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Conserved domains on  [gi|1632313899|gb|QCI61990|]
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cytochrome oxidase subunit 1, partial (mitochondrion) [Cataglyphis velox]

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 ...
 1-167 4.18e-115

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: 335.30  E-value: 4.18e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899   1 LGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWITTLHGTKIYNNSSLWWAMGFIFLFTMGGLTGVMLSNSS 80
Cdd:MTH00153  281 LGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSS 360

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899  81 IDIILHDTYYVVAHFHYVLSMGAVFAIIASFIHWFPLITGFSLNNYFLNIQFLSMFIGVNMTFFPQHFLGLSGMPRRYSD 160
Cdd:MTH00153  361 IDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSD 440


                  ....*..
gi 1632313899 161 YPDTFLS 167
Cdd:MTH00153  441 YPDAYTS 447
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-167 4.18e-115

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 335.30  E-value: 4.18e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899   1 LGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWITTLHGTKIYNNSSLWWAMGFIFLFTMGGLTGVMLSNSS 80
Cdd:MTH00153  281 LGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSS 360

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899  81 IDIILHDTYYVVAHFHYVLSMGAVFAIIASFIHWFPLITGFSLNNYFLNIQFLSMFIGVNMTFFPQHFLGLSGMPRRYSD 160
Cdd:MTH00153  361 IDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSD 440


                  ....*..
gi 1632313899 161 YPDTFLS 167
Cdd:MTH00153  441 YPDAYTS 447
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-165 1.22e-105

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: 310.57  E-value: 1.22e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899   1 LGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWITTLHGTKIYNNSSLWWAMGFIFLFTMGGLTGVMLSNSS 80
Cdd:cd01663   274 LGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSS 353

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899  81 IDIILHDTYYVVAHFHYVLSMGAVFAIIASFIHWFPLITGFSLNNYFLNIQFLSMFIGVNMTFFPQHFLGLSGMPRRYSD 160
Cdd:cd01663   354 LDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPD 433


                  ....*
gi 1632313899 161 YPDTF 165
Cdd:cd01663   434 YPDAY 438
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-163 6.66e-65

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: 206.31  E-value: 6.66e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899   1 LGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWITTLHGTKIYNNSSLWWAMGFIFLFTMGGLTGVMLSNSS 80
Cdd:TIGR02891 275 LSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVP 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899  81 IDIILHDTYYVVAHFHYVLSMGAVFAIIASFIHWFPLITGFSLNNYFLNIQFLSMFIGVNMTFFPQHFLGLSGMPRRYSD 160
Cdd:TIGR02891 355 LDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYT 434


                  ...
gi 1632313899 161 YPD 163
Cdd:TIGR02891 435 YPP 437
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-165 1.53e-64

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 206.13  E-value: 1.53e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899   1 LGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWITTLHGTKIYNNSSLWWAMGFIFLFTMGGLTGVMLSNSS 80
Cdd:COG0843   284 LSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVP 363

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899  81 IDIILHDTYYVVAHFHYVLSMGAVFAIIASFIHWFPLITGFSLNNYFLNIQFLSMFIGVNMTFFPQHFLGLSGMPRRYSD 160
Cdd:COG0843   364 LDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYAT 443


                  ....*
gi 1632313899 161 YPDTF 165
Cdd:COG0843   444 YPPEP 448
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-160 6.40e-50

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: 165.82  E-value: 6.40e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899   1 LGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWITTLHGTKI-YNNSSLWWAMGFIFLFTMGGLTGVMLSNS 79
Cdd:pfam00115 250 LGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIrFRTTPMLFFLGFAFLFIIGGLTGVMLALP 329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899  80 SIDIILHDTYYVVAHFHYVLSMGAVFAIIASFIHWFPLITGFSLNNYFLNIQFLSMFIGVNMTFFPQHFLGLSGMPRRYS 159
Cdd:pfam00115 330 PVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYA 409


                  .
gi 1632313899 160 D 160
Cdd:pfam00115 410 P 410
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-167 4.18e-115

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 335.30  E-value: 4.18e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899   1 LGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWITTLHGTKIYNNSSLWWAMGFIFLFTMGGLTGVMLSNSS 80
Cdd:MTH00153  281 LGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSS 360

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899  81 IDIILHDTYYVVAHFHYVLSMGAVFAIIASFIHWFPLITGFSLNNYFLNIQFLSMFIGVNMTFFPQHFLGLSGMPRRYSD 160
Cdd:MTH00153  361 IDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSD 440


                  ....*..
gi 1632313899 161 YPDTFLS 167
Cdd:MTH00153  441 YPDAYTS 447
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-165 1.22e-105

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: 310.57  E-value: 1.22e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899   1 LGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWITTLHGTKIYNNSSLWWAMGFIFLFTMGGLTGVMLSNSS 80
Cdd:cd01663   274 LGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSS 353

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899  81 IDIILHDTYYVVAHFHYVLSMGAVFAIIASFIHWFPLITGFSLNNYFLNIQFLSMFIGVNMTFFPQHFLGLSGMPRRYSD 160
Cdd:cd01663   354 LDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPD 433


                  ....*
gi 1632313899 161 YPDTF 165
Cdd:cd01663   434 YPDAY 438
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-165 7.08e-98

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 291.61  E-value: 7.08e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899   1 LGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWITTLHGTKIYNNSSLWWAMGFIFLFTMGGLTGVMLSNSS 80
Cdd:MTH00116  283 LGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSS 362

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899  81 IDIILHDTYYVVAHFHYVLSMGAVFAIIASFIHWFPLITGFSLNNYFLNIQFLSMFIGVNMTFFPQHFLGLSGMPRRYSD 160
Cdd:MTH00116  363 LDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSD 442


                  ....*
gi 1632313899 161 YPDTF 165
Cdd:MTH00116  443 YPDAY 447
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-166 9.76e-97

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 288.50  E-value: 9.76e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899   1 LGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWITTLHGTKIYNNSSLWWAMGFIFLFTMGGLTGVMLSNSS 80
Cdd:MTH00167  283 LGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSS 362

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899  81 IDIILHDTYYVVAHFHYVLSMGAVFAIIASFIHWFPLITGFSLNNYFLNIQFLSMFIGVNMTFFPQHFLGLSGMPRRYSD 160
Cdd:MTH00167  363 LDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSD 442


                  ....*.
gi 1632313899 161 YPDTFL 166
Cdd:MTH00167  443 YPDAYT 448
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-165 8.18e-96

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 286.10  E-value: 8.18e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899   1 LGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWITTLHGTKIYNNSSLWWAMGFIFLFTMGGLTGVMLSNSS 80
Cdd:MTH00223  280 LGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSS 359

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899  81 IDIILHDTYYVVAHFHYVLSMGAVFAIIASFIHWFPLITGFSLNNYFLNIQFLSMFIGVNMTFFPQHFLGLSGMPRRYSD 160
Cdd:MTH00223  360 LDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSD 439


                  ....*
gi 1632313899 161 YPDTF 165
Cdd:MTH00223  440 YPDCY 444
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-167 3.18e-92

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 276.99  E-value: 3.18e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899   1 LGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWITTLHGTKIYNNSSLWWAMGFIFLFTMGGLTGVMLSNSS 80
Cdd:MTH00142  281 LGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSS 360

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899  81 IDIILHDTYYVVAHFHYVLSMGAVFAIIASFIHWFPLITGFSLNNYFLNIQFLSMFIGVNMTFFPQHFLGLSGMPRRYSD 160
Cdd:MTH00142  361 LDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSD 440


                  ....*..
gi 1632313899 161 YPDTFLS 167
Cdd:MTH00142  441 YPDAYTT 447
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-166 1.71e-85

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 259.83  E-value: 1.71e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899   1 LGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWITTLHGTKIYNNSSLWWAMGFIFLFTMGGLTGVMLSNSS 80
Cdd:MTH00007  280 LGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSS 359

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899  81 IDIILHDTYYVVAHFHYVLSMGAVFAIIASFIHWFPLITGFSLNNYFLNIQFLSMFIGVNMTFFPQHFLGLSGMPRRYSD 160
Cdd:MTH00007  360 LDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSD 439


                  ....*.
gi 1632313899 161 YPDTFL 166
Cdd:MTH00007  440 YPDAYT 445
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-165 2.21e-85

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 259.43  E-value: 2.21e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899   1 LGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWITTLHGTKIYNNSSLWWAMGFIFLFTMGGLTGVMLSNSS 80
Cdd:MTH00103  283 LGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSS 362

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899  81 IDIILHDTYYVVAHFHYVLSMGAVFAIIASFIHWFPLITGFSLNNYFLNIQFLSMFIGVNMTFFPQHFLGLSGMPRRYSD 160
Cdd:MTH00103  363 LDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSD 442


                  ....*
gi 1632313899 161 YPDTF 165
Cdd:MTH00103  443 YPDAY 447
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-165 1.69e-83

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 254.85  E-value: 1.69e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899   1 LGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWITTLHGTKIYNNSSLWWAMGFIFLFTMGGLTGVMLSNSS 80
Cdd:MTH00183  283 LGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSS 362

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899  81 IDIILHDTYYVVAHFHYVLSMGAVFAIIASFIHWFPLITGFSLNNYFLNIQFLSMFIGVNMTFFPQHFLGLSGMPRRYSD 160
Cdd:MTH00183  363 LDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSD 442


                  ....*
gi 1632313899 161 YPDTF 165
Cdd:MTH00183  443 YPDAY 447
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-165 4.43e-83

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 253.71  E-value: 4.43e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899   1 LGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWITTLHGTKIYNNSSLWWAMGFIFLFTMGGLTGVMLSNSS 80
Cdd:MTH00077  283 LGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSS 362

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899  81 IDIILHDTYYVVAHFHYVLSMGAVFAIIASFIHWFPLITGFSLNNYFLNIQFLSMFIGVNMTFFPQHFLGLSGMPRRYSD 160
Cdd:MTH00077  363 LDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSD 442


                  ....*
gi 1632313899 161 YPDTF 165
Cdd:MTH00077  443 YPDAY 447
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-167 4.40e-82

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 251.29  E-value: 4.40e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899   1 LGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWITTLHGTKIYNNSSLWWAMGFIFLFTMGGLTGVMLSNSS 80
Cdd:MTH00037  283 LGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSS 362

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899  81 IDIILHDTYYVVAHFHYVLSMGAVFAIIASFIHWFPLITGFSLNNYFLNIQFLSMFIGVNMTFFPQHFLGLSGMPRRYSD 160
Cdd:MTH00037  363 IDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSD 442


                  ....*..
gi 1632313899 161 YPDTFLS 167
Cdd:MTH00037  443 YPDAYTL 449
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-166 1.08e-79

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 244.59  E-value: 1.08e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899   1 LGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWITTLHGTKIYNNSSLWWAMGFIFLFTMGGLTGVMLSNSS 80
Cdd:MTH00079  283 IGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSS 362

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899  81 IDIILHDTYYVVAHFHYVLSMGAVFAIIASFIHWFPLITGFSLNNYFLNIQFLSMFIGVNMTFFPQHFLGLSGMPRRYSD 160
Cdd:MTH00079  363 LDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLD 442


                  ....*.
gi 1632313899 161 YPDTFL 166
Cdd:MTH00079  443 YPDVYS 448
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-165 7.67e-75

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 232.79  E-value: 7.67e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899   1 LGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWITTLHGTKIYNNSSLWWAMGFIFLFTMGGLTGVMLSNSS 80
Cdd:MTH00182  285 LGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSS 364

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899  81 IDIILHDTYYVVAHFHYVLSMGAVFAIIASFIHWFPLITGFSLNNYFLNIQFLSMFIGVNMTFFPQHFLGLSGMPRRYSD 160
Cdd:MTH00182  365 LDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSD 444


                  ....*
gi 1632313899 161 YPDTF 165
Cdd:MTH00182  445 FADAF 449
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-165 2.51e-74

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 231.25  E-value: 2.51e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899   1 LGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWITTLHGTKIYNNSSLWWAMGFIFLFTMGGLTGVMLSNSS 80
Cdd:MTH00184  285 LGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSS 364

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899  81 IDIILHDTYYVVAHFHYVLSMGAVFAIIASFIHWFPLITGFSLNNYFLNIQFLSMFIGVNMTFFPQHFLGLSGMPRRYSD 160
Cdd:MTH00184  365 LDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSD 444


                  ....*
gi 1632313899 161 YPDTF 165
Cdd:MTH00184  445 FHDSF 449
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-166 1.25e-71

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: 222.79  E-value: 1.25e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899   1 LGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWITTLHGTKIYNNSSLWWAMGFIFLFTMGGLTGVMLSNSS 80
Cdd:cd00919   270 LSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDPPMLFALGFLFLFTIGGLTGVVLANVP 349

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899  81 IDIILHDTYYVVAHFHYVLSMGAVFAIIASFIHWFPLITGFSLNNYFLNIQFLSMFIGVNMTFFPQHFLGLSGMPRRYSD 160
Cdd:cd00919   350 LDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIHFWLWFIGFNLTFFPMHFLGLLGMPRRYAD 429


                  ....*.
gi 1632313899 161 YPDTFL 166
Cdd:cd00919   430 YPDGFA 435
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-163 6.66e-65

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: 206.31  E-value: 6.66e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899   1 LGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWITTLHGTKIYNNSSLWWAMGFIFLFTMGGLTGVMLSNSS 80
Cdd:TIGR02891 275 LSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVP 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899  81 IDIILHDTYYVVAHFHYVLSMGAVFAIIASFIHWFPLITGFSLNNYFLNIQFLSMFIGVNMTFFPQHFLGLSGMPRRYSD 160
Cdd:TIGR02891 355 LDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYT 434


                  ...
gi 1632313899 161 YPD 163
Cdd:TIGR02891 435 YPP 437
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-165 1.53e-64

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 206.13  E-value: 1.53e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899   1 LGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWITTLHGTKIYNNSSLWWAMGFIFLFTMGGLTGVMLSNSS 80
Cdd:COG0843   284 LSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVP 363

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899  81 IDIILHDTYYVVAHFHYVLSMGAVFAIIASFIHWFPLITGFSLNNYFLNIQFLSMFIGVNMTFFPQHFLGLSGMPRRYSD 160
Cdd:COG0843   364 LDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYAT 443


                  ....*
gi 1632313899 161 YPDTF 165
Cdd:COG0843   444 YPPEP 448
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-165 8.23e-64

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 204.48  E-value: 8.23e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899   1 LGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWITTLHGT--KIYNNSSLWWAMGFIFLFTMGGLTGVMLSN 78
Cdd:MTH00026  284 LGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSgrNLIFTTPMAWALGFIFLFTIGGLTGIVLSN 363

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899  79 SSIDIILHDTYYVVAHFHYVLSMGAVFAIIASFIHWFPLITGFSLNNYFLNIQFLSMFIGVNMTFFPQHFLGLSGMPRRY 158
Cdd:MTH00026  364 SSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRY 443


                  ....*..
gi 1632313899 159 SDYPDTF 165
Cdd:MTH00026  444 ADYPDNF 450
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-165 3.84e-61

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 196.82  E-value: 3.84e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899   1 LGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWITTLHGTKIY-NNSSLWWAMGFIFLFTMGGLTGVMLSNS 79
Cdd:MTH00048  281 LGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRkSDPVVWWVVSFIVLFTIGGVTGIVLSAS 360

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899  80 SIDIILHDTYYVVAHFHYVLSMGAVFAIIASFIHWFPLITGFSLNNYFLNIQFLSMFIGVNMTFFPQHFLGLSGMPRRYS 159
Cdd:MTH00048  361 VLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVC 440


                  ....*.
gi 1632313899 160 DYPDTF 165
Cdd:MTH00048  441 VYEPSY 446
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-163 2.26e-59

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: 192.03  E-value: 2.26e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899   1 LGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWITTLHGTKIYNNSSLWWAMGFIFLFTMGGLTGVMLSNSS 80
Cdd:cd01662   276 LSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPP 355

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899  81 IDIILHDTYYVVAHFHYVLSMGAVFAIIASFIHWFPLITGFSLNNYFLNIQFLSMFIGVNMTFFPQHFLGLSGMPRRYSD 160
Cdd:cd01662   356 ADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYT 435


                  ...
gi 1632313899 161 YPD 163
Cdd:cd01662   436 YLP 438
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-160 6.40e-50

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: 165.82  E-value: 6.40e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899   1 LGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWITTLHGTKI-YNNSSLWWAMGFIFLFTMGGLTGVMLSNS 79
Cdd:pfam00115 250 LGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIrFRTTPMLFFLGFAFLFIIGGLTGVMLALP 329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899  80 SIDIILHDTYYVVAHFHYVLSMGAVFAIIASFIHWFPLITGFSLNNYFLNIQFLSMFIGVNMTFFPQHFLGLSGMPRRYS 159
Cdd:pfam00115 330 PVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYA 409


                  .
gi 1632313899 160 D 160
Cdd:pfam00115 410 P 410
CyoB TIGR02843
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ...
 1-163 2.46e-41

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: 145.97  E-value: 2.46e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899   1 LGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWITTLHGTKIYNNSSLWWAMGFIFLFTMGGLTGVMLSNSS 80
Cdd:TIGR02843 325 LSFIVWLHHFFTMGAGANVNAFFGIATMIIAIPTGVKIFNWLFTMYKGRIRFETPMLWTIGFMVTFSIGGMTGVLLAVPP 404

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899  81 IDIILHDTYYVVAHFHYVLSMGAVFAIIASFIHWFPLITGFSLNNYFLNIQFLSMFIGVNMTFFPQHFLGLSGMPRRYSD 160
Cdd:TIGR02843 405 ADFVLHNSLFLIAHFHNVIIGGVVFGCFAGLTYWFPKAFGFKLNEKLGKRSFWCWFIGFYLAFMPLYILGFMGMTRRLNH 484


                  ...
gi 1632313899 161 YPD 163
Cdd:TIGR02843 485 YDN 487
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 1-163 7.64e-38

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 136.60  E-value: 7.64e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899   1 LGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWITTLHGTKIYNNSSLWWAMGFIFLFTMGGLTGVMLSNSS 80
Cdd:PRK15017  326 LSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPG 405

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899  81 IDIILHDTYYVVAHFHYVLSMGAVFAIIASFIHWFPLITGFSLNNYFLNIQFLSMFIGVNMTFFPQHFLGLSGMPRRYSD 160
Cdd:PRK15017  406 ADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQ 485


                  ...
gi 1632313899 161 YPD 163
Cdd:PRK15017  486 QID 488
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 27-163 7.33e-07

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: 47.67  E-value: 7.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632313899  27 TMIIAIPTGIKIFSWITTL-HGTKIYNNSSLWW---------------AMGFIFlFTMGGLTGVMLSNSSIDIILHDTYY 90
Cdd:cd01660   282 TFMVALPSLLTAFTVFASLeIAGRLRGGKGLFGwiralpwgdpmflalFLAMLM-FIPGGAGGIINASYQLNYVVHNTAW 360

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1632313899  91 VVAHFHYVLSMGAVFAIIASFIHWFPLITGFSL-NNYFLNIQFLSMFIGVNMTFFPQHFLGLSGMPRR--YSDYPD 163
Cdd:cd01660   361 VPGHFHLTVGGAVALTFMAVAYWLVPHLTGRELaAKRLALAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYGG 436
 
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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