NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|374711898|gb|AEZ64466|]
View 

cytochrome oxidase subunit 1, partial (mitochondrion) [Leptacis sp. 1 CL-2012]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 1-150 2.46e-100

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: 296.78  E-value: 2.46e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374711898   1 GVLSMIYAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATIHGMKLIFSPVMLWVIGFIFLF 80
Cdd:MTH00153 267 GTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLF 346

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374711898  81 TLGGLTGIMLSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIIGGFINWFPLFTGLSLNNFWLKIQFFSMF 150
Cdd:MTH00153 347 TIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMF 416
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-150 2.46e-100

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 296.78  E-value: 2.46e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374711898   1 GVLSMIYAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATIHGMKLIFSPVMLWVIGFIFLF 80
Cdd:MTH00153 267 GTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLF 346

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374711898  81 TLGGLTGIMLSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIIGGFINWFPLFTGLSLNNFWLKIQFFSMF 150
Cdd:MTH00153 347 TIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMF 416
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-150 1.99e-90

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: 270.89  E-value: 1.99e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374711898   1 GVLSMIYAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATIHGMKLIFSPVMLWVIGFIFLF 80
Cdd:cd01663  260 GYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLF 339

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374711898  81 TLGGLTGIMLSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIIGGFINWFPLFTGLSLNNFWLKIQFFSMF 150
Cdd:cd01663  340 TIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMF 409
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
4-150 1.18e-54

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 179.55  E-value: 1.18e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374711898   4 SMIYAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATIHGMKLIFSPVMLWVIGFIFLFTLG 83
Cdd:COG0843  273 AMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIG 352

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 374711898  84 GLTGIMLSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIIGGFINWFPLFTGLSLNNFWLKIQFFSMF 150
Cdd:COG0843  353 GLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWF 419
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-150 1.84e-53

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: 175.49  E-value: 1.84e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374711898    1 GVLSMIYAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATIHGMKLIFSPVMLWVIGFIFLF 80
Cdd:TIGR02891 261 GYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLF 340

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374711898   81 TLGGLTGIMLSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIIGGFINWFPLFTGLSLNNFWLKIQFFSMF 150
Cdd:TIGR02891 341 VIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTF 410
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 4-150 5.12e-36

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: 128.46  E-value: 5.12e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374711898    4 SMIYAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATIHGMKLIF-SPVMLWVIGFIFLFTL 82
Cdd:pfam00115 239 LSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrTTPMLFFLGFAFLFII 318

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 374711898   83 GGLTGIMLSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIIGGFINWFPLFTGLSLNNFWLKIQFFSMF 150
Cdd:pfam00115 319 GGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLF 386
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-150 2.46e-100

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 296.78  E-value: 2.46e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374711898   1 GVLSMIYAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATIHGMKLIFSPVMLWVIGFIFLF 80
Cdd:MTH00153 267 GTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLF 346

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374711898  81 TLGGLTGIMLSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIIGGFINWFPLFTGLSLNNFWLKIQFFSMF 150
Cdd:MTH00153 347 TIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMF 416
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-150 1.99e-90

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: 270.89  E-value: 1.99e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374711898   1 GVLSMIYAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATIHGMKLIFSPVMLWVIGFIFLF 80
Cdd:cd01663  260 GYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLF 339

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374711898  81 TLGGLTGIMLSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIIGGFINWFPLFTGLSLNNFWLKIQFFSMF 150
Cdd:cd01663  340 TIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMF 409
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-150 5.87e-83

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 252.71  E-value: 5.87e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374711898   1 GVLSMIYAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATIHGMKLIFSPVMLWVIGFIFLF 80
Cdd:MTH00116 269 GYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLF 348

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374711898  81 TLGGLTGIMLSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIIGGFINWFPLFTGLSLNNFWLKIQFFSMF 150
Cdd:MTH00116 349 TIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWTKAQFGVMF 418
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-150 1.02e-82

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 251.82  E-value: 1.02e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374711898   1 GVLSMIYAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATIHGMKLIFSPVMLWVIGFIFLF 80
Cdd:MTH00223 266 GTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEAPMLWALGFIFLF 345

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374711898  81 TLGGLTGIMLSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIIGGFINWFPLFTGLSLNNFWLKIQFFSMF 150
Cdd:MTH00223 346 TVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRRWAKAHFFLMF 415
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-150 8.86e-82

