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Conserved domains on  [gi|2022047582|gb|QTN57304|]
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cytochrome c oxidase subunit I, partial (mitochondrion) [Chondrocladia sagari]

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 ...
 1-205 6.45e-147

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 cd01663:

Pssm-ID: 469701  Cd Length: 488  Bit Score: 417.27  E-value: 6.45e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582   1 TAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKLIFGYLGMVYAMVSIGVLGFIVWAHHMFTVG 80
Cdd:cd01663   208 TSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVG 287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582  81 MDVDTRAYFTAATMIIAVPTGIKIFSWIATMFGGALRLDTPMLWAIGFVFLFTMGGLTGIVLANSALDVVLHDTYYVVAH 160
Cdd:cd01663   288 LDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAH 367

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2022047582 161 FHYVLSMGAIFSIFGGFYYWFGKMTGYCYNETYGKIHFWLMFIGV 205
Cdd:cd01663   368 FHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGV 412
 
Name Accession Description Interval E-value
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-205 6.45e-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: 6.45e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582   1 TAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKLIFGYLGMVYAMVSIGVLGFIVWAHHMFTVG 80
Cdd:cd01663   208 TSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVG 287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582  81 MDVDTRAYFTAATMIIAVPTGIKIFSWIATMFGGALRLDTPMLWAIGFVFLFTMGGLTGIVLANSALDVVLHDTYYVVAH 160
Cdd:cd01663   288 LDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAH 367

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2022047582 161 FHYVLSMGAIFSIFGGFYYWFGKMTGYCYNETYGKIHFWLMFIGV 205
Cdd:cd01663   368 FHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGV 412
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-205 8.47e-134

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 384.60  E-value: 8.47e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582   1 TAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKLIFGYLGMVYAMVSIGVLGFIVWAHHMFTVG 80
Cdd:MTH00153  215 TSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVG 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582  81 MDVDTRAYFTAATMIIAVPTGIKIFSWIATMFGGALRLDTPMLWAIGFVFLFTMGGLTGIVLANSALDVVLHDTYYVVAH 160
Cdd:MTH00153  295 MDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAH 374

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2022047582 161 FHYVLSMGAIFSIFGGFYYWFGKMTGYCYNETYGKIHFWLMFIGV 205
Cdd:MTH00153  375 FHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGV 419
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-205 1.63e-103

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 308.21  E-value: 1.63e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582   1 TAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKlIFGYLGMVYAMVSIGVLGFIVWAHHMFTVG 80
Cdd:COG0843   219 THFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPG 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582  81 MDVDTRAYFTAATMIIAVPTGIKIFSWIATMFGGALRLDTPMLWAIGFVFLFTMGGLTGIVLANSALDVVLHDTYYVVAH 160
Cdd:COG0843   298 ISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAH 377

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2022047582 161 FHYVLSMGAIFSIFGGFYYWFGKMTGYCYNETYGKIHFWLMFIGV 205
Cdd:COG0843   378 FHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGF 422
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-205 2.46e-103

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: 306.84  E-value: 2.46e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582   1 TAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKlIFGYLGMVYAMVSIGVLGFIVWAHHMFTVG 80
Cdd:TIGR02891 210 THFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTG 288

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582  81 MDVDTRAYFTAATMIIAVPTGIKIFSWIATMFGGALRLDTPMLWAIGFVFLFTMGGLTGIVLANSALDVVLHDTYYVVAH 160
Cdd:TIGR02891 289 MPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAH 368

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2022047582 161 FHYVLSMGAIFSIFGGFYYWFGKMTGYCYNETYGKIHFWLMFIGV 205
Cdd:TIGR02891 369 FHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGF 413
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 6-205 3.08e-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: 219.75  E-value: 3.08e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582   6 PAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKlIFGYLGMVYAMVSIGVLGFIVWAHHMFTVGMDVDT 85
Cdd:pfam00115 190 GAGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWL 268

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582  86 RAYFTAATMIIAVPTGIKIFSWIATMFGGALRL-DTPMLWAIGFVFLFTMGGLTGIVLANSALDVVLHDTYYVVAHFHYV 164
Cdd:pfam00115 269 QALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYV 348

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2022047582 165 LSMGAIFSIFGGFYYWFGKMTGYCYNETYGKIHFWLMFIGV 205
Cdd:pfam00115 349 LFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGF 389
 
Name Accession Description Interval E-value
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-205 6.45e-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: 6.45e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582   1 TAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKLIFGYLGMVYAMVSIGVLGFIVWAHHMFTVG 80
Cdd:cd01663   208 TSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVG 287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582  81 MDVDTRAYFTAATMIIAVPTGIKIFSWIATMFGGALRLDTPMLWAIGFVFLFTMGGLTGIVLANSALDVVLHDTYYVVAH 160
Cdd:cd01663   288 LDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAH 367

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2022047582 161 FHYVLSMGAIFSIFGGFYYWFGKMTGYCYNETYGKIHFWLMFIGV 205
Cdd:cd01663   368 FHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGV 412
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-205 8.47e-134

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 384.60  E-value: 8.47e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582   1 TAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKLIFGYLGMVYAMVSIGVLGFIVWAHHMFTVG 80
Cdd:MTH00153  215 TSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVG 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582  81 MDVDTRAYFTAATMIIAVPTGIKIFSWIATMFGGALRLDTPMLWAIGFVFLFTMGGLTGIVLANSALDVVLHDTYYVVAH 160
Cdd:MTH00153  295 MDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAH 374

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2022047582 161 FHYVLSMGAIFSIFGGFYYWFGKMTGYCYNETYGKIHFWLMFIGV 205
Cdd:MTH00153  375 FHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGV 419
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-205 2.42e-127

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 368.77  E-value: 2.42e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582   1 TAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKLIFGYLGMVYAMVSIGVLGFIVWAHHMFTVG 80
Cdd:MTH00184  219 TTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVG 298

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582  81 MDVDTRAYFTAATMIIAVPTGIKIFSWIATMFGGALRLDTPMLWAIGFVFLFTMGGLTGIVLANSALDVVLHDTYYVVAH 160
Cdd:MTH00184  299 MDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAH 378

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2022047582 161 FHYVLSMGAIFSIFGGFYYWFGKMTGYCYNETYGKIHFWLMFIGV 205
Cdd:MTH00184  379 FHYVLSMGAVFAIFGGFYYWFGKITGYCYNEVYGKIHFWLMFIGV 423
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-205 1.46e-125

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 364.00  E-value: 1.46e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582   1 TAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKLIFGYLGMVYAMVSIGVLGFIVWAHHMFTVG 80
Cdd:MTH00167  217 TTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVG 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582  81 MDVDTRAYFTAATMIIAVPTGIKIFSWIATMFGGALRLDTPMLWAIGFVFLFTMGGLTGIVLANSALDVVLHDTYYVVAH 160
Cdd:MTH00167  297 MDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAH 376

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2022047582 161 FHYVLSMGAIFSIFGGFYYWFGKMTGYCYNETYGKIHFWLMFIGV 205
Cdd:MTH00167  377 FHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETWTKIHFFVMFIGV 421
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-205 9.40e-125

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 362.22  E-value: 9.40e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582   1 TAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKLIFGYLGMVYAMVSIGVLGFIVWAHHMFTVG 80
Cdd:MTH00182  219 TTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVG 298

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582  81 MDVDTRAYFTAATMIIAVPTGIKIFSWIATMFGGALRLDTPMLWAIGFVFLFTMGGLTGIVLANSALDVVLHDTYYVVAH 160
Cdd:MTH00182  299 MDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAH 378

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2022047582 161 FHYVLSMGAIFSIFGGFYYWFGKMTGYCYNETYGKIHFWLMFIGV 205
Cdd:MTH00182  379 FHYVLSMGAVFAIFGGFYYWFGKITGYCYNELYGKIHFWLMFIGV 423
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-205 3.60e-124

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 360.56  E-value: 3.60e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582   1 TAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKLIFGYLGMVYAMVSIGVLGFIVWAHHMFTVG 80
Cdd:MTH00116  217 TTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVG 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582  81 MDVDTRAYFTAATMIIAVPTGIKIFSWIATMFGGALRLDTPMLWAIGFVFLFTMGGLTGIVLANSALDVVLHDTYYVVAH 160
Cdd:MTH00116  297 MDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAH 376

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2022047582 161 FHYVLSMGAIFSIFGGFYYWFGKMTGYCYNETYGKIHFWLMFIGV 205
Cdd:MTH00116  377 FHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWTKAQFGVMFTGV 421
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-205 2.66e-123

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 358.14  E-value: 2.66e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582   1 TAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKLIFGYLGMVYAMVSIGVLGFIVWAHHMFTVG 80
Cdd:MTH00223  214 TSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVG 293

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582  81 MDVDTRAYFTAATMIIAVPTGIKIFSWIATMFGGALRLDTPMLWAIGFVFLFTMGGLTGIVLANSALDVVLHDTYYVVAH 160
Cdd:MTH00223  294 MDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAH 373

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2022047582 161 FHYVLSMGAIFSIFGGFYYWFGKMTGYCYNETYGKIHFWLMFIGV 205
Cdd:MTH00223  374 FHYVLSMGAVFALFAGFNHWFPLFTGVTLHRRWAKAHFFLMFLGV 418
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-205 2.62e-116

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 340.16  E-value: 2.62e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582   1 TAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKLIFGYLGMVYAMVSIGVLGFIVWAHHMFTVG 80
Cdd:MTH00142  215 TSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVG 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582  81 MDVDTRAYFTAATMIIAVPTGIKIFSWIATMFGGALRLDTPMLWAIGFVFLFTMGGLTGIVLANSALDVVLHDTYYVVAH 160
Cdd:MTH00142  295 MDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAH 374

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2022047582 161 FHYVLSMGAIFSIFGGFYYWFGKMTGYCYNETYGKIHFWLMFIGV 205
Cdd:MTH00142  375 FHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWLKAHFYTMFIGV 419
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-205 6.96e-107

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 316.48  E-value: 6.96e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582   1 TAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKLIFGYLGMVYAMVSIGVLGFIVWAHHMFTVG 80
Cdd:MTH00183  217 TTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVG 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582  81 MDVDTRAYFTAATMIIAVPTGIKIFSWIATMFGGALRLDTPMLWAIGFVFLFTMGGLTGIVLANSALDVVLHDTYYVVAH 160
Cdd:MTH00183  297 MDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAH 376

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2022047582 161 FHYVLSMGAIFSIFGGFYYWFGKMTGYCYNETYGKIHFWLMFIGV 205
Cdd:MTH00183  377 FHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWTKIHFGVMFVGV 421
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-205 5.68e-106

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 314.07  E-value: 5.68e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582   1 TAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKLIFGYLGMVYAMVSIGVLGFIVWAHHMFTVG 80
Cdd:MTH00037  217 TTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVG 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582  81 MDVDTRAYFTAATMIIAVPTGIKIFSWIATMFGGALRLDTPMLWAIGFVFLFTMGGLTGIVLANSALDVVLHDTYYVVAH 160
Cdd:MTH00037  297 MDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAH 376

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2022047582 161 FHYVLSMGAIFSIFGGFYYWFGKMTGYCYNETYGKIHFWLMFIGV 205
Cdd:MTH00037  377 FHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLWSKVHFFLMFIGV 421
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-205 1.46e-105

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 312.97  E-value: 1.46e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582   1 TAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKLIFGYLGMVYAMVSIGVLGFIVWAHHMFTVG 80
Cdd:MTH00103  217 TTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVG 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582  81 MDVDTRAYFTAATMIIAVPTGIKIFSWIATMFGGALRLDTPMLWAIGFVFLFTMGGLTGIVLANSALDVVLHDTYYVVAH 160
Cdd:MTH00103  297 MDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAH 376

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2022047582 161 FHYVLSMGAIFSIFGGFYYWFGKMTGYCYNETYGKIHFWLMFIGV 205
Cdd:MTH00103  377 FHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHFTIMFVGV 421
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-205 5.42e-105

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 311.49  E-value: 5.42e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582   1 TAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKLIFGYLGMVYAMVSIGVLGFIVWAHHMFTVG 80
Cdd:MTH00077  217 TTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVD 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582  81 MDVDTRAYFTAATMIIAVPTGIKIFSWIATMFGGALRLDTPMLWAIGFVFLFTMGGLTGIVLANSALDVVLHDTYYVVAH 160
Cdd:MTH00077  297 LNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAH 376

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2022047582 161 FHYVLSMGAIFSIFGGFYYWFGKMTGYCYNETYGKIHFWLMFIGV 205
Cdd:MTH00077  377 FHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWSKIHFGVMFIGV 421
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-205 3.97e-104

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 309.14  E-value: 3.97e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582   1 TAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKLIFGYLGMVYAMVSIGVLGFIVWAHHMFTVG 80
Cdd:MTH00007  214 TSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVG 293

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582  81 MDVDTRAYFTAATMIIAVPTGIKIFSWIATMFGGALRLDTPMLWAIGFVFLFTMGGLTGIVLANSALDVVLHDTYYVVAH 160
Cdd:MTH00007  294 MDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAH 373

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2022047582 161 FHYVLSMGAIFSIFGGFYYWFGKMTGYCYNETYGKIHFWLMFIGV 205
Cdd:MTH00007  374 FHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRWAKAHFFLMFLGV 418
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-205 1.15e-103

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 307.76  E-value: 1.15e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582   1 TAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKLIFGYLGMVYAMVSIGVLGFIVWAHHMFTVG 80
Cdd:MTH00079  217 TSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVG 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582  81 MDVDTRAYFTAATMIIAVPTGIKIFSWIATMFGGALRLDTPMLWAIGFVFLFTMGGLTGIVLANSALDVVLHDTYYVVAH 160
Cdd:MTH00079  297 MDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSH 376

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2022047582 161 FHYVLSMGAIFSIFGGFYYWFGKMTGYCYNETYGKIHFWLMFIGV 205
Cdd:MTH00079  377 FHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMMSAVFFLMFVGV 421
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-205 1.63e-103

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 308.21  E-value: 1.63e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582   1 TAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKlIFGYLGMVYAMVSIGVLGFIVWAHHMFTVG 80
Cdd:COG0843   219 THFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPG 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582  81 MDVDTRAYFTAATMIIAVPTGIKIFSWIATMFGGALRLDTPMLWAIGFVFLFTMGGLTGIVLANSALDVVLHDTYYVVAH 160
Cdd:COG0843   298 ISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAH 377

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2022047582 161 FHYVLSMGAIFSIFGGFYYWFGKMTGYCYNETYGKIHFWLMFIGV 205
Cdd:COG0843   378 FHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGF 422
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-205 2.46e-103

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: 306.84  E-value: 2.46e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582   1 TAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKlIFGYLGMVYAMVSIGVLGFIVWAHHMFTVG 80
Cdd:TIGR02891 210 THFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTG 288

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582  81 MDVDTRAYFTAATMIIAVPTGIKIFSWIATMFGGALRLDTPMLWAIGFVFLFTMGGLTGIVLANSALDVVLHDTYYVVAH 160
Cdd:TIGR02891 289 MPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAH 368

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2022047582 161 FHYVLSMGAIFSIFGGFYYWFGKMTGYCYNETYGKIHFWLMFIGV 205
Cdd:TIGR02891 369 FHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGF 413
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-205 2.01e-98

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 295.38  E-value: 2.01e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582   1 TAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKLIFGYLGMVYAMVSIGVLGFIVWAHHMFTVG 80
Cdd:MTH00026  218 TTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVG 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582  81 MDVDTRAYFTAATMIIAVPTGIKIFSWIATMFGGA--LRLDTPMLWAIGFVFLFTMGGLTGIVLANSALDVVLHDTYYVV 158
Cdd:MTH00026  298 MDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSGrnLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVV 377

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2022047582 159 AHFHYVLSMGAIFSIFGGFYYWFGKMTGYCYNETYGKIHFWLMFIGV 205
Cdd:MTH00026  378 AHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDIYGLIHFWLMFIGV 424
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-205 3.40e-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: 292.51  E-value: 3.40e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582   1 TAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKlIFGYLGMVYAMVSIGVLGFIVWAHHMFTVG 80
Cdd:cd00919   205 TSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFSGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMFTVG 283

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582  81 MDVDTRAYFTAATMIIAVPTGIKIFSWIATMFGGALRLDTPMLWAIGFVFLFTMGGLTGIVLANSALDVVLHDTYYVVAH 160
Cdd:cd00919   284 LPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAH 363

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2022047582 161 FHYVLSMGAIFSIFGGFYYWFGKMTGYCYNETYGKIHFWLMFIGV 205
Cdd:cd00919   364 FHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIHFWLWFIGF 408
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-204 5.20e-97

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: 290.64  E-value: 5.20e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582   1 TAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKLiFGYLGMVYAMVSIGVLGFIVWAHHMFTVG 80
Cdd:cd01662   211 THFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFSRKPL-FGYRSMVYATVAIGFLSFGVWVHHMFTTG 289

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582  81 MDVDTRAYFTAATMIIAVPTGIKIFSWIATMFGGALRLDTPMLWAIGFVFLFTMGGLTGIVLANSALDVVLHDTYYVVAH 160
Cdd:cd01662   290 AGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAH 369

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2022047582 161 FHYVLSMGAIFSIFGGFYYWFGKMTGYCYNETYGKIHFWLMFIG 204
Cdd:cd01662   370 FHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERLGKWSFWLWFIG 413
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-204 3.13e-78

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 242.66  E-value: 3.13e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582   1 TAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKLIFGYLGMVYAMVSIGVLGFIVWAHHMFTVG 80
Cdd:MTH00048  215 SAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVG 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582  81 MDVDTRAYFTAATMIIAVPTGIKIFSWIATMFGGALRLDTPML-WAIGFVFLFTMGGLTGIVLANSALDVVLHDTYYVVA 159
Cdd:MTH00048  295 LDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKSDPVVwWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVA 374

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2022047582 160 HFHYVLSMGAIFSIFGGFYYWFGKMTGYCYNETYGKIHFWLMFIG 204
Cdd:MTH00048  375 HFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQCHCIISMIG 419
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 6-205 3.08e-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: 219.75  E-value: 3.08e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582   6 PAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKlIFGYLGMVYAMVSIGVLGFIVWAHHMFTVGMDVDT 85
Cdd:pfam00115 190 GAGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWL 268

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582  86 RAYFTAATMIIAVPTGIKIFSWIATMFGGALRL-DTPMLWAIGFVFLFTMGGLTGIVLANSALDVVLHDTYYVVAHFHYV 164
Cdd:pfam00115 269 QALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYV 348

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2022047582 165 LSMGAIFSIFGGFYYWFGKMTGYCYNETYGKIHFWLMFIGV 205
Cdd:pfam00115 349 LFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGF 389
CyoB TIGR02843
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ...
 1-204 5.16e-70

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: 224.55  E-value: 5.16e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582   1 TAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKLiFGYLGMVYAMVSIGVLGFIVWAHHMFTVG 80
Cdd:TIGR02843 260 MHFFTNEAGGNPMMYVNLIWAWGHPEVYILILPAFGIFSEVVATFSRKRL-FGYTSMVWATIAITVLSFIVWLHHFFTMG 338

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582  81 MDVDTRAYFTAATMIIAVPTGIKIFSWIATMFGGALRLDTPMLWAIGFVFLFTMGGLTGIVLANSALDVVLHDTYYVVAH 160
Cdd:TIGR02843 339 AGANVNAFFGIATMIIAIPTGVKIFNWLFTMYKGRIRFETPMLWTIGFMVTFSIGGMTGVLLAVPPADFVLHNSLFLIAH 418

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2022047582 161 FHYVLSMGAIFSIFGGFYYWFGKMTGYCYNETYGKIHFWLMFIG 204
Cdd:TIGR02843 419 FHNVIIGGVVFGCFAGLTYWFPKAFGFKLNEKLGKRSFWCWFIG 462
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 1-204 3.91e-59

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 196.31  E-value: 3.91e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582   1 TAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKLiFGYLGMVYAMVSIGVLGFIVWAHHMFTVG 80
Cdd:PRK15017  261 THFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFSRKRL-FGYTSLVWATVCITVLSFIVWLHHFFTMG 339

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582  81 MDVDTRAYFTAATMIIAVPTGIKIFSWIATMFGGALRLDTPMLWAIGFVFLFTMGGLTGIVLANSALDVVLHDTYYVVAH 160
Cdd:PRK15017  340 AGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAH 419

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2022047582 161 FHYVLSMGAIFSIFGGFYYWFGKMTGYCYNETYGKIHFWLMFIG 204
Cdd:PRK15017  420 FHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIG 463
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 11-204 9.61e-12

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


Pssm-ID: 238830  Cd Length: 473  Bit Score: 63.07  E-value: 9.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582  11 DPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKLIFGYLGMVyAMVSIGVLGFIVWAHHMFT-VGMDVDTRAYF 89
Cdd:cd01660   200 DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKLFSDPLARL-AFILFLLFSTPVGFHHQFAdPGIGPGWKFIH 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022047582  90 TAATMIIAVPTGIKIFSWIATM------------FG--GALRLDTPMLWAIGFVFL-FTMGGLTGIVLANSALDVVLHDT 154
Cdd:cd01660   279 MVLTFMVALPSLLTAFTVFASLeiagrlrggkglFGwiRALPWGDPMFLALFLAMLmFIPGGAGGIINASYQLNYVVHNT 358

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2022047582 155 YYVVAHFHYVLSMGAIFSIFGGFYYWFGKMTGY-CYNETYGKIHFWLMFIG 204
Cdd:cd01660   359 AWVPGHFHLTVGGAVALTFMAVAYWLVPHLTGReLAAKRLALAQPWLWFVG 409
 
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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