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Conserved domains on  [gi|1217100911|gb|ASM57831|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Prumna fauriei]

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 ...
 1-215 8.46e-122

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: 354.56  E-value: 8.46e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217100911   1 MDVDTRAYFTSATMIIAVPTGIKVFSSLATLYGTKFKFNPPLLSALGFIFLFTIGGLTGLVLANSSLDIVLQDTYYFVPH 80
Cdd:MTH00153  295 MDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAH 374

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217100911  81 FHYVLSMGAVFAIMGGIIQSYPLFTGLTMNNTCLKMQFTIMFIGVNLTFFPQHFLGLAEMPRSYSEYPVAYTSYHVISSI 160
Cdd:MTH00153  375 FHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSI 454

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1217100911 161 GSTISIVGIIMFILIMSKSMITNRTIMFSLNMKSSTECLQNIPPAEHSYPKLPFI 215
Cdd:MTH00153  455 GSTISLISILFFIFIIWESMISKRPVLFSLNLSSSIEWLQNLPPAEHSYSELPLL 509
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-215 8.46e-122

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 354.56  E-value: 8.46e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217100911   1 MDVDTRAYFTSATMIIAVPTGIKVFSSLATLYGTKFKFNPPLLSALGFIFLFTIGGLTGLVLANSSLDIVLQDTYYFVPH 80
Cdd:MTH00153  295 MDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAH 374

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217100911  81 FHYVLSMGAVFAIMGGIIQSYPLFTGLTMNNTCLKMQFTIMFIGVNLTFFPQHFLGLAEMPRSYSEYPVAYTSYHVISSI 160
Cdd:MTH00153  375 FHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSI 454

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1217100911 161 GSTISIVGIIMFILIMSKSMITNRTIMFSLNMKSSTECLQNIPPAEHSYPKLPFI 215
Cdd:MTH00153  455 GSTISLISILFFIFIIWESMISKRPVLFSLNLSSSIEWLQNLPPAEHSYSELPLL 509
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-196 2.31e-92

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: 278.60  E-value: 2.31e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217100911   1 MDVDTRAYFTSATMIIAVPTGIKVFSSLATLYGTKFKFNPPLLSALGFIFLFTIGGLTGLVLANSSLDIVLQDTYYFVPH 80
Cdd:cd01663   288 LDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAH 367

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217100911  81 FHYVLSMGAVFAIMGGIIQSYPLFTGLTMNNTCLKMQFTIMFIGVNLTFFPQHFLGLAEMPRSYSEYPVAYTSYHVISSI 160
Cdd:cd01663   368 FHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSI 447

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1217100911 161 GSTISIVGIIMFILIMSKSMITNRTIMFSLNMKSST 196
Cdd:cd01663   448 GSLISFVSVLLFLFIVWESFVSGRKVIFNVGEGSTS 483
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-180 7.28e-55

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 182.63  E-value: 7.28e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217100911   1 MDVDTRAYFTSATMIIAVPTGIKVFSSLATLYGTKFKFNPPLLSALGFIFLFTIGGLTGLVLANSSLDIVLQDTYYFVPH 80
Cdd:COG0843   298 ISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAH 377

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217100911  81 FHYVLSMGAVFAIMGGIIQSYPLFTGLTMNNTCLKMQFTIMFIGVNLTFFPQHFLGLAEMPRSYSEYP--VAYTSYHVIS 158
Cdd:COG0843   378 FHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLIS 457

                         170       180
                  ....*....|....*....|..
gi 1217100911 159 SIGSTISIVGIIMFILIMSKSM 180
Cdd:COG0843   458 TIGAFILAVGFLLFLINLVVSL 479
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-156 2.72e-39

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: 139.63  E-value: 2.72e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217100911   1 MDVDTRAYFTSATMIIAVPTGIKVFSSLATLYGTKFKFN-PPLLSALGFIFLFTIGGLTGLVLANSSLDIVLQDTYYFVP 79
Cdd:pfam00115 264 LPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFRtTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVA 343

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217100911  80 HFHYVLSMGAVFAIMGGIIQSYPLFTGLTMNNTCLKMQFTIMFIGVNLTFFPQHFLGLAEMPR----SYSEYPVAYTSYH 155
Cdd:pfam00115 344 HFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRryapPFIETVPAFQPLN 423


                  .
gi 1217100911 156 V 156
Cdd:pfam00115 424 W 424
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-215 8.46e-122

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 354.56  E-value: 8.46e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217100911   1 MDVDTRAYFTSATMIIAVPTGIKVFSSLATLYGTKFKFNPPLLSALGFIFLFTIGGLTGLVLANSSLDIVLQDTYYFVPH 80
Cdd:MTH00153  295 MDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAH 374

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217100911  81 FHYVLSMGAVFAIMGGIIQSYPLFTGLTMNNTCLKMQFTIMFIGVNLTFFPQHFLGLAEMPRSYSEYPVAYTSYHVISSI 160
Cdd:MTH00153  375 FHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSI 454

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1217100911 161 GSTISIVGIIMFILIMSKSMITNRTIMFSLNMKSSTECLQNIPPAEHSYPKLPFI 215
Cdd:MTH00153  455 GSTISLISILFFIFIIWESMISKRPVLFSLNLSSSIEWLQNLPPAEHSYSELPLL 509
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-215 9.36e-95

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 285.80  E-value: 9.36e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217100911   1 MDVDTRAYFTSATMIIAVPTGIKVFSSLATLYGTKFKFNPPLLSALGFIFLFTIGGLTGLVLANSSLDIVLQDTYYFVPH 80
Cdd:MTH00167  297 MDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAH 376

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217100911  81 FHYVLSMGAVFAIMGGIIQSYPLFTGLTMNNTCLKMQFTIMFIGVNLTFFPQHFLGLAEMPRSYSEYPVAYTSYHVISSI 160
Cdd:MTH00167  377 FHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSI 456

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1217100911 161 GSTISIVGIIMFILIMSKSMITNRTIMFSLNMKSSTECLQNIPPAEHSYPKLPFI 215
Cdd:MTH00167  457 GSLISLVAVILFLFIIWEAFSSKRKLLPVELTSTNVEWLHGCPPPHHTWEEPPFV 511
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-215 2.14e-94

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 284.68  E-value: 2.14e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217100911   1 MDVDTRAYFTSATMIIAVPTGIKVFSSLATLYGTKFKFNPPLLSALGFIFLFTIGGLTGLVLANSSLDIVLQDTYYFVPH 80
Cdd:MTH00116  297 MDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAH 376

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217100911  81 FHYVLSMGAVFAIMGGIIQSYPLFTGLTMNNTCLKMQFTIMFIGVNLTFFPQHFLGLAEMPRSYSEYPVAYTSYHVISSI 160
Cdd:MTH00116  377 FHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSI 456

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1217100911 161 GSTISIVGIIMFILIMSKSMITNRTIMFSLNMKSSTECLQNIPPAEHSYPKLPFI 215
Cdd:MTH00116  457 GSLISMTAVIMLMFIIWEAFSSKRKVLQPELTTTNIEWIHGCPPPYHTFEEPAFV 511
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-213 6.95e-93

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 280.84  E-value: 6.95e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217100911   1 MDVDTRAYFTSATMIIAVPTGIKVFSSLATLYGTKFKFNPPLLSALGFIFLFTIGGLTGLVLANSSLDIVLQDTYYFVPH 80
Cdd:MTH00142  295 MDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAH 374

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217100911  81 FHYVLSMGAVFAIMGGIIQSYPLFTGLTMNNTCLKMQFTIMFIGVNLTFFPQHFLGLAEMPRSYSEYPVAYTSYHVISSI 160
Cdd:MTH00142  375 FHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSL 454

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1217100911 161 GSTISIVGIIMFILIMSKSMITNRTIMFSLNMKSSTECLQNIPPAEHSYPKLP 213
Cdd:MTH00142  455 GSMISFIAVLMFVFIVWESFVSQRLVMWSSHLSTSLEWSHRLPPDFHTYDELP 507
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-196 2.31e-92

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: 278.60  E-value: 2.31e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217100911   1 MDVDTRAYFTSATMIIAVPTGIKVFSSLATLYGTKFKFNPPLLSALGFIFLFTIGGLTGLVLANSSLDIVLQDTYYFVPH 80
Cdd:cd01663   288 LDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAH 367

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217100911  81 FHYVLSMGAVFAIMGGIIQSYPLFTGLTMNNTCLKMQFTIMFIGVNLTFFPQHFLGLAEMPRSYSEYPVAYTSYHVISSI 160
Cdd:cd01663   368 FHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSI 447

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1217100911 161 GSTISIVGIIMFILIMSKSMITNRTIMFSLNMKSST 196
Cdd:cd01663   448 GSLISFVSVLLFLFIVWESFVSGRKVIFNVGEGSTS 483
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-215 4.65e-92

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 278.78  E-value: 4.65e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217100911   1 MDVDTRAYFTSATMIIAVPTGIKVFSSLATLYGTKFKFNPPLLSALGFIFLFTIGGLTGLVLANSSLDIVLQDTYYFVPH 80
Cdd:MTH00223  294 MDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAH 373

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217100911  81 FHYVLSMGAVFAIMGGIIQSYPLFTGLTMNNTCLKMQFTIMFIGVNLTFFPQHFLGLAEMPRSYSEYPVAYTSYHVISSI 160
Cdd:MTH00223  374 FHYVLSMGAVFALFAGFNHWFPLFTGVTLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSF 453

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1217100911 161 GSTISIVGIIMFILIMSKSMITNRTIMFSLNMKSSTECLQNIPPAEHSYPKLPFI 215
Cdd:MTH00223  454 GSMISFVSVLFFMFIVWEAFVSQRSVVWSGHLSTSLEWDNLLPADFHNNSETGAL 508
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-215 1.52e-81

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 251.77  E-value: 1.52e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217100911   1 MDVDTRAYFTSATMIIAVPTGIKVFSSLATLYGTKFKFNPPLLSALGFIFLFTIGGLTGLVLANSSLDIVLQDTYYFVPH 80
Cdd:MTH00183  297 MDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAH 376

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217100911  81 FHYVLSMGAVFAIMGGIIQSYPLFTGLTMNNTCLKMQFTIMFIGVNLTFFPQHFLGLAEMPRSYSEYPVAYTSYHVISSI 160
Cdd:MTH00183  377 FHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSI 456

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1217100911 161 GSTISIVGIIMFILIMSKSMITNRTIMFSLNMKSSTECLQNIPPAEHSYPKLPFI 215
Cdd:MTH00183  457 GSLISLVAVIMFLFILWEAFAAKREVLSVELTSTNVEWLHGCPPPYHTFEEPAFV 511
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-215 1.72e-81

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 251.73  E-value: 1.72e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217100911   1 MDVDTRAYFTSATMIIAVPTGIKVFSSLATLYGTKFKFNPPLLSALGFIFLFTIGGLTGLVLANSSLDIVLQDTYYFVPH 80
Cdd:MTH00103  297 MDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAH 376

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217100911  81 FHYVLSMGAVFAIMGGIIQSYPLFTGLTMNNTCLKMQFTIMFIGVNLTFFPQHFLGLAEMPRSYSEYPVAYTSYHVISSI 160
Cdd:MTH00103  377 FHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSM 456

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1217100911 161 GSTISIVGIIMFILIMSKSMITNRTIMFSLNMKSSTECLQNIPPAEHSYPKLPFI 215
Cdd:MTH00103  457 GSFISLTAVMLMIFMIWEAFASKREVLTVELTTTNLEWLHGCPPPYHTFEEPTYV 511
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-214 9.49e-78

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 242.04  E-value: 9.49e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217100911   1 MDVDTRAYFTSATMIIAVPTGIKVFSSLATLYGTKFKFNPPLLSALGFIFLFTIGGLTGLVLANSSLDIVLQDTYYFVPH 80
Cdd:MTH00037  297 MDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAH 376

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217100911  81 FHYVLSMGAVFAIMGGIIQSYPLFTGLTMNNTCLKMQFTIMFIGVNLTFFPQHFLGLAEMPRSYSEYPVAYTSYHVISSI 160
Cdd:MTH00037  377 FHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSI 456

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1217100911 161 GSTISIVGIIMFILIMSKSMITNRTIMFSLNMKSSTEC-LQNIPPAEHSYPKLPF 214
Cdd:MTH00037  457 GSTISLVATLFFLFLIWEAFASQREVISPEFSSSSLEWqYSSFPPSHHTFDETPS 511
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-215 1.21e-77

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 241.77  E-value: 1.21e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217100911   1 MDVDTRAYFTSATMIIAVPTGIKVFSSLATLYGTKFKFNPPLLSALGFIFLFTIGGLTGLVLANSSLDIVLQDTYYFVPH 80
Cdd:MTH00077  297 LNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAH 376

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217100911  81 FHYVLSMGAVFAIMGGIIQSYPLFTGLTMNNTCLKMQFTIMFIGVNLTFFPQHFLGLAEMPRSYSEYPVAYTSYHVISSI 160
Cdd:MTH00077  377 FHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSI 456

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1217100911 161 GSTISIVGIIMFILIMSKSMITNRTIMFSLNMKSSTECLQNIPPAEHSYPKLPFI 215
Cdd:MTH00077  457 GSLISLVAVIMMMFIIWEAFSSKREVLTTELTSTNIEWLHGCPPPYHTFEEPSFV 511
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-215 1.15e-76

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 239.03  E-value: 1.15e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217100911   1 MDVDTRAYFTSATMIIAVPTGIKVFSSLATLYGTKFKFNPPLLSALGFIFLFTIGGLTGLVLANSSLDIVLQDTYYFVPH 80
Cdd:MTH00007  294 MDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAH 373

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217100911  81 FHYVLSMGAVFAIMGGIIQSYPLFTGLTMNNTCLKMQFTIMFIGVNLTFFPQHFLGLAEMPRSYSEYPVAYTSYHVISSI 160
Cdd:MTH00007  374 FHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSF 453

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1217100911 161 GSTISIVGIIMFILIMSKSMITNRTIMFSLNMKSSTECLQNIPPAEHSYPKLPFI 215
Cdd:MTH00007  454 GSMLSFVALLLFIFILWEAFSAQRGVIASPHMSSSLEWQDTLPLDFHNLPETGII 508
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-209 3.79e-72

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 227.26  E-value: 3.79e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217100911   1 MDVDTRAYFTSATMIIAVPTGIKVFSSLATLYGTKFKFNPPLLSALGFIFLFTIGGLTGLVLANSSLDIVLQDTYYFVPH 80
Cdd:MTH00079  297 MDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSH 376

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217100911  81 FHYVLSMGAVFAIMGGIIQSYPLFTGLTMNNTCLKMQFTIMFIGVNLTFFPQHFLGLAEMPRSYSEYPVAYTSYHVISSI 160
Cdd:MTH00079  377 FHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSY 456

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1217100911 161 GSTISIVGIIMFILIMSKSMITNRTIMFSLNMKSSTECLQNIPPAEHSY 209
Cdd:MTH00079  457 GSMISVFALFLFIYVLLESFFSYRLVLHDNYINSSPEYSLSSYVFGHSY 505
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-215 4.27e-69

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 219.69  E-value: 4.27e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217100911   1 MDVDTRAYFTSATMIIAVPTGIKVFSSLATLYGTKFKFNPPLLSALGFIFLFTIGGLTGLVLANSSLDIVLQDTYYFVPH 80
Cdd:MTH00182  299 MDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAH 378

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217100911  81 FHYVLSMGAVFAIMGGIIQSYPLFTGLTMNNTCLKMQFTIMFIGVNLTFFPQHFLGLAEMPRSYSEYPVAYTSYHVISSI 160
Cdd:MTH00182  379 FHYVLSMGAVFAIFGGFYYWFGKITGYCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSL 458

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1217100911 161 GSTISIVGIIMFILIMSKSMITNRTIM----FSLNMKSSTECLQNIPPAEHSYPKLPFI 215
Cdd:MTH00182  459 GSIISIVGVVWFIYIIYDAYVREEKFIgwkeGTGESWASLEWVHSSPPLFHTYNELPFV 517
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-215 1.79e-66

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 212.76  E-value: 1.79e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217100911   1 MDVDTRAYFTSATMIIAVPTGIKVFSSLATLYGTKFKFNPPLLSALGFIFLFTIGGLTGLVLANSSLDIVLQDTYYFVPH 80
Cdd:MTH00184  299 MDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAH 378

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217100911  81 FHYVLSMGAVFAIMGGIIQSYPLFTGLTMNNTCLKMQFTIMFIGVNLTFFPQHFLGLAEMPRSYSEYPVAYTSYHVISSI 160
Cdd:MTH00184  379 FHYVLSMGAVFAIFGGFYYWFGKITGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSL 458

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217100911 161 GSTISIVGIIMFILIMSKSMItnRTIMF-----SLNMKSSTECLQNIPPAEHSYPKLPFI 215
Cdd:MTH00184  459 GSVISIVGVVWFIYIVYDAYV--REIKFvgwveDSGHYPSLEWAQTSPPAHHTYNELPYV 516
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-180 7.71e-62

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: 199.29  E-value: 7.71e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217100911   1 MDVDTRAYFTSATMIIAVPTGIKVFSSLATLYGTKFKFNPPLLSALGFIFLFTIGGLTGLVLANSSLDIVLQDTYYFVPH 80
Cdd:cd00919   284 LPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAH 363

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217100911  81 FHYVLSMGAVFAIMGGIIQSYPLFTGLTMNNTCLKMQFTIMFIGVNLTFFPQHFLGLAEMPRSYSEYPVAYTSYHVISSI 160
Cdd:cd00919   364 FHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSV 443

                         170       180
                  ....*....|....*....|
gi 1217100911 161 GSTISIVGIIMFILIMSKSM 180
Cdd:cd00919   444 GAFILGLGLLLFLGNLFLSL 463
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-180 7.28e-55

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 182.63  E-value: 7.28e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217100911   1 MDVDTRAYFTSATMIIAVPTGIKVFSSLATLYGTKFKFNPPLLSALGFIFLFTIGGLTGLVLANSSLDIVLQDTYYFVPH 80
Cdd:COG0843   298 ISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAH 377

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217100911  81 FHYVLSMGAVFAIMGGIIQSYPLFTGLTMNNTCLKMQFTIMFIGVNLTFFPQHFLGLAEMPRSYSEYP--VAYTSYHVIS 158
Cdd:COG0843   378 FHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLIS 457

                         170       180
                  ....*....|....*....|..
gi 1217100911 159 SIGSTISIVGIIMFILIMSKSM 180
Cdd:COG0843   458 TIGAFILAVGFLLFLINLVVSL 479
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-215 2.47e-52

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 176.36  E-value: 2.47e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217100911   1 MDVDTRAYFTSATMIIAVPTGIKVFSSLATLYGT--KFKFNPPLLSALGFIFLFTIGGLTGLVLANSSLDIVLQDTYYFV 78
Cdd:MTH00026  298 MDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSgrNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVV 377

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217100911  79 PHFHYVLSMGAVFAIMGGIIQSYPLFTGLTMNNTCLKMQFTIMFIGVNLTFFPQHFLGLAEMPRSYSEYPVAYTSYHVIS 158
Cdd:MTH00026  378 AHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQIS 457

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217100911 159 SIGSTISIVGIIMFILIMSKSMITNRTIMFSLNMK-------------SSTECLQNIPPAEHSYPKLPFI 215
Cdd:MTH00026  458 SFGSIISIIAVIWFIVVIFDAYYREEPFDINIMAKgplipfscqpahfDTLEWSLTSPPEHHTYNELPYI 527
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 7-174 2.53e-46

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: 159.67  E-value: 2.53e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217100911   7 AYFTSATMIIAVPTGIKVFSSLATLYGTKFKFNPPLLSALGFIFLFTIGGLTGLVLANSSLDIVLQDTYYFVPHFHYVLS 86
Cdd:cd01662   296 AFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLI 375

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217100911  87 MGAVFAIMGGIIQSYPLFTGLTMNNTCLKMQFTIMFIGVNLTFFPQHFLGLAEMPRSYSEYP--VAYTSYHVISSIGSTI 164
Cdd:cd01662   376 GGVVFPLFAGFYYWFPKMFGRMLNERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpgPGWDPLNLISTIGAFL 455

                         170
                  ....*....|
gi 1217100911 165 SIVGIIMFIL 174
Cdd:cd01662   456 IAAGVLLFLI 465
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-208 5.16e-42

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 148.29  E-value: 5.16e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217100911   1 MDVDTRAYFTSATMIIAVPTGIKVFSSLATLYGTKFKFNPPLLS-ALGFIFLFTIGGLTGLVLANSSLDIVLQDTYYFVP 79
Cdd:MTH00048  295 LDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKSDPVVWwVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVA 374

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217100911  80 HFHYVLSMGAVFAIMGGIIQSYPLFTGLTMNNTCLKMQFTIMFIGVNLTFFPQHFLGLAEMPRSYSEYPVAYTSYHVISS 159
Cdd:MTH00048  375 HFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCT 454

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1217100911 160 IGSTISIVGIIMFILIMSKSMITNRTIMFSLNMKSSTECLQNIPPAEHS 208
Cdd:MTH00048  455 VGSFISAFSGCFFVFILWESLVVKNEVLGLWGSSSCVVNVLMSPVPYHN 503
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-156 2.72e-39

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: 139.63  E-value: 2.72e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217100911   1 MDVDTRAYFTSATMIIAVPTGIKVFSSLATLYGTKFKFN-PPLLSALGFIFLFTIGGLTGLVLANSSLDIVLQDTYYFVP 79
Cdd:pfam00115 264 LPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFRtTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVA 343

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217100911  80 HFHYVLSMGAVFAIMGGIIQSYPLFTGLTMNNTCLKMQFTIMFIGVNLTFFPQHFLGLAEMPR----SYSEYPVAYTSYH 155
Cdd:pfam00115 344 HFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRryapPFIETVPAFQPLN 423


                  .
gi 1217100911 156 V 156
Cdd:pfam00115 424 W 424
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 13-180 7.25e-10

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: 57.68  E-value: 7.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217100911  13 TMIIAVPTGIKVFSSLAT------------LYG--TKFKFNPPLLSALGF-IFLFTIGGLTGLVLANSSLDIVLQDTYYF 77
Cdd:cd01660   282 TFMVALPSLLTAFTVFASleiagrlrggkgLFGwiRALPWGDPMFLALFLaMLMFIPGGAGGIINASYQLNYVVHNTAWV 361

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217100911  78 VPHFHyvLSMGAVFAI--MGGIIQSYPLFTGLTM-NNTCLKMQFTIMFIGVNLTFFPQHFLGLAEMPR--SYSEY----- 147
Cdd:cd01660   362 PGHFH--LTVGGAVALtfMAVAYWLVPHLTGRELaAKRLALAQPWLWFVGMTIMSTAMHVAGLLGAPRrtAEAQYgglpa 439

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1217100911 148 PVAYTSYHVISSIGSTISIVGIIMFILIMSKSM 180
Cdd:cd01660   440 AGEWAPYQQLMAIGGTILFVSGALFLYILFRTL 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.
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