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Conserved domains on  [gi|1318866517|gb|AUJ87834|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Icosta sp. 2 ES-2018]

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 ...
 1-191 6.60e-122

Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. Membership in the superfamily is defined by subunit I, which contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons to the binuclear center. Only subunit I is common to the entire superfamily. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from the electron donor on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I of cytochrome c oxidase (CcO) and ubiquinol oxidase. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electron transfer occurs in two segments: from the electron donor to the low-spin heme, and from the low-spin heme to the binuclear center. The first segment can be a multi-step process and varies among the different families, while the second segment, a direct transfer, is consistent throughout the superfamily.


The actual alignment was detected with superfamily member MTH00153:

Pssm-ID: 469701  Cd Length: 511  Bit Score: 353.79  E-value: 6.60e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318866517   1 GIKIFSWLATLHGTQLSYSPAMLWTLGFIFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHW 80
Cdd:MTH00153  315 GIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHW 394

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318866517  81 YPLLSGFTMNKFLLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVISSIGSSISLLGIIMFFIIIWESI 160
Cdd:MTH00153  395 FPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESM 474

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1318866517 161 ISKRMVIFNNHLNSSIEWLQNNPPAEHSYSE 191
Cdd:MTH00153  475 ISKRPVLFSLNLSSSIEWLQNLPPAEHSYSE 505
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-191 6.60e-122

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 353.79  E-value: 6.60e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318866517   1 GIKIFSWLATLHGTQLSYSPAMLWTLGFIFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHW 80
Cdd:MTH00153  315 GIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHW 394

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318866517  81 YPLLSGFTMNKFLLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVISSIGSSISLLGIIMFFIIIWESI 160
Cdd:MTH00153  395 FPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESM 474

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1318866517 161 ISKRMVIFNNHLNSSIEWLQNNPPAEHSYSE 191
Cdd:MTH00153  475 ISKRPVLFSLNLSSSIEWLQNLPPAEHSYSE 505
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-180 4.52e-96

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: 287.07  E-value: 4.52e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318866517   1 GIKIFSWLATLHGTQLSYSPAMLWTLGFIFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHW 80
Cdd:cd01663   308 GIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYW 387

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318866517  81 YPLLSGFTMNKFLLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVISSIGSSISLLGIIMFFIIIWESI 160
Cdd:cd01663   388 FPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESF 467

                         170       180
                  ....*....|....*....|.
gi 1318866517 161 ISKRMVIFN-NHLNSSIEWLQ 180
Cdd:cd01663   468 VSGRKVIFNvGEGSTSLEWTL 488
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-187 2.08e-59

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 193.81  E-value: 2.08e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318866517   1 GIKIFSWLATLHGTQLSYSPAMLWTLGFIFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHW 80
Cdd:COG0843   318 GVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYW 397

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318866517  81 YPLLSGFTMNKFLLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTTWNVISSIGSSISLLGIIMFFIIIWE 158
Cdd:COG0843   398 FPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVV 477

                         170       180
                  ....*....|....*....|....*....
gi 1318866517 159 SIISKRMVIFNNHLNSSIEWLQNNPPAEH 187
Cdd:COG0843   478 SLRKGPKAGGNPWGARTLEWATPSPPPLY 506
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-189 3.86e-56

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: 184.35  E-value: 3.86e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318866517   1 GIKIFSWLATLHGTQLSYSPAMLWTLGFIFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHW 80
Cdd:TIGR02891 309 GVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYW 388

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318866517  81 YPLLSGFTMNKFLLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDA--YTTWNVISSIGSSISLLGIIMFFIIIWE 158
Cdd:TIGR02891 389 FPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIW 468

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1318866517 159 SIISKRMVIFNNHLNSSIEWLQNNPPAEHSY 189
Cdd:TIGR02891 469 SLRKGPKAGANPWGATTLEWTTSSPPPAHNF 499
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-136 6.30e-40

