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Conserved domains on  [gi|1280074445|gb|ATY36925|]
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cytochrome c oxidase subunit 1, partial (mitochondrion) [Sinipta hectorisperonii]

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 ...
 1-212 1.94e-133

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


The actual alignment was detected with superfamily member MTH00153:

Pssm-ID: 469701  Cd Length: 511  Bit Score: 384.22  E-value: 1.94e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280074445   1 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDMGAGTGWTVYPPLAGA*AHGGASVDLAIFSLHLAGVSSIL 80
Cdd:MTH00153   78 NWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSIL 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280074445  81 GAVNFITTAINMRSESMTLDQTPL*VWSVAITALLLLLSLPVLAGAITMLL*DRNLNTSFFDPAGGGDPILYQHLFWFFG 160
Cdd:MTH00153  158 GAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFG 237

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1280074445 161 HPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHH 212
Cdd:MTH00153  238 HPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHH 289
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-212 1.94e-133

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 384.22  E-value: 1.94e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280074445   1 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDMGAGTGWTVYPPLAGA*AHGGASVDLAIFSLHLAGVSSIL 80
Cdd:MTH00153   78 NWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSIL 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280074445  81 GAVNFITTAINMRSESMTLDQTPL*VWSVAITALLLLLSLPVLAGAITMLL*DRNLNTSFFDPAGGGDPILYQHLFWFFG 160
Cdd:MTH00153  158 GAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFG 237

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1280074445 161 HPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHH 212
Cdd:MTH00153  238 HPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHH 289
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-212 5.64e-121

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: 351.79  E-value: 5.64e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280074445   1 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDMGAGTGWTVYPPLAGA*AHGGASVDLAIFSLHLAGVSSIL 80
Cdd:cd01663    71 NWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSIL 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280074445  81 GAVNFITTAINMRSESMTLDQTPL*VWSVAITALLLLLSLPVLAGAITMLL*DRNLNTSFFDPAGGGDPILYQHLFWFFG 160
Cdd:cd01663   151 GAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFG 230

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1280074445 161 HPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHH 212
Cdd:cd01663   231 HPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHH 282
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-212 5.75e-78

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: 241.74  E-value: 5.75e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280074445   1 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDMGAGTGWTVYPPLAGA*AHGGASVDLAIFSLHLAGVSSIL 80
Cdd:TIGR02891  73 NYLLPLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSIL 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280074445  81 GAVNFITTAINMRSESMTLDQTPL*VWSVAITALLLLLSLPVLAGAITMLL*DRNLNTSFFDPAGGGDPILYQHLFWFFG 160
Cdd:TIGR02891 153 GAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFG 232

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1280074445 161 HPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHH 212
Cdd:TIGR02891 233 HPEVYIIFLPAFGIISEILPTFARK-PIFGYRAMVYATVAIGFLSFGVWAHH 283
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-212 7.39e-76

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 237.33  E-value: 7.39e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280074445   1 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDMGAGTGWTVYPPLAGA*AHGGASVDLAIFSLHLAGVSSIL 80
Cdd:COG0843    82 NYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSIL 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280074445  81 GAVNFITTAINMRSESMTLDQTPL*VWSVAITALLLLLSLPVLAGAITMLL*DRNLNTSFFDPAGGGDPILYQHLFWFFG 160
Cdd:COG0843   162 GGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFG 241

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1280074445 161 HPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHH 212
Cdd:COG0843   242 HPEVYILILPAFGIVSEIIPTFSRK-PLFGYKAMVLATVAIAFLSFLVWAHH 292
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-212 2.31e-48

Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key enzyme in aerobic metabolism. Proton pumping haem-copper oxidases represent the terminal, energy-transfer enzymes of respiratory chains in prokaryotes and eukaryotes. The CuB-haem a3 (or haem o) binuclear centre, associated with the largest subunit I of cytochrome c and ubiquinol oxidases (E.C:1.10.3.11), is directly involved in the coupling between dioxygen reduction and proton pumping. Some terminal oxidases generate a transmembrane proton gradient across the plasma membrane (prokaryotes) or the mitochondrial inner membrane (eukaryotes). The enzyme complex consists of 3-4 subunits (prokaryotes) up to 13 polypeptides (mammals) of which only the catalytic subunit (equivalent to mammalian subunit I (COXI) is found in all haem-copper respiratory oxidases. The presence of a bimetallic centre (formed by a high-spin haem and copper B) as well as a low-spin haem, both ligated to six conserved histidine residues near the outer side of four transmembrane spans within CO I is common to all family members.


