNNMSFWLVPPSFVLLLTSASIENGAGTGWTIYPPLSSNIAHAGSSVDLAIFSLHLAGASSIL 80
Cdd:MTH00153  78 NWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSIL 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301350664  81 ASINFITTIINMRTPGVSFDRLPLFVWSVFITAFLLILSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFG 160
Cdd:MTH00153 158 GAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFG 237

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 301350664 161 HPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMAAIGILGFLVWAHHMFTVG 217
Cdd:MTH00153 238 HPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVG 294
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-217 1.92e-154

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: 436.91  E-value: 1.92e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301350664   1 NWLIPLMIGAPDMAFPRMNNMSFWLVPPSFVLLLTSASIENGAGTGWTIYPPLSSNIAHAGSSVDLAIFSLHLAGASSIL 80
Cdd:cd01663   71 NWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSIL 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301350664  81 ASINFITTIINMRTPGVSFDRLPLFVWSVFITAFLLILSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFG 160
Cdd:cd01663  151 GAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFG 230

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 301350664 161 HPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMAAIGILGFLVWAHHMFTVG 217
Cdd:cd01663  231 HPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVG 287
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-217 9.18e-99

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


Pssm-ID: 213748  Cd Length: 499  Bit Score: 295.67  E-value: 9.18e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301350664    1 NWLIPLMIGAPDMAFPRMNNMSFWLVPPSFVLLLTSASIENGAGTGWTIYPPLSSNIAHAGSSVDLAIFSLHLAGASSIL 80
Cdd:TIGR02891  73 NYLLPLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSIL 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301350664   81 ASINFITTIINMRTPGVSFDRLPLFVWSVFITAFLLILSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFG 160
Cdd:TIGR02891 153 GAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFG 232

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 301350664  161 HPEVYILILPGFGMISHVIAHYSGKqEPFGYLGMVYAMAAIGILGFLVWAHHMFTVG 217
Cdd:TIGR02891 233 HPEVYIIFLPAFGIISEILPTFARK-PIFGYRAMVYATVAIGFLSFGVWAHHMFTTG 288
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-217 5.31e-98

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 294.73  E-value: 5.31e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301350664   1 NWLIPLMIGAPDMAFPRMNNMSFWLVPPSFVLLLTSASIENGAGTGWTIYPPLSSNIAHAGSSVDLAIFSLHLAGASSIL 80
Cdd:COG0843   82 NYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSIL 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301350664  81 ASINFITTIINMRTPGVSFDRLPLFVWSVFITAFLLILSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFG 160
Cdd:COG0843  162 GGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFG 241

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 301350664 161 HPEVYILILPGFGMISHVIAHYSGKqEPFGYLGMVYAMAAIGILGFLVWAHHMFTVG 217
Cdd:COG0843  242 HPEVYILILPAFGIVSEIIPTFSRK-PLFGYKAMVLATVAIAFLSFLVWAHHMFTPG 297
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-217 2.39e-61

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: 197.41  E-value: 2.39e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301350664    1 NWLIPLMIGAPDMAFPRMNNMSFWLVPPSFVLLLTSAsieNGAGTGWTIYPPLSSniahagssVDLAIFSLHLAGASSIL 80
Cdd:pfam00115  66 NYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLL 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301350664   81 ASINFITTIINMRTPGVSFdRLPLFVWSVFITAFLLILSLPVLAGAITMLLTDRNINttffdpAGGGDPILFQHLFWFFG 160
Cdd:pfam00115 135 GAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFG 207

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 301350664  161 HPEVYILILPGFGMISHVIAHYSGKqEPFGYLGMVYAMAAIGILGFLVWAHHMFTVG 217
Cdd:pfam00115 208 HPEVYILILPAFGIIYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTG 263
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-217 3.17e-157

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 444.70  E-value: 3.17e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301350664   1 NWLIPLMIGAPDMAFPRMNNMSFWLVPPSFVLLLTSASIENGAGTGWTIYPPLSSNIAHAGSSVDLAIFSLHLAGASSIL 80
Cdd:MTH00153  78 NWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSIL 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301350664  81 ASINFITTIINMRTPGVSFDRLPLFVWSVFITAFLLILSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFG 160
Cdd:MTH00153 158 GAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFG 237

