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Conserved domains on  [gi|1805522424|gb|QHU48535|]
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cytochrome c oxidase subunit I, partial (mitochondrion) [Blaesoxipha plinthopyga]

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 ...
 1-158 1.95e-105

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: 310.26  E-value: 1.95e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805522424   1 V*LANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTLNSKMLKSQFIIMFMGVNLTFFPQHFLGLAG 80
Cdd:MTH00153  354 VVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAG 433

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1805522424  81 MPRRYSDYPDAYTTWNVISTIGSTISLLGILFFFFIIWESLTSQRQVMFPI*LNSSIEWL*NTPPAEHSYSELPLLTN 158
Cdd:MTH00153  434 MPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNLSSSIEWLQNLPPAEHSYSELPLLTN 511
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-158 1.95e-105

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 310.26  E-value: 1.95e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805522424   1 V*LANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTLNSKMLKSQFIIMFMGVNLTFFPQHFLGLAG 80
Cdd:MTH00153  354 VVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAG 433

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1805522424  81 MPRRYSDYPDAYTTWNVISTIGSTISLLGILFFFFIIWESLTSQRQVMFPI*LNSSIEWL*NTPPAEHSYSELPLLTN 158
Cdd:MTH00153  434 MPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNLSSSIEWLQNLPPAEHSYSELPLLTN 511
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-140 4.12e-79

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: 242.39  E-value: 4.12e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805522424   1 V*LANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTLNSKMLKSQFIIMFMGVNLTFFPQHFLGLAG 80
Cdd:cd01663   347 VVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAG 426

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1805522424  81 MPRRYSDYPDAYTTWNVISTIGSTISLLGILFFFFIIWESLTSQRQVMFPI-*LNSSIEWL 140
Cdd:cd01663   427 MPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVgEGSTSLEWT 487
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-157 2.23e-47

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 160.68  E-value: 2.23e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805522424   1 V*LANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTLNSKMLKSQFIIMFMGVNLTFFPQHFLGLAG 80
Cdd:COG0843   357 VMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLG 436

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805522424  81 MPRRYSDYP--DAYTTWNVISTIGSTISLLGILFFFFIIWESLTSQRQV-MFPI*LNsSIEWL*NTPPAEHSYSELPLLT 157
Cdd:COG0843   437 MPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGPKAgGNPWGAR-TLEWATPSPPPLYNFASIPVVR 515
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-150 4.11e-44

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: 151.22  E-value: 4.11e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805522424   1 V*LANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTLNSKMLKSQFIIMFMGVNLTFFPQHFLGLAG 80
Cdd:TIGR02891 348 VMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLG 427

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1805522424  81 MPRRYSDYPDA--YTTWNVISTIGSTISLLGILFFFFIIWESLTSQRQVMFPI*LNSSIEWL*NTPPAEHSY 150
Cdd:TIGR02891 428 MPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGANPWGATTLEWTTSSPPPAHNF 499
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-105 2.85e-29

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: 110.74  E-value: 2.85e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805522424   1 V*LANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTLNSKMLKSQFIIMFMGVNLTFFPQHFLGLAG 80
Cdd:pfam00115 324 VMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLG 403

                          90       100
                  ....*....|....*....|....*....
gi 1805522424  81 MPRRYS----DYPDAYTTWNVISTIGSTI 105
Cdd:pfam00115 404 MPRRYAppfiETVPAFQPLNWIRTIGGVL 432
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-158 1.95e-105

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 310.26  E-value: 1.95e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805522424   1 V*LANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTLNSKMLKSQFIIMFMGVNLTFFPQHFLGLAG 80
Cdd:MTH00153  354 VVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAG 433

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1805522424  81 MPRRYSDYPDAYTTWNVISTIGSTISLLGILFFFFIIWESLTSQRQVMFPI*LNSSIEWL*NTPPAEHSYSELPLLTN 158
Cdd:MTH00153  434 MPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNLSSSIEWLQNLPPAEHSYSELPLLTN 511
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-158 5.38e-81

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 248.08  E-value: 5.38e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805522424   1 V*LANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTLNSKMLKSQFIIMFMGVNLTFFPQHFLGLAG 80
Cdd:MTH00116  356 IVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAG 435

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1805522424  81 MPRRYSDYPDAYTTWNVISTIGSTISLLGILFFFFIIWESLTSQRQVMFPI*LNSSIEWL*NTPPAEHSYSELPLLTN 158
Cdd:MTH00116  436 MPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKRKVLQPELTTTNIEWIHGCPPPYHTFEEPAFVQV 513
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-156 9.13e-81

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 247.28  E-value: 9.13e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805522424   1 V*LANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTLNSKMLKSQFIIMFMGVNLTFFPQHFLGLAG 80
Cdd:MTH00167  356 IVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAG 435

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1805522424  81 MPRRYSDYPDAYTTWNVISTIGSTISLLGILFFFFIIWESLTSQRQVMFPI*LNSSIEWL*NTPPAEHSYSELPLL 156
Cdd:MTH00167  436 MPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRKLLPVELTSTNVEWLHGCPPPHHTWEEPPFV 511
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-158 2.79e-79

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 243.48  E-value: 2.79e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805522424   1 V*LANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTLNSKMLKSQFIIMFMGVNLTFFPQHFLGLAG 80
Cdd:MTH00142  354 IVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAG 433

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1805522424  81 MPRRYSDYPDAYTTWNVISTIGSTISLLGILFFFFIIWESLTSQRQVMFPI*LNSSIEWL*NTPPAEHSYSELPLLTN 158
Cdd:MTH00142  434 MPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLVMWSSHLSTSLEWSHRLPPDFHTYDELPILVV 511
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-140 4.12e-79

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: 242.39  E-value: 4.12e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805522424   1 V*LANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTLNSKMLKSQFIIMFMGVNLTFFPQHFLGLAG 80
Cdd:cd01663   347 VVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAG 426

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1805522424  81 MPRRYSDYPDAYTTWNVISTIGSTISLLGILFFFFIIWESLTSQRQVMFPI-*LNSSIEWL 140
Cdd:cd01663   427 MPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVgEGSTSLEWT 487
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-154 1.35e-77

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 239.11  E-value: 1.35e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805522424   1 V*LANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTLNSKMLKSQFIIMFMGVNLTFFPQHFLGLAG 80
Cdd:MTH00223  353 IILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAG 432

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1805522424  81 MPRRYSDYPDAYTTWNVISTIGSTISLLGILFFFFIIWESLTSQRQVMFPI*LNSSIEWL*NTPPAEHSYSELP 154
Cdd:MTH00223  433 MPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSVVWSGHLSTSLEWDNLLPADFHNNSETG 506
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-152 1.07e-68

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 216.33  E-value: 1.07e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805522424   1 V*LANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTLNSKMLKSQFIIMFMGVNLTFFPQHFLGLAG 80
Cdd:MTH00183  356 IVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAG 435

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1805522424  81 MPRRYSDYPDAYTTWNVISTIGSTISLLGILFFFFIIWESLTSQRQVMFPI*LNSSIEWL*NTPPAEHSYSE 152
Cdd:MTH00183  436 MPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKREVLSVELTSTNVEWLHGCPPPYHTFEE 507
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-152 1.59e-68

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 215.52  E-value: 1.59e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805522424   1 V*LANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTLNSKMLKSQFIIMFMGVNLTFFPQHFLGLAG 80
Cdd:MTH00103  356 IVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSG 435

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1805522424  81 MPRRYSDYPDAYTTWNVISTIGSTISLLGILFFFFIIWESLTSQRQVMFPI*LNSSIEWL*NTPPAEHSYSE 152
Cdd:MTH00103  436 MPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKREVLTVELTTTNLEWLHGCPPPYHTFEE 507
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-155 2.95e-68

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 215.08  E-value: 2.95e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805522424   1 V*LANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTLNSKMLKSQFIIMFMGVNLTFFPQHFLGLAG 80
Cdd:MTH00037  356 IVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAG 435

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1805522424  81 MPRRYSDYPDAYTTWNVISTIGSTISLLGILFFFFIIWESLTSQRQVMFPI*LNSSIEWL*NT-PPAEHSYSELPL 155
Cdd:MTH00037  436 MPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQREVISPEFSSSSLEWQYSSfPPSHHTFDETPS 511
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-158 5.70e-68

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 214.42  E-value: 5.70e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805522424   1 V*LANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTLNSKMLKSQFIIMFMGVNLTFFPQHFLGLAG 80
Cdd:MTH00077  356 IVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAG 435

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1805522424  81 MPRRYSDYPDAYTTWNVISTIGSTISLLGILFFFFIIWESLTSQRQVMFPI*LNSSIEWL*NTPPAEHSYSELPLLTN 158
Cdd:MTH00077  436 MPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKREVLTTELTSTNIEWLHGCPPPYHTFEEPSFVQT 513
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-157 1.11e-64

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 205.52  E-value: 1.11e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805522424   1 V*LANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTLNSKMLKSQFIIMFMGVNLTFFPQHFLGLAG 80
Cdd:MTH00007  353 IVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRWAKAHFFLMFLGVNLTFFPQHFLGLSG 432

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1805522424  81 MPRRYSDYPDAYTTWNVISTIGSTISLLGILFFFFIIWESLTSQRQVMFPI*LNSSIEWL*NTPPAEHSYSELPLLT 157
Cdd:MTH00007  433 MPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVIASPHMSSSLEWQDTLPLDFHNLPETGIIT 509
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-156 5.73e-54

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 178.09  E-value: 5.73e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805522424   1 V*LANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTLNSKMLKSQFIIMFMGVNLTFFPQHFLGLAG 80
Cdd:MTH00182  358 VVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAG 437

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805522424  81 MPRRYSDYPDAYTTWNVISTIGSTISLLGILFFFFIIWESLTSQRQ----VMFPI*LNSSIEWL*NTPPAEHSYSELPLL 156
Cdd:MTH00182  438 FPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEKfigwKEGTGESWASLEWVHSSPPLFHTYNELPFV 517
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-152 7.12e-54

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 177.18  E-value: 7.12e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805522424   1 V*LANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTLNSKMLKSQFIIMFMGVNLTFFPQHFLGLAG 80
Cdd:MTH00079  356 VILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHG 435

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1805522424  81 MPRRYSDYPDAYTTWNVISTIGSTISLLGILFFFFIIWESLTSQRQVMFPI*LNSSIEWL*NTPPAEHSYSE 152
Cdd:MTH00079  436 MPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYRLVLHDNYINSSPEYSLSSYVFGHSYQS 507
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-156 4.48e-52

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 172.70  E-value: 4.48e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805522424   1 V*LANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTLNSKMLKSQFIIMFMGVNLTFFPQHFLGLAG 80
Cdd:MTH00184  358 IVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAG 437

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1805522424  81 MPRRYSDYPDAYTTWNVISTIGSTISLLGILFFFFIIWESLTSQRQV---MFPI*LNSSIEWL*NTPPAEHSYSELPLL 156
Cdd:MTH00184  438 LPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYVREIKFvgwVEDSGHYPSLEWAQTSPPAHHTYNELPYV 516
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-121 1.36e-51

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: 170.40  E-value: 1.36e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805522424   1 V*LANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTLNSKMLKSQFIIMFMGVNLTFFPQHFLGLAG 80
Cdd:cd00919   343 VVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIHFWLWFIGFNLTFFPMHFLGLLG 422

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1805522424  81 MPRRYSDYPDAYTTWNVISTIGSTISLLGILFFFFIIWESL 121
Cdd:cd00919   423 MPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-157 2.23e-47

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 160.68  E-value: 2.23e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805522424   1 V*LANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTLNSKMLKSQFIIMFMGVNLTFFPQHFLGLAG 80
Cdd:COG0843   357 VMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLG 436

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805522424  81 MPRRYSDYP--DAYTTWNVISTIGSTISLLGILFFFFIIWESLTSQRQV-MFPI*LNsSIEWL*NTPPAEHSYSELPLLT 157
Cdd:COG0843   437 MPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGPKAgGNPWGAR-TLEWATPSPPPLYNFASIPVVR 515
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-150 4.11e-44

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: 151.22  E-value: 4.11e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805522424   1 V*LANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTLNSKMLKSQFIIMFMGVNLTFFPQHFLGLAG 80
Cdd:TIGR02891 348 VMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLG 427

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1805522424  81 MPRRYSDYPDA--YTTWNVISTIGSTISLLGILFFFFIIWESLTSQRQVMFPI*LNSSIEWL*NTPPAEHSY 150
Cdd:TIGR02891 428 MPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGANPWGATTLEWTTSSPPPAHNF 499
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-156 1.42e-39

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 139.76  E-value: 1.42e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805522424   1 V*LANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTLNSKMLKSQFIIMFMGVNLTFFPQHFLGLAG 80
Cdd:MTH00026  359 IVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAG 438

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805522424  81 MPRRYSDYPDAYTTWNVISTIGSTISLLGILFFFFIIWESLTSQRQVMFPI*LN-------------SSIEWL*NTPPAE 147
Cdd:MTH00026  439 LPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDAYYREEPFDINIMAKgplipfscqpahfDTLEWSLTSPPEH 518


                  ....*....
gi 1805522424 148 HSYSELPLL 156
Cdd:MTH00026  519 HTYNELPYI 527
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-149 7.84e-38

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 134.81  E-value: 7.84e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805522424   1 V*LANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTLNSKMLKSQFIIMFMGVNLTFFPQHFLGLAG 80
Cdd:MTH00048  355 IVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCG 434

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1805522424  81 MPRRYSDYPDAYTTWNVISTIGSTISLLGILFFFFIIWESLTSQRQVMFPI*LNSSIEWL*NTPPAEHS 149
Cdd:MTH00048  435 LPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVVKNEVLGLWGSSSCVVNVLMSPVPYHN 503
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-150 9.22e-38

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: 134.63  E-value: 9.22e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805522424   1 V*LANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTLNSKMLKSQFIIMFMGVNLTFFPQHFLGLAG 80
Cdd:cd01662   349 VMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERLGKWSFWLWFIGFNLTFFPMHILGLMG 428

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1805522424  81 MPRRYSDYP--DAYTTWNVISTIGSTISLLGILFFFFIIWESLTSQRQVMFPI*LN-SSIEWL*NTPPAEHSY 150
Cdd:cd01662   429 MPRRVYTYLpgPGWDPLNLISTIGAFLIAAGVLLFLINVIVSIRKGKRDATGDPWGaRTLEWATSSPPPAYNF 501
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-105 2.85e-29

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: 110.74  E-value: 2.85e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805522424   1 V*LANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTLNSKMLKSQFIIMFMGVNLTFFPQHFLGLAG 80
Cdd:pfam00115 324 VMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLG 403

                          90       100
                  ....*....|....*....|....*....
gi 1805522424  81 MPRRYS----DYPDAYTTWNVISTIGSTI 105
Cdd:pfam00115 404 MPRRYAppfiETVPAFQPLNWIRTIGGVL 432
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 1-154 8.44e-25

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


Pssm-ID: 131928  Cd Length: 643  Bit Score: 99.16  E-value: 8.44e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805522424   1 V*LANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTLNSKMLKSQFIIMFMGVNLTFFPQHFLGLAG 80
Cdd:TIGR02882 392 VMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYKLNERLGKWCFWFFMIGFNVCFFPMYILGLDG 471

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1805522424  81 MPRRYSDY--PDAYTTWNVISTIGSTISLLGILFFFF-IIWESLTSQRQVMFPI*LNSSIEWL*NTPPAEHSYSELP 154
Cdd:TIGR02882 472 MPRRMYTYspSDGWFPLNLISTIGALLMAIGFIFLVYnIYYSHRKSPREATGDPWNGRTLEWATASPPPKYNFAVTP 548
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 1-154 2.91e-16

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 74.97  E-value: 2.91e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805522424   1 V*LANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTLNSKMLKSQFIIMFMGVNLTFFPQHFLGLAG 80
Cdd:PRK15017  399 VLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMG 478

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1805522424  81 MPRRYSDYPDA-YTTWNVISTIGSTISLLGILFFFFIIWESLTSQ---RQVMFPI*LNSSIEWL*NTPPAEHSYSELP 154
Cdd:PRK15017  479 MTRRLSQQIDPqFHTMLMIAASGAALIALGILCQVIQMYVSIRDRdqnRDLTGDPWGGRTLEWATSSPPPFYNFAVVP 556
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 4-122 2.36e-11

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


Pssm-ID: 238830  Cd Length: 473  Bit Score: 60.38  E-value: 2.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805522424   4 ANSSIDIILHDTYYVVAHFHyvLSMGAVFAIMA-GFVHWY-PLFTGLTLNSKMLKS-QFIIMFMGVNLTFFPQHFLGLAG 80
Cdd:cd01660   347 ASYQLNYVVHNTAWVPGHFH--LTVGGAVALTFmAVAYWLvPHLTGRELAAKRLALaQPWLWFVGMTIMSTAMHVAGLLG 424

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1805522424  81 MPRR--YSDYPDAY-----TTWNVISTIGSTISLLGILFFFFIIWESLT 122
Cdd:cd01660   425 APRRtaEAQYGGLPaagewAPYQQLMAIGGTILFVSGALFLYILFRTLL 473
 
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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