Pssm-ID: 459678  Cd Length: 432  Bit Score: 163.51  E-value: 2.31e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280074445   1 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMvdmGAGTGWTVYPPLAga*ahggaSVDLAIFSLHLAGVSSIL 80
Cdd:pfam00115  66 NYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPLV--------GVDLWYIGLLLAGVSSLL 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280074445  81 GAVNFITTAINMRSESMTLdQTPL*VWSVAITALLLLLSLPVLAGAITMLL*DRNLNtsffdpAGGGDPILYQHLFWFFG 160
Cdd:pfam00115 135 GAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFG 207

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1280074445 161 HPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHH 212
Cdd:pfam00115 208 HPEVYILILPAFGIIYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHH 258
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-212 1.94e-133

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 384.22  E-value: 1.94e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280074445   1 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDMGAGTGWTVYPPLAGA*AHGGASVDLAIFSLHLAGVSSIL 80
Cdd:MTH00153   78 NWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSIL 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280074445  81 GAVNFITTAINMRSESMTLDQTPL*VWSVAITALLLLLSLPVLAGAITMLL*DRNLNTSFFDPAGGGDPILYQHLFWFFG 160
Cdd:MTH00153  158 GAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFG 237

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1280074445 161 HPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHH 212
Cdd:MTH00153  238 HPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHH 289
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-212 5.64e-121

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: 351.79  E-value: 5.64e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280074445   1 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDMGAGTGWTVYPPLAGA*AHGGASVDLAIFSLHLAGVSSIL 80
Cdd:cd01663    71 NWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSIL 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280074445  81 GAVNFITTAINMRSESMTLDQTPL*VWSVAITALLLLLSLPVLAGAITMLL*DRNLNTSFFDPAGGGDPILYQHLFWFFG 160
Cdd:cd01663   151 GAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFG 230

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1280074445 161 HPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHH 212
Cdd:cd01663   231 HPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHH 282
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-212 1.17e-111

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 328.86  E-value: 1.17e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280074445   1 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDMGAGTGWTVYPPLAGA*AHGGASVDLAIFSLHLAGVSSIL 80
Cdd:MTH00223   77 NWLVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSIL 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280074445  81 GAVNFITTAINMRSESMTLDQTPL*VWSVAITALLLLLSLPVLAGAITMLL*DRNLNTSFFDPAGGGDPILYQHLFWFFG 160
Cdd:MTH00223  157 GAINFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFG 236

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1280074445 161 HPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHH 212
Cdd:MTH00223  237 HPEVYILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHH 288
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-212 3.89e-110

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 324.71  E-value: 3.89e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280074445   1 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDMGAGTGWTVYPPLAGA*AHGGASVDLAIFSLHLAGVSSIL 80
Cdd:MTH00167   80 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSIL 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280074445  81 GAVNFITTAINMRSESMTLDQTPL*VWSVAITALLLLLSLPVLAGAITMLL*DRNLNTSFFDPAGGGDPILYQHLFWFFG 160
Cdd:MTH00167  160 GSINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 239

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1280074445 161 HPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHH 212
Cdd:MTH00167  240 HPEVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHH 291
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-212 8.51e-110

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 323.97  E-value: 8.51e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280074445   1 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDMGAGTGWTVYPPLAGA*AHGGASVDLAIFSLHLAGVSSIL 80
Cdd:MTH00116   80 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSIL 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280074445  81 GAVNFITTAINMRSESMTLDQTPL*VWSVAITALLLLLSLPVLAGAITMLL*DRNLNTSFFDPAGGGDPILYQHLFWFFG 160
Cdd:MTH00116  160 GAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 239

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1280074445 161 HPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHH 212
Cdd:MTH00116  240 HPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHH 291
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-212 3.31e-109

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 322.44  E-value: 3.31e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280074445   1 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDMGAGTGWTVYPPLAGA*AHGGASVDLAIFSLHLAGVSSIL 80
Cdd:MTH00142   78 NWLVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSIL 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280074445  81 GAVNFITTAINMRSESMTLDQTPL*VWSVAITALLLLLSLPVLAGAITMLL*DRNLNTSFFDPAGGGDPILYQHLFWFFG 160
Cdd:MTH00142  158 GAINFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFG 237

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1280074445 161 HPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHH 212
Cdd:MTH00142  238 HPEVYILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHH 289
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-212 3.46e-100

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 299.51  E-value: 3.46e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280074445   1 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDMGAGTGWTVYPPLAGA*AHGGASVDLAIFSLHLAGVSSIL 80
Cdd:MTH00007   77 NWLVPLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSIL 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280074445  81 GAVNFITTAINMRSESMTLDQTPL*VWSVAITALLLLLSLPVLAGAITMLL*DRNLNTSFFDPAGGGDPILYQHLFWFFG 160
Cdd:MTH00007  157 GAINFITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFG 236

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1280074445 161 HPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHH 212
Cdd:MTH00007  237 HPEVYILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHH 288
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-212 9.74e-99

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 295.70  E-value: 9.74e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280074445   1 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDMGAGTGWTVYPPLAGA*AHGGASVDLAIFSLHLAGVSSIL 80
Cdd:MTH00077   80 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSIL 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280074445  81 GAVNFITTAINMRSESMTLDQTPL*VWSVAITALLLLLSLPVLAGAITMLL*DRNLNTSFFDPAGGGDPILYQHLFWFFG 160
Cdd:MTH00077  160 GAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFG 239

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1280074445 161 HPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHH 212
Cdd:MTH00077  240 HPEVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHH 291
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-212 4.69e-98

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 294.10  E-value: 4.69e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280074445   1 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDMGAGTGWTVYPPLAGA*AHGGASVDLAIFSLHLAGVSSIL 80
Cdd:MTH00103   80 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSIL 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280074445  81 GAVNFITTAINMRSESMTLDQTPL*VWSVAITALLLLLSLPVLAGAITMLL*DRNLNTSFFDPAGGGDPILYQHLFWFFG 160
Cdd:MTH00103  160 GAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 239

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1280074445 161 HPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHH 212
Cdd:MTH00103  240 HPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHH 291
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-212 5.05e-96

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 289.04  E-value: 5.05e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280074445   1 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDMGAGTGWTVYPPLAGA*AHGGASVDLAIFSLHLAGVSSIL 80
Cdd:MTH00037   80 NWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSIL 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280074445  81 GAVNFITTAINMRSESMTLDQTPL*VWSVAITALLLLLSLPVLAGAITMLL*DRNLNTSFFDPAGGGDPILYQHLFWFFG 160
Cdd:MTH00037  160 ASINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFG 239

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1280074445 161 HPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHH 212
Cdd:MTH00037  240 HPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHH 291
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-212 8.08e-96

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 288.36  E-value: 8.08e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280074445   1 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDMGAGTGWTVYPPLAGA*AHGGASVDLAIFSLHLAGVSSIL 80
Cdd:MTH00183   80 NWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSIL 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280074445  81 GAVNFITTAINMRSESMTLDQTPL*VWSVAITALLLLLSLPVLAGAITMLL*DRNLNTSFFDPAGGGDPILYQHLFWFFG 160
Cdd:MTH00183  160 GAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 239

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1280074445 161 HPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHH 212
Cdd:MTH00183  240 HPEVYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHH 291
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-212 3.38e-95

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 286.58  E-value: 3.38e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280074445   1 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDMGAGTGWTVYPPLAGA*AHGGaSVDLAIFSLHLAGVSSIL 80
Cdd:MTH00079   81 NWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLSTLGHPGS-SVDLAIFSLHCAGISSIL 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280074445  81 GAVNFITTAINMRSESMTLDQTPL*VWSVAITALLLLLSLPVLAGAITMLL*DRNLNTSFFDPAGGGDPILYQHLFWFFG 160
Cdd:MTH00079  160 GGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFG 239

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1280074445 161 HPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHH 212
Cdd:MTH00079  240 HPEVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHH 291
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-212 1.20e-91