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 301350664 161 HPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMAAIGILGFLVWAHHMFTVG 217
Cdd:MTH00153 238 HPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVG 294
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-217 1.92e-154

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: 436.91  E-value: 1.92e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301350664   1 NWLIPLMIGAPDMAFPRMNNMSFWLVPPSFVLLLTSASIENGAGTGWTIYPPLSSNIAHAGSSVDLAIFSLHLAGASSIL 80
Cdd:cd01663   71 NWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSIL 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301350664  81 ASINFITTIINMRTPGVSFDRLPLFVWSVFITAFLLILSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFG 160
Cdd:cd01663  151 GAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFG 230

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 301350664 161 HPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMAAIGILGFLVWAHHMFTVG 217
Cdd:cd01663  231 HPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVG 287
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-217 9.92e-143

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 407.91  E-value: 9.92e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301350664   1 NWLIPLMIGAPDMAFPRMNNMSFWLVPPSFVLLLTSASIENGAGTGWTIYPPLSSNIAHAGSSVDLAIFSLHLAGASSIL 80
Cdd:MTH00167  80 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSIL 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301350664  81 ASINFITTIINMRTPGVSFDRLPLFVWSVFITAFLLILSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFG 160
Cdd:MTH00167 160 GSINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 239

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 301350664 161 HPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMAAIGILGFLVWAHHMFTVG 217
Cdd:MTH00167 240 HPEVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVG 296
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-217 3.58e-141

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 404.09  E-value: 3.58e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301350664   1 NWLIPLMIGAPDMAFPRMNNMSFWLVPPSFVLLLTSASIENGAGTGWTIYPPLSSNIAHAGSSVDLAIFSLHLAGASSIL 80
Cdd:MTH00116  80 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSIL 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301350664  81 ASINFITTIINMRTPGVSFDRLPLFVWSVFITAFLLILSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFG 160
Cdd:MTH00116 160 GAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 239

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 301350664 161 HPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMAAIGILGFLVWAHHMFTVG 217
Cdd:MTH00116 240 HPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVG 296
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-217 4.99e-141

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 403.59  E-value: 4.99e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301350664   1 NWLIPLMIGAPDMAFPRMNNMSFWLVPPSFVLLLTSASIENGAGTGWTIYPPLSSNIAHAGSSVDLAIFSLHLAGASSIL 80
Cdd:MTH00223  77 NWLVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSIL 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301350664  81 ASINFITTIINMRTPGVSFDRLPLFVWSVFITAFLLILSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFG 160
Cdd:MTH00223 157 GAINFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFG 236

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 301350664 161 HPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMAAIGILGFLVWAHHMFTVG 217
Cdd:MTH00223 237 HPEVYILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVG 293
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-217 2.06e-139

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 399.97  E-value: 2.06e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301350664   1 NWLIPLMIGAPDMAFPRMNNMSFWLVPPSFVLLLTSASIENGAGTGWTIYPPLSSNIAHAGSSVDLAIFSLHLAGASSIL 80
Cdd:MTH00037  80 NWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSIL 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301350664  81 ASINFITTIINMRTPGVSFDRLPLFVWSVFITAFLLILSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFG 160
Cdd:MTH00037 160 ASINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFG 239

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 301350664 161 HPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMAAIGILGFLVWAHHMFTVG 217
Cdd:MTH00037 240 HPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVG 296
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-217 2.32e-137

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 394.48  E-value: 2.32e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301350664   1 NWLIPLMIGAPDMAFPRMNNMSFWLVPPSFVLLLTSASIENGAGTGWTIYPPLSSNIAHAGSSVDLAIFSLHLAGASSIL 80
Cdd:MTH00142  78 NWLVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSIL 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301350664  81 ASINFITTIINMRTPGVSFDRLPLFVWSVFITAFLLILSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFG 160
Cdd:MTH00142 158 GAINFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFG 237

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 301350664 161 HPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMAAIGILGFLVWAHHMFTVG 217
Cdd:MTH00142 238 HPEVYILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVG 294
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-217 2.87e-124

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 361.16  E-value: 2.87e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301350664   1 NWLIPLMIGAPDMAFPRMNNMSFWLVPPSFVLLLTSASIENGAGTGWTIYPPLSSNIAHAGSSVDLAIFSLHLAGASSIL 80
Cdd:MTH00183  80 NWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSIL 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301350664  81 ASINFITTIINMRTPGVSFDRLPLFVWSVFITAFLLILSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFG 160
Cdd:MTH00183 160 GAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 239

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 301350664 161 HPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMAAIGILGFLVWAHHMFTVG 217
Cdd:MTH00183 240 HPEVYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVG 296
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-217 9.35e-123

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 357.27  E-value: 9.35e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301350664   1 NWLIPLMIGAPDMAFPRMNNMSFWLVPPSFVLLLTSASIENGAGTGWTIYPPLSSNIAHAGSSVDLAIFSLHLAGASSIL 80
Cdd:MTH00103  80 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSIL 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301350664  81 ASINFITTIINMRTPGVSFDRLPLFVWSVFITAFLLILSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFG 160
Cdd:MTH00103 160 GAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 239

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 301350664 161 HPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMAAIGILGFLVWAHHMFTVG 217
Cdd:MTH00103 240 HPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVG 296
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-217 2.90e-122

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 356.13  E-value: 2.90e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301350664   1 NWLIPLMIGAPDMAFPRMNNMSFWLVPPSFVLLLTSASIENGAGTGWTIYPPLSSNIAHAGSSVDLAIFSLHLAGASSIL 80
Cdd:MTH00007  77 NWLVPLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSIL 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301350664  81 ASINFITTIINMRTPGVSFDRLPLFVWSVFITAFLLILSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFG 160
Cdd:MTH00007 157 GAINFITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFG 236

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 301350664 161 HPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMAAIGILGFLVWAHHMFTVG 217
Cdd:MTH00007 237 HPEVYILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVG 293
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-217 4.35e-121

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 353.09  E-value: 4.35e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301350664   1 NWLIPLMIGAPDMAFPRMNNMSFWLVPPSFVLLLTSASIENGAGTGWTIYPPLSSNIAHAGSSVDLAIFSLHLAGASSIL 80
Cdd:MTH00077  80 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSIL 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301350664  81 ASINFITTIINMRTPGVSFDRLPLFVWSVFITAFLLILSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFG 160
Cdd:MTH00077 160 GAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFG 239

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 301350664 161 HPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMAAIGILGFLVWAHHMFTVG 217
Cdd:MTH00077 240 HPEVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVD 296
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-217 4.80e-120

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 350.66  E-value: 4.80e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301350664   1 NWLIPLMIGAPDMAFPRMNNMSFWLVPPSFVLLLTSASIENGAGTGWTIYPPLSSNIAHAGSSVDLAIFSLHLAGASSIL 80
Cdd:MTH00182  82 NWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSIL 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301350664  81 ASINFITTIINMRTPGVSFDRLPLFVWSVFITAFLLILSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFG 160
Cdd:MTH00182 162 GAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFG 241

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 301350664 161 HPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMAAIGILGFLVWAHHMFTVG 217
Cdd:MTH00182 242 HPEVYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVG 298
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-217 2.96e-116

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 341.04  E-value: 2.96e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301350664   1 NWLIPLMIGAPDMAFPRMNNMSFWLVPPSFVLLLTSASIENGAGTGWTIYPPLSSNIAHAGSSVDLAIFSLHLAGASSIL 80
Cdd:MTH00184  82 NWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSIL 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301350664  81 ASINFITTIINMRTPGVSFDRLPLFVWSVFITAFLLILSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFG 160
Cdd:MTH00184 162 GAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFG 241

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 301350664 161 HPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMAAIGILGFLVWAHHMFTVG 217
Cdd:MTH00184 242 HPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVG 298
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-217 1.05e-110

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 326.25  E-value: 1.05e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301350664   1 NWLIPLMIGAPDMAFPRMNNMSFWLVPPSFVLLLTSASIENGAGTGWTIYPPLSSnIAHAGSSVDLAIFSLHLAGASSIL 80
Cdd:MTH00079  81 NWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSIL 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301350664  81 ASINFITTIINMRTPGVSFDRLPLFVWSVFITAFLLILSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFG 160
Cdd:MTH00079 160 GGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFG 239

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 301350664 161 HPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMAAIGILGFLVWAHHMFTVG 217
Cdd:MTH00079 240 HPEVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVG 296
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-217 2.05e-102

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 306.17  E-value: 2.05e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301350664   1 NWLIPLMIGAPDMAFPRMNNMSFWLVPPSFVLLLTSASIENGAGTGWTIYPPLSSNIAHAGSSVDLAIFSLHLAGASSIL 80
Cdd:MTH00026  81 NWFVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSIL 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301350664  81 ASINFITTIINMRTPGVSFDRLPLFVWSVFITAFLLILSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFG 160
Cdd:MTH00026 161 GAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFG 240

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 301350664 161 HPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMAAIGILGFLVWAHHMFTVG 217
Cdd:MTH00026 241 HPEVYILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVG 297
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-217 3.27e-99

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: 295.59  E-value: 3.27e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301350664   1 NWLIPLMIGAPDMAFPRMNNMSFWLVPPSFVLLLTSASIENGAGTGWTIYPPLSSNIAHAGSSVDLAIFSLHLAGASSIL 80
Cdd:cd00919   68 GNLLPPLIGARDLAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSIL 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301350664  81 ASINFITTIINMRTPGVSFDRLPLFVWSVFITAFLLILSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFG 160
Cdd:cd00919  148 GAINFITTILNMRAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFG 227

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 301350664 161 HPEVYILILPGFGMISHVIAHYSGKqEPFGYLGMVYAMAAIGILGFLVWAHHMFTVG 217
Cdd:cd00919  228 HPEVYILILPAFGAISEIIPTFSGK-PLFGYKLMVYAFLAIGFLSFLVWAHHMFTVG 283
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-217 9.18e-99

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


Pssm-ID: 213748  Cd Length: 499  Bit Score: 295.67  E-value: 9.18e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301350664    1 NWLIPLMIGAPDMAFPRMNNMSFWLVPPSFVLLLTSASIENGAGTGWTIYPPLSSNIAHAGSSVDLAIFSLHLAGASSIL 80
Cdd:TIGR02891  73 NYLLPLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSIL 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301350664   81 ASINFITTIINMRTPGVSFDRLPLFVWSVFITAFLLILSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFG 160
Cdd:TIGR02891 153 GAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFG 232

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 301350664  161 HPEVYILILPGFGMISHVIAHYSGKqEPFGYLGMVYAMAAIGILGFLVWAHHMFTVG 217
Cdd:TIGR02891 233 HPEVYIIFLPAFGIISEILPTFARK-PIFGYRAMVYATVAIGFLSFGVWAHHMFTTG 288
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-217 5.31e-98

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 294.73  E-value: 5.31e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301350664   1 NWLIPLMIGAPDMAFPRMNNMSFWLVPPSFVLLLTSASIENGAGTGWTIYPPLSSNIAHAGSSVDLAIFSLHLAGASSIL 80
Cdd:COG0843   82 NYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSIL 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301350664  81 ASINFITTIINMRTPGVSFDRLPLFVWSVFITAFLLILSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFG 160
Cdd:COG0843  162 GGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFG 241

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 301350664 161 HPEVYILILPGFGMISHVIAHYSGKqEPFGYLGMVYAMAAIGILGFLVWAHHMFTVG 217
Cdd:COG0843  242 HPEVYILILPAFGIVSEIIPTFSRK-PLFGYKAMVLATVAIAFLSFLVWAHHMFTPG 297
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-217 2.66e-88

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 269.24  E-value: 2.66e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301350664   1 NWLIPLMIGAPDMAFPRMNNMSFWLVPPSFVLLLTSASIenGAGTGWTIYPPLSSNIAHAGSSVDLAIFSLHLAGASSIL 80
Cdd:MTH00048  81 NYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLF 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301350664  81 ASINFITTIINMRTPGVSFdRLPLFVWSVFITAFLLILSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFG 160
Cdd:MTH00048 159 GSINFICTIYSAFMTNVFS-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFG 237

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 301350664 161 HPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMAAIGILGFLVWAHHMFTVG 217
Cdd:MTH00048 238 HPEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVG 294
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-217 5.92e-83

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: 255.20  E-value: 5.92e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301350664   1 NWLIPLMIGAPDMAFPRMNNMSFWLVPPSFVLLLTSASIENGAGTGWTIYPPLSSNIAHAGSSVDLAIFSLHLAGASSIL 80
Cdd:cd01662   74 NYLVPLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLL 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301350664  81 ASINFITTIINMRTPGVSFDRLPLFVWSVFITAFLLILSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFG 160
Cdd:cd01662  154 GAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFG 233

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 301350664 161 HPEVYILILPGFGMISHVIAHYSGKQePFGYLGMVYAMAAIGILGFLVWAHHMFTVG 217
Cdd:cd01662  234 HPEVYILILPAFGIFSEIVPTFSRKP-LFGYRSMVYATVAIGFLSFGVWVHHMFTTG 289
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-217 2.39e-61

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: 197.41  E-value: 2.39e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301350664    1 NWLIPLMIGAPDMAFPRMNNMSFWLVPPSFVLLLTSAsieNGAGTGWTIYPPLSSniahagssVDLAIFSLHLAGASSIL 80
Cdd:pfam00115  66 NYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLL 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301350664   81 ASINFITTIINMRTPGVSFdRLPLFVWSVFITAFLLILSLPVLAGAITMLLTDRNINttffdpAGGGDPILFQHLFWFFG 160
Cdd:pfam00115 135 GAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFG 207

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 301350664  161 HPEVYILILPGFGMISHVIAHYSGKqEPFGYLGMVYAMAAIGILGFLVWAHHMFTVG 217
Cdd:pfam00115 208 HPEVYILILPAFGIIYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTG 263
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 1-217 5.27e-53

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: 180.05  E-value: 5.27e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301350664    1 NWLIPLMIGAPDMAFPRMNNMSFWLVPPSFVLLLTSASIENGAGTGWTIYPPLSSNIAHAGSSVDLAIFSLHLAGASSIL 80
Cdd:TIGR02882 117 NIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLM 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301350664   81 ASINFITTIINMRTPGVSFDRLPLFVWSVFITAFLLILSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFG 160
Cdd:TIGR02882 197 TGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWG 276

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 301350664  161 HPEVYILILPGFGMISHVIAHYSGKQePFGYLGMVYAMAAIGILGFLVWAHHMFTVG 217
Cdd:TIGR02882 277 HPEVYIVILPAFGIYSEIISTFAQKR-LFGYKSMVWSTVGIAFLSFLVWVHHFFTMG 332
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 1-217 5.56e-53

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 180.13  E-value: 5.56e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301350664   1 NWLIPLMIGAPDMAFPRMNNMSFWLVPPSFVLLLTSASIENGAGTGWTIYPPLSSNIAHAGSSVDLAIFSLHLAGASSIL 80
Cdd:PRK15017 124 NLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTL 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301350664  81 ASINFITTIINMRTPGVSFDRLPLFVWSVFITAFLLILSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFG 160
Cdd:PRK15017 204 TGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWG 283

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 301350664 161 HPEVYILILPGFGMISHVIAHYSgKQEPFGYLGMVYAMAAIGILGFLVWAHHMFTVG 217
Cdd:PRK15017 284 HPEVYILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFFTMG 339
 
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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