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: 140.40  E-value: 6.30e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318866517   1 GIKIFSWLATLHGTQLS-YSPAMLWTLGFIFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIH 79
Cdd:pfam00115 284 GVKVFNWLATLWGGWIRfRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYY 363

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1318866517  80 WYPLLSGFTMNKFLLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYS----DYPDAYTTWNV 136
Cdd:pfam00115 364 WLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNW 424
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-191 6.60e-122

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 353.79  E-value: 6.60e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318866517   1 GIKIFSWLATLHGTQLSYSPAMLWTLGFIFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHW 80
Cdd:MTH00153  315 GIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHW 394

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318866517  81 YPLLSGFTMNKFLLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVISSIGSSISLLGIIMFFIIIWESI 160
Cdd:MTH00153  395 FPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESM 474

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1318866517 161 ISKRMVIFNNHLNSSIEWLQNNPPAEHSYSE 191
Cdd:MTH00153  475 ISKRPVLFSLNLSSSIEWLQNLPPAEHSYSE 505
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-191 3.38e-96

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 288.11  E-value: 3.38e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318866517   1 GIKIFSWLATLHGTQLSYSPAMLWTLGFIFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHW 80
Cdd:MTH00167  317 GIKVFSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHW 396

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318866517  81 YPLLSGFTMNKFLLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVISSIGSSISLLGIIMFFIIIWESI 160
Cdd:MTH00167  397 FPLFTGLTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAF 476

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1318866517 161 ISKRMVIFNNHLNSSIEWLQNNPPAEHSYSE 191
Cdd:MTH00167  477 SSKRKLLPVELTSTNVEWLHGCPPPHHTWEE 507
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-180 4.52e-96

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: 287.07  E-value: 4.52e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318866517   1 GIKIFSWLATLHGTQLSYSPAMLWTLGFIFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHW 80
Cdd:cd01663   308 GIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYW 387

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318866517  81 YPLLSGFTMNKFLLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVISSIGSSISLLGIIMFFIIIWESI 160
Cdd:cd01663   388 FPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESF 467

                         170       180
                  ....*....|....*....|.
gi 1318866517 161 ISKRMVIFN-NHLNSSIEWLQ 180
Cdd:cd01663   468 VSGRKVIFNvGEGSTSLEWTL 488
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-191 5.55e-94

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 282.75  E-value: 5.55e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318866517   1 GIKIFSWLATLHGTQLSYSPAMLWTLGFIFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHW 80
Cdd:MTH00116  317 GIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHW 396

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318866517  81 YPLLSGFTMNKFLLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVISSIGSSISLLGIIMFFIIIWESI 160
Cdd:MTH00116  397 FPLFTGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAF 476

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1318866517 161 ISKRMVIFNNHLNSSIEWLQNNPPAEHSYSE 191
Cdd:MTH00116  477 SSKRKVLQPELTTTNIEWIHGCPPPYHTFEE 507
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-191 2.75e-93

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 280.84  E-value: 2.75e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318866517   1 GIKIFSWLATLHGTQLSYSPAMLWTLGFIFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHW 80
Cdd:MTH00142  315 GIKVFSWLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHW 394

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318866517  81 YPLLSGFTMNKFLLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVISSIGSSISLLGIIMFFIIIWESI 160
Cdd:MTH00142  395 FPLFTGLTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESF 474

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1318866517 161 ISKRMVIFNNHLNSSIEWLQNNPPAEHSYSE 191
Cdd:MTH00142  475 VSQRLVMWSSHLSTSLEWSHRLPPDFHTYDE 505
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-191 4.23e-92

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 277.63  E-value: 4.23e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318866517   1 GIKIFSWLATLHGTQLSYSPAMLWTLGFIFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHW 80
Cdd:MTH00223  314 GIKVFSWLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHW 393

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318866517  81 YPLLSGFTMNKFLLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVISSIGSSISLLGIIMFFIIIWESI 160
Cdd:MTH00223  394 FPLFTGVTLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAF 473

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1318866517 161 ISKRMVIFNNHLNSSIEWLQNNPPAEHSYSE 191
Cdd:MTH00223  474 VSQRSVVWSGHLSTSLEWDNLLPADFHNNSE 504
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-191 1.46e-84

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 258.66  E-value: 1.46e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318866517   1 GIKIFSWLATLHGTQLSYSPAMLWTLGFIFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHW 80
Cdd:MTH00103  317 GVKVFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHW 396

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318866517  81 YPLLSGFTMNKFLLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVISSIGSSISLLGIIMFFIIIWESI 160
Cdd:MTH00103  397 FPLFSGYTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAF 476

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1318866517 161 ISKRMVIFNNHLNSSIEWLQNNPPAEHSYSE 191
Cdd:MTH00103  477 ASKREVLTVELTTTNLEWLHGCPPPYHTFEE 507
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-191 5.31e-82

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 251.78  E-value: 5.31e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318866517   1 GIKIFSWLATLHGTQLSYSPAMLWTLGFIFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHW 80
Cdd:MTH00077  317 GVKVFSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHW 396

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318866517  81 YPLLSGFTMNKFLLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVISSIGSSISLLGIIMFFIIIWESI 160
Cdd:MTH00077  397 FPLFSGYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAF 476

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1318866517 161 ISKRMVIFNNHLNSSIEWLQNNPPAEHSYSE 191
Cdd:MTH00077  477 SSKREVLTTELTSTNIEWLHGCPPPYHTFEE 507
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-191 1.10e-81

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 251.00  E-value: 1.10e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318866517   1 GIKIFSWLATLHGTQLSYSPAMLWTLGFIFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHW 80
Cdd:MTH00183  317 GVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHW 396

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318866517  81 YPLLSGFTMNKFLLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVISSIGSSISLLGIIMFFIIIWESI 160
Cdd:MTH00183  397 FPLFSGYTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAF 476

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1318866517 161 ISKRMVIFNNHLNSSIEWLQNNPPAEHSYSE 191
Cdd:MTH00183  477 AAKREVLSVELTSTNVEWLHGCPPPYHTFEE 507
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-191 4.75e-79

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 244.43  E-value: 4.75e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318866517   1 GIKIFSWLATLHGTQLSYSPAMLWTLGFIFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHW 80
Cdd:MTH00007  314 GIKVFSWLATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHW 393

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318866517  81 YPLLSGFTMNKFLLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVISSIGSSISLLGIIMFFIIIWESI 160
Cdd:MTH00007  394 FPLFTGLTLHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAF 473

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1318866517 161 ISKRMVIFNNHLNSSIEWLQNNPPAEHSYSE 191
Cdd:MTH00007  474 SAQRGVIASPHMSSSLEWQDTLPLDFHNLPE 504
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-191 4.98e-79

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 244.35  E-value: 4.98e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318866517   1 GIKIFSWLATLHGTQLSYSPAMLWTLGFIFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHW 80
Cdd:MTH00037  317 GIKVFSWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHW 396

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318866517  81 YPLLSGFTMNKFLLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVISSIGSSISLLGIIMFFIIIWESI 160
Cdd:MTH00037  397 FPLFSGVSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAF 476

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1318866517 161 ISKRMVIFNNHLNSSIEWLQNN-PPAEHSYSE 191
Cdd:MTH00037  477 ASQREVISPEFSSSSLEWQYSSfPPSHHTFDE 508
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-191 1.73e-73

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 229.57  E-value: 1.73e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318866517   1 GIKIFSWLATLHGTQLSYSPAMLWTLGFIFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHW 80
Cdd:MTH00079  317 GVKVFSWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLW 396

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318866517  81 YPLLSGFTMNKFLLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVISSIGSSISLLGIIMFFIIIWESI 160
Cdd:MTH00079  397 WPFMTGIVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESF 476

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1318866517 161 ISKRMVIFNNHLNSSIEWLQNNPPAEHSYSE 191
Cdd:MTH00079  477 FSYRLVLHDNYINSSPEYSLSSYVFGHSYQS 507
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-191 2.91e-65

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 208.91  E-value: 2.91e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318866517   1 GIKIFSWLATLHGTQLSYSPAMLWTLGFIFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHW 80
Cdd:MTH00182  319 GIKVFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYW 398

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318866517  81 YPLLSGFTMNKFLLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVISSIGSSISLLGIIMFFIIIWESI 160
Cdd:MTH00182  399 FGKITGYCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAY 478

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1318866517 161 ISKRMVIFNNHLN----SSIEWLQNNPPAEHSYSE 191
Cdd:MTH00182  479 VREEKFIGWKEGTgeswASLEWVHSSPPLFHTYNE 513
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-191 2.65e-63

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 203.52  E-value: 2.65e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318866517   1 GIKIFSWLATLHGTQLSYSPAMLWTLGFIFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHW 80
Cdd:MTH00184  319 GIKIFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYW 398

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318866517  81 YPLLSGFTMNKFLLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVISSIGSSISLLGIIMFFIIIWESI 160
Cdd:MTH00184  399 FGKITGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAY 478

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1318866517 161 isKRMVIF-----NNHLNSSIEWLQNNPPAEHSYSE 191
Cdd:MTH00184  479 --VREIKFvgwveDSGHYPSLEWAQTSPPAHHTYNE 512
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-160 1.70e-62

Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. Membership in the superfamily is defined by subunit I, which contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons to the binuclear center. Only subunit I is common to the entire superfamily. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from the electron donor on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I of cytochrome c oxidase (CcO) and ubiquinol oxidase. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electron transfer occurs in two segments: from the electron donor to the low-spin heme, and from the low-spin heme to the binuclear center. The first segment can be a multi-step process and varies among the different families, while the second segment, a direct transfer, is consistent throughout the superfamily.


Pssm-ID: 238461  Cd Length: 463  Bit Score: 200.06  E-value: 1.70e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318866517   1 GIKIFSWLATLHGTQLSYSPAMLWTLGFIFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHW 80
Cdd:cd00919   304 GIKVFNWLATLWGGRIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYW 383

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318866517  81 YPLLSGFTMNKFLLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVISSIGSSISLLGIIMFFIIIWESI 160
Cdd:cd00919   384 FPKMTGRMLSEKLGKIHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-187 2.08e-59

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 193.81  E-value: 2.08e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318866517   1 GIKIFSWLATLHGTQLSYSPAMLWTLGFIFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHW 80
Cdd:COG0843   318 GVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYW 397

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318866517  81 YPLLSGFTMNKFLLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTTWNVISSIGSSISLLGIIMFFIIIWE 158
Cdd:COG0843   398 FPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVV 477

                         170       180
                  ....*....|....*....|....*....
gi 1318866517 159 SIISKRMVIFNNHLNSSIEWLQNNPPAEH 187
Cdd:COG0843   478 SLRKGPKAGGNPWGARTLEWATPSPPPLY 506
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-189 3.86e-56

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: 184.35  E-value: 3.86e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318866517   1 GIKIFSWLATLHGTQLSYSPAMLWTLGFIFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHW 80
Cdd:TIGR02891 309 GVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYW 388

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318866517  81 YPLLSGFTMNKFLLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDA--YTTWNVISSIGSSISLLGIIMFFIIIWE 158
Cdd:TIGR02891 389 FPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIW 468

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1318866517 159 SIISKRMVIFNNHLNSSIEWLQNNPPAEHSY 189
Cdd:TIGR02891 469 SLRKGPKAGANPWGATTLEWTTSSPPPAHNF 499
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-189 2.01e-53

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


Pssm-ID: 238832  Cd Length: 501  Bit Score: 177.39  E-value: 2.01e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318866517   1 GIKIFSWLATLHGTQLSYSPAMLWTLGFIFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHW 80
Cdd:cd01662   310 GVKIFNWLFTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYW 389

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318866517  81 YPLLSGFTMNKFLLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTTWNVISSIGSSISLLGIIMFFIIIWE 158
Cdd:cd01662   390 FPKMFGRMLNERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpgPGWDPLNLISTIGAFLIAAGVLLFLINVIV 469

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1318866517 159 SIISKRMVIFNNHLN-SSIEWLQNNPPAEHSY 189
Cdd:cd01662   470 SIRKGKRDATGDPWGaRTLEWATSSPPPAYNF 501
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-191 1.32e-48

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 165.19  E-value: 1.32e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318866517   1 GIKIFSWLATLHGT--QLSYSPAMLWTLGFIFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFI 78
Cdd:MTH00026  318 GIKIFSWLATVSGSgrNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFY 397

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318866517  79 HWYPLLSGFTMNKFLLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVISSIGSSISLLGIIMFFIIIWE 158
Cdd:MTH00026  398 LWFGKITGYAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFD 477

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1318866517 159 SIISKRMVIFNNHLN-------------SSIEWLQNNPPAEHSYSE 191
Cdd:MTH00026  478 AYYREEPFDINIMAKgplipfscqpahfDTLEWSLTSPPEHHTYNE 523
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-188 2.37e-48

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 164.08  E-value: 2.37e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318866517   1 GIKIFSWLATLHGTQLSYS-PAMLWTLGFIFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIH 79
Cdd:MTH00048  315 GIKVFSWLYMLLNSRVRKSdPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIW 394

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318866517  80 WYPLLSGFTMNKFLLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVISSIGSSISLLGIIMFFIIIWES 159
Cdd:MTH00048  395 WWPLITGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWES 474

                         170       180
                  ....*....|....*....|....*....
gi 1318866517 160 IISKRMVIFNNHLNSSIEWLQNNPPAEHS 188
Cdd:MTH00048  475 LVVKNEVLGLWGSSSCVVNVLMSPVPYHN 503
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-136 6.30e-40

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: 140.40  E-value: 6.30e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318866517   1 GIKIFSWLATLHGTQLS-YSPAMLWTLGFIFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIH 79
Cdd:pfam00115 284 GVKVFNWLATLWGGWIRfRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYY 363

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1318866517  80 WYPLLSGFTMNKFLLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYS----DYPDAYTTWNV 136
Cdd:pfam00115 364 WLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNW 424
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 1-190 2.13e-34

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: 127.66  E-value: 2.13e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318866517   1 GIKIFSWLATLHGTQLSYSPAMLWTLGFIFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHW 80
Cdd:TIGR02882 353 GVKIFNWLLTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYW 432

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318866517  81 YPLLSGFTMNKFLLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDY--PDAYTTWNVISSI-GSSISLLGIIMFFIIIW 157
Cdd:TIGR02882 433 YPKMFGYKLNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYspSDGWFPLNLISTIgALLMAIGFIFLVYNIYY 512

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1318866517 158 ESIISKRMVIFNNHLNSSIEWLQNNPPAEHSYS 190
Cdd:TIGR02882 513 SHRKSPREATGDPWNGRTLEWATASPPPKYNFA 545
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 1-129 3.59e-29

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 113.11  E-value: 3.59e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318866517   1 GIKIFSWLATLHGTQLSYSPAMLWTLGFIFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHW 80
Cdd:PRK15017  360 GVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYW 439

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1318866517  81 YPLLSGFTMNKFLLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPD 129
Cdd:PRK15017  440 WPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQID 488
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 1-134 8.82e-11

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: 59.99  E-value: 8.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318866517   1 GIKIFSWLATLHGTQLSYSPAMLWTLGFIFlftvGGLTGVILANSSIDIILHDTYYVVAHFHyvLSMGAVFAIMA-GFIH 79
Cdd:cd01660   309 GKGLFGWIRALPWGDPMFLALFLAMLMFIP----GGAGGIINASYQLNYVVHNTAWVPGHFH--LTVGGAVALTFmAVAY 382

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1318866517  80 WY-PLLSGFTM-NKFLLKSQFIIMFIGVNLTFFPQHFLGLAGMPRR--YSDYPD--AYTTW 134
Cdd:cd01660   383 WLvPHLTGRELaAKRLALAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYGGlpAAGEW 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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