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Conserved domains on  [gi|2104715123|gb|UBT84219|]
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cytochrome oxidase subunit 1, partial (mitochondrion) [Ischnura genei]

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 ...
 1-218 4.12e-152

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: 431.98  E-value: 4.12e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123   1 GMDVDTRAYFTSATMVIAVPTGIKIFSWLATLHGSQLSYSPSLLWALGFVFLFTVGGLTGVVLANSSIDIAMHDTYYVVA 80
Cdd:MTH00153  294 GMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVA 373

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123  81 HFHYVLSMGAVFAIMGGLIHWFPLFTGTSMNSQMLKVQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDSYTAWNIVST 160
Cdd:MTH00153  374 HFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISS 453

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2104715123 161 LGSSISMMGVIMLLFIIWEALASQRQVLATNSMNTSIEWYQKTPPTEHCYSELPLMIK 218
Cdd:MTH00153  454 IGSTISLISILFFIFIIWESMISKRPVLFSLNLSSSIEWLQNLPPAEHSYSELPLLTN 511
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-218 4.12e-152

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 431.98  E-value: 4.12e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123   1 GMDVDTRAYFTSATMVIAVPTGIKIFSWLATLHGSQLSYSPSLLWALGFVFLFTVGGLTGVVLANSSIDIAMHDTYYVVA 80
Cdd:MTH00153  294 GMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVA 373

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123  81 HFHYVLSMGAVFAIMGGLIHWFPLFTGTSMNSQMLKVQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDSYTAWNIVST 160
Cdd:MTH00153  374 HFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISS 453

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2104715123 161 LGSSISMMGVIMLLFIIWEALASQRQVLATNSMNTSIEWYQKTPPTEHCYSELPLMIK 218
Cdd:MTH00153  454 IGSTISLISILFFIFIIWESMISKRPVLFSLNLSSSIEWLQNLPPAEHSYSELPLLTN 511
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-199 7.26e-122

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: 354.10  E-value: 7.26e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123   1 GMDVDTRAYFTSATMVIAVPTGIKIFSWLATLHGSQLSYSPSLLWALGFVFLFTVGGLTGVVLANSSIDIAMHDTYYVVA 80
Cdd:cd01663   287 GLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVA 366

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123  81 HFHYVLSMGAVFAIMGGLIHWFPLFTGTSMNSQMLKVQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDSYTAWNIVST 160
Cdd:cd01663   367 HFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISS 446

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2104715123 161 LGSSISMMGVIMLLFIIWEALASQRQVLA-TNSMNTSIEW 199
Cdd:cd01663   447 IGSLISFVSVLLFLFIVWESFVSGRKVIFnVGEGSTSLEW 486
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-208 4.25e-72

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: 227.11  E-value: 4.25e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123   1 GMDVDTRAYFTSATMVIAVPTGIKIFSWLATLHGSQLSYSPSLLWALGFVFLFTVGGLTGVVLANSSIDIAMHDTYYVVA 80
Cdd:TIGR02891 288 GMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVA 367

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123  81 HFHYVLSMGAVFAIMGGLIHWFPLFTGTSMNSQMLKVQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDS--YTAWNIV 158
Cdd:TIGR02891 368 HFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLI 447

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2104715123 159 STLGSSISMMGVIMLLFIIWEALASQRQVLATNSMNTSIEWYQKTPPTEH 208
Cdd:TIGR02891 448 STIGAFILAAGFLVFLWNLIWSLRKGPKAGANPWGATTLEWTTSSPPPAH 497
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-215 1.07e-71

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 226.93  E-value: 1.07e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123   1 GMDVDTRAYFTSATMVIAVPTGIKIFSWLATLHGSQLSYSPSLLWALGFVFLFTVGGLTGVVLANSSIDIAMHDTYYVVA 80
Cdd:COG0843   297 GISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVA 376

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123  81 HFHYVLSMGAVFAIMGGLIHWFPLFTGTSMNSQMLKVQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DSYTAWNIV 158
Cdd:COG0843   377 HFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLI 456

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2104715123 159 STLGSSISMMGVIMLLFIIWEALASqRQVLATNSMN-TSIEWYQKTPPTEHCYSELPL 215
Cdd:COG0843   457 STIGAFILAVGFLLFLINLVVSLRK-GPKAGGNPWGaRTLEWATPSPPPLYNFASIPV 513
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-165 1.09e-49

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: 166.98  E-value: 1.09e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123   1 GMDVDTRAYFTSATMVIAVPTGIKIFSWLATLHGSQLS-YSPSLLWALGFVFLFTVGGLTGVVLANSSIDIAMHDTYYVV 79
Cdd:pfam00115 263 GLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRfRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVV 342

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123  80 AHFHYVLSMGAVFAIMGGLIHWFPLFTGTSMNSQMLKVQFLTMFIGVNLTFFPQHFLGLAGMPRRYS----DYPDSYTAW 155
Cdd:pfam00115 343 AHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPL 422

                         170
                  ....*....|
gi 2104715123 156 NIVSTLGSSI 165
Cdd:pfam00115 423 NWIRTIGGVL 432
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-218 4.12e-152

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 431.98  E-value: 4.12e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123   1 GMDVDTRAYFTSATMVIAVPTGIKIFSWLATLHGSQLSYSPSLLWALGFVFLFTVGGLTGVVLANSSIDIAMHDTYYVVA 80
Cdd:MTH00153  294 GMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVA 373

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123  81 HFHYVLSMGAVFAIMGGLIHWFPLFTGTSMNSQMLKVQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDSYTAWNIVST 160
Cdd:MTH00153  374 HFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISS 453

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2104715123 161 LGSSISMMGVIMLLFIIWEALASQRQVLATNSMNTSIEWYQKTPPTEHCYSELPLMIK 218
Cdd:MTH00153  454 IGSTISLISILFFIFIIWESMISKRPVLFSLNLSSSIEWLQNLPPAEHSYSELPLLTN 511
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-216 4.55e-124

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 360.95  E-value: 4.55e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123   1 GMDVDTRAYFTSATMVIAVPTGIKIFSWLATLHGSQLSYSPSLLWALGFVFLFTVGGLTGVVLANSSIDIAMHDTYYVVA 80
Cdd:MTH00116  296 GMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVA 375

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123  81 HFHYVLSMGAVFAIMGGLIHWFPLFTGTSMNSQMLKVQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDSYTAWNIVST 160
Cdd:MTH00116  376 HFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISS 455

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2104715123 161 LGSSISMMGVIMLLFIIWEALASQRQVLATNSMNTSIEWYQKTPPTEHCYSELPLM 216
Cdd:MTH00116  456 IGSLISMTAVIMLMFIIWEAFSSKRKVLQPELTTTNIEWIHGCPPPYHTFEEPAFV 511
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-199 7.26e-122

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: 354.10  E-value: 7.26e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123   1 GMDVDTRAYFTSATMVIAVPTGIKIFSWLATLHGSQLSYSPSLLWALGFVFLFTVGGLTGVVLANSSIDIAMHDTYYVVA 80
Cdd:cd01663   287 GLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVA 366

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123  81 HFHYVLSMGAVFAIMGGLIHWFPLFTGTSMNSQMLKVQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDSYTAWNIVST 160
Cdd:cd01663   367 HFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISS 446

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2104715123 161 LGSSISMMGVIMLLFIIWEALASQRQVLA-TNSMNTSIEW 199
Cdd:cd01663   447 IGSLISFVSVLLFLFIVWESFVSGRKVIFnVGEGSTSLEW 486
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-216 5.26e-121

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 352.83  E-value: 5.26e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123   1 GMDVDTRAYFTSATMVIAVPTGIKIFSWLATLHGSQLSYSPSLLWALGFVFLFTVGGLTGVVLANSSIDIAMHDTYYVVA 80
Cdd:MTH00167  296 GMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVA 375

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123  81 HFHYVLSMGAVFAIMGGLIHWFPLFTGTSMNSQMLKVQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDSYTAWNIVST 160
Cdd:MTH00167  376 HFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSS 455

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2104715123 161 LGSSISMMGVIMLLFIIWEALASQRQVLATNSMNTSIEWYQKTPPTEHCYSELPLM 216
Cdd:MTH00167  456 IGSLISLVAVILFLFIIWEAFSSKRKLLPVELTSTNVEWLHGCPPPHHTWEEPPFV 511
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-218 4.86e-119

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 347.87  E-value: 4.86e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123   1 GMDVDTRAYFTSATMVIAVPTGIKIFSWLATLHGSQLSYSPSLLWALGFVFLFTVGGLTGVVLANSSIDIAMHDTYYVVA 80
Cdd:MTH00142  294 GMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVA 373

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123  81 HFHYVLSMGAVFAIMGGLIHWFPLFTGTSMNSQMLKVQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDSYTAWNIVST 160
Cdd:MTH00142  374 HFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSS 453

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2104715123 161 LGSSISMMGVIMLLFIIWEALASQRQVLATNSMNTSIEWYQKTPPTEHCYSELPLMIK 218
Cdd:MTH00142  454 LGSMISFIAVLMFVFIVWESFVSQRLVMWSSHLSTSLEWSHRLPPDFHTYDELPILVV 511
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-219 4.11e-116

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 340.42  E-value: 4.11e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123   1 GMDVDTRAYFTSATMVIAVPTGIKIFSWLATLHGSQLSYSPSLLWALGFVFLFTVGGLTGVVLANSSIDIAMHDTYYVVA 80
Cdd:MTH00223  293 GMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVA 372

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123  81 HFHYVLSMGAVFAIMGGLIHWFPLFTGTSMNSQMLKVQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDSYTAWNIVST 160
Cdd:MTH00223  373 HFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSS 452

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2104715123 161 LGSSISMMGVIMLLFIIWEALASQRQVLATNSMNTSIEWYQKTPPTEHCYSELPLMIKF 219
Cdd:MTH00223  453 FGSMISFVSVLFFMFIVWEAFVSQRSVVWSGHLSTSLEWDNLLPADFHNNSETGALVIN 511
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-212 2.77e-108

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 320.68  E-value: 2.77e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123   1 GMDVDTRAYFTSATMVIAVPTGIKIFSWLATLHGSQLSYSPSLLWALGFVFLFTVGGLTGVVLANSSIDIAMHDTYYVVA 80
Cdd:MTH00103  296 GMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVA 375

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123  81 HFHYVLSMGAVFAIMGGLIHWFPLFTGTSMNSQMLKVQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDSYTAWNIVST 160
Cdd:MTH00103  376 HFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSS 455

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2104715123 161 LGSSISMMGVIMLLFIIWEALASQRQVLATNSMNTSIEWYQKTPPTEHCYSE 212
Cdd:MTH00103  456 MGSFISLTAVMLMIFMIWEAFASKREVLTVELTTTNLEWLHGCPPPYHTFEE 507
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-219 8.03e-106

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 314.46  E-value: 8.03e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123   1 GMDVDTRAYFTSATMVIAVPTGIKIFSWLATLHGSQLSYSPSLLWALGFVFLFTVGGLTGVVLANSSIDIAMHDTYYVVA 80
Cdd:MTH00037  296 GMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVA 375

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123  81 HFHYVLSMGAVFAIMGGLIHWFPLFTGTSMNSQMLKVQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDSYTAWNIVST 160
Cdd:MTH00037  376 HFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSS 455

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123 161 LGSSISMMGVIMLLFIIWEALASQRQVLATNSMNTSIEW-YQKTPPTEHCYSELPLMIKF 219
Cdd:MTH00037  456 IGSTISLVATLFFLFLIWEAFASQREVISPEFSSSSLEWqYSSFPPSHHTFDETPSTVIL 515
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-212 1.51e-105

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 313.78  E-value: 1.51e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123   1 GMDVDTRAYFTSATMVIAVPTGIKIFSWLATLHGSQLSYSPSLLWALGFVFLFTVGGLTGVVLANSSIDIAMHDTYYVVA 80
Cdd:MTH00183  296 GMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVA 375

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123  81 HFHYVLSMGAVFAIMGGLIHWFPLFTGTSMNSQMLKVQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDSYTAWNIVST 160
Cdd:MTH00183  376 HFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSS 455

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2104715123 161 LGSSISMMGVIMLLFIIWEALASQRQVLATNSMNTSIEWYQKTPPTEHCYSE 212
Cdd:MTH00183  456 IGSLISLVAVIMFLFILWEAFAAKREVLSVELTSTNVEWLHGCPPPYHTFEE 507
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-218 4.41e-103

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 307.25  E-value: 4.41e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123   1 GMDVDTRAYFTSATMVIAVPTGIKIFSWLATLHGSQLSYSPSLLWALGFVFLFTVGGLTGVVLANSSIDIAMHDTYYVVA 80
Cdd:MTH00077  296 DLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVA 375

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123  81 HFHYVLSMGAVFAIMGGLIHWFPLFTGTSMNSQMLKVQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDSYTAWNIVST 160
Cdd:MTH00077  376 HFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSS 455

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2104715123 161 LGSSISMMGVIMLLFIIWEALASQRQVLATNSMNTSIEWYQKTPPTEHCYSELPLMIK 218
Cdd:MTH00077  456 IGSLISLVAVIMMMFIIWEAFSSKREVLTTELTSTNIEWLHGCPPPYHTFEEPSFVQT 513
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-212 7.74e-100

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 298.74  E-value: 7.74e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123   1 GMDVDTRAYFTSATMVIAVPTGIKIFSWLATLHGSQLSYSPSLLWALGFVFLFTVGGLTGVVLANSSIDIAMHDTYYVVA 80
Cdd:MTH00007  293 GMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVA 372

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123  81 HFHYVLSMGAVFAIMGGLIHWFPLFTGTSMNSQMLKVQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDSYTAWNIVST 160
Cdd:MTH00007  373 HFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSS 452

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2104715123 161 LGSSISMMGVIMLLFIIWEALASQRQVLATNSMNTSIEWYQKTPPTEHCYSE 212
Cdd:MTH00007  453 FGSMLSFVALLLFIFILWEAFSAQRGVIASPHMSSSLEWQDTLPLDFHNLPE 504
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-219 1.35e-91

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 278.24  E-value: 1.35e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123   1 GMDVDTRAYFTSATMVIAVPTGIKIFSWLATLHGSQLSYSPSLLWALGFVFLFTVGGLTGVVLANSSIDIAMHDTYYVVA 80
Cdd:MTH00182  298 GMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVA 377

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123  81 HFHYVLSMGAVFAIMGGLIHWFPLFTGTSMNSQMLKVQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDSYTAWNIVST 160
Cdd:MTH00182  378 HFHYVLSMGAVFAIFGGFYYWFGKITGYCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSS 457

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2104715123 161 LGSSISMMGVIMLLFIIWEALASQRQVLA----TNSMNTSIEWYQKTPPTEHCYSELPLMIKF 219
Cdd:MTH00182  458 LGSIISIVGVVWFIYIIYDAYVREEKFIGwkegTGESWASLEWVHSSPPLFHTYNELPFVYKS 520
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-212 8.27e-90

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 273.09  E-value: 8.27e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123   1 GMDVDTRAYFTSATMVIAVPTGIKIFSWLATLHGSQLSYSPSLLWALGFVFLFTVGGLTGVVLANSSIDIAMHDTYYVVA 80
Cdd:MTH00079  296 GMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVS 375

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123  81 HFHYVLSMGAVFAIMGGLIHWFPLFTGTSMNSQMLKVQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDSYTAWNIVST 160
Cdd:MTH00079  376 HFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISS 455

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2104715123 161 LGSSISMMGVIMLLFIIWEALASQRQVLATNSMNTSIEWYQKTPPTEHCYSE 212
Cdd:MTH00079  456 YGSMISVFALFLFIYVLLESFFSYRLVLHDNYINSSPEYSLSSYVFGHSYQS 507
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-219 2.21e-88

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 269.77  E-value: 2.21e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123   1 GMDVDTRAYFTSATMVIAVPTGIKIFSWLATLHGSQLSYSPSLLWALGFVFLFTVGGLTGVVLANSSIDIAMHDTYYVVA 80
Cdd:MTH00184  298 GMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVA 377

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123  81 HFHYVLSMGAVFAIMGGLIHWFPLFTGTSMNSQMLKVQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDSYTAWNIVST 160
Cdd:MTH00184  378 HFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISS 457

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2104715123 161 LGSSISMMGVIMLLFIIWEALASQRQVLA---TNSMNTSIEWYQKTPPTEHCYSELPLMIKF 219
Cdd:MTH00184  458 LGSVISIVGVVWFIYIVYDAYVREIKFVGwveDSGHYPSLEWAQTSPPAHHTYNELPYVYKG 519
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-181 1.54e-80

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: 247.83  E-value: 1.54e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123   1 GMDVDTRAYFTSATMVIAVPTGIKIFSWLATLHGSQLSYSPSLLWALGFVFLFTVGGLTGVVLANSSIDIAMHDTYYVVA 80
Cdd:cd00919   283 GLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVA 362

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123  81 HFHYVLSMGAVFAIMGGLIHWFPLFTGTSMNSQMLKVQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDSYTAWNIVST 160
Cdd:cd00919   363 HFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISS 442

                         170       180
                  ....*....|....*....|.
gi 2104715123 161 LGSSISMMGVIMLLFIIWEAL 181
Cdd:cd00919   443 VGAFILGLGLLLFLGNLFLSL 463
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-208 4.25e-72

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: 227.11  E-value: 4.25e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123   1 GMDVDTRAYFTSATMVIAVPTGIKIFSWLATLHGSQLSYSPSLLWALGFVFLFTVGGLTGVVLANSSIDIAMHDTYYVVA 80
Cdd:TIGR02891 288 GMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVA 367

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123  81 HFHYVLSMGAVFAIMGGLIHWFPLFTGTSMNSQMLKVQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDS--YTAWNIV 158
Cdd:TIGR02891 368 HFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLI 447

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2104715123 159 STLGSSISMMGVIMLLFIIWEALASQRQVLATNSMNTSIEWYQKTPPTEH 208
Cdd:TIGR02891 448 STIGAFILAAGFLVFLWNLIWSLRKGPKAGANPWGATTLEWTTSSPPPAH 497
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-215 1.07e-71

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 226.93  E-value: 1.07e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123   1 GMDVDTRAYFTSATMVIAVPTGIKIFSWLATLHGSQLSYSPSLLWALGFVFLFTVGGLTGVVLANSSIDIAMHDTYYVVA 80
Cdd:COG0843   297 GISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVA 376

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123  81 HFHYVLSMGAVFAIMGGLIHWFPLFTGTSMNSQMLKVQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DSYTAWNIV 158
Cdd:COG0843   377 HFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLI 456

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2104715123 159 STLGSSISMMGVIMLLFIIWEALASqRQVLATNSMN-TSIEWYQKTPPTEHCYSELPL 215
Cdd:COG0843   457 STIGAFILAVGFLLFLINLVVSLRK-GPKAGGNPWGaRTLEWATPSPPPLYNFASIPV 513
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-217 1.10e-69

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 221.81  E-value: 1.10e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123   1 GMDVDTRAYFTSATMVIAVPTGIKIFSWLATLHGS--QLSYSPSLLWALGFVFLFTVGGLTGVVLANSSIDIAMHDTYYV 78
Cdd:MTH00026  297 GMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSgrNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYV 376

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123  79 VAHFHYVLSMGAVFAIMGGLIHWFPLFTGTSMNSQMLKVQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDSYTAWNIV 158
Cdd:MTH00026  377 VAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQI 456

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2104715123 159 STLGSSISMMGVIMLLFIIWEALASQR----QVLATNSM---------NTSIEWYQKTPPTEHCYSELPLMI 217
Cdd:MTH00026  457 SSFGSIISIIAVIWFIVVIFDAYYREEpfdiNIMAKGPLipfscqpahFDTLEWSLTSPPEHHTYNELPYIV 528
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 8-208 2.06e-63

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: 204.74  E-value: 2.06e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123   8 AYFTSATMVIAVPTGIKIFSWLATLHGSQLSYSPSLLWALGFVFLFTVGGLTGVVLANSSIDIAMHDTYYVVAHFHYVLS 87
Cdd:cd01662   296 AFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLI 375

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123  88 MGAVFAIMGGLIHWFPLFTGTSMNSQMLKVQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DSYTAWNIVSTLGSSI 165
Cdd:cd01662   376 GGVVFPLFAGFYYWFPKMFGRMLNERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpgPGWDPLNLISTIGAFL 455

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2104715123 166 SMMGVIMLLFIIWEALASQRQVLATNSMNT-SIEWYQKTPPTEH 208
Cdd:cd01662   456 IAAGVLLFLINVIVSIRKGKRDATGDPWGArTLEWATSSPPPAY 499
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-188 3.84e-61

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 199.13  E-value: 3.84e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123   1 GMDVDTRAYFTSATMVIAVPTGIKIFSWLATLHGSQLSYS-PSLLWALGFVFLFTVGGLTGVVLANSSIDIAMHDTYYVV 79
Cdd:MTH00048  294 GLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKSdPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVV 373

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123  80 AHFHYVLSMGAVFAIMGGLIHWFPLFTGTSMNSQMLKVQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDSYTAWNIVS 159
Cdd:MTH00048  374 AHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVC 453

                         170       180
                  ....*....|....*....|....*....
gi 2104715123 160 TLGSSISMMGVIMLLFIIWEALASQRQVL 188
Cdd:MTH00048  454 TVGSFISAFSGCFFVFILWESLVVKNEVL 482
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-165 1.09e-49

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: 166.98  E-value: 1.09e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123   1 GMDVDTRAYFTSATMVIAVPTGIKIFSWLATLHGSQLS-YSPSLLWALGFVFLFTVGGLTGVVLANSSIDIAMHDTYYVV 79
Cdd:pfam00115 263 GLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRfRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVV 342

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123  80 AHFHYVLSMGAVFAIMGGLIHWFPLFTGTSMNSQMLKVQFLTMFIGVNLTFFPQHFLGLAGMPRRYS----DYPDSYTAW 155
Cdd:pfam00115 343 AHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPL 422

                         170
                  ....*....|
gi 2104715123 156 NIVSTLGSSI 165
Cdd:pfam00115 423 NWIRTIGGVL 432
CyoB TIGR02843
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ...
 8-214 1.95e-39

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: 142.89  E-value: 1.95e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123   8 AYFTSATMVIAVPTGIKIFSWLATLHGSQLSYSPSLLWALGFVFLFTVGGLTGVVLANSSIDIAMHDTYYVVAHFHYVLS 87
Cdd:TIGR02843 345 AFFGIATMIIAIPTGVKIFNWLFTMYKGRIRFETPMLWTIGFMVTFSIGGMTGVLLAVPPADFVLHNSLFLIAHFHNVII 424

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123  88 MGAVFAIMGGLIHWFPLFTGTSMNSQMLKVQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPD-SYTAWNIVSTLGSSIS 166
Cdd:TIGR02843 425 GGVVFGCFAGLTYWFPKAFGFKLNEKLGKRSFWCWFIGFYLAFMPLYILGFMGMTRRLNHYDNpEWHPMLIIAAFGAFLI 504

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2104715123 167 MMGVIMLLFIIWEALASQRQVLATNS---MNTSIEWYQKTPPTEHCYSELP 214
Cdd:TIGR02843 505 ACGILCQIIQIFVSIRDRDQNRDTTGdpwGGRTLEWSTSSPPPFYNFAVIP 555
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 1-214 3.24e-34

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 128.51  E-value: 3.24e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123   1 GMDVDTRAYFTSATMVIAVPTGIKIFSWLATLHGSQLSYSPSLLWALGFVFLFTVGGLTGVVLANSSIDIAMHDTYYVVA 80
Cdd:PRK15017  339 GAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIA 418

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123  81 HFHYVLSMGAVFAIMGGLIHWFPLFTGTSMNSQMLKVQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPD-SYTAWNIVS 159
Cdd:PRK15017  419 HFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDpQFHTMLMIA 498

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2104715123 160 TLGSSISMMGVIMLLFIIWEALASQ---RQVLATNSMNTSIEWYQKTPPTEHCYSELP 214
Cdd:PRK15017  499 ASGAALIALGILCQVIQMYVSIRDRdqnRDLTGDPWGGRTLEWATSSPPPFYNFAVVP 556
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 14-177 5.73e-13

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


Pssm-ID: 238830  Cd Length: 473  Bit Score: 66.93  E-value: 5.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123  14 TMVIAVPTGIKIFSWLATL-HGSQLSYSPSLLW---------------ALGFVFlFTVGGLTGVVLANSSIDIAMHDTYY 77
Cdd:cd01660   282 TFMVALPSLLTAFTVFASLeIAGRLRGGKGLFGwiralpwgdpmflalFLAMLM-FIPGGAGGIINASYQLNYVVHNTAW 360

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104715123  78 VVAHFHyvLSMGAVFAIMG-GLIHWF-PLFTGTSMNSQML-KVQFLTMFIGVNLTFFPQHFLGLAGMPRR--YSDYPDSY 152
Cdd:cd01660   361 VPGHFH--LTVGGAVALTFmAVAYWLvPHLTGRELAAKRLaLAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYGGLP 438

                         170       180       190
                  ....*....|....*....|....*....|
gi 2104715123 153 -----TAWNIVSTLGSSISMMGVIMLLFII 177
Cdd:cd01660   439 aagewAPYQQLMAIGGTILFVSGALFLYIL 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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