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Conserved domains on  [gi|34537029|gb|AAQ73974|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Amazona versicolor]

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 ...
 1-187 2.47e-131

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 MTH00116:

Pssm-ID: 469701  Cd Length: 515  Bit Score: 377.90  E-value: 2.47e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029    1 FGHPEVYILILPGFGIISHVVAYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTG 80
Cdd:MTH00116 238 FGHPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTG 317

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029   81 IKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIILANSSLDIALHDTYYVVAHFHYVLSMGAVFAILAGLTHWF 160
Cdd:MTH00116 318 IKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWF 397

                        170       180
                 ....*....|....*....|....*..
gi 34537029  161 PLFTGYTLNQSWAKAHFGVMFTGVNLT 187
Cdd:MTH00116 398 PLFTGYTLHQTWTKAQFGVMFTGVNLT 424
 
Name Accession Description Interval E-value
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-187 2.47e-131

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 377.90  E-value: 2.47e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029    1 FGHPEVYILILPGFGIISHVVAYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTG 80
Cdd:MTH00116 238 FGHPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTG 317

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029   81 IKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIILANSSLDIALHDTYYVVAHFHYVLSMGAVFAILAGLTHWF 160
Cdd:MTH00116 318 IKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWF 397

                        170       180
                 ....*....|....*....|....*..
gi 34537029  161 PLFTGYTLNQSWAKAHFGVMFTGVNLT 187
Cdd:MTH00116 398 PLFTGYTLHQTWTKAQFGVMFTGVNLT 424
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-187 1.02e-129

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: 372.59  E-value: 1.02e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029   1 FGHPEVYILILPGFGIISHVVAYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTG 80
Cdd:cd01663 229 FGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTG 308

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029  81 IKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIILANSSLDIALHDTYYVVAHFHYVLSMGAVFAILAGLTHWF 160
Cdd:cd01663 309 IKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWF 388

                       170       180
                ....*....|....*....|....*..
gi 34537029 161 PLFTGYTLNQSWAKAHFGVMFTGVNLT 187
Cdd:cd01663 389 PKITGLSYNETLGKIHFWLMFIGVNLT 415
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-187 3.00e-84

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 258.13  E-value: 3.00e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029   1 FGHPEVYILILPGFGIISHVVAYYAGKKePFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTG 80
Cdd:COG0843 240 FGHPEVYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTG 318

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029  81 IKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIILANSSLDIALHDTYYVVAHFHYVLSMGAVFAILAGLTHWF 160
Cdd:COG0843 319 VKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWF 398

                       170       180
                ....*....|....*....|....*..
gi 34537029 161 PLFTGYTLNQSWAKAHFGVMFTGVNLT 187
Cdd:COG0843 399 PKMTGRMLNERLGKIHFWLWFIGFNLT 425
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-187 5.49e-83

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: 253.68  E-value: 5.49e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029     1 FGHPEVYILILPGFGIISHVVAYYAGKKePFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTG 80
Cdd:TIGR02891 231 FGHPEVYIIFLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTG 309

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029    81 IKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIILANSSLDIALHDTYYVVAHFHYVLSMGAVFAILAGLTHWF 160
Cdd:TIGR02891 310 VKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWF 389

                         170       180
                  ....*....|....*....|....*..
gi 34537029   161 PLFTGYTLNQSWAKAHFGVMFTGVNLT 187
Cdd:TIGR02891 390 PKVTGRMYNERLGRWHFWLTFVGFNLT 416
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-187 2.18e-59

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: 191.25  E-value: 2.18e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029     1 FGHPEVYILILPGFGIISHVVAYYAGKKePFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTG 80
Cdd:pfam00115 206 FGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSG 284

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029    81 IKVFSWLATLHGGTIKW-DPPMLWALGFIFLFTIGGLTGIILANSSLDIALHDTYYVVAHFHYVLSMGAVFAILAGLTHW 159
Cdd:pfam00115 285 VKVFNWLATLWGGWIRFrTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYW 364

                         170       180
                  ....*....|....*....|....*...
gi 34537029   160 FPLFTGYTLNQSWAKAHFGVMFTGVNLT 187
Cdd:pfam00115 365 LPKLTGRMYSEKLGKLHFWLLFIGFNLT 392
 