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 249.59  E-value: 8.86e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374711898   1 GVLSMIYAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATIHGMKLIFSPVMLWVIGFIFLF 80
Cdd:MTH00167 269 GYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWETPMLWALGFIFLF 348

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374711898  81 TLGGLTGIMLSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIIGGFINWFPLFTGLSLNNFWLKIQFFSMF 150
Cdd:MTH00167 349 TVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETWTKIHFFVMF 418
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-150 2.99e-80

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 245.40  E-value: 2.99e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374711898   1 GVLSMIYAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATIHGMKLIFSPVMLWVIGFIFLF 80
Cdd:MTH00142 267 GTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEPPMLWALGFIFLF 346

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374711898  81 TLGGLTGIMLSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIIGGFINWFPLFTGLSLNNFWLKIQFFSMF 150
Cdd:MTH00142 347 TVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWLKAHFYTMF 416
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-150 8.67e-74

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 229.00  E-value: 8.67e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374711898   1 GVLSMIYAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATIHGMKLIFSPVMLWVIGFIFLF 80
Cdd:MTH00103 269 GYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFLF 348

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374711898  81 TLGGLTGIMLSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIIGGFINWFPLFTGLSLNNFWLKIQFFSMF 150
Cdd:MTH00103 349 TVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHFTIMF 418
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-150 3.14e-71

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 222.08  E-value: 3.14e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374711898   1 GVLSMIYAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATIHGMKLIFSPVMLWVIGFIFLF 80
Cdd:MTH00007 266 GTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYETPMLWALGFIFLF 345

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374711898  81 TLGGLTGIMLSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIIGGFINWFPLFTGLSLNNFWLKIQFFSMF 150
Cdd:MTH00007 346 TTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRWAKAHFFLMF 415
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-150 9.79e-70

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 218.64  E-value: 9.79e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374711898   1 GVLSMIYAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATIHGMKLIFSPVMLWVIGFIFLF 80
Cdd:MTH00183 269 GYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLF 348

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374711898  81 TLGGLTGIMLSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIIGGFINWFPLFTGLSLNNFWLKIQFFSMF 150
Cdd:MTH00183 349 TVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWTKIHFGVMF 418
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-150 3.58e-69

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 217.00  E-value: 3.58e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374711898   1 GVLSMIYAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATIHGMKLIFSPVMLWVIGFIFLF 80
Cdd:MTH00037 269 GYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWETPLLWALGFVFLF 348

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374711898  81 TLGGLTGIMLSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIIGGFINWFPLFTGLSLNNFWLKIQFFSMF 150
Cdd:MTH00037 349 TIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLWSKVHFFLMF 418
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-150 4.41e-69

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 216.73  E-value: 4.41e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374711898   1 GVLSMIYAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATIHGMKLIFSPVMLWVIGFIFLF 80
Cdd:MTH00077 269 GYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDAAMLWALGFIFLF 348

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374711898  81 TLGGLTGIMLSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIIGGFINWFPLFTGLSLNNFWLKIQFFSMF 150
Cdd:MTH00077 349 TVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWSKIHFGVMF 418
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-150 4.52e-68

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 213.77  E-value: 4.52e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374711898   1 GVLSMIYAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATIHGMKLIFSPVMLWVIGFIFLF 80
Cdd:MTH00079 269 GSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPLLLWVLGFIFLF 348

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374711898  81 TLGGLTGIMLSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIIGGFINWFPLFTGLSLNNFWLKIQFFSMF 150
Cdd:MTH00079 349 TIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMMSAVFFLMF 418
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-150 1.56e-64

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 205.06  E-value: 1.56e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374711898   1 GVLSMIYAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATIHGMKLIFSPVMLWVIGFIFLF 80
Cdd:MTH00182 271 GYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDTPMLWAMGFVFLF 350

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374711898  81 TLGGLTGIMLSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIIGGFINWFPLFTGLSLNNFWLKIQFFSMF 150
Cdd:MTH00182 351 TLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNELYGKIHFWLMF 420
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-150 6.13e-62

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 198.13  E-value: 6.13e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374711898   1 GVLSMIYAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATIHGMKLIFSPVMLWVIGFIFLF 80
Cdd:MTH00184 271 GYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDTPMLWAIGFVFLF 350

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374711898  81 TLGGLTGIMLSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIIGGFINWFPLFTGLSLNNFWLKIQFFSMF 150
Cdd:MTH00184 351 TMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEVYGKIHFWLMF 420
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-150 2.11e-56

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: 182.35  E-value: 2.11e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374711898   1 GVLSMIYAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATIHGMKLIFSPVMLWVIGFIFLF 80
Cdd:cd00919  256 GYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDPPMLFALGFLFLF 335

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374711898  81 TLGGLTGIMLSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIIGGFINWFPLFTGLSLNNFWLKIQFFSMF 150
Cdd:cd00919  336 TIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIHFWLWF 405
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
4-150 1.18e-54

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 179.55  E-value: 1.18e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374711898   4 SMIYAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATIHGMKLIFSPVMLWVIGFIFLFTLG 83
Cdd:COG0843  273 AMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIG 352

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 374711898  84 GLTGIMLSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIIGGFINWFPLFTGLSLNNFWLKIQFFSMF 150
Cdd:COG0843  353 GLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWF 419
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-150 1.12e-53

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 177.13  E-value: 1.12e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374711898   1 GVLSMIYAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATIHG--MKLIFSPVMLWVIGFIF 78
Cdd:MTH00026 270 GYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGsgRNLIFTTPMAWALGFIF 349

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 374711898  79 LFTLGGLTGIMLSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIIGGFINWFPLFTGLSLNNFWLKIQFFSMF 150
Cdd:MTH00026 350 LFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDIYGLIHFWLMF 421
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-150 1.84e-53

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: 175.49  E-value: 1.84e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374711898    1 GVLSMIYAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATIHGMKLIFSPVMLWVIGFIFLF 80
Cdd:TIGR02891 261 GYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLF 340

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374711898   81 TLGGLTGIMLSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIIGGFINWFPLFTGLSLNNFWLKIQFFSMF 150
Cdd:TIGR02891 341 VIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTF 410
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-150 5.03e-52

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: 172.00  E-value: 5.03e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374711898   1 GVLSMIYAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATIHGMKLIFSPVMLWVIGFIFLF 80
Cdd:cd01662  262 GYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLWAIGFLVTF 341

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374711898  81 TLGGLTGIMLSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIIGGFINWFPLFTGLSLNNFWLKIQFFSMF 150
Cdd:cd01662  342 VIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERLGKWSFWLWF 411
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-147 3.28e-49

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 164.85  E-value: 3.28e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374711898   1 GVLSMIYAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATIHGMKLIFS-PVMLWVIGFIFL 79
Cdd:MTH00048 267 GYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKSdPVVWWVVSFIVL 346

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 374711898  80 FTLGGLTGIMLSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIIGGFINWFPLFTGLSLNNFWLKIQFF 147
Cdd:MTH00048 347 FTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQCHCI 414
CyoB TIGR02843
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ...
 1-150 1.13e-40

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: 143.66  E-value: 1.13e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374711898    1 GVLSMIYAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATIHGMKLIFSPVMLWVIGFIFLF 80
Cdd:TIGR02843 311 GYTSMVWATIAITVLSFIVWLHHFFTMGAGANVNAFFGIATMIIAIPTGVKIFNWLFTMYKGRIRFETPMLWTIGFMVTF 390

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374711898   81 TLGGLTGIMLSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIIGGFINWFPLFTGLSLNNFWLKIQFFSMF 150
Cdd:TIGR02843 391 SIGGMTGVLLAVPPADFVLHNSLFLIAHFHNVIIGGVVFGCFAGLTYWFPKAFGFKLNEKLGKRSFWCWF 460
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 4-150 5.12e-36

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: 128.46  E-value: 5.12e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374711898    4 SMIYAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATIHGMKLIF-SPVMLWVIGFIFLFTL 82
Cdd:pfam00115 239 LSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrTTPMLFFLGFAFLFII 318

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 374711898   83 GGLTGIMLSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIIGGFINWFPLFTGLSLNNFWLKIQFFSMF 150
Cdd:pfam00115 319 GGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLF 386
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 1-147 2.40e-34

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 126.20  E-value: 2.40e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374711898   1 GVLSMIYAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATIHGMKLIFSPVMLWVIGFIFLF 80
Cdd:PRK15017 312 GYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTF 391

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 374711898  81 TLGGLTGIMLSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIIGGFINWFPLFTGLSLNNFWLKIQFF 147
Cdd:PRK15017 392 SVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFW 458
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH