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Conserved domains on  [gi|213054032|gb|ACJ39243|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Haplotropis sp. FGJ-2008]

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 1.41e-145

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: 415.42  E-value: 1.41e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213054032   1 GMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVA 80
Cdd:MTH00153 294 GMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVA 373

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213054032  81 HFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISS 160
Cdd:MTH00153 374 HFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISS 453

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 213054032 161 IGSTISIVGIIMFIIIMWESMISNRTVMFSSNMSSSTEWLQNNPPAEHSYSELPLITS 218
Cdd:MTH00153 454 IGSTISLISILFFIFIIWESMISKRPVLFSLNLSSSIEWLQNLPPAEHSYSELPLLTN 511
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-218 1.41e-145

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 415.42  E-value: 1.41e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213054032   1 GMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVA 80
Cdd:MTH00153 294 GMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVA 373

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213054032  81 HFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISS 160
Cdd:MTH00153 374 HFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISS 453

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 213054032 161 IGSTISIVGIIMFIIIMWESMISNRTVMFSSNMSSSTEWLQNNPPAEHSYSELPLITS 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 ...
 1-201 7.41e-113

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: 331.37  E-value: 7.41e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213054032   1 GMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVA 80
Cdd:cd01663  287 GLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVA 366

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213054032  81 HFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISS 160
Cdd:cd01663  367 HFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISS 446

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 213054032 161 IGSTISIVGIIMFIIIMWESMISNRTVMFSSN-MSSSTEWLQ 201
Cdd:cd01663  447 IGSLISFVSVLLFLFIVWESFVSGRKVIFNVGeGSTSLEWTL 488
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-157 8.15e-69

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 219.61  E-value: 8.15e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213054032   1 GMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVA 80
Cdd:COG0843  297 GISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVA 376

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 213054032  81 HFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTSWNV 157
Cdd:COG0843  377 HFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNL 455
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-210 3.89e-66

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: 211.70  E-value: 3.89e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213054032    1 GMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVA 80
Cdd:TIGR02891 288 GMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVA 367

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213054032   81 HFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDA--YTSWNVI 158
Cdd:TIGR02891 368 HFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLI 447

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 213054032  159 SSIGSTISIVGIIMFIIIMWESMISNRTVMFSSNMSSSTEWLQNNPPAEHSY 210
Cdd:TIGR02891 448 STIGAFILAAGFLVFLWNLIWSLRKGPKAGANPWGATTLEWTTSSPPPAHNF 499
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-157 3.94e-50

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: 168.14  E-value: 3.94e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213054032    1 GMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFN-PPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVV 79
Cdd:pfam00115 263 GLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFRtTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVV 342

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213054032   80 AHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYS----DYPDAYTSW 155
Cdd:pfam00115 343 AHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPL 422


                  ..
gi 213054032  156 NV 157
Cdd:pfam00115 423 NW 424
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-218 1.41e-145

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 415.42  E-value: 1.41e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213054032   1 GMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVA 80
Cdd:MTH00153 294 GMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVA 373

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213054032  81 HFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISS 160
Cdd:MTH00153 374 HFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISS 453

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 213054032 161 IGSTISIVGIIMFIIIMWESMISNRTVMFSSNMSSSTEWLQNNPPAEHSYSELPLITS 218
Cdd:MTH00153 454 IGSTISLISILFFIFIIWESMISKRPVLFSLNLSSSIEWLQNLPPAEHSYSELPLLTN 511
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-216 2.02e-113

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 333.57  E-value: 2.02e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213054032   1 GMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVA 80
Cdd:MTH00167 296 GMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVA 375

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213054032  81 HFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISS 160
Cdd:MTH00167 376 HFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSS 455

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 213054032 161 IGSTISIVGIIMFIIIMWESMISNRTVMFSSNMSSSTEWLQNNPPAEHSYSELPLI 216
Cdd:MTH00167 456 IGSLISLVAVILFLFIIWEAFSSKRKLLPVELTSTNVEWLHGCPPPHHTWEEPPFV 511
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-201 7.41e-113

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: 331.37  E-value: 7.41e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213054032   1 GMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVA 80
Cdd:cd01663  287 GLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVA 366

