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Conserved domains on  [gi|90655160|gb|ABD96107|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Ceracris hoffmanni]

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 2.44e-143

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: 409.26  E-value: 2.44e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90655160    1 RAYFTSATMIIAVPTGIKVFSWMATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVL 80
Cdd:MTH00153 300 RAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVL 379

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90655160   81 SMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFTIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTIS 160
Cdd:MTH00153 380 SMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTIS 459

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 90655160  161 IVGIIMFIVIMWESMITNRTIMFSANMNSSTEWLQNNPPAEHSYSELPLISS 212
Cdd:MTH00153 460 LISILFFIFIIWESMISKRPVLFSLNLSSSIEWLQNLPPAEHSYSELPLLTN 511
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-212 2.44e-143

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 409.26  E-value: 2.44e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90655160    1 RAYFTSATMIIAVPTGIKVFSWMATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVL 80
Cdd:MTH00153 300 RAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVL 379

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90655160   81 SMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFTIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTIS 160
Cdd:MTH00153 380 SMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTIS 459

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 90655160  161 IVGIIMFIVIMWESMITNRTIMFSANMNSSTEWLQNNPPAEHSYSELPLISS 212
Cdd:MTH00153 460 LISILFFIFIIWESMISKRPVLFSLNLSSSIEWLQNLPPAEHSYSELPLLTN 511
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-195 3.16e-109

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: 321.74  E-value: 3.16e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90655160   1 RAYFTSATMIIAVPTGIKVFSWMATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVL 80
Cdd:cd01663 293 RAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVL 372

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90655160  81 SMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFTIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTIS 160
Cdd:cd01663 373 SMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLIS 452

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 90655160 161 IVGIIMFIVIMWESMITNRTIMFSANMNSST-EWLQ 195
Cdd:cd01663 453 FVSVLLFLFIVWESFVSGRKVIFNVGEGSTSlEWTL 488
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-212 8.34e-70

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 221.92  E-value: 8.34e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90655160   1 RAYFTSATMIIAVPTGIKVFSWMATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVL 80
Cdd:COG0843 303 KAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVL 382

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90655160  81 SMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFTIMFVGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTSWNVISSIGST 158
Cdd:COG0843 383 IGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAF 462

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 90655160 159 ISIVGIIMFIVIMWESMITNRTImfSAN-MNSST-EWLQNNPPAEHSYSELPLISS 212
Cdd:COG0843 463 ILAVGFLLFLINLVVSLRKGPKA--GGNpWGARTlEWATPSPPPLYNFASIPVVRS 516
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-204 2.32e-65

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: 209.39  E-value: 2.32e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90655160     1 RAYFTSATMIIAVPTGIKVFSWMATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVL 80
Cdd:TIGR02891 294 LAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVL 373

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90655160    81 SMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFTIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDA--YTSWNVISSIGST 158
Cdd:TIGR02891 374 VGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAF 453

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 90655160   159 ISIVGIIMFIVIMWESMITNRtiMFSANMNSST--EWLQNNPPAEHSY 204
Cdd:TIGR02891 454 ILAAGFLVFLWNLIWSLRKGP--KAGANPWGATtlEWTTSSPPPAHNF 499
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-141 6.17e-46

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


Pssm-ID: 459678  Cd Length: 432  Bit Score: 156.96  E-value: 6.17e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90655160     1 RAYFTSATMIIAVPTGIKVFSWMATLYGTKFKFN-PPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYV 79
Cdd:pfam00115 269 QALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFRtTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYV 348

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90655160    80 LSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFTIMFVGVNLTFFPQHFLGLAGMPRRYSD 141
Cdd:pfam00115 349 LFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAP 410
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-212 2.44e-143

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 409.26  E-value: 2.44e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90655160    1 RAYFTSATMIIAVPTGIKVFSWMATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVL 80
Cdd:MTH00153 300 RAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVL 379

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90655160   81 SMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFTIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTIS 160
Cdd:MTH00153 380 SMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTIS 459

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 90655160  161 IVGIIMFIVIMWESMITNRTIMFSANMNSSTEWLQNNPPAEHSYSELPLISS 212
Cdd:MTH00153 460 LISILFFIFIIWESMISKRPVLFSLNLSSSIEWLQNLPPAEHSYSELPLLTN 511
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-210 3.60e-111

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 327.40  E-value: 3.60e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90655160    1 RAYFTSATMIIAVPTGIKVFSWMATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVL 80
Cdd:MTH00167 302 RAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVL 381

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90655160   81 SMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFTIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTIS 160
Cdd:MTH00167 382 SMGAVFAIMAGFTHWFPLFTGLTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLIS 461

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 90655160  161 IVGIIMFIVIMWESMITNRTIMFSANMNSSTEWLQNNPPAEHSYSELPLI 210
Cdd:MTH00167 462 LVAVILFLFIIWEAFSSKRKLLPVELTSTNVEWLHGCPPPHHTWEEPPFV 511
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-210 1.52e-109

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 323.58  E-value: 1.52e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90655160    1 RAYFTSATMIIAVPTGIKVFSWMATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVL 80
Cdd:MTH00116 302 RAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVL 381

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90655160   81 SMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFTIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTIS 160
Cdd:MTH00116 382 SMGAVFAIMAGFTHWFPLFTGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLIS 461

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 90655160  161 IVGIIMFIVIMWESMITNRTIMFSANMNSSTEWLQNNPPAEHSYSELPLI 210
Cdd:MTH00116 462 MTAVIMLMFIIWEAFSSKRKVLQPELTTTNIEWIHGCPPPYHTFEEPAFV 511
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-195 3.16e-109

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: 321.74  E-value: 3.16e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90655160   1 RAYFTSATMIIAVPTGIKVFSWMATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVL 80
Cdd:cd01663 293 RAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVL 372

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90655160  81 SMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFTIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTIS 160
Cdd:cd01663 373 SMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLIS 452

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 90655160 161 IVGIIMFIVIMWESMITNRTIMFSANMNSST-EWLQ 195
Cdd:cd01663 453 FVSVLLFLFIVWESFVSGRKVIFNVGEGSTSlEWTL 488
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-210 1.64e-108

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 320.52  E-value: 1.64e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90655160    1 RAYFTSATMIIAVPTGIKVFSWMATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVL 80
Cdd:MTH00142 300 RAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVL 379

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90655160   81 SMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFTIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTIS 160
Cdd:MTH00142 380 SMGAVFALFAGFIHWFPLFTGLTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMIS 459

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 90655160  161 IVGIIMFIVIMWESMITNRTIMFSANMNSSTEWLQNNPPAEHSYSELPLI 210
Cdd:MTH00142 460 FIAVLMFVFIVWESFVSQRLVMWSSHLSTSLEWSHRLPPDFHTYDELPIL 509
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-210 1.24e-107

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 318.46  E-value: 1.24e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90655160    1 RAYFTSATMIIAVPTGIKVFSWMATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVL 80
Cdd:MTH00223 299 RAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVL 378

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90655160   81 SMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFTIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTIS 160
Cdd:MTH00223 379 SMGAVFALFAGFNHWFPLFTGVTLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMIS 458

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 90655160  161 IVGIIMFIVIMWESMITNRTIMFSANMNSSTEWLQNNPPAEHSYSELPLI 210
Cdd:MTH00223 459 FVSVLFFMFIVWEAFVSQRSVVWSGHLSTSLEWDNLLPADFHNNSETGAL 508
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-212 9.27e-95

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 285.62  E-value: 9.27e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90655160    1 RAYFTSATMIIAVPTGIKVFSWMATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVL 80
Cdd:MTH00103 302 RAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVL 381

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90655160   81 SMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFTIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTIS 160
Cdd:MTH00103 382 SMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFIS 461

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 90655160  161 IVGIIMFIVIMWESMITNRTIMFSANMNSSTEWLQNNPPAEHSYSELPLISS 212
Cdd:MTH00103 462 LTAVMLMIFMIWEAFASKREVLTVELTTTNLEWLHGCPPPYHTFEEPTYVKL 513
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-210 1.15e-94

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 285.66  E-value: 1.15e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90655160    1 RAYFTSATMIIAVPTGIKVFSWMATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVL 80
Cdd:MTH00183 302 RAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVL 381

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90655160   81 SMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFTIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTIS 160
Cdd:MTH00183 382 SMGAVFAIMAAFVHWFPLFSGYTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLIS 461

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 90655160  161 IVGIIMFIVIMWESMITNRTIMFSANMNSSTEWLQNNPPAEHSYSELPLI 210
Cdd:MTH00183 462 LVAVIMFLFILWEAFAAKREVLSVELTSTNVEWLHGCPPPYHTFEEPAFV 511
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-206 1.29e-92

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 280.29  E-value: 1.29e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90655160    1 RAYFTSATMIIAVPTGIKVFSWMATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVL 80
Cdd:MTH00077 302 RAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVL 381

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90655160   81 SMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFTIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTIS 160
Cdd:MTH00077 382 SMGAVFAIMGGFVHWFPLFSGYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLIS 461

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 90655160  161 IVGIIMFIVIMWESMITNRTIMFSANMNSSTEWLQNNPPAEHSYSE 206
Cdd:MTH00077 462 LVAVIMMMFIIWEAFSSKREVLTTELTSTNIEWLHGCPPPYHTFEE 507
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-209 1.92e-92

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 279.79  E-value: 1.92e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90655160    1 RAYFTSATMIIAVPTGIKVFSWMATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVL 80
Cdd:MTH00037 302 RAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVL 381

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90655160   81 SMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFTIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTIS 160
Cdd:MTH00037 382 SMGAVFAIFAGFTHWFPLFSGVSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTIS 461

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 90655160  161 IVGIIMFIVIMWESMITNRTIMFSANMNSSTEWLQNN-PPAEHSYSELPL 209
Cdd:MTH00037 462 LVATLFFLFLIWEAFASQREVISPEFSSSSLEWQYSSfPPSHHTFDETPS 511
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-212 2.60e-91

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 276.78  E-value: 2.60e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90655160    1 RAYFTSATMIIAVPTGIKVFSWMATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVL 80
Cdd:MTH00007 299 RAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVL 378

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90655160   81 SMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFTIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTIS 160
Cdd:MTH00007 379 SMGAVFAIFAAFNHWFPLFTGLTLHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLS 458

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 90655160  161 IVGIIMFIVIMWESMITNRTIMFSANMNSSTEWLQNNPPAEHSYSELPLISS 212
Cdd:MTH00007 459 FVALLLFIFILWEAFSAQRGVIASPHMSSSLEWQDTLPLDFHNLPETGIITT 510
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-206 2.50e-83

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 256.15  E-value: 2.50e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90655160    1 RAYFTSATMIIAVPTGIKVFSWMATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVL 80
Cdd:MTH00079 302 RAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVL 381

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90655160   81 SMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFTIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTIS 160
Cdd:MTH00079 382 SLGAVFGIFTGISLWWPFMTGIVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMIS 461

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 90655160  161 IVGIIMFIVIMWESMITNRTIMFSANMNSSTEWLQNNPPAEHSYSE 206
Cdd:MTH00079 462 VFALFLFIYVLLESFFSYRLVLHDNYINSSPEYSLSSYVFGHSYQS 507
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-213 1.31e-80

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 249.74  E-value: 1.31e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90655160    1 RAYFTSATMIIAVPTGIKVFSWMATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVL 80
Cdd:MTH00182 304 RAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVL 383

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90655160   81 SMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFTIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTIS 160
Cdd:MTH00182 384 SMGAVFAIFGGFYYWFGKITGYCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIIS 463

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 90655160  161 IVGIIMFIVIMWESMITNRTIMFSANMN----SSTEWLQNNPPAEHSYSELPLISSF 213
Cdd:MTH00182 464 IVGVVWFIYIIYDAYVREEKFIGWKEGTgeswASLEWVHSSPPLFHTYNELPFVYKS 520
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-213 1.33e-78

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 244.35  E-value: 1.33e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90655160    1 RAYFTSATMIIAVPTGIKVFSWMATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVL 80
Cdd:MTH00184 304 RAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVL 383

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90655160   81 SMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFTIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTIS 160
Cdd:MTH00184 384 SMGAVFAIFGGFYYWFGKITGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVIS 463

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 90655160  161 IVGIIMFIVIMWESMItnRTIMF-----SANMNSSTEWLQNNPPAEHSYSELPLISSF 213
Cdd:MTH00184 464 IVGVVWFIYIVYDAYV--REIKFvgwveDSGHYPSLEWAQTSPPAHHTYNELPYVYKG 519
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-175 4.51e-73

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: 228.18  E-value: 4.51e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90655160   1 RAYFTSATMIIAVPTGIKVFSWMATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVL 80
Cdd:cd00919 289 RAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVL 368

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90655160  81 SMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFTIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTIS 160
Cdd:cd00919 369 SGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFIL 448

                       170
                ....*....|....*
gi 90655160 161 IVGIIMFIVIMWESM 175
Cdd:cd00919 449 GLGLLLFLGNLFLSL 463
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-212 8.34e-70

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 221.92  E-value: 8.34e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90655160   1 RAYFTSATMIIAVPTGIKVFSWMATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVL 80
Cdd:COG0843 303 KAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVL 382

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90655160  81 SMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFTIMFVGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTSWNVISSIGST 158
Cdd:COG0843 383 IGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAF 462

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 90655160 159 ISIVGIIMFIVIMWESMITNRTImfSAN-MNSST-EWLQNNPPAEHSYSELPLISS 212
Cdd:COG0843 463 ILAVGFLLFLINLVVSLRKGPKA--GGNpWGARTlEWATPSPPPLYNFASIPVVRS 516
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-204 2.32e-65

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: 209.39  E-value: 2.32e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90655160     1 RAYFTSATMIIAVPTGIKVFSWMATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVL 80
Cdd:TIGR02891 294 LAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVL 373

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90655160    81 SMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFTIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDA--YTSWNVISSIGST 158
Cdd:TIGR02891 374 VGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAF 453

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 90655160   159 ISIVGIIMFIVIMWESMITNRtiMFSANMNSST--EWLQNNPPAEHSY 204
Cdd:TIGR02891 454 ILAAGFLVFLWNLIWSLRKGP--KAGANPWGATtlEWTTSSPPPAHNF 499
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-210 5.20e-63

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 204.09  E-value: 5.20e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90655160    1 RAYFTSATMIIAVPTGIKVFSWMATLYGT--KFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHY 78
Cdd:MTH00026 303 RAYFTAATMIIAVPTGIKIFSWLATVSGSgrNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHF 382

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90655160   79 VLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFTIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGST 158
Cdd:MTH00026 383 VLSMGAVFAIFGGFYLWFGKITGYAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSI 462

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90655160  159 ISIVGIIMFIVIMWES-----------MITNRTIMFSAN--MNSSTEWLQNNPPAEHSYSELPLI 210
Cdd:MTH00026 463 ISIIAVIWFIVVIFDAyyreepfdiniMAKGPLIPFSCQpaHFDTLEWSLTSPPEHHTYNELPYI 527
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 2-204 1.08e-60

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: 197.42  E-value: 1.08e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90655160   2 AYFTSATMIIAVPTGIKVFSWMATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLS 81
Cdd:cd01662 296 AFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLI 375

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90655160  82 MGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFTIMFVGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTSWNVISSIGSTI 159
Cdd:cd01662 376 GGVVFPLFAGFYYWFPKMFGRMLNERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpgPGWDPLNLISTIGAFL 455

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 90655160 160 SIVGIIMFIVIMWESMITNRTIMFSANMNSST-EWLQNNPPAEHSY 204
Cdd:cd01662 456 IAAGVLLFLINVIVSIRKGKRDATGDPWGARTlEWATSSPPPAYNF 501
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 3-203 7.26e-53

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 177.18  E-value: 7.26e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90655160    3 YFTSATMIIAVPTGIKVFSWMATLYGTKFKFNPPLL-WALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLS 81
Cdd:MTH00048 302 FFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKSDPVVwWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLS 381

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90655160   82 MGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFTIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISI 161
Cdd:MTH00048 382 LGSYSSVVIMFIWWWPLITGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISA 461

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 90655160  162 VGIIMFIVIMWESMITNRTIMFSANMNSSTEWLQNNPPAEHS 203
Cdd:MTH00048 462 FSGCFFVFILWESLVVKNEVLGLWGSSSCVVNVLMSPVPYHN 503
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-141 6.17e-46

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


Pssm-ID: 459678  Cd Length: 432  Bit Score: 156.96  E-value: 6.17e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90655160     1 RAYFTSATMIIAVPTGIKVFSWMATLYGTKFKFN-PPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYV 79
Cdd:pfam00115 269 QALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFRtTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYV 348

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90655160    80 LSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFTIMFVGVNLTFFPQHFLGLAGMPRRYSD 141
Cdd:pfam00115 349 LFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAP 410
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 2-213 9.36e-40

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: 143.84  E-value: 9.36e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90655160     2 AYFTSATMIIAVPTGIKVFSWMATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLS 81
Cdd:TIGR02882 339 SFFSITTMAIAIPTGVKIFNWLLTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLI 418

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90655160    82 MGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFTIMFVGVNLTFFPQHFLGLAGMPRRYSDY--PDAYTSWNVISSIGSTI 159
Cdd:TIGR02882 419 TGVVFACLAGLIYWYPKMFGYKLNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYspSDGWFPLNLISTIGALL 498

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 90655160   160 SIVGIIMFIVIMWESMITNRTIMFSANMNSST-EWLQNNPPAEHSYSELPLISSF 213
Cdd:TIGR02882 499 MAIGFIFLVYNIYYSHRKSPREATGDPWNGRTlEWATASPPPKYNFAVTPDVNDY 553
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 2-210 2.06e-35

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 131.60  E-value: 2.06e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90655160    2 AYFTSATMIIAVPTGIKVFSWMATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLS 81
Cdd:PRK15017 346 AFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVII 425

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90655160   82 MGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFTIMFVGVNLTFFPQHFLGLAGMPRRYSDYPD-AYTSWNVISSIGSTIS 160
Cdd:PRK15017 426 GGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDpQFHTMLMIAASGAALI 505

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 90655160  161 IVGIIMFIVIMWESMI---TNRTIMFSANMNSSTEWLQNNPPAEHSYSELPLI 210
Cdd:PRK15017 506 ALGILCQVIQMYVSIRdrdQNRDLTGDPWGGRTLEWATSSPPPFYNFAVVPHV 558
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 8-175 5.39e-13

ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and some archaea which catalyze the reduction of O2 and simultaneously pump protons across the membrane. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. The ba3 family contains oxidases that lack the conserved residues that form the D- and K-pathways in CcO and ubiquinol oxidase. Instead they contain a potential alternative K-pathway. Additional proton channels have been proposed for this family of oxidases but none have been identified definitively. For general information on the heme-copper oxidase superfamily, please see cd00919.


Pssm-ID: 238830  Cd Length: 473  Bit Score: 66.93  E-value: 5.39e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90655160   8 TMIIAVPTGIKVFSWMATL-YGTKFKFNPPLLW---------------ALGFIFlFTIGGLTGLVLANSSLDIVLHDTYY 71
Cdd:cd01660 282 TFMVALPSLLTAFTVFASLeIAGRLRGGKGLFGwiralpwgdpmflalFLAMLM-FIPGGAGGIINASYQLNYVVHNTAW 360

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90655160  72 VVAHFHyvLSMGAVFAIMG-GIIQWY-PLFTGLTMNNTWL-KIQFTIMFVGVNLTFFPQHFLGLAGMPRR--YSDYPDAY 146
Cdd:cd01660 361 VPGHFH--LTVGGAVALTFmAVAYWLvPHLTGRELAAKRLaLAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYGGLP 438

                       170       180       190
                ....*....|....*....|....*....|....
gi 90655160 147 -----TSWNVISSIGSTISIVGIIMFIVIMWESM 175
Cdd:cd01660 439 aagewAPYQQLMAIGGTILFVSGALFLYILFRTL 472
 
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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