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Conserved domains on  [gi|2015601057|gb|QTE08790|]
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cytochrome c oxidase subunit I, partial (mitochondrion) [Gonatoxia helleri]

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 ...
 1-204 1.05e-130

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: 376.90  E-value: 1.05e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015601057   1 MIIAVPTGIKIFSWLATLHGAQLSYSPALLCALGFVFLFTIGGLSGVVLPNSSIDIILHDTYYVVAHFHYVLSMGAVFAI 80
Cdd:MTH00153  308 MIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAI 387

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015601057  81 MAGLIQSYPLFTGLSLNPKSLQIQFFTMFVGVNLSFFPQHFLGLAGMPRRYSDYPDSYTSCNILSTFGSSISLIGIIMLL 160
Cdd:MTH00153  388 MGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFI 467

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2015601057 161 FIIWESMLSNRVTLFPMSMSSSLESYQNLPPSEHSYSELPMLSN 204
Cdd:MTH00153  468 FIIWESMISKRPVLFSLNLSSSIEWLQNLPPAEHSYSELPLLTN 511
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-204 1.05e-130

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 376.90  E-value: 1.05e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015601057   1 MIIAVPTGIKIFSWLATLHGAQLSYSPALLCALGFVFLFTIGGLSGVVLPNSSIDIILHDTYYVVAHFHYVLSMGAVFAI 80
Cdd:MTH00153  308 MIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAI 387

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015601057  81 MAGLIQSYPLFTGLSLNPKSLQIQFFTMFVGVNLSFFPQHFLGLAGMPRRYSDYPDSYTSCNILSTFGSSISLIGIIMLL 160
Cdd:MTH00153  388 MGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFI 467

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2015601057 161 FIIWESMLSNRVTLFPMSMSSSLESYQNLPPSEHSYSELPMLSN 204
Cdd:MTH00153  468 FIIWESMISKRPVLFSLNLSSSIEWLQNLPPAEHSYSELPLLTN 511
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-184 9.92e-98

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: 292.08  E-value: 9.92e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015601057   1 MIIAVPTGIKIFSWLATLHGAQLSYSPALLCALGFVFLFTIGGLSGVVLPNSSIDIILHDTYYVVAHFHYVLSMGAVFAI 80
Cdd:cd01663   301 MIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAI 380

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015601057  81 MAGLIQSYPLFTGLSLNPKSLQIQFFTMFVGVNLSFFPQHFLGLAGMPRRYSDYPDSYTSCNILSTFGSSISLIGIIMLL 160
Cdd:cd01663   381 FAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFL 460

                         170       180
                  ....*....|....*....|....*
gi 2015601057 161 FIIWESMLSNRVTLF-PMSMSSSLE 184
Cdd:cd01663   461 FIVWESFVSGRKVIFnVGEGSTSLE 485
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-200 1.74e-61

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 199.97  E-value: 1.74e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015601057   1 MIIAVPTGIKIFSWLATLHGAQLSYSPALLCALGFVFLFTIGGLSGVVLPNSSIDIILHDTYYVVAHFHYVLSMGAVFAI 80
Cdd:COG0843   311 MLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAF 390

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015601057  81 MAGLIQSYPLFTGLSLNPKSLQIQFFTMFVGVNLSFFPQHFLGLAGMPRRYSDYP--DSYTSCNILSTFGSSISLIGIIM 158
Cdd:COG0843   391 FAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLL 470

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2015601057 159 LLFIIWESMLSN-RVTLFPMSmSSSLESYQNLPPSEHSYSELP 200
Cdd:COG0843   471 FLINLVVSLRKGpKAGGNPWG-ARTLEWATPSPPPLYNFASIP 512
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-151 3.82e-41

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: 144.25  E-value: 3.82e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015601057   1 MIIAVPTGIKIFSWLATLHGAQLS-YSPALLCALGFVFLFTIGGLSGVVLPNSSIDIILHDTYYVVAHFHYVLSMGAVFA 79
Cdd:pfam00115 277 MLIAVPSGVKVFNWLATLWGGWIRfRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFA 356

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2015601057  80 IMAGLIQSYPLFTGLSLNPKSLQIQFFTMFVGVNLSFFPQHFLGLAGMPRRYS----DYPDSYTSCNILSTFGSSI 151
Cdd:pfam00115 357 LFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-204 1.05e-130

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 376.90  E-value: 1.05e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015601057   1 MIIAVPTGIKIFSWLATLHGAQLSYSPALLCALGFVFLFTIGGLSGVVLPNSSIDIILHDTYYVVAHFHYVLSMGAVFAI 80
Cdd:MTH00153  308 MIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAI 387

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015601057  81 MAGLIQSYPLFTGLSLNPKSLQIQFFTMFVGVNLSFFPQHFLGLAGMPRRYSDYPDSYTSCNILSTFGSSISLIGIIMLL 160
Cdd:MTH00153  388 MGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFI 467

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2015601057 161 FIIWESMLSNRVTLFPMSMSSSLESYQNLPPSEHSYSELPMLSN 204
Cdd:MTH00153  468 FIIWESMISKRPVLFSLNLSSSIEWLQNLPPAEHSYSELPLLTN 511
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-204 8.85e-100

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 298.18  E-value: 8.85e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015601057   1 MIIAVPTGIKIFSWLATLHGAQLSYSPALLCALGFVFLFTIGGLSGVVLPNSSIDIILHDTYYVVAHFHYVLSMGAVFAI 80
Cdd:MTH00142  308 MVIAVPTGIKVFSWLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAL 387

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015601057  81 MAGLIQSYPLFTGLSLNPKSLQIQFFTMFVGVNLSFFPQHFLGLAGMPRRYSDYPDSYTSCNILSTFGSSISLIGIIMLL 160
Cdd:MTH00142  388 FAGFIHWFPLFTGLTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFV 467

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2015601057 161 FIIWESMLSNRVTLFPMSMSSSLESYQNLPPSEHSYSELPMLSN 204
Cdd:MTH00142  468 FIVWESFVSQRLVMWSSHLSTSLEWSHRLPPDFHTYDELPILVV 511
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-204 1.37e-98

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 295.08  E-value: 1.37e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015601057   1 MIIAVPTGIKIFSWLATLHGAQLSYSPALLCALGFVFLFTIGGLSGVVLPNSSIDIILHDTYYVVAHFHYVLSMGAVFAI 80
Cdd:MTH00116  310 MIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAI 389

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015601057  81 MAGLIQSYPLFTGLSLNPKSLQIQFFTMFVGVNLSFFPQHFLGLAGMPRRYSDYPDSYTSCNILSTFGSSISLIGIIMLL 160
Cdd:MTH00116  390 MAGFTHWFPLFTGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLM 469

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2015601057 161 FIIWESMLSNRVTLFPMSMSSSLESYQNLPPSEHSYSELPMLSN 204
Cdd:MTH00116  470 FIIWEAFSSKRKVLQPELTTTNIEWIHGCPPPYHTFEEPAFVQV 513
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-202 5.39e-98

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 293.51  E-value: 5.39e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015601057   1 MIIAVPTGIKIFSWLATLHGAQLSYSPALLCALGFVFLFTIGGLSGVVLPNSSIDIILHDTYYVVAHFHYVLSMGAVFAI 80
Cdd:MTH00167  310 MIIAVPTGIKVFSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAI 389

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015601057  81 MAGLIQSYPLFTGLSLNPKSLQIQFFTMFVGVNLSFFPQHFLGLAGMPRRYSDYPDSYTSCNILSTFGSSISLIGIIMLL 160
Cdd:MTH00167  390 MAGFTHWFPLFTGLTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFL 469

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2015601057 161 FIIWESMLSNRVTLFPMSMSSSLESYQNLPPSEHSYSELPML 202
Cdd:MTH00167  470 FIIWEAFSSKRKLLPVELTSTNVEWLHGCPPPHHTWEEPPFV 511
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-184 9.92e-98

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: 292.08  E-value: 9.92e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015601057   1 MIIAVPTGIKIFSWLATLHGAQLSYSPALLCALGFVFLFTIGGLSGVVLPNSSIDIILHDTYYVVAHFHYVLSMGAVFAI 80
Cdd:cd01663   301 MIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAI 380

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015601057  81 MAGLIQSYPLFTGLSLNPKSLQIQFFTMFVGVNLSFFPQHFLGLAGMPRRYSDYPDSYTSCNILSTFGSSISLIGIIMLL 160
Cdd:cd01663   381 FAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFL 460

                         170       180
                  ....*....|....*....|....*
gi 2015601057 161 FIIWESMLSNRVTLF-PMSMSSSLE 184
Cdd:cd01663   461 FIVWESFVSGRKVIFnVGEGSTSLE 485
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-200 6.32e-97

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 290.73  E-value: 6.32e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015601057   1 MIIAVPTGIKIFSWLATLHGAQLSYSPALLCALGFVFLFTIGGLSGVVLPNSSIDIILHDTYYVVAHFHYVLSMGAVFAI 80
Cdd:MTH00223  307 MIIAVPTGIKVFSWLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFAL 386

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015601057  81 MAGLIQSYPLFTGLSLNPKSLQIQFFTMFVGVNLSFFPQHFLGLAGMPRRYSDYPDSYTSCNILSTFGSSISLIGIIMLL 160
Cdd:MTH00223  387 FAGFNHWFPLFTGVTLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFM 466

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2015601057 161 FIIWESMLSNRVTLFPMSMSSSLESYQNLPPSEHSYSELP 200
Cdd:MTH00223  467 FIVWEAFVSQRSVVWSGHLSTSLEWDNLLPADFHNNSETG 506
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-200 1.03e-86

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 264.77  E-value: 1.03e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015601057   1 MIIAVPTGIKIFSWLATLHGAQLSYSPALLCALGFVFLFTIGGLSGVVLPNSSIDIILHDTYYVVAHFHYVLSMGAVFAI 80
Cdd:MTH00037  310 MIIAVPTGIKVFSWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAI 389

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015601057  81 MAGLIQSYPLFTGLSLNPKSLQIQFFTMFVGVNLSFFPQHFLGLAGMPRRYSDYPDSYTSCNILSTFGSSISLIGIIMLL 160
Cdd:MTH00037  390 FAGFTHWFPLFSGVSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFL 469

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2015601057 161 FIIWESMLSNRVTLFPMSMSSSLE-SYQNLPPSEHSYSELP 200
Cdd:MTH00037  470 FLIWEAFASQREVISPEFSSSSLEwQYSSFPPSHHTFDETP 510
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-198 3.00e-84

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 258.27  E-value: 3.00e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015601057   1 MIIAVPTGIKIFSWLATLHGAQLSYSPALLCALGFVFLFTIGGLSGVVLPNSSIDIILHDTYYVVAHFHYVLSMGAVFAI 80
Cdd:MTH00103  310 MIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAI 389

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015601057  81 MAGLIQSYPLFTGLSLNPKSLQIQFFTMFVGVNLSFFPQHFLGLAGMPRRYSDYPDSYTSCNILSTFGSSISLIGIIMLL 160
Cdd:MTH00103  390 MGGFVHWFPLFSGYTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMI 469

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2015601057 161 FIIWESMLSNRVTLFPMSMSSSLESYQNLPPSEHSYSE 198
Cdd:MTH00103  470 FMIWEAFASKREVLTVELTTTNLEWLHGCPPPYHTFEE 507
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-204 1.52e-83

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 256.41  E-value: 1.52e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015601057   1 MIIAVPTGIKIFSWLATLHGAQLSYSPALLCALGFVFLFTIGGLSGVVLPNSSIDIILHDTYYVVAHFHYVLSMGAVFAI 80
Cdd:MTH00077  310 MIIAIPTGVKVFSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAI 389

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015601057  81 MAGLIQSYPLFTGLSLNPKSLQIQFFTMFVGVNLSFFPQHFLGLAGMPRRYSDYPDSYTSCNILSTFGSSISLIGIIMLL 160
Cdd:MTH00077  390 MGGFVHWFPLFSGYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMM 469

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2015601057 161 FIIWESMLSNRVTLFPMSMSSSLESYQNLPPSEHSYSELPMLSN 204
Cdd:MTH00077  470 FIIWEAFSSKREVLTTELTSTNIEWLHGCPPPYHTFEEPSFVQT 513
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-198 3.75e-81

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 250.61  E-value: 3.75e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015601057   1 MIIAVPTGIKIFSWLATLHGAQLSYSPALLCALGFVFLFTIGGLSGVVLPNSSIDIILHDTYYVVAHFHYVLSMGAVFAI 80
Cdd:MTH00183  310 MIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAI 389

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015601057  81 MAGLIQSYPLFTGLSLNPKSLQIQFFTMFVGVNLSFFPQHFLGLAGMPRRYSDYPDSYTSCNILSTFGSSISLIGIIMLL 160
Cdd:MTH00183  390 MAAFVHWFPLFSGYTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFL 469

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2015601057 161 FIIWESMLSNRVTLFPMSMSSSLESYQNLPPSEHSYSE 198
Cdd:MTH00183  470 FILWEAFAAKREVLSVELTSTNVEWLHGCPPPYHTFEE 507
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-203 2.98e-80

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 247.89  E-value: 2.98e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015601057   1 MIIAVPTGIKIFSWLATLHGAQLSYSPALLCALGFVFLFTIGGLSGVVLPNSSIDIILHDTYYVVAHFHYVLSMGAVFAI 80
Cdd:MTH00007  307 MIIAVPTGIKVFSWLATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAI 386

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015601057  81 MAGLIQSYPLFTGLSLNPKSLQIQFFTMFVGVNLSFFPQHFLGLAGMPRRYSDYPDSYTSCNILSTFGSSISLIGIIMLL 160
Cdd:MTH00007  387 FAAFNHWFPLFTGLTLHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFI 466

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2015601057 161 FIIWESMLSNRVTLFPMSMSSSLESYQNLPPSEHSYSELPMLS 203
Cdd:MTH00007  467 FILWEAFSAQRGVIASPHMSSSLEWQDTLPLDFHNLPETGIIT 509
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-198 1.32e-71

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 225.72  E-value: 1.32e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015601057   1 MIIAVPTGIKIFSWLATLHGAQLSYSPALLCALGFVFLFTIGGLSGVVLPNSSIDIILHDTYYVVAHFHYVLSMGAVFAI 80
Cdd:MTH00079  310 MVIAVPTGVKVFSWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGI 389

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015601057  81 MAGLIQSYPLFTGLSLNPKSLQIQFFTMFVGVNLSFFPQHFLGLAGMPRRYSDYPDSYTSCNILSTFGSSISLIGIIMLL 160
Cdd:MTH00079  390 FTGISLWWPFMTGIVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFI 469

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2015601057 161 FIIWESMLSNRVTLFPMSMSSSLESYQNLPPSEHSYSE 198
Cdd:MTH00079  470 YVLLESFFSYRLVLHDNYINSSPEYSLSSYVFGHSYQS 507
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-202 7.73e-69

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 218.92  E-value: 7.73e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015601057   1 MIIAVPTGIKIFSWLATLHGAQLSYSPALLCALGFVFLFTIGGLSGVVLPNSSIDIILHDTYYVVAHFHYVLSMGAVFAI 80
Cdd:MTH00182  312 MIIAVPTGIKVFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAI 391

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015601057  81 MAGLIQSYPLFTGLSLNPKSLQIQFFTMFVGVNLSFFPQHFLGLAGMPRRYSDYPDSYTSCNILSTFGSSISLIGIIMLL 160
Cdd:MTH00182  392 FGGFYYWFGKITGYCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFI 471

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2015601057 161 FIIWESMLSNRVTL----FPMSMSSSLESYQNLPPSEHSYSELPML 202
Cdd:MTH00182  472 YIIYDAYVREEKFIgwkeGTGESWASLEWVHSSPPLFHTYNELPFV 517
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-167 4.79e-67

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: 212.39  E-value: 4.79e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015601057   1 MIIAVPTGIKIFSWLATLHGAQLSYSPALLCALGFVFLFTIGGLSGVVLPNSSIDIILHDTYYVVAHFHYVLSMGAVFAI 80
Cdd:cd00919   297 MIIAVPTGIKVFNWLATLWGGRIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAI 376

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015601057  81 MAGLIQSYPLFTGLSLNPKSLQIQFFTMFVGVNLSFFPQHFLGLAGMPRRYSDYPDSYTSCNILSTFGSSISLIGIIMLL 160
Cdd:cd00919   377 FAGLYYWFPKMTGRMLSEKLGKIHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFL 456


                  ....*..
gi 2015601057 161 FIIWESM 167
Cdd:cd00919   457 GNLFLSL 463
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-205 1.02e-66

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 213.15  E-value: 1.02e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015601057   1 MIIAVPTGIKIFSWLATLHGAQLSYSPALLCALGFVFLFTIGGLSGVVLPNSSIDIILHDTYYVVAHFHYVLSMGAVFAI 80
Cdd:MTH00184  312 MIIAVPTGIKIFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAI 391

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015601057  81 MAGLIQSYPLFTGLSLNPKSLQIQFFTMFVGVNLSFFPQHFLGLAGMPRRYSDYPDSYTSCNILSTFGSSISLIGIIMLL 160
Cdd:MTH00184  392 FGGFYYWFGKITGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFI 471

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2015601057 161 FIIWESMLSN---RVTLFPMSMSSSLESYQNLPPSEHSYSELPMLSNY 205
Cdd:MTH00184  472 YIVYDAYVREikfVGWVEDSGHYPSLEWAQTSPPAHHTYNELPYVYKG 519
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-200 1.74e-61

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 199.97  E-value: 1.74e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015601057   1 MIIAVPTGIKIFSWLATLHGAQLSYSPALLCALGFVFLFTIGGLSGVVLPNSSIDIILHDTYYVVAHFHYVLSMGAVFAI 80
Cdd:COG0843   311 MLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAF 390

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015601057  81 MAGLIQSYPLFTGLSLNPKSLQIQFFTMFVGVNLSFFPQHFLGLAGMPRRYSDYP--DSYTSCNILSTFGSSISLIGIIM 158
Cdd:COG0843   391 FAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLL 470

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2015601057 159 LLFIIWESMLSN-RVTLFPMSmSSSLESYQNLPPSEHSYSELP 200
Cdd:COG0843   471 FLINLVVSLRKGpKAGGNPWG-ARTLEWATPSPPPLYNFASIP 512
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-202 2.03e-54

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 181.36  E-value: 2.03e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015601057   1 MIIAVPTGIKIFSWLATLHGA--QLSYSPALLCALGFVFLFTIGGLSGVVLPNSSIDIILHDTYYVVAHFHYVLSMGAVF 78
Cdd:MTH00026  311 MIIAVPTGIKIFSWLATVSGSgrNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVF 390

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015601057  79 AIMAGLIQSYPLFTGLSLNPKSLQIQFFTMFVGVNLSFFPQHFLGLAGMPRRYSDYPDSYTSCNILSTFGSSISLIGIIM 158
Cdd:MTH00026  391 AIFGGFYLWFGKITGYAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIW 470

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2015601057 159 LLFIIWESM---------LSNRVTLFPMSMS----SSLESYQNLPPSEHSYSELPML 202
Cdd:MTH00026  471 FIVVIFDAYyreepfdinIMAKGPLIPFSCQpahfDTLEWSLTSPPEHHTYNELPYI 527
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-167 6.65e-53

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: 176.62  E-value: 6.65e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015601057   1 MIIAVPTGIKIFSWLATLHGAQLSYSPALLCALGFVFLFTIGGLSGVVLPNSSIDIILHDTYYVVAHFHYVLSMGAVFAI 80
Cdd:cd01662   303 MIIAVPTGVKIFNWLFTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPL 382

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015601057  81 MAGLIQSYPLFTGLSLNPKSLQIQFFTMFVGVNLSFFPQHFLGLAGMPRRYSDYP--DSYTSCNILSTFGSSISLIGIIM 158
Cdd:cd01662   383 FAGFYYWFPKMFGRMLNERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpgPGWDPLNLISTIGAFLIAAGVLL 462


                  ....*....
gi 2015601057 159 LLFIIWESM 167
Cdd:cd01662   463 FLINVIVSI 471
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-195 7.16e-51

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 171.40  E-value: 7.16e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015601057   1 MIIAVPTGIKIFSWLATLHGAQLSYS-PALLCALGFVFLFTIGGLSGVVLPNSSIDIILHDTYYVVAHFHYVLSMGAVFA 79
Cdd:MTH00048  308 MIIGVPTGIKVFSWLYMLLNSRVRKSdPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSS 387

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015601057  80 IMAGLIQSYPLFTGLSLNPKSLQIQFFTMFVGVNLSFFPQHFLGLAGMPRRYSDYPDSYTSCNILSTFGSSISLIGIIML 159
Cdd:MTH00048  388 VVIMFIWWWPLITGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFF 467

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2015601057 160 LFIIWESMLSNRVTLFPMSMSSSLESYQNLPPSEHS 195
Cdd:MTH00048  468 VFILWESLVVKNEVLGLWGSSSCVVNVLMSPVPYHN 503
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-151 3.82e-41

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: 144.25  E-value: 3.82e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015601057   1 MIIAVPTGIKIFSWLATLHGAQLS-YSPALLCALGFVFLFTIGGLSGVVLPNSSIDIILHDTYYVVAHFHYVLSMGAVFA 79
Cdd:pfam00115 277 MLIAVPSGVKVFNWLATLWGGWIRfRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFA 356

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2015601057  80 IMAGLIQSYPLFTGLSLNPKSLQIQFFTMFVGVNLSFFPQHFLGLAGMPRRYS----DYPDSYTSCNILSTFGSSI 151
Cdd:pfam00115 357 LFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 1-167 1.17e-27

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 109.25  E-value: 1.17e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015601057   1 MIIAVPTGIKIFSWLATLHGAQLSYSPALLCALGFVFLFTIGGLSGVVLPNSSIDIILHDTYYVVAHFHYVLSMGAVFAI 80
Cdd:PRK15017  353 MIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGC 432

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015601057  81 MAGLIQSYPLFTGLSLNPKSLQIQFFTMFVGVNLSFFPQHFLGLAGMPRRYSDYPD-SYTSCNILSTFGSSISLIGIIML 159
Cdd:PRK15017  433 FAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDpQFHTMLMIAASGAALIALGILCQ 512


                  ....*...
gi 2015601057 160 LFIIWESM 167
Cdd:PRK15017  513 VIQMYVSI 520
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 8-168 1.07e-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: 68.85  E-value: 1.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015601057   8 GIKIFSWLATLHGAQLSYSPallCALGFVFlFTIGGLSGVVLPNSSIDIILHDTYYVVAHFHyvLSMGAVFAIMAGLIQS 87
Cdd:cd01660   309 GKGLFGWIRALPWGDPMFLA---LFLAMLM-FIPGGAGGIINASYQLNYVVHNTAWVPGHFH--LTVGGAVALTFMAVAY 382

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015601057  88 Y--PLFTGLSLNPKSLQI-QFFTMFVGVNLSFFPQHFLGLAGMPRR--YSDYPDSY-----TSCNILSTFGSSISLIGII 157
Cdd:cd01660   383 WlvPHLTGRELAAKRLALaQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYGGLPaagewAPYQQLMAIGGTILFVSGA 462

                         170
                  ....*....|.
gi 2015601057 158 MLLFIIWESML 168
Cdd:cd01660   463 LFLYILFRTLL 473
 
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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