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Conserved domains on  [gi|1194587590|gb|ARR97102|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Hyperolius parkeri]

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 ...
 1-269 0e+00

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: 545.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590   1 PVLAAGITMLLTDR*LNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVAYYSNKKEPFGYMGMVWAMLS 80
Cdd:MTH00153  198 PVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLA 277

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590  81 IGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATIHGGTIKWETPMLWALGFIFLFTVGGLTGIVLA 160
Cdd:MTH00153  278 IGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLA 357

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590 161 NSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLTLHSTWVKIHFVVMFVGVNLTFFPQHFLGLAGMPRR 240
Cdd:MTH00153  358 NSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRR 437

                         250       260
                  ....*....|....*....|....*....
gi 1194587590 241 YSDYPDAYTLWNSVSSIGSLISLVAVIMM 269
Cdd:MTH00153  438 YSDYPDAYTSWNVISSIGSTISLISILFF 466
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-269 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 545.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590   1 PVLAAGITMLLTDR*LNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVAYYSNKKEPFGYMGMVWAMLS 80
Cdd:MTH00153  198 PVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLA 277

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590  81 IGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATIHGGTIKWETPMLWALGFIFLFTVGGLTGIVLA 160
Cdd:MTH00153  278 IGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLA 357

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590 161 NSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLTLHSTWVKIHFVVMFVGVNLTFFPQHFLGLAGMPRR 240
Cdd:MTH00153  358 NSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRR 437

                         250       260
                  ....*....|....*....|....*....
gi 1194587590 241 YSDYPDAYTLWNSVSSIGSLISLVAVIMM 269
Cdd:MTH00153  438 YSDYPDAYTSWNVISSIGSTISLISILFF 466
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-269 0e+00

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: 533.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590   1 PVLAAGITMLLTDR*LNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVAYYSNKKEPFGYMGMVWAMLS 80
Cdd:cd01663   191 PVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLS 270

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590  81 IGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATIHGGTIKWETPMLWALGFIFLFTVGGLTGIVLA 160
Cdd:cd01663   271 IGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLA 350

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590 161 NSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLTLHSTWVKIHFVVMFVGVNLTFFPQHFLGLAGMPRR 240
Cdd:cd01663   351 NSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRR 430

                         250       260
                  ....*....|....*....|....*....
gi 1194587590 241 YSDYPDAYTLWNSVSSIGSLISLVAVIMM 269
Cdd:cd01663   431 YPDYPDAYAGWNMISSIGSLISFVSVLLF 459
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-269 1.23e-125

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 367.53  E-value: 1.23e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590   1 PVLAAGITMLLTDR*LNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVAYYSnKKEPFGYMGMVWAMLS 80
Cdd:COG0843   202 PVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFS-RKPLFGYKAMVLATVA 280

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590  81 IGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATIHGGTIKWETPMLWALGFIFLFTVGGLTGIVLA 160
Cdd:COG0843   281 IAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLA 360

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590 161 NSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLTLHSTWVKIHFVVMFVGVNLTFFPQHFLGLAGMPRR 240
Cdd:COG0843   361 SVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRR 440

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1194587590 241 YSDYP--DAYTLWNSVSSIGSLISLVAVIMM 269
Cdd:COG0843   441 YATYPpePGWQPLNLISTIGAFILAVGFLLF 471
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-269 1.68e-121

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: 355.76  E-value: 1.68e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590   1 PVLAAGITMLLTDR*LNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVAYYSnKKEPFGYMGMVWAMLS 80
Cdd:TIGR02891 193 PVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFA-RKPIFGYRAMVYATVA 271

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590  81 IGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATIHGGTIKWETPMLWALGFIFLFTVGGLTGIVLA 160
Cdd:TIGR02891 272 IGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLA 351

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590 161 NSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLTLHSTWVKIHFVVMFVGVNLTFFPQHFLGLAGMPRR 240
Cdd:TIGR02891 352 SVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRR 431

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1194587590 241 YSDYPDA--YTLWNSVSSIGSLISLVAVIMM 269
Cdd:TIGR02891 432 YYTYPPQmgFATLNLISTIGAFILAAGFLVF 462
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-261 6.20e-84

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: 257.50  E-value: 6.20e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590   1 PVLAAGITMLLTDR*LNTtffdptGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVAYYSNKKePFGYMGMVWAMLS 80
Cdd:pfam00115 174 PVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWL 246

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590  81 IGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATIHGGTIKW-ETPMLWALGFIFLFTVGGLTGIVL 159
Cdd:pfam00115 247 IAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrTTPMLFFLGFAFLFIIGGLTGVML 326

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590 160 ANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLTLHSTWVKIHFVVMFVGVNLTFFPQHFLGLAGMPR 239
Cdd:pfam00115 327 ALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPR 406

                         250       260
                  ....*....|....*....|....*.
gi 1194587590 240 RYS----DYPDAYTLWNSVSSIGSLI 261
Cdd:pfam00115 407 RYAppfiETVPAFQPLNWIRTIGGVL 432
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-269 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 545.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590   1 PVLAAGITMLLTDR*LNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVAYYSNKKEPFGYMGMVWAMLS 80
Cdd:MTH00153  198 PVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLA 277

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590  81 IGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATIHGGTIKWETPMLWALGFIFLFTVGGLTGIVLA 160
Cdd:MTH00153  278 IGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLA 357

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590 161 NSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLTLHSTWVKIHFVVMFVGVNLTFFPQHFLGLAGMPRR 240
Cdd:MTH00153  358 NSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRR 437

                         250       260
                  ....*....|....*....|....*....
gi 1194587590 241 YSDYPDAYTLWNSVSSIGSLISLVAVIMM 269
Cdd:MTH00153  438 YSDYPDAYTSWNVISSIGSTISLISILFF 466
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-269 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 536.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590   1 PVLAAGITMLLTDR*LNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVAYYSNKKEPFGYMGMVWAMLS 80
Cdd:MTH00116  200 PVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLS 279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590  81 IGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATIHGGTIKWETPMLWALGFIFLFTVGGLTGIVLA 160
Cdd:MTH00116  280 IGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLA 359

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590 161 NSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLTLHSTWVKIHFVVMFVGVNLTFFPQHFLGLAGMPRR 240
Cdd:MTH00116  360 NSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRR 439

                         250       260
                  ....*....|....*....|....*....
gi 1194587590 241 YSDYPDAYTLWNSVSSIGSLISLVAVIMM 269
Cdd:MTH00116  440 YSDYPDAYTLWNTISSIGSLISMTAVIML 468
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-269 0e+00

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: 533.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590   1 PVLAAGITMLLTDR*LNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVAYYSNKKEPFGYMGMVWAMLS 80
Cdd:cd01663   191 PVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLS 270

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590  81 IGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATIHGGTIKWETPMLWALGFIFLFTVGGLTGIVLA 160
Cdd:cd01663   271 IGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLA 350

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590 161 NSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLTLHSTWVKIHFVVMFVGVNLTFFPQHFLGLAGMPRR 240
Cdd:cd01663   351 NSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRR 430

                         250       260
                  ....*....|....*....|....*....
gi 1194587590 241 YSDYPDAYTLWNSVSSIGSLISLVAVIMM 269
Cdd:cd01663   431 YPDYPDAYAGWNMISSIGSLISFVSVLLF 459
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-268 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 519.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590   1 PVLAAGITMLLTDR*LNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVAYYSNKKEPFGYMGMVWAMLS 80
Cdd:MTH00167  200 PVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMA 279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590  81 IGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATIHGGTIKWETPMLWALGFIFLFTVGGLTGIVLA 160
Cdd:MTH00167  280 IGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLA 359

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590 161 NSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLTLHSTWVKIHFVVMFVGVNLTFFPQHFLGLAGMPRR 240
Cdd:MTH00167  360 NSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRR 439

                         250       260
                  ....*....|....*....|....*...
gi 1194587590 241 YSDYPDAYTLWNSVSSIGSLISLVAVIM 268
Cdd:MTH00167  440 YSDYPDAYTLWNVVSSIGSLISLVAVIL 467
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-269 3.06e-178

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 500.62  E-value: 3.06e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590   1 PVLAAGITMLLTDR*LNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVAYYSNKKEPFGYMGMVWAMLS 80
Cdd:MTH00077  200 PVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMS 279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590  81 IGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATIHGGTIKWETPMLWALGFIFLFTVGGLTGIVLA 160
Cdd:MTH00077  280 IGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLA 359

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590 161 NSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLTLHSTWVKIHFVVMFVGVNLTFFPQHFLGLAGMPRR 240
Cdd:MTH00077  360 NSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRR 439

                         250       260
                  ....*....|....*....|....*....
gi 1194587590 241 YSDYPDAYTLWNSVSSIGSLISLVAVIMM 269
Cdd:MTH00077  440 YSDYPDAYTLWNTVSSIGSLISLVAVIMM 468
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-268 6.82e-173

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 486.79  E-value: 6.82e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590   1 PVLAAGITMLLTDR*LNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVAYYSNKKEPFGYMGMVWAMLS 80
Cdd:MTH00223  197 PVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLS 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590  81 IGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATIHGGTIKWETPMLWALGFIFLFTVGGLTGIVLA 160
Cdd:MTH00223  277 IGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILS 356

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590 161 NSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLTLHSTWVKIHFVVMFVGVNLTFFPQHFLGLAGMPRR 240
Cdd:MTH00223  357 NSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRR 436

                         250       260
                  ....*....|....*....|....*...
gi 1194587590 241 YSDYPDAYTLWNSVSSIGSLISLVAVIM 268
Cdd:MTH00223  437 YSDYPDCYTKWNQVSSFGSMISFVSVLF 464
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-269 7.65e-172

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 484.43  E-value: 7.65e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590   1 PVLAAGITMLLTDR*LNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVAYYSNKKEPFGYMGMVWAMLS 80
Cdd:MTH00183  200 PVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMA 279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590  81 IGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATIHGGTIKWETPMLWALGFIFLFTVGGLTGIVLA 160
Cdd:MTH00183  280 IGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLA 359

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590 161 NSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLTLHSTWVKIHFVVMFVGVNLTFFPQHFLGLAGMPRR 240
Cdd:MTH00183  360 NSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRR 439

                         250       260
                  ....*....|....*....|....*....
gi 1194587590 241 YSDYPDAYTLWNSVSSIGSLISLVAVIMM 269
Cdd:MTH00183  440 YSDYPDAYTLWNTVSSIGSLISLVAVIMF 468
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-268 6.92e-170

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 479.22  E-value: 6.92e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590   1 PVLAAGITMLLTDR*LNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVAYYSNKKEPFGYMGMVWAMLS 80
Cdd:MTH00142  198 PVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLS 277

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590  81 IGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATIHGGTIKWETPMLWALGFIFLFTVGGLTGIVLA 160
Cdd:MTH00142  278 IGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLA 357

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590 161 NSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLTLHSTWVKIHFVVMFVGVNLTFFPQHFLGLAGMPRR 240
Cdd:MTH00142  358 NSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRR 437

                         250       260
                  ....*....|....*....|....*...
gi 1194587590 241 YSDYPDAYTLWNSVSSIGSLISLVAVIM 268
Cdd:MTH00142  438 YSDYPDAYTTWNVVSSLGSMISFIAVLM 465
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-269 3.60e-169

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 477.45  E-value: 3.60e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590   1 PVLAAGITMLLTDR*LNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVAYYSNKKEPFGYMGMVWAMLS 80
Cdd:MTH00103  200 PVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMS 279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590  81 IGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATIHGGTIKWETPMLWALGFIFLFTVGGLTGIVLA 160
Cdd:MTH00103  280 IGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLA 359

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590 161 NSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLTLHSTWVKIHFVVMFVGVNLTFFPQHFLGLAGMPRR 240
Cdd:MTH00103  360 NSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRR 439

                         250       260
                  ....*....|....*....|....*....
gi 1194587590 241 YSDYPDAYTLWNSVSSIGSLISLVAVIMM 269
Cdd:MTH00103  440 YSDYPDAYTTWNTVSSMGSFISLTAVMLM 468
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-267 5.37e-156

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 444.27  E-value: 5.37e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590   1 PVLAAGITMLLTDR*LNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVAYYSNKKEPFGYMGMVWAMLS 80
Cdd:MTH00037  200 PVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIA 279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590  81 IGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATIHGGTIKWETPMLWALGFIFLFTVGGLTGIVLA 160
Cdd:MTH00037  280 IGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLA 359

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590 161 NSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLTLHSTWVKIHFVVMFVGVNLTFFPQHFLGLAGMPRR 240
Cdd:MTH00037  360 NSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRR 439

                         250       260
                  ....*....|....*....|....*..
gi 1194587590 241 YSDYPDAYTLWNSVSSIGSLISLVAVI 267
Cdd:MTH00037  440 YSDYPDAYTLWNTVSSIGSTISLVATL 466
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-268 9.92e-153

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 435.87  E-value: 9.92e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590   1 PVLAAGITMLLTDR*LNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVAYYSNKKEPFGYMGMVWAMLS 80
Cdd:MTH00007  197 PVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLG 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590  81 IGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATIHGGTIKWETPMLWALGFIFLFTVGGLTGIVLA 160
Cdd:MTH00007  277 IGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLS 356

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590 161 NSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLTLHSTWVKIHFVVMFVGVNLTFFPQHFLGLAGMPRR 240
Cdd:MTH00007  357 NSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRR 436

                         250       260
                  ....*....|....*....|....*...
gi 1194587590 241 YSDYPDAYTLWNSVSSIGSLISLVAVIM 268
Cdd:MTH00007  437 YSDYPDAYTKWNVVSSFGSMLSFVALLL 464
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-267 3.94e-138

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 399.20  E-value: 3.94e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590   1 PVLAAGITMLLTDR*LNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVAYYSNKKEPFGYMGMVWAMLS 80
Cdd:MTH00182  202 PVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLS 281

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590  81 IGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATIHGGTIKWETPMLWALGFIFLFTVGGLTGIVLA 160
Cdd:MTH00182  282 IGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLA 361

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590 161 NSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLTLHSTWVKIHFVVMFVGVNLTFFPQHFLGLAGMPRR 240
Cdd:MTH00182  362 NSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRR 441

                         250       260
                  ....*....|....*....|....*..
gi 1194587590 241 YSDYPDAYTLWNSVSSIGSLISLVAVI 267
Cdd:MTH00182  442 YSDFADAFAGWNLVSSLGSIISIVGVV 468
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-269 5.39e-138

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 398.28  E-value: 5.39e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590   1 PVLAAGITMLLTDR*LNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVAYYSNKKEPFGYMGMVWAMLS 80
Cdd:MTH00079  200 PVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILS 279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590  81 IGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATIHGGTIKWETPMLWALGFIFLFTVGGLTGIVLA 160
Cdd:MTH00079  280 IGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILS 359

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590 161 NSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLTLHSTWVKIHFVVMFVGVNLTFFPQHFLGLAGMPRR 240
Cdd:MTH00079  360 NSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRK 439

                         250       260
                  ....*....|....*....|....*....
gi 1194587590 241 YSDYPDAYTLWNSVSSIGSLISLVAVIMM 269
Cdd:MTH00079  440 YLDYPDVYSVWNVISSYGSMISVFALFLF 468
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-267 1.72e-135

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 392.27  E-value: 1.72e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590   1 PVLAAGITMLLTDR*LNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVAYYSNKKEPFGYMGMVWAMLS 80
Cdd:MTH00184  202 PVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVS 281

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590  81 IGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATIHGGTIKWETPMLWALGFIFLFTVGGLTGIVLA 160
Cdd:MTH00184  282 IGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLA 361

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590 161 NSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLTLHSTWVKIHFVVMFVGVNLTFFPQHFLGLAGMPRR 240
Cdd:MTH00184  362 NSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRR 441

                         250       260
                  ....*....|....*....|....*..
gi 1194587590 241 YSDYPDAYTLWNSVSSIGSLISLVAVI 267
Cdd:MTH00184  442 YSDFHDSFAGWNQISSLGSVISIVGVV 468
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-269 3.22e-129

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: 374.17  E-value: 3.22e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590   1 PVLAAGITMLLTDR*LNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVAYYSNKKePFGYMGMVWAMLS 80
Cdd:cd00919   188 PVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFSGKP-LFGYKLMVYAFLA 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590  81 IGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATIHGGTIKWETPMLWALGFIFLFTVGGLTGIVLA 160
Cdd:cd00919   267 IGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDPPMLFALGFLFLFTIGGLTGVVLA 346

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590 161 NSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLTLHSTWVKIHFVVMFVGVNLTFFPQHFLGLAGMPRR 240
Cdd:cd00919   347 NVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIHFWLWFIGFNLTFFPMHFLGLLGMPRR 426

                         250       260
                  ....*....|....*....|....*....
gi 1194587590 241 YSDYPDAYTLWNSVSSIGSLISLVAVIMM 269
Cdd:cd00919   427 YADYPDGFAPWNFISSVGAFILGLGLLLF 455
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-269 1.23e-125

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 367.53  E-value: 1.23e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590   1 PVLAAGITMLLTDR*LNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVAYYSnKKEPFGYMGMVWAMLS 80
Cdd:COG0843   202 PVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFS-RKPLFGYKAMVLATVA 280

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590  81 IGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATIHGGTIKWETPMLWALGFIFLFTVGGLTGIVLA 160
Cdd:COG0843   281 IAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLA 360

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590 161 NSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLTLHSTWVKIHFVVMFVGVNLTFFPQHFLGLAGMPRR 240
Cdd:COG0843   361 SVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRR 440

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1194587590 241 YSDYP--DAYTLWNSVSSIGSLISLVAVIMM 269
Cdd:COG0843   441 YATYPpePGWQPLNLISTIGAFILAVGFLLF 471
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-269 1.68e-121

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: 355.76  E-value: 1.68e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590   1 PVLAAGITMLLTDR*LNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVAYYSnKKEPFGYMGMVWAMLS 80
Cdd:TIGR02891 193 PVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFA-RKPIFGYRAMVYATVA 271

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590  81 IGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATIHGGTIKWETPMLWALGFIFLFTVGGLTGIVLA 160
Cdd:TIGR02891 272 IGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLA 351

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590 161 NSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLTLHSTWVKIHFVVMFVGVNLTFFPQHFLGLAGMPRR 240
Cdd:TIGR02891 352 SVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRR 431

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1194587590 241 YSDYPDA--YTLWNSVSSIGSLISLVAVIMM 269
Cdd:TIGR02891 432 YYTYPPQmgFATLNLISTIGAFILAAGFLVF 462
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-267 1.24e-116

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 344.69  E-value: 1.24e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590   1 PVLAAGITMLLTDR*LNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVAYYSNKKEPFGYMGMVWAMLS 80
Cdd:MTH00026  201 PVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLA 280

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590  81 IGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATIHGG--TIKWETPMLWALGFIFLFTVGGLTGIV 158
Cdd:MTH00026  281 IGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSgrNLIFTTPMAWALGFIFLFTIGGLTGIV 360

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590 159 LANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLTLHSTWVKIHFVVMFVGVNLTFFPQHFLGLAGMP 238
Cdd:MTH00026  361 LSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLP 440

                         250       260
                  ....*....|....*....|....*....
gi 1194587590 239 RRYSDYPDAYTLWNSVSSIGSLISLVAVI 267
Cdd:MTH00026  441 RRYADYPDNFEDFNQISSFGSIISIIAVI 469
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-268 1.01e-113

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: 336.09  E-value: 1.01e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590   1 PVLAAGITMLLTDR*LNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVAYYSnKKEPFGYMGMVWAMLS 80
Cdd:cd01662   194 PVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFS-RKPLFGYRSMVYATVA 272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590  81 IGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATIHGGTIKWETPMLWALGFIFLFTVGGLTGIVLA 160
Cdd:cd01662   273 IGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLA 352

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590 161 NSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLTLHSTWVKIHFVVMFVGVNLTFFPQHFLGLAGMPRR 240
Cdd:cd01662   353 SPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRR 432

                         250       260       270
                  ....*....|....*....|....*....|
gi 1194587590 241 YSDYP--DAYTLWNSVSSIGSLISLVAVIM 268
Cdd:cd01662   433 VYTYLpgPGWDPLNLISTIGAFLIAAGVLL 462
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-265 2.86e-109

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 325.09  E-value: 2.86e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590   1 PVLAAGITMLLTDR*LNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVAYYSNKKEPFGYMGMVWAMLS 80
Cdd:MTH00048  198 PVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFS 277

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590  81 IGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATIHGGTIKWETPML-WALGFIFLFTVGGLTGIVL 159
Cdd:MTH00048  278 IVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKSDPVVwWVVSFIVLFTIGGVTGIVL 357

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590 160 ANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLTLHSTWVKIHFVVMFVGVNLTFFPQHFLGLAGMPR 239
Cdd:MTH00048  358 SASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPR 437

                         250       260
                  ....*....|....*....|....*.
gi 1194587590 240 RYSDYPDAYTLWNSVSSIGSLISLVA 265
Cdd:MTH00048  438 RVCVYEPSYYWINVVCTVGSFISAFS 463
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-261 6.20e-84

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: 257.50  E-value: 6.20e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590   1 PVLAAGITMLLTDR*LNTtffdptGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVAYYSNKKePFGYMGMVWAMLS 80
Cdd:pfam00115 174 PVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWL 246

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590  81 IGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATIHGGTIKW-ETPMLWALGFIFLFