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Conserved domains on  [gi|22022383|gb|AAM22265|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Chauliognathus sp. VM-1]

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 ...
1-226 6.48e-165

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: 464.73  E-value: 6.48e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383    1 FGMISHIVSQESGKKETFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 80
Cdd:MTH00153 249 FGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGS 328
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383   81 KINYSPQMLWSLGFIFLFTVGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLKMKNKML 160
Cdd:MTH00153 329 QINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWL 408
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22022383  161 KIQFLTMFVGVNMTFFPQHFLGLSGMPRRYSDYPNFFLSWNIISSVGSLISTVSMVFFIYIMWESF 226
Cdd:MTH00153 409 KIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESM 474
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
1-226 6.48e-165

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 464.73  E-value: 6.48e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383    1 FGMISHIVSQESGKKETFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 80
Cdd:MTH00153 249 FGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGS 328
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383   81 KINYSPQMLWSLGFIFLFTVGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLKMKNKML 160
Cdd:MTH00153 329 QINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWL 408
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22022383  161 KIQFLTMFVGVNMTFFPQHFLGLSGMPRRYSDYPNFFLSWNIISSVGSLISTVSMVFFIYIMWESF 226
Cdd:MTH00153 409 KIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESM 474
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
1-226 5.03e-146

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: 416.11  E-value: 5.03e-146
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383   1 FGMISHIVSQESGKKETFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 80
Cdd:cd01663 242 FGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGG 321
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383  81 KINYSPQMLWSLGFIFLFTVGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLKMKNKML 160
Cdd:cd01663 322 SIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLG 401
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22022383 161 KIQFLTMFVGVNMTFFPQHFLGLSGMPRRYSDYPNFFLSWNIISSVGSLISTVSMVFFIYIMWESF 226
Cdd:cd01663 402 KIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESF 467
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-226 1.62e-89

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 273.16  E-value: 1.62e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383   1 FGMISHIVSQESGKKeTFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 80
Cdd:COG0843 253 FGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRG 331
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383  81 KINYSPQMLWSLGFIFLFTVGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLKMKNKML 160
Cdd:COG0843 332 RIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLG 411
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22022383 161 KIQFLTMFVGVNMTFFPQHFLGLSGMPRRYSDYPNF--FLSWNIISSVGSLISTVSMVFFIYIMWESF 226
Cdd:COG0843 412 KIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPPEpgWQPLNLISTIGAFILAVGFLLFLINLVVSL 479
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
1-226 2.24e-86

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


Pssm-ID: 213748  Cd Length: 499  Bit Score: 264.09  E-value: 2.24e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383     1 FGMISHIVSQESGKKeTFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 80
Cdd:TIGR02891 244 FGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGG 322
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383    81 KINYSPQMLWSLGFIFLFTVGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLKMKNKML 160
Cdd:TIGR02891 323 SIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLG 402
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22022383   161 KIQFLTMFVGVNMTFFPQHFLGLSGMPRRYSDYP--NFFLSWNIISSVGSLISTVSMVFFIYIMWESF 226
Cdd:TIGR02891 403 RWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPpqMGFATLNLISTIGAFILAAGFLVFLWNLIWSL 470
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
1-210 2.27e-61

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


Pssm-ID: 459678  Cd Length: 432  Bit Score: 197.80  E-value: 2.27e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383     1 FGMISHIVSQESGKKeTFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 80
Cdd:pfam00115 219 FGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGG 297
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383    81 KIN-YSPQMLWSLGFIFLFTVGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLKMKNKM 159
Cdd:pfam00115 298 WIRfRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKL 377
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 22022383   160 LKIQFLTMFVGVNMTFFPQHFLGLSGMPRRYS----DYPNFFLSWNIISSVGSLI 210
Cdd:pfam00115 378 GKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
1-226 6.48e-165

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 464.73  E-value: 6.48e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383    1 FGMISHIVSQESGKKETFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 80
Cdd:MTH00153 249 FGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGS 328
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383   81 KINYSPQMLWSLGFIFLFTVGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLKMKNKML 160
Cdd:MTH00153 329 QINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWL 408
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22022383  161 KIQFLTMFVGVNMTFFPQHFLGLSGMPRRYSDYPNFFLSWNIISSVGSLISTVSMVFFIYIMWESF 226
Cdd:MTH00153 409 KIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESM 474
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
1-226 5.03e-146

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: 416.11  E-value: 5.03e-146
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383   1 FGMISHIVSQESGKKETFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 80
Cdd:cd01663 242 FGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGG 321
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383  81 KINYSPQMLWSLGFIFLFTVGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLKMKNKML 160
Cdd:cd01663 322 SIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLG 401
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22022383 161 KIQFLTMFVGVNMTFFPQHFLGLSGMPRRYSDYPNFFLSWNIISSVGSLISTVSMVFFIYIMWESF 226
Cdd:cd01663 402 KIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESF 467
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
1-226 1.63e-135

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 390.19  E-value: 1.63e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383    1 FGMISHIVSQESGKKETFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 80
Cdd:MTH00167 251 FGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGG 330
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383   81 KINYSPQMLWSLGFIFLFTVGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLKMKNKML 160
Cdd:MTH00167 331 KIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETWT 410
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22022383  161 KIQFLTMFVGVNMTFFPQHFLGLSGMPRRYSDYPNFFLSWNIISSVGSLISTVSMVFFIYIMWESF 226
Cdd:MTH00167 411 KIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAF 476
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
1-226 1.93e-135

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 390.22  E-value: 1.93e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383    1 FGMISHIVSQESGKKETFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 80
Cdd:MTH00116 251 FGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGG 330
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383   81 KINYSPQMLWSLGFIFLFTVGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLKMKNKML 160
Cdd:MTH00116 331 TIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWT 410
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22022383  161 KIQFLTMFVGVNMTFFPQHFLGLSGMPRRYSDYPNFFLSWNIISSVGSLISTVSMVFFIYIMWESF 226
Cdd:MTH00116 411 KAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAF 476
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
1-226 1.57e-131

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 379.84  E-value: 1.57e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383    1 FGMISHIVSQESGKKETFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 80
Cdd:MTH00142 249 FGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGS 328
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383   81 KINYSPQMLWSLGFIFLFTVGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLKMKNKML 160
Cdd:MTH00142 329 KVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWL 408
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22022383  161 KIQFLTMFVGVNMTFFPQHFLGLSGMPRRYSDYPNFFLSWNIISSVGSLISTVSMVFFIYIMWESF 226
Cdd:MTH00142 409 KAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESF 474
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
1-226 1.91e-131

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 379.71  E-value: 1.91e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383    1 FGMISHIVSQESGKKETFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 80
Cdd:MTH00223 248 FGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGS 327
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383   81 KINYSPQMLWSLGFIFLFTVGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLKMKNKML 160
Cdd:MTH00223 328 KIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRRWA 407
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22022383  161 KIQFLTMFVGVNMTFFPQHFLGLSGMPRRYSDYPNFFLSWNIISSVGSLISTVSMVFFIYIMWESF 226
Cdd:MTH00223 408 KAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAF 473
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
1-226 5.71e-120

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 350.72  E-value: 5.71e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383    1 FGMISHIVSQESGKKETFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 80
Cdd:MTH00103 251 FGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGG 330
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383   81 KINYSPQMLWSLGFIFLFTVGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLKMKNKML 160
Cdd:MTH00103 331 NIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWA 410
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22022383  161 KIQFLTMFVGVNMTFFPQHFLGLSGMPRRYSDYPNFFLSWNIISSVGSLISTVSMVFFIYIMWESF 226
Cdd:MTH00103 411 KIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAF 476
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
1-226 8.08e-118

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 345.37  E-value: 8.08e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383    1 FGMISHIVSQESGKKETFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 80
Cdd:MTH00183 251 FGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGG 330
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383   81 KINYSPQMLWSLGFIFLFTVGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLKMKNKML 160
Cdd:MTH00183 331 SIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWT 410
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22022383  161 KIQFLTMFVGVNMTFFPQHFLGLSGMPRRYSDYPNFFLSWNIISSVGSLISTVSMVFFIYIMWESF 226
Cdd:MTH00183 411 KIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAF 476
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
1-226 2.19e-117

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 343.81  E-value: 2.19e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383    1 FGMISHIVSQESGKKETFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 80
Cdd:MTH00007 248 FGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGS 327
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383   81 KINYSPQMLWSLGFIFLFTVGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLKMKNKML 160
Cdd:MTH00007 328 PIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRWA 407
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22022383  161 KIQFLTMFVGVNMTFFPQHFLGLSGMPRRYSDYPNFFLSWNIISSVGSLISTVSMVFFIYIMWESF 226
Cdd:MTH00007 408 KAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAF 473
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
1-226 4.16e-115

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 338.34  E-value: 4.16e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383    1 FGMISHIVSQESGKKETFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 80
Cdd:MTH00037 251 FGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGS 330
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383   81 KINYSPQMLWSLGFIFLFTVGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLKMKNKML 160
Cdd:MTH00037 331 NLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLWS 410
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22022383  161 KIQFLTMFVGVNMTFFPQHFLGLSGMPRRYSDYPNFFLSWNIISSVGSLISTVSMVFFIYIMWESF 226
Cdd:MTH00037 411 KVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAF 476
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
1-226 9.99e-115

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 337.30  E-value: 9.99e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383    1 FGMISHIVSQESGKKETFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 80
Cdd:MTH00077 251 FGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGG 330
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383   81 KINYSPQMLWSLGFIFLFTVGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLKMKNKML 160
Cdd:MTH00077 331 AIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWS 410
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22022383  161 KIQFLTMFVGVNMTFFPQHFLGLSGMPRRYSDYPNFFLSWNIISSVGSLISTVSMVFFIYIMWESF 226
Cdd:MTH00077 411 KIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAF 476
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
1-226 1.55e-108

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 321.24  E-value: 1.55e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383    1 FGMISHIVSQESGKKETFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 80
Cdd:MTH00079 251 FGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGM 330
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383   81 KINYSPQMLWSLGFIFLFTVGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLKMKNKML 160
Cdd:MTH00079 331 KMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMM 410
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22022383  161 KIQFLTMFVGVNMTFFPQHFLGLSGMPRRYSDYPNFFLSWNIISSVGSLISTVSMVFFIYIMWESF 226
Cdd:MTH00079 411 SAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESF 476
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
1-226 7.66e-101

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 302.13  E-value: 7.66e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383    1 FGMISHIVSQESGKKETFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 80
Cdd:MTH00182 253 FGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGG 332
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383   81 KINYSPQMLWSLGFIFLFTVGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLKMKNKML 160
Cdd:MTH00182 333 TLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNELYG 412
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22022383  161 KIQFLTMFVGVNMTFFPQHFLGLSGMPRRYSDYPNFFLSWNIISSVGSLISTVSMVFFIYIMWESF 226
Cdd:MTH00182 413 KIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAY 478
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
1-226 2.11e-98

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 295.58  E-value: 2.11e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383    1 FGMISHIVSQESGKKETFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 80
Cdd:MTH00184 253 FGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGG 332
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383   81 KINYSPQMLWSLGFIFLFTVGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLKMKNKML 160
Cdd:MTH00184 333 SLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEVYG 412
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22022383  161 KIQFLTMFVGVNMTFFPQHFLGLSGMPRRYSDYPNFFLSWNIISSVGSLISTVSMVFFIYIMWESF 226
Cdd:MTH00184 413 KIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAY 478
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
1-226 6.60e-97

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: 290.20  E-value: 6.60e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383   1 FGMISHIVSQESGKKeTFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 80
Cdd:cd00919 239 FGAISEIIPTFSGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGG 317
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383  81 KINYSPQMLWSLGFIFLFTVGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLKMKNKML 160
Cdd:cd00919 318 RIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLG 397
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22022383 161 KIQFLTMFVGVNMTFFPQHFLGLSGMPRRYSDYPNFFLSWNIISSVGSLISTVSMVFFIYIMWESF 226
Cdd:cd00919 398 KIHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-226 1.62e-89

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 273.16  E-value: 1.62e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383   1 FGMISHIVSQESGKKeTFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 80
Cdd:COG0843 253 FGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRG 331
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383  81 KINYSPQMLWSLGFIFLFTVGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLKMKNKML 160
Cdd:COG0843 332 RIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLG 411
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22022383 161 KIQFLTMFVGVNMTFFPQHFLGLSGMPRRYSDYPNF--FLSWNIISSVGSLISTVSMVFFIYIMWESF 226
Cdd:COG0843 412 KIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPPEpgWQPLNLISTIGAFILAVGFLLFLINLVVSL 479
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
1-226 2.24e-86

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


Pssm-ID: 213748  Cd Length: 499  Bit Score: 264.09  E-value: 2.24e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383     1 FGMISHIVSQESGKKeTFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 80
Cdd:TIGR02891 244 FGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGG 322
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383    81 KINYSPQMLWSLGFIFLFTVGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLKMKNKML 160
Cdd:TIGR02891 323 SIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLG 402
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22022383   161 KIQFLTMFVGVNMTFFPQHFLGLSGMPRRYSDYP--NFFLSWNIISSVGSLISTVSMVFFIYIMWESF 226
Cdd:TIGR02891 403 RWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPpqMGFATLNLISTIGAFILAAGFLVFLWNLIWSL 470
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
1-226 1.32e-85

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 263.41  E-value: 1.32e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383    1 FGMISHIVSQESGKKETFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 80
Cdd:MTH00026 252 FGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGS 331
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383   81 KIN--YSPQMLWSLGFIFLFTVGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLKMKNK 158
Cdd:MTH00026 332 GRNliFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDI 411
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22022383  159 MLKIQFLTMFVGVNMTFFPQHFLGLSGMPRRYSDYPNFFLSWNIISSVGSLISTVSMVFFIYIMWESF 226
Cdd:MTH00026 412 YGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDAY 479
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
1-226 7.19e-80

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 247.67  E-value: 7.19e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383    1 FGMISHIVSQESGKKETFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 80
Cdd:MTH00048 249 FGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNS 328
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383   81 KINYS-PQMLWSLGFIFLFTVGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLKMKNKM 159
Cdd:MTH00048 329 RVRKSdPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYL 408
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22022383  160 LKIQFLTMFVGVNMTFFPQHFLGLSGMPRRYSDYPNFFLSWNIISSVGSLISTVSMVFFIYIMWESF 226
Cdd:MTH00048 409 LQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESL 475
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
1-226 1.79e-78

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: 244.03  E-value: 1.79e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383   1 FGMISHIVSQESGKKeTFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 80
Cdd:cd01662 245 FGIFSEIVPTFSRKP-LFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRG 323
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383  81 KINYSPQMLWSLGFIFLFTVGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLKMKNKML 160
Cdd:cd01662 324 RIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERLG 403
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22022383 161 KIQFLTMFVGVNMTFFPQHFLGLSGMPRRYSDYPNF--FLSWNIISSVGSLISTVSMVFFIYIMWESF 226
Cdd:cd01662 404 KWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLPGpgWDPLNLISTIGAFLIAAGVLLFLINVIVSI 471
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
1-210 2.27e-61

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


Pssm-ID: 459678  Cd Length: 432  Bit Score: 197.80  E-value: 2.27e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383     1 FGMISHIVSQESGKKeTFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 80
Cdd:pfam00115 219 FGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGG 297
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383    81 KIN-YSPQMLWSLGFIFLFTVGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLKMKNKM 159
Cdd:pfam00115 298 WIRfRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKL 377
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 22022383   160 LKIQFLTMFVGVNMTFFPQHFLGLSGMPRRYS----DYPNFFLSWNIISSVGSLI 210
Cdd:pfam00115 378 GKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
CyoB TIGR02843
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ...
1-226 1.89e-54

cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the component of the aerobic respiratory chain which reacts with oxygen, reducing it to water with the concomitant transport of 4 protons across the membrane. Also known as the cytochrome bo complex, cytochrome o ubiquinol oxidase contains four subunits, two heme b cofactors and a copper atom which is believed to be the oxygen active site. This complex is structurally related to the cytochrome caa3 oxidases which utilize cytochrome c as the reductant and contain heme a cofactors, as well as the intermediate form aa3 oxidases which also react directly with quinones as the reductant. [Energy metabolism, Electron transport]


Pssm-ID: 131890  Cd Length: 646  Bit Score: 184.11  E-value: 1.89e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383     1 FGMISHIVSQESGKKeTFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 80
Cdd:TIGR02843 294 FGIFSEVVATFSRKR-LFGYTSMVWATIAITVLSFIVWLHHFFTMGAGANVNAFFGIATMIIAIPTGVKIFNWLFTMYKG 372
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383    81 KINYSPQMLWSLGFIFLFTVGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLKMKNKML 160
Cdd:TIGR02843 373 RIRFETPMLWTIGFMVTFSIGGMTGVLLAVPPADFVLHNSLFLIAHFHNVIIGGVVFGCFAGLTYWFPKAFGFKLNEKLG 452
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22022383   161 KIQFLTMFVGVNMTFFPQHFLGLSGMPRRYSDYPN-FFLSWNIISSVGSLISTVSMVFFIYIMWESF 226
Cdd:TIGR02843 453 KRSFWCWFIGFYLAFMPLYILGFMGMTRRLNHYDNpEWHPMLIIAAFGAFLIACGILCQIIQIFVSI 519
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
1-210 1.41e-44

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 157.79  E-value: 1.41e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383    1 FGMISHIVSQESgKKETFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 80
Cdd:PRK15017 295 FGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQG 373
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383   81 KINYSPQMLWSLGFIFLFTVGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLKMKNKML 160
Cdd:PRK15017 374 RIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWG 453
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 22022383  161 KIQFLTMFVGVNMTFFPQHFLGLSGMPRRYS-DYPNFFLSWNIISSVGSLI 210
Cdd:PRK15017 454 KRAFWFWIIGFFVAFMPLYALGFMGMTRRLSqQIDPQFHTMLMIAASGAAL 504
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
67-222 4.03e-14

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: 70.39  E-value: 4.03e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383  67 GIKIFSWLATLHGTKINYSPQMLWSLGFIFlftvGGLTGIILSNSSIDIILHDTYYVVAHFHyvLSMGAVFAIMG-GLIH 145
Cdd:cd01660 309 GKGLFGWIRALPWGDPMFLALFLAMLMFIP----GGAGGIINASYQLNYVVHNTAWVPGHFH--LTVGGAVALTFmAVAY 382
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22022383 146 WF-PLFTGLKMK-NKMLKIQFLTMFVGVNMTFFPQHFLGLSGMPRR--YSDYPNFFL-----SWNIISSVGSLISTVSMV 216
Cdd:cd01660 383 WLvPHLTGRELAaKRLALAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYGGLPAagewaPYQQLMAIGGTILFVSGA 462

                ....*.
gi 22022383 217 FFIYIM 222
Cdd:cd01660 463 LFLYIL 468
 
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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