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213054032  81 HFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISS 160
Cdd:cd01663  367 HFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISS 446

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 213054032 161 IGSTISIVGIIMFIIIMWESMISNRTVMFSSN-MSSSTEWLQ 201
Cdd:cd01663  447 IGSLISFVSVLLFLFIVWESFVSGRKVIFNVGeGSTSLEWTL 488
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-216 5.50e-112

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 330.13  E-value: 5.50e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213054032   1 GMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVA 80
Cdd:MTH00116 296 GMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVA 375

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213054032  81 HFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISS 160
Cdd:MTH00116 376 HFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISS 455

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 213054032 161 IGSTISIVGIIMFIIIMWESMISNRTVMFSSNMSSSTEWLQNNPPAEHSYSELPLI 216
Cdd:MTH00116 456 IGSLISMTAVIMLMFIIWEAFSSKRKVLQPELTTTNIEWIHGCPPPYHTFEEPAFV 511
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-216 1.82e-111

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 328.61  E-value: 1.82e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213054032   1 GMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVA 80
Cdd:MTH00142 294 GMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVA 373

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213054032  81 HFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISS 160
Cdd:MTH00142 374 HFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSS 453

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 213054032 161 IGSTISIVGIIMFIIIMWESMISNRTVMFSSNMSSSTEWLQNNPPAEHSYSELPLI 216
Cdd:MTH00142 454 LGSMISFIAVLMFVFIVWESFVSQRLVMWSSHLSTSLEWSHRLPPDFHTYDELPIL 509
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-219 2.80e-110

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 325.39  E-value: 2.80e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213054032   1 GMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVA 80
Cdd:MTH00223 293 GMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVA 372

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213054032  81 HFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISS 160
Cdd:MTH00223 373 HFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSS 452

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 213054032 161 IGSTISIVGIIMFIIIMWESMISNRTVMFSSNMSSSTEWLQNNPPAEHSYSELPLITSF 219
Cdd:MTH00223 453 FGSMISFVSVLFFMFIVWEAFVSQRSVVWSGHLSTSLEWDNLLPADFHNNSETGALVIN 511
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-218 4.79e-99

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 296.79  E-value: 4.79e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213054032   1 GMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVA 80
Cdd:MTH00103 296 GMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVA 375

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213054032  81 HFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISS 160
Cdd:MTH00103 376 HFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSS 455

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 213054032 161 IGSTISIVGIIMFIIIMWESMISNRTVMFSSNMSSSTEWLQNNPPAEHSYSELPLITS 218
Cdd:MTH00103 456 MGSFISLTAVMLMIFMIWEAFASKREVLTVELTTTNLEWLHGCPPPYHTFEEPTYVKL 513
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-216 7.82e-98

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 293.75  E-value: 7.82e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213054032   1 GMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVA 80
Cdd:MTH00183 296 GMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVA 375

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213054032  81 HFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISS 160
Cdd:MTH00183 376 HFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSS 455

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 213054032 161 IGSTISIVGIIMFIIIMWESMISNRTVMFSSNMSSSTEWLQNNPPAEHSYSELPLI 216
Cdd:MTH00183 456 IGSLISLVAVIMFLFILWEAFAAKREVLSVELTSTNVEWLHGCPPPYHTFEEPAFV 511
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-217 3.08e-95

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 287.11  E-value: 3.08e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213054032   1 GMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVA 80
Cdd:MTH00037 296 GMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVA 375

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213054032  81 HFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISS 160
Cdd:MTH00037 376 HFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSS 455

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 213054032 161 IGSTISIVGIIMFIIIMWESMISNRTVMFSSNMSSSTEWLQNN-PPAEHSYSELPLIT 217
Cdd:MTH00037 456 IGSTISLVATLFFLFLIWEAFASQREVISPEFSSSSLEWQYSSfPPSHHTFDETPSTV 513
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-218 1.08e-94

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 285.64  E-value: 1.08e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213054032   1 GMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVA 80
Cdd:MTH00007 293 GMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVA 372

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213054032  81 HFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISS 160
Cdd:MTH00007 373 HFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSS 452

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 213054032 161 IGSTISIVGIIMFIIIMWESMISNRTVMFSSNMSSSTEWLQNNPPAEHSYSELPLITS 218
Cdd:MTH00007 453 FGSMLSFVALLLFIFILWEAFSAQRGVIASPHMSSSLEWQDTLPLDFHNLPETGIITT 510
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-212 6.37e-94

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 283.76  E-value: 6.37e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213054032   1 GMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVA 80
Cdd:MTH00077 296 DLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVA 375

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213054032  81 HFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISS 160
Cdd:MTH00077 376 HFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSS 455

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 213054032 161 IGSTISIVGIIMFIIIMWESMISNRTVMFSSNMSSSTEWLQNNPPAEHSYSE 212
Cdd:MTH00077 456 IGSLISLVAVIMMMFIIWEAFSSKREVLTTELTSTNIEWLHGCPPPYHTFEE 507
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-212 1.41e-85

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 261.92  E-value: 1.41e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213054032   1 GMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVA 80
Cdd:MTH00079 296 GMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVS 375

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213054032  81 HFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISS 160
Cdd:MTH00079 376 HFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISS 455

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 213054032 161 IGSTISIVGIIMFIIIMWESMISNRTVMFSSNMSSSTEWLQNNPPAEHSYSE 212
Cdd:MTH00079 456 YGSMISVFALFLFIYVLLESFFSYRLVLHDNYINSSPEYSLSSYVFGHSYQS 507
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-219 5.15e-82

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 253.59  E-value: 5.15e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213054032   1 GMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVA 80
Cdd:MTH00182 298 GMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVA 377

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213054032  81 HFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISS 160
Cdd:MTH00182 378 HFHYVLSMGAVFAIFGGFYYWFGKITGYCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSS 457

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 213054032 161 IGSTISIVGIIMFIIIMWESMISNRT----VMFSSNMSSSTEWLQNNPPAEHSYSELPLITSF 219
Cdd:MTH00182 458 LGSIISIVGVVWFIYIIYDAYVREEKfigwKEGTGESWASLEWVHSSPPLFHTYNELPFVYKS 520
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-216 2.05e-80

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 248.97  E-value: 2.05e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213054032   1 GMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVA 80
Cdd:MTH00184 298 GMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVA 377

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213054032  81 HFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISS 160
Cdd:MTH00184 378 HFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISS 457

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 213054032 161 IGSTISIVGIIMFIIIMWESM---ISNRTVMFSSNMSSSTEWLQNNPPAEHSYSELPLI 216
Cdd:MTH00184 458 LGSVISIVGVVWFIYIVYDAYvreIKFVGWVEDSGHYPSLEWAQTSPPAHHTYNELPYV 516
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-157 8.02e-76

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: 235.50  E-value: 8.02e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213054032   1 GMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVA 80
Cdd:cd00919  283 GLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVA 362

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 213054032  81 HFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNV 157
Cdd:cd00919  363 HFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNF 439
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-157 8.15e-69

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 219.61  E-value: 8.15e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213054032   1 GMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVA 80
Cdd:COG0843  297 GISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVA 376

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 213054032  81 HFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTSWNV 157
Cdd:COG0843  377 HFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNL 455
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-210 3.89e-66

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: 211.70  E-value: 3.89e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213054032    1 GMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVA 80
Cdd:TIGR02891 288 GMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVA 367

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213054032   81 HFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDA--YTSWNVI 158
Cdd:TIGR02891 368 HFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLI 447

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 213054032  159 SSIGSTISIVGIIMFIIIMWESMISNRTVMFSSNMSSSTEWLQNNPPAEHSY 210
Cdd:TIGR02891 448 STIGAFILAAGFLVFLWNLIWSLRKGPKAGANPWGATTLEWTTSSPPPAHNF 499
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-216 4.70e-64

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 207.17  E-value: 4.70e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213054032   1 GMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGT--KFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYV 78
Cdd:MTH00026 297 GMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSgrNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYV 376

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213054032  79 VAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVI 158
Cdd:MTH00026 377 VAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQI 456

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 213054032 159 SSIGSTISIVGIIMFIIIMWES-----------MISNRTVMFSSNMS--SSTEWLQNNPPAEHSYSELPLI 216
Cdd:MTH00026 457 SSFGSIISIIAVIWFIVVIFDAyyreepfdiniMAKGPLIPFSCQPAhfDTLEWSLTSPPEHHTYNELPYI 527
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 8-157 1.89e-60

Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory chains of aerobic bacteria, is a multi-chain transmembrane protein located in the cell membrane. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits in ubiquinol oxidase varies from two to five. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons from ubiquinol to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from ubiquinol on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. It is generally believed that the channels contain water molecules that act as 'proton wires' to transfer the protons. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are believed to be transferred directly from ubiquinol (the electron donor) to the low-spin heme, and directly from the low-spin heme to the binuclear center.


Pssm-ID: 238832  Cd Length: 501  Bit Score: 197.03  E-value: 1.89e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213054032   8 AYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLS 87
Cdd:cd01662  296 AFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLI 375

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 213054032  88 MGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTSWNV 157
Cdd:cd01662  376 GGVVFPLFAGFYYWFPKMFGRMLNERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpgPGWDPLNL 447
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-209 3.15e-55

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 183.34  E-value: 3.15e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213054032   1 GMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLL-WALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVV 79
Cdd:MTH00048 294 GLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKSDPVVwWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVV 373

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213054032  80 AHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVIS 159
Cdd:MTH00048 374 AHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVC 453

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 213054032 160 SIGSTISIVGIIMFIIIMWESMISNRTVMFSSNMSSSTEWLQNNPPAEHS 209
Cdd:MTH00048 454 TVGSFISAFSGCFFVFILWESLVVKNEVLGLWGSSSCVVNVLMSPVPYHN 503
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-157 3.94e-50

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: 168.14  E-value: 3.94e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213054032    1 GMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFN-PPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVV 79
Cdd:pfam00115 263 GLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFRtTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVV 342

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213054032   80 AHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYS----DYPDAYTSW 155
Cdd:pfam00115 343 AHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPL 422


                  ..
gi 213054032  156 NV 157
Cdd:pfam00115 423 NW 424
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 6-219 2.26e-38

cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]


Pssm-ID: 131928  Cd Length: 643  Bit Score: 139.99  E-value: 2.26e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213054032    6 TRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYV 85
Cdd:TIGR02882 337 INSFFSITTMAIAIPTGVKIFNWLLTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYV 416

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213054032   86 LSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDY--PDAYTSWNVISSIGS 163
Cdd:TIGR02882 417 LITGVVFACLAGLIYWYPKMFGYKLNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYspSDGWFPLNLISTIGA 496

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 213054032  164 TISIVGIIMFIIIMWESMISNRTVMFSSNMSSST-EWLQNNPPAEHSYSELPLITSF 219
Cdd:TIGR02882 497 LLMAIGFIFLVYNIYYSHRKSPREATGDPWNGRTlEWATASPPPKYNFAVTPDVNDY 553
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 1-150 1.44e-35

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 132.37  E-value: 1.44e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213054032   1 GMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVA 80
Cdd:PRK15017 339 GAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIA 418

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213054032  81 HFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPD 150
Cdd:PRK15017 419 HFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQID 488
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 14-155 6.75e-12

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: 63.84  E-value: 6.75e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213054032  14 TMIIAVPTGIKVFSWLATL-YGTKFKFNPPLLW---------------ALGFIFlFTIGGLTGLILANSSLDIVLHDTYY 77
Cdd:cd01660  282 TFMVALPSLLTAFTVFASLeIAGRLRGGKGLFGwiralpwgdpmflalFLAMLM-FIPGGAGGIINASYQLNYVVHNTAW 360

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213054032  78 VVAHFHyvLSMGAVFAIMG-GIIQWY-PLFTGLTMNNTWL-KIQFAIMFIGVNLTFFPQHFLGLAGMPRR--YSDYPD-- 150
Cdd:cd01660  361 VPGHFH--LTVGGAVALTFmAVAYWLvPHLTGRELAAKRLaLAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYGGlp 438


                 ....*
gi 213054032 151 AYTSW 155
Cdd:cd01660  439 AAGEW 443
 
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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