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Conserved domains on  [gi|11118465|gb|AAG30335|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Pteraster tesselatus]

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 ...
 1-208 2.99e-154

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: 436.99  E-value: 2.99e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465    1 WFFGHPEVYILILPGFGMISHVIAHYSNKTEPFGYLGMVYAIISIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVP 80
Cdd:MTH00153 234 WFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVP 313

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465   81 TGIKIFSWMATLQGSNLNWDTPLLWALGFIFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIFAGFTH 160
Cdd:MTH00153 314 TGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIH 393

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 11118465  161 WFPLFTGLSLHPLWSKIHFIIMFIGVNLTFFPQHFLGLAGMPRRYSDY 208
Cdd:MTH00153 394 WFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDY 441
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-208 2.99e-154

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 436.99  E-value: 2.99e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465    1 WFFGHPEVYILILPGFGMISHVIAHYSNKTEPFGYLGMVYAIISIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVP 80
Cdd:MTH00153 234 WFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVP 313

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465   81 TGIKIFSWMATLQGSNLNWDTPLLWALGFIFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIFAGFTH 160
Cdd:MTH00153 314 TGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIH 393

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 11118465  161 WFPLFTGLSLHPLWSKIHFIIMFIGVNLTFFPQHFLGLAGMPRRYSDY 208
Cdd:MTH00153 394 WFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDY 441
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-208 8.22e-147

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: 417.27  E-value: 8.22e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465   1 WFFGHPEVYILILPGFGMISHVIAHYSNKTEPFGYLGMVYAIISIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVP 80
Cdd:cd01663 227 WFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVP 306

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465  81 TGIKIFSWMATLQGSNLNWDTPLLWALGFIFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIFAGFTH 160
Cdd:cd01663 307 TGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYY 386

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 11118465 161 WFPLFTGLSLHPLWSKIHFIIMFIGVNLTFFPQHFLGLAGMPRRYSDY 208
Cdd:cd01663 387 WFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDY 434
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-208 7.71e-97

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 291.26  E-value: 7.71e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465   1 WFFGHPEVYILILPGFGMISHVIAHYSNKtEPFGYLGMVYAIISIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVP 80
Cdd:COG0843 238 WFFGHPEVYILILPAFGIVSEIIPTFSRK-PLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVP 316

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465  81 TGIKIFSWMATLQGSNLNWDTPLLWALGFIFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIFAGFTH 160
Cdd:COG0843 317 TGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYY 396

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 11118465 161 WFPLFTGLSLHPLWSKIHFIIMFIGVNLTFFPQHFLGLAGMPRRYSDY 208
Cdd:COG0843 397 WFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATY 444
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-208 4.00e-94

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: 283.35  E-value: 4.00e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465     1 WFFGHPEVYILILPGFGMISHVIAHYSNKtEPFGYLGMVYAIISIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVP 80
Cdd:TIGR02891 229 WFFGHPEVYIIFLPAFGIISEILPTFARK-PIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVP 307

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465    81 TGIKIFSWMATLQGSNLNWDTPLLWALGFIFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIFAGFTH 160
Cdd:TIGR02891 308 TGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYY 387

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 11118465   161 WFPLFTGLSLHPLWSKIHFIIMFIGVNLTFFPQHFLGLAGMPRRYSDY 208
Cdd:TIGR02891 388 WFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTY 435
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-207 1.29e-70

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: 220.91  E-value: 1.29e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465     1 WFFGHPEVYILILPGFGMISHVIAHYSNKtEPFGYLGMVYAIISIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVP 80
Cdd:pfam00115 204 WWFGHPEVYILILPAFGIIYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVP 282

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465    81 TGIKIFSWMATLQGSNLNW-DTPLLWALGFIFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIFAGFT 159
Cdd:pfam00115 283 SGVKVFNWLATLWGGWIRFrTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIY 362

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 11118465   160 HWFPLFTGLSLHPLWSKIHFIIMFIGVNLTFFPQHFLGLAGMPRRYSD 207
Cdd:pfam00115 363 YWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAP 410
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-208 2.99e-154

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 436.99  E-value: 2.99e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465    1 WFFGHPEVYILILPGFGMISHVIAHYSNKTEPFGYLGMVYAIISIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVP 80
Cdd:MTH00153 234 WFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVP 313

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465   81 TGIKIFSWMATLQGSNLNWDTPLLWALGFIFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIFAGFTH 160
Cdd:MTH00153 314 TGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIH 393

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 11118465  161 WFPLFTGLSLHPLWSKIHFIIMFIGVNLTFFPQHFLGLAGMPRRYSDY 208
Cdd:MTH00153 394 WFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDY 441
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-208 8.22e-147

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: 417.27  E-value: 8.22e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465   1 WFFGHPEVYILILPGFGMISHVIAHYSNKTEPFGYLGMVYAIISIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVP 80
Cdd:cd01663 227 WFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVP 306

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465  81 TGIKIFSWMATLQGSNLNWDTPLLWALGFIFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIFAGFTH 160
Cdd:cd01663 307 TGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYY 386

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 11118465 161 WFPLFTGLSLHPLWSKIHFIIMFIGVNLTFFPQHFLGLAGMPRRYSDY 208
Cdd:cd01663 387 WFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDY 434
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-208 1.07e-139

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 399.82  E-value: 1.07e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465    1 WFFGHPEVYILILPGFGMISHVIAHYSNKTEPFGYLGMVYAIISIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVP 80
Cdd:MTH00167 236 WFFGHPEVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVP 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465   81 TGIKIFSWMATLQGSNLNWDTPLLWALGFIFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIFAGFTH 160
Cdd:MTH00167 316 TGIKVFSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTH 395

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 11118465  161 WFPLFTGLSLHPLWSKIHFIIMFIGVNLTFFPQHFLGLAGMPRRYSDY 208
Cdd:MTH00167 396 WFPLFTGLTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDY 443
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-208 1.36e-137

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 394.84  E-value: 1.36e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465    1 WFFGHPEVYILILPGFGMISHVIAHYSNKTEPFGYLGMVYAIISIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVP 80
Cdd:MTH00116 236 WFFGHPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIP 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465   81 TGIKIFSWMATLQGSNLNWDTPLLWALGFIFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIFAGFTH 160
Cdd:MTH00116 316 TGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTH 395

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 11118465  161 WFPLFTGLSLHPLWSKIHFIIMFIGVNLTFFPQHFLGLAGMPRRYSDY 208
Cdd:MTH00116 396 WFPLFTGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDY 443
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-208 1.75e-135

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 389.34  E-value: 1.75e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465    1 WFFGHPEVYILILPGFGMISHVIAHYSNKTEPFGYLGMVYAIISIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVP 80
Cdd:MTH00223 233 WFFGHPEVYILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVP 312

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465   81 TGIKIFSWMATLQGSNLNWDTPLLWALGFIFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIFAGFTH 160
Cdd:MTH00223 313 TGIKVFSWLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNH 392

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 11118465  161 WFPLFTGLSLHPLWSKIHFIIMFIGVNLTFFPQHFLGLAGMPRRYSDY 208
Cdd:MTH00223 393 WFPLFTGVTLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDY 440
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-208 1.85e-133

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 384.08  E-value: 1.85e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465    1 WFFGHPEVYILILPGFGMISHVIAHYSNKTEPFGYLGMVYAIISIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVP 80
Cdd:MTH00142 234 WFFGHPEVYILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVP 313

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465   81 TGIKIFSWMATLQGSNLNWDTPLLWALGFIFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIFAGFTH 160
Cdd:MTH00142 314 TGIKVFSWLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIH 393

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 11118465  161 WFPLFTGLSLHPLWSKIHFIIMFIGVNLTFFPQHFLGLAGMPRRYSDY 208
Cdd:MTH00142 394 WFPLFTGLTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDY 441
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-208 4.97e-131

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 378.02  E-value: 4.97e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465    1 WFFGHPEVYILILPGFGMISHVIAHYSNKTEPFGYLGMVYAIISIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVP 80
Cdd:MTH00037 236 WFFGHPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVP 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465   81 TGIKIFSWMATLQGSNLNWDTPLLWALGFIFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIFAGFTH 160
Cdd:MTH00037 316 TGIKVFSWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTH 395

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 11118465  161 WFPLFTGLSLHPLWSKIHFIIMFIGVNLTFFPQHFLGLAGMPRRYSDY 208
Cdd:MTH00037 396 WFPLFSGVSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDY 443
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-208 4.52e-121

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 352.69  E-value: 4.52e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465    1 WFFGHPEVYILILPGFGMISHVIAHYSNKTEPFGYLGMVYAIISIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVP 80
Cdd:MTH00183 236 WFFGHPEVYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIP 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465   81 TGIKIFSWMATLQGSNLNWDTPLLWALGFIFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIFAGFTH 160
Cdd:MTH00183 316 TGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVH 395

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 11118465  161 WFPLFTGLSLHPLWSKIHFIIMFIGVNLTFFPQHFLGLAGMPRRYSDY 208
Cdd:MTH00183 396 WFPLFSGYTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDY 443
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-208 3.14e-120

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 350.39  E-value: 3.14e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465    1 WFFGHPEVYILILPGFGMISHVIAHYSNKTEPFGYLGMVYAIISIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVP 80
Cdd:MTH00077 236 WFFGHPEVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIP 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465   81 TGIKIFSWMATLQGSNLNWDTPLLWALGFIFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIFAGFTH 160
Cdd:MTH00077 316 TGVKVFSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVH 395

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 11118465  161 WFPLFTGLSLHPLWSKIHFIIMFIGVNLTFFPQHFLGLAGMPRRYSDY 208
Cdd:MTH00077 396 WFPLFSGYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDY 443
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-208 2.32e-119

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 348.41  E-value: 2.32e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465    1 WFFGHPEVYILILPGFGMISHVIAHYSNKTEPFGYLGMVYAIISIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVP 80
Cdd:MTH00103 236 WFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIP 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465   81 TGIKIFSWMATLQGSNLNWDTPLLWALGFIFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIFAGFTH 160
Cdd:MTH00103 316 TGVKVFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVH 395

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 11118465  161 WFPLFTGLSLHPLWSKIHFIIMFIGVNLTFFPQHFLGLAGMPRRYSDY 208
Cdd:MTH00103 396 WFPLFSGYTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDY 443
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-208 2.28e-118

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 345.73  E-value: 2.28e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465    1 WFFGHPEVYILILPGFGMISHVIAHYSNKTEPFGYLGMVYAIISIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVP 80
Cdd:MTH00007 233 WFFGHPEVYILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVP 312

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465   81 TGIKIFSWMATLQGSNLNWDTPLLWALGFIFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIFAGFTH 160
Cdd:MTH00007 313 TGIKVFSWLATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNH 392

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 11118465  161 WFPLFTGLSLHPLWSKIHFIIMFIGVNLTFFPQHFLGLAGMPRRYSDY 208
Cdd:MTH00007 393 WFPLFTGLTLHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDY 440
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-208 4.40e-108

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 319.84  E-value: 4.40e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465    1 WFFGHPEVYILILPGFGMISHVIAHYSNKTEPFGYLGMVYAIISIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVP 80
Cdd:MTH00182 238 WFFGHPEVYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVP 317

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465   81 TGIKIFSWMATLQGSNLNWDTPLLWALGFIFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIFAGFTH 160
Cdd:MTH00182 318 TGIKVFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYY 397

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 11118465  161 WFPLFTGLSLHPLWSKIHFIIMFIGVNLTFFPQHFLGLAGMPRRYSDY 208
Cdd:MTH00182 398 WFGKITGYCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDF 445
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-208 1.14e-106

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 315.85  E-value: 1.14e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465    1 WFFGHPEVYILILPGFGMISHVIAHYSNKTEPFGYLGMVYAIISIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVP 80
Cdd:MTH00079 236 WFFGHPEVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVP 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465   81 TGIKIFSWMATLQGSNLNWDTPLLWALGFIFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIFAGFTH 160
Cdd:MTH00079 316 TGVKVFSWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISL 395

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 11118465  161 WFPLFTGLSLHPLWSKIHFIIMFIGVNLTFFPQHFLGLAGMPRRYSDY 208
Cdd:MTH00079 396 WWPFMTGIVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDY 443
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-208 1.13e-105

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 313.69  E-value: 1.13e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465    1 WFFGHPEVYILILPGFGMISHVIAHYSNKTEPFGYLGMVYAIISIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVP 80
Cdd:MTH00184 238 WFFGHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVP 317

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465   81 TGIKIFSWMATLQGSNLNWDTPLLWALGFIFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIFAGFTH 160
Cdd:MTH00184 318 TGIKIFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYY 397

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 11118465  161 WFPLFTGLSLHPLWSKIHFIIMFIGVNLTFFPQHFLGLAGMPRRYSDY 208
Cdd:MTH00184 398 WFGKITGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDF 445
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-208 6.51e-98

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: 291.74  E-value: 6.51e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465   1 WFFGHPEVYILILPGFGMISHVIAHYSNKtEPFGYLGMVYAIISIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVP 80
Cdd:cd00919 224 WFFGHPEVYILILPAFGAISEIIPTFSGK-PLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVP 302

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465  81 TGIKIFSWMATLQGSNLNWDTPLLWALGFIFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIFAGFTH 160
Cdd:cd00919 303 TGIKVFNWLATLWGGRIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYY 382

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 11118465 161 WFPLFTGLSLHPLWSKIHFIIMFIGVNLTFFPQHFLGLAGMPRRYSDY 208
Cdd:cd00919 383 WFPKMTGRMLSEKLGKIHFWLWFIGFNLTFFPMHFLGLLGMPRRYADY 430
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-208 7.71e-97

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 291.26  E-value: 7.71e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465   1 WFFGHPEVYILILPGFGMISHVIAHYSNKtEPFGYLGMVYAIISIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVP 80
Cdd:COG0843 238 WFFGHPEVYILILPAFGIVSEIIPTFSRK-PLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVP 316

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465  81 TGIKIFSWMATLQGSNLNWDTPLLWALGFIFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIFAGFTH 160
Cdd:COG0843 317 TGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYY 396

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 11118465 161 WFPLFTGLSLHPLWSKIHFIIMFIGVNLTFFPQHFLGLAGMPRRYSDY 208
Cdd:COG0843 397 WFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATY 444
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-208 4.00e-94

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: 283.35  E-value: 4.00e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465     1 WFFGHPEVYILILPGFGMISHVIAHYSNKtEPFGYLGMVYAIISIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVP 80
Cdd:TIGR02891 229 WFFGHPEVYIIFLPAFGIISEILPTFARK-PIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVP 307

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465    81 TGIKIFSWMATLQGSNLNWDTPLLWALGFIFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIFAGFTH 160
Cdd:TIGR02891 308 TGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYY 387

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 11118465   161 WFPLFTGLSLHPLWSKIHFIIMFIGVNLTFFPQHFLGLAGMPRRYSDY 208
Cdd:TIGR02891 388 WFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTY 435
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-208 4.43e-91

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 276.51  E-value: 4.43e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465    1 WFFGHPEVYILILPGFGMISHVIAHYSNKTEPFGYLGMVYAIISIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVP 80
Cdd:MTH00026 237 WFFGHPEVYILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVP 316

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465   81 TGIKIFSWMATLQGS--NLNWDTPLLWALGFIFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIFAGF 158
Cdd:MTH00026 317 TGIKIFSWLATVSGSgrNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGF 396

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 11118465  159 THWFPLFTGLSLHPLWSKIHFIIMFIGVNLTFFPQHFLGLAGMPRRYSDY 208
Cdd:MTH00026 397 YLWFGKITGYAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADY 446
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-208 1.03e-88

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: 269.45  E-value: 1.03e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465   1 WFFGHPEVYILILPGFGMISHVIAHYSNKtEPFGYLGMVYAIISIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVP 80
Cdd:cd01662 230 WIFGHPEVYILILPAFGIFSEIVPTFSRK-PLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVP 308

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465  81 TGIKIFSWMATLQGSNLNWDTPLLWALGFIFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIFAGFTH 160
Cdd:cd01662 309 TGVKIFNWLFTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYY 388

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 11118465 161 WFPLFTGLSLHPLWSKIHFIIMFIGVNLTFFPQHFLGLAGMPRRYSDY 208
Cdd:cd01662 389 WFPKMFGRMLNERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTY 436
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-208 9.18e-82

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 251.91  E-value: 9.18e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465    1 WFFGHPEVYILILPGFGMISHVIAHYSNKTEPFGYLGMVYAIISIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVP 80
Cdd:MTH00048 234 WFFGHPEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVP 313

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465   81 TGIKIFSWMATLQGSNLNWDTPLL-WALGFIFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIFAGFT 159
Cdd:MTH00048 314 TGIKVFSWLYMLLNSRVRKSDPVVwWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFI 393

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 11118465  160 HWFPLFTGLSLHPLWSKIHFIIMFIGVNLTFFPQHFLGLAGMPRRYSDY 208
Cdd:MTH00048 394 WWWPLITGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVY 442
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-207 1.29e-70

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: 220.91  E-value: 1.29e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465     1 WFFGHPEVYILILPGFGMISHVIAHYSNKtEPFGYLGMVYAIISIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVP 80
Cdd:pfam00115 204 WWFGHPEVYILILPAFGIIYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVP 282

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465    81 TGIKIFSWMATLQGSNLNW-DTPLLWALGFIFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIFAGFT 159
Cdd:pfam00115 283 SGVKVFNWLATLWGGWIRFrTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIY 362

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 11118465   160 HWFPLFTGLSLHPLWSKIHFIIMFIGVNLTFFPQHFLGLAGMPRRYSD 207
Cdd:pfam00115 363 YWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAP 410
CyoB TIGR02843
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ...
 1-208 2.61e-64

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: 209.53  E-value: 2.61e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465     1 WFFGHPEVYILILPGFGMISHVIAHYSNKtEPFGYLGMVYAIISIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVP 80
Cdd:TIGR02843 279 WAWGHPEVYILILPAFGIFSEVVATFSRK-RLFGYTSMVWATIAITVLSFIVWLHHFFTMGAGANVNAFFGIATMIIAIP 357

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465    81 TGIKIFSWMATLQGSNLNWDTPLLWALGFIFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIFAGFTH 160
Cdd:TIGR02843 358 TGVKIFNWLFTMYKGRIRFETPMLWTIGFMVTFSIGGMTGVLLAVPPADFVLHNSLFLIAHFHNVIIGGVVFGCFAGLTY 437

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 11118465   161 WFPLFTGLSLHPLWSKIHFIIMFIGVNLTFFPQHFLGLAGMPRRYSDY 208
Cdd:TIGR02843 438 WFPKAFGFKLNEKLGKRSFWCWFIGFYLAFMPLYILGFMGMTRRLNHY 485
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 1-206 1.11e-54

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 184.37  E-value: 1.11e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465    1 WFFGHPEVYILILPGFGMISHVIAHYSNKtEPFGYLGMVYAIISIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVP 80
Cdd:PRK15017 280 WAWGHPEVYILILPVFGVFSEIAATFSRK-RLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIP 358

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465   81 TGIKIFSWMATLQGSNLNWDTPLLWALGFIFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIFAGFTH 160
Cdd:PRK15017 359 TGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTY 438

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 11118465  161 WFPLFTGLSLHPLWSKIHFIIMFIGVNLTFFPQHFLGLAGMPRRYS 206
Cdd:PRK15017 439 WWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLS 484
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 1-204 1.95e-12

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


Pssm-ID: 238830  Cd Length: 473  Bit Score: 65.00  E-value: 1.95e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465   1 WFFGHPEVYILILPGFgMISHVIAHYSNKTEPFGYLGMVYAIISIGILGFLVWAHHMFT-VGMDVDTRAYFTAATMIIAV 79
Cdd:cd01660 209 WWFGHPLVYFWLLPAY-IAWYTILPKIAGGKLFSDPLARLAFILFLLFSTPVGFHHQFAdPGIGPGWKFIHMVLTFMVAL 287

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11118465  80 PTGIKIFSWMATLQGS--------------NLNWDTPLLWALGF-IFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHY 144
Cdd:cd01660 288 PSLLTAFTVFASLEIAgrlrggkglfgwirALPWGDPMFLALFLaMLMFIPGGAGGIINASYQLNYVVHNTAWVPGHFHL 367

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 11118465 145 VLSmGAVFAIFAGFTHWF-PLFTGlslHPLWSK----IHFIIMFIGVNLTFFPQHFLGLAGMPRR 204
Cdd:cd01660 368 TVG-GAVALTFMAVAYWLvPHLTG---RELAAKrlalAQPWLWFVGMTIMSTAMHVAGLLGAPRR 428
 
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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