Name Accession Description Interval E-value
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-187 2.47e-131

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 377.90  E-value: 2.47e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029    1 FGHPEVYILILPGFGIISHVVAYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTG 80
Cdd:MTH00116 238 FGHPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTG 317

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029   81 IKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIILANSSLDIALHDTYYVVAHFHYVLSMGAVFAILAGLTHWF 160
Cdd:MTH00116 318 IKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWF 397

                        170       180
                 ....*....|....*....|....*..
gi 34537029  161 PLFTGYTLNQSWAKAHFGVMFTGVNLT 187
Cdd:MTH00116 398 PLFTGYTLHQTWTKAQFGVMFTGVNLT 424
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-187 8.63e-131

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 376.13  E-value: 8.63e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029    1 FGHPEVYILILPGFGIISHVVAYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTG 80
Cdd:MTH00153 236 FGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTG 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029   81 IKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIILANSSLDIALHDTYYVVAHFHYVLSMGAVFAILAGLTHWF 160
Cdd:MTH00153 316 IKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWF 395

                        170       180
                 ....*....|....*....|....*..
gi 34537029  161 PLFTGYTLNQSWAKAHFGVMFTGVNLT 187
Cdd:MTH00153 396 PLFTGLTMNPKWLKIQFFIMFIGVNLT 422
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-187 1.02e-129

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: 372.59  E-value: 1.02e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029   1 FGHPEVYILILPGFGIISHVVAYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTG 80
Cdd:cd01663 229 FGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTG 308

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029  81 IKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIILANSSLDIALHDTYYVVAHFHYVLSMGAVFAILAGLTHWF 160
Cdd:cd01663 309 IKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWF 388

                       170       180
                ....*....|....*....|....*..
gi 34537029 161 PLFTGYTLNQSWAKAHFGVMFTGVNLT 187
Cdd:cd01663 389 PKITGLSYNETLGKIHFWLMFIGVNLT 415
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-187 1.45e-126

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 365.54  E-value: 1.45e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029    1 FGHPEVYILILPGFGIISHVVAYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTG 80
Cdd:MTH00167 238 FGHPEVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTG 317

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029   81 IKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIILANSSLDIALHDTYYVVAHFHYVLSMGAVFAILAGLTHWF 160
Cdd:MTH00167 318 IKVFSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWF 397

                        170       180
                 ....*....|....*....|....*..
gi 34537029  161 PLFTGYTLNQSWAKAHFGVMFTGVNLT 187
Cdd:MTH00167 398 PLFTGLTLNETWTKIHFFVMFIGVNLT 424
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-187 1.18e-116

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 340.42  E-value: 1.18e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029    1 FGHPEVYILILPGFGIISHVVAYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTG 80
Cdd:MTH00223 235 FGHPEVYILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTG 314

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029   81 IKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIILANSSLDIALHDTYYVVAHFHYVLSMGAVFAILAGLTHWF 160
Cdd:MTH00223 315 IKVFSWLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWF 394

                        170       180
                 ....*....|....*....|....*..
gi 34537029  161 PLFTGYTLNQSWAKAHFGVMFTGVNLT 187
Cdd:MTH00223 395 PLFTGVTLHRRWAKAHFFLMFLGVNLT 421
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-187 5.36e-114

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 333.77  E-value: 5.36e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029    1 FGHPEVYILILPGFGIISHVVAYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTG 80
Cdd:MTH00103 238 FGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTG 317

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029   81 IKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIILANSSLDIALHDTYYVVAHFHYVLSMGAVFAILAGLTHWF 160
Cdd:MTH00103 318 VKVFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWF 397

                        170       180
                 ....*....|....*....|....*..
gi 34537029  161 PLFTGYTLNQSWAKAHFGVMFTGVNLT 187
Cdd:MTH00103 398 PLFSGYTLNDTWAKIHFTIMFVGVNMT 424
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-187 6.94e-113

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 330.53  E-value: 6.94e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029    1 FGHPEVYILILPGFGIISHVVAYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTG 80
Cdd:MTH00142 236 FGHPEVYILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTG 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029   81 IKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIILANSSLDIALHDTYYVVAHFHYVLSMGAVFAILAGLTHWF 160
Cdd:MTH00142 316 IKVFSWLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWF 395

                        170       180
                 ....*....|....*....|....*..
gi 34537029  161 PLFTGYTLNQSWAKAHFGVMFTGVNLT 187
Cdd:MTH00142 396 PLFTGLTLNPRWLKAHFYTMFIGVNLT 422
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-187 1.34e-112

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 330.35  E-value: 1.34e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029    1 FGHPEVYILILPGFGIISHVVAYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTG 80
Cdd:MTH00183 238 FGHPEVYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTG 317

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029   81 IKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIILANSSLDIALHDTYYVVAHFHYVLSMGAVFAILAGLTHWF 160
Cdd:MTH00183 318 VKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWF 397

                        170       180
                 ....*....|....*....|....*..
gi 34537029  161 PLFTGYTLNQSWAKAHFGVMFTGVNLT 187
Cdd:MTH00183 398 PLFSGYTLHSTWTKIHFGVMFVGVNLT 424
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-187 1.19e-111

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 327.67  E-value: 1.19e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029    1 FGHPEVYILILPGFGIISHVVAYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTG 80
Cdd:MTH00077 238 FGHPEVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTG 317

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029   81 IKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIILANSSLDIALHDTYYVVAHFHYVLSMGAVFAILAGLTHWF 160
Cdd:MTH00077 318 VKVFSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWF 397

                        170       180
                 ....*....|....*....|....*..
gi 34537029  161 PLFTGYTLNQSWAKAHFGVMFTGVNLT 187
Cdd:MTH00077 398 PLFSGYTLHSTWSKIHFGVMFIGVNLT 424
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-187 2.03e-104

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 309.45  E-value: 2.03e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029    1 FGHPEVYILILPGFGIISHVVAYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTG 80
Cdd:MTH00037 238 FGHPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTG 317

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029   81 IKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIILANSSLDIALHDTYYVVAHFHYVLSMGAVFAILAGLTHWF 160
Cdd:MTH00037 318 IKVFSWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWF 397

                        170       180
                 ....*....|....*....|....*..
gi 34537029  161 PLFTGYTLNQSWAKAHFGVMFTGVNLT 187
Cdd:MTH00037 398 PLFSGVSLHPLWSKVHFFLMFIGVNLT 424
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-187 3.10e-100

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 298.35  E-value: 3.10e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029    1 FGHPEVYILILPGFGIISHVVAYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTG 80
Cdd:MTH00007 235 FGHPEVYILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTG 314

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029   81 IKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIILANSSLDIALHDTYYVVAHFHYVLSMGAVFAILAGLTHWF 160
Cdd:MTH00007 315 IKVFSWLATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWF 394

                        170       180
                 ....*....|....*....|....*..
gi 34537029  161 PLFTGYTLNQSWAKAHFGVMFTGVNLT 187
Cdd:MTH00007 395 PLFTGLTLHDRWAKAHFFLMFLGVNLT 421
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-187 1.09e-93

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 281.57  E-value: 1.09e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029    1 FGHPEVYILILPGFGIISHVVAYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTG 80
Cdd:MTH00079 238 FGHPEVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTG 317

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029   81 IKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIILANSSLDIALHDTYYVVAHFHYVLSMGAVFAILAGLTHWF 160
Cdd:MTH00079 318 VKVFSWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWW 397

                        170       180
                 ....*....|....*....|....*..
gi 34537029  161 PLFTGYTLNQSWAKAHFGVMFTGVNLT 187
Cdd:MTH00079 398 PFMTGIVYDKLMMSAVFFLMFVGVNLT 424
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-187 6.72e-92

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 277.47  E-value: 6.72e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029    1 FGHPEVYILILPGFGIISHVVAYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTG 80
Cdd:MTH00182 240 FGHPEVYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTG 319

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029   81 IKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIILANSSLDIALHDTYYVVAHFHYVLSMGAVFAILAGLTHWF 160
Cdd:MTH00182 320 IKVFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWF 399

                        170       180
                 ....*....|....*....|....*..
gi 34537029  161 PLFTGYTLNQSWAKAHFGVMFTGVNLT 187
Cdd:MTH00182 400 GKITGYCYNELYGKIHFWLMFIGVNLT 426
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-187 6.04e-89

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 269.77  E-value: 6.04e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029    1 FGHPEVYILILPGFGIISHVVAYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTG 80
Cdd:MTH00184 240 FGHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTG 319

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029   81 IKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIILANSSLDIALHDTYYVVAHFHYVLSMGAVFAILAGLTHWF 160
Cdd:MTH00184 320 IKIFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWF 399

                        170       180
                 ....*....|....*....|....*..
gi 34537029  161 PLFTGYTLNQSWAKAHFGVMFTGVNLT 187
Cdd:MTH00184 400 GKITGYCYNEVYGKIHFWLMFIGVNLT 426
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-187 5.93e-85

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: 257.84  E-value: 5.93e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029   1 FGHPEVYILILPGFGIISHVVAYYAGKKePFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTG 80
Cdd:cd00919 226 FGHPEVYILILPAFGAISEIIPTFSGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTG 304

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029  81 IKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIILANSSLDIALHDTYYVVAHFHYVLSMGAVFAILAGLTHWF 160
Cdd:cd00919 305 IKVFNWLATLWGGRIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWF 384

                       170       180
                ....*....|....*....|....*..
gi 34537029 161 PLFTGYTLNQSWAKAHFGVMFTGVNLT 187
Cdd:cd00919 385 PKMTGRMLSEKLGKIHFWLWFIGFNLT 411
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-187 3.00e-84

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 258.13  E-value: 3.00e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029   1 FGHPEVYILILPGFGIISHVVAYYAGKKePFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTG 80
Cdd:COG0843 240 FGHPEVYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTG 318

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029  81 IKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIILANSSLDIALHDTYYVVAHFHYVLSMGAVFAILAGLTHWF 160
Cdd:COG0843 319 VKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWF 398

                       170       180
                ....*....|....*....|....*..
gi 34537029 161 PLFTGYTLNQSWAKAHFGVMFTGVNLT 187
Cdd:COG0843 399 PKMTGRMLNERLGKIHFWLWFIGFNLT 425
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-187 5.49e-83

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: 253.68  E-value: 5.49e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029     1 FGHPEVYILILPGFGIISHVVAYYAGKKePFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTG 80
Cdd:TIGR02891 231 FGHPEVYIIFLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTG 309

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029    81 IKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIILANSSLDIALHDTYYVVAHFHYVLSMGAVFAILAGLTHWF 160
Cdd:TIGR02891 310 VKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWF 389

                         170       180
                  ....*....|....*....|....*..
gi 34537029   161 PLFTGYTLNQSWAKAHFGVMFTGVNLT 187
Cdd:TIGR02891 390 PKVTGRMYNERLGRWHFWLTFVGFNLT 416
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-187 7.97e-78

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


Pssm-ID: 238832  Cd Length: 501  Bit Score: 240.56  E-value: 7.97e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029   1 FGHPEVYILILPGFGIISHVVAYYAGKKePFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTG 80
Cdd:cd01662 232 FGHPEVYILILPAFGIFSEIVPTFSRKP-LFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTG 310

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029  81 IKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIILANSSLDIALHDTYYVVAHFHYVLSMGAVFAILAGLTHWF 160
Cdd:cd01662 311 VKIFNWLFTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWF 390

                       170       180
                ....*....|....*....|....*..
gi 34537029 161 PLFTGYTLNQSWAKAHFGVMFTGVNLT 187
Cdd:cd01662 391 PKMFGRMLNERLGKWSFWLWFIGFNLT 417
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-187 3.50e-73

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 229.51  E-value: 3.50e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029    1 FGHPEVYILILPGFGIISHVVAYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTG 80
Cdd:MTH00026 239 FGHPEVYILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTG 318

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029   81 IKVFSWLATLHGG--TIKWDPPMLWALGFIFLFTIGGLTGIILANSSLDIALHDTYYVVAHFHYVLSMGAVFAILAGLTH 158
Cdd:MTH00026 319 IKIFSWLATVSGSgrNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYL 398

                        170       180
                 ....*....|....*....|....*....
gi 34537029  159 WFPLFTGYTLNQSWAKAHFGVMFTGVNLT 187
Cdd:MTH00026 399 WFGKITGYAYKDIYGLIHFWLMFIGVNIT 427
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-186 7.91e-73

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 228.02  E-value: 7.91e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029    1 FGHPEVYILILPGFGIISHVVAYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTG 80
Cdd:MTH00048 236 FGHPEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTG 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029   81 IKVFSWLATLHG-GTIKWDPPMLWALGFIFLFTIGGLTGIILANSSLDIALHDTYYVVAHFHYVLSMGAVFAILAGLTHW 159
Cdd:MTH00048 316 IKVFSWLYMLLNsRVRKSDPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWW 395

                        170       180
                 ....*....|....*....|....*..
gi 34537029  160 FPLFTGYTLNQSWAKAHFGVMFTGVNL 186
Cdd:MTH00048 396 WPLITGLSLNKYLLQCHCIISMIGFNL 422
CyoB TIGR02843
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ...
 1-183 1.28e-61

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


Pssm-ID: 131890  Cd Length: 646  Bit Score: 201.82  E-value: 1.28e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029     1 FGHPEVYILILPGFGIISHVVAYYAGKKEpFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTG 80
Cdd:TIGR02843 281 WGHPEVYILILPAFGIFSEVVATFSRKRL-FGYTSMVWATIAITVLSFIVWLHHFFTMGAGANVNAFFGIATMIIAIPTG 359

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029    81 IKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIILANSSLDIALHDTYYVVAHFHYVLSMGAVFAILAGLTHWF 160
Cdd:TIGR02843 360 VKIFNWLFTMYKGRIRFETPMLWTIGFMVTFSIGGMTGVLLAVPPADFVLHNSLFLIAHFHNVIIGGVVFGCFAGLTYWF 439

                         170       180
                  ....*....|....*....|...
gi 34537029   161 PLFTGYTLNQSWAKAHFGVMFTG 183
Cdd:TIGR02843 440 PKAFGFKLNEKLGKRSFWCWFIG 462
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-187 2.18e-59

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: 191.25  E-value: 2.18e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029     1 FGHPEVYILILPGFGIISHVVAYYAGKKePFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTG 80
Cdd:pfam00115 206 FGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSG 284

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029    81 IKVFSWLATLHGGTIKW-DPPMLWALGFIFLFTIGGLTGIILANSSLDIALHDTYYVVAHFHYVLSMGAVFAILAGLTHW 159
Cdd:pfam00115 285 VKVFNWLATLWGGWIRFrTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYW 364

                         170       180
                  ....*....|....*....|....*...
gi 34537029   160 FPLFTGYTLNQSWAKAHFGVMFTGVNLT 187
Cdd:pfam00115 365 LPKLTGRMYSEKLGKLHFWLLFIGFNLT 392
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 1-177 1.02e-52

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 178.21  E-value: 1.02e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029    1 FGHPEVYILILPGFGIISHVVAYYAgKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTG 80
Cdd:PRK15017 282 WGHPEVYILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTG 360

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029   81 IKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIILANSSLDIALHDTYYVVAHFHYVLSMGAVFAILAGLTHWF 160
Cdd:PRK15017 361 VKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWW 440

                        170
                 ....*....|....*..
gi 34537029  161 PLFTGYTLNQSWAKAHF 177
Cdd:PRK15017 441 PKAFGFKLNETWGKRAF 457
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 1-165 2.54e-06

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: 46.51  E-value: 2.54e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029   1 FGHPEVYILILPGFGIISHVVAYYAGKK---EPFGYMGMVWAMLsigfLGFIVWAHHMFT-VGMDVDTRAYFTSATMIIA 76
Cdd:cd01660 211 FGHPLVYFWLLPAYIAWYTILPKIAGGKlfsDPLARLAFILFLL----FSTPVGFHHQFAdPGIGPGWKFIHMVLTFMVA 286

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34537029  77 IPTGIKVFSWLATL-HGGTIK-------------WDPPMLWALGF-IFLFTIGGLTGIILANSSLDIALHDTYYVVAHFH 141
Cdd:cd01660 287 LPSLLTAFTVFASLeIAGRLRggkglfgwiralpWGDPMFLALFLaMLMFIPGGAGGIINASYQLNYVVHNTAWVPGHFH 366

                       170       180
                ....*....|....*....|....*.
gi 34537029 142 yvLSMGAVFAILA-GLTHWF-PLFTG 165
Cdd:cd01660 367 --LTVGGAVALTFmAVAYWLvPHLTG 390
 
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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