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 277.86  E-value: 1.20e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280074445   1 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDMGAGTGWTVYPPLAGA*AHGGASVDLAIFSLHLAGVSSIL 80
Cdd:MTH00182   82 NWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSIL 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280074445  81 GAVNFITTAINMRSESMTLDQTPL*VWSVAITALLLLLSLPVLAGAITMLL*DRNLNTSFFDPAGGGDPILYQHLFWFFG 160
Cdd:MTH00182  162 GAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFG 241

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1280074445 161 HPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHH 212
Cdd:MTH00182  242 HPEVYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHH 293
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-212 2.77e-90

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 274.40  E-value: 2.77e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280074445   1 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDMGAGTGWTVYPPLAGA*AHGGASVDLAIFSLHLAGVSSIL 80
Cdd:MTH00184   82 NWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSIL 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280074445  81 GAVNFITTAINMRSESMTLDQTPL*VWSVAITALLLLLSLPVLAGAITMLL*DRNLNTSFFDPAGGGDPILYQHLFWFFG 160
Cdd:MTH00184  162 GAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFG 241

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1280074445 161 HPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHH 212
Cdd:MTH00184  242 HPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHH 293
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-212 5.44e-84

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 258.40  E-value: 5.44e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280074445   1 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDMGAGTGWTVYPPLAGA*AHGGASVDLAIFSLHLAGVSSIL 80
Cdd:MTH00026   81 NWFVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSIL 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280074445  81 GAVNFITTAINMRSESMTLDQTPL*VWSVAITALLLLLSLPVLAGAITMLL*DRNLNTSFFDPAGGGDPILYQHLFWFFG 160
Cdd:MTH00026  161 GAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFG 240

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1280074445 161 HPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHH 212
Cdd:MTH00026  241 HPEVYILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHH 292
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-212 1.46e-78

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: 242.44  E-value: 1.46e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280074445   1 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDMGAGTGWTVYPPLAGA*AHGGASVDLAIFSLHLAGVSSIL 80
Cdd:cd00919    68 GNLLPPLIGARDLAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSIL 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280074445  81 GAVNFITTAINMRSESMTLDQTPL*VWSVAITALLLLLSLPVLAGAITMLL*DRNLNTSFFDPAGGGDPILYQHLFWFFG 160
Cdd:cd00919   148 GAINFITTILNMRAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFG 227

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1280074445 161 HPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHH 212
Cdd:cd00919   228 HPEVYILILPAFGAISEIIPTFSGK-PLFGYKLMVYAFLAIGFLSFLVWAHH 278
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-212 5.75e-78

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: 241.74  E-value: 5.75e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280074445   1 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDMGAGTGWTVYPPLAGA*AHGGASVDLAIFSLHLAGVSSIL 80
Cdd:TIGR02891  73 NYLLPLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSIL 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280074445  81 GAVNFITTAINMRSESMTLDQTPL*VWSVAITALLLLLSLPVLAGAITMLL*DRNLNTSFFDPAGGGDPILYQHLFWFFG 160
Cdd:TIGR02891 153 GAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFG 232

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1280074445 161 HPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHH 212
Cdd:TIGR02891 233 HPEVYIIFLPAFGIISEILPTFARK-PIFGYRAMVYATVAIGFLSFGVWAHH 283
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-212 7.39e-76

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 237.33  E-value: 7.39e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280074445   1 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDMGAGTGWTVYPPLAGA*AHGGASVDLAIFSLHLAGVSSIL 80
Cdd:COG0843    82 NYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSIL 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280074445  81 GAVNFITTAINMRSESMTLDQTPL*VWSVAITALLLLLSLPVLAGAITMLL*DRNLNTSFFDPAGGGDPILYQHLFWFFG 160
Cdd:COG0843   162 GGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFG 241

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1280074445 161 HPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHH 212
Cdd:COG0843   242 HPEVYILILPAFGIVSEIIPTFSRK-PLFGYKAMVLATVAIAFLSFLVWAHH 292
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-212 1.10e-67

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 215.70  E-value: 1.10e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280074445   1 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMvdMGAGTGWTVYPPLAGA*AHGGASVDLAIFSLHLAGVSSIL 80
Cdd:MTH00048   81 NYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMC--LGAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLF 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280074445  81 GAVNFITTAINMRSESMTLdQTPL*VWSVAITALLLLLSLPVLAGAITMLL*DRNLNTSFFDPAGGGDPILYQHLFWFFG 160
Cdd:MTH00048  159 GSINFICTIYSAFMTNVFS-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFG 237

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1280074445 161 HPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHH 212
Cdd:MTH00048  238 HPEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHH 289
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-212 5.47e-66

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: 210.90  E-value: 5.47e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280074445   1 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDMGAGTGWTVYPPLAGA*AHGGASVDLAIFSLHLAGVSSIL 80
Cdd:cd01662    74 NYLVPLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLL 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280074445  81 GAVNFITTAINMRSESMTLDQTPL*VWSVAITALLLLLSLPVLAGAITMLL*DRNLNTSFFDPAGGGDPILYQHLFWFFG 160
Cdd:cd01662   154 GAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFG 233

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1280074445 161 HPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHH 212
Cdd:cd01662   234 HPEVYILILPAFGIFSEIVPTFSRK-PLFGYRSMVYATVAIGFLSFGVWVHH 284
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-212 2.31e-48

Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key enzyme in aerobic metabolism. Proton pumping haem-copper oxidases represent the terminal, energy-transfer enzymes of respiratory chains in prokaryotes and eukaryotes. The CuB-haem a3 (or haem o) binuclear centre, associated with the largest subunit I of cytochrome c and ubiquinol oxidases (E.C:1.10.3.11), is directly involved in the coupling between dioxygen reduction and proton pumping. Some terminal oxidases generate a transmembrane proton gradient across the plasma membrane (prokaryotes) or the mitochondrial inner membrane (eukaryotes). The enzyme complex consists of 3-4 subunits (prokaryotes) up to 13 polypeptides (mammals) of which only the catalytic subunit (equivalent to mammalian subunit I (COXI) is found in all haem-copper respiratory oxidases. The presence of a bimetallic centre (formed by a high-spin haem and copper B) as well as a low-spin haem, both ligated to six conserved histidine residues near the outer side of four transmembrane spans within CO I is common to all family members.


Pssm-ID: 459678  Cd Length: 432  Bit Score: 163.51  E-value: 2.31e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280074445   1 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMvdmGAGTGWTVYPPLAga*ahggaSVDLAIFSLHLAGVSSIL 80
Cdd:pfam00115  66 NYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPLV--------GVDLWYIGLLLAGVSSLL 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280074445  81 GAVNFITTAINMRSESMTLdQTPL*VWSVAITALLLLLSLPVLAGAITMLL*DRNLNtsffdpAGGGDPILYQHLFWFFG 160
Cdd:pfam00115 135 GAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFG 207

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1280074445 161 HPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHH 212
Cdd:pfam00115 208 HPEVYILILPAFGIIYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHH 258
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 1-212 8.92e-40

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 143.92  E-value: 8.92e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280074445   1 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDMGAGTGWTVYPPLAGA*AHGGASVDLAIFSLHLAGVSSIL 80
Cdd:PRK15017  124 NLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTL 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280074445  81 GAVNFITTAINMRSESMTLDQTPL*VWSVAITALLLLLSLPVLAGAITMLL*DRNLNTSFFDPAGGGDPILYQHLFWFFG 160
Cdd:PRK15017  204 TGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWG 283

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1280074445 161 HPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHH 212
Cdd:PRK15017  284 HPEVYILILPVFGVFSEIAATFSRK-RLFGYTSLVWATVCITVLSFIVWLHH 334
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 1-212 7.10e-39

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: 141.14  E-value: 7.10e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280074445   1 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDMGAGTGWTVYPPLAGA*AHGGASVDLAIFSLHLAGVSSIL 80
Cdd:TIGR02882 117 NIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLM 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280074445  81 GAVNFITTAINMRSESMTLDQTPL*VWSVAITALLLLLSLPVLAGAITMLL*DRNLNTSFFDPAGGGDPILYQHLFWFFG 160
Cdd:TIGR02882 197 TGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWG 276

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1280074445 161 HPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHH 212
Cdd:TIGR02882 277 HPEVYIVILPAFGIYSEIISTFAQK-RLFGYKSMVWSTVGIAFLSFLVWVHH 327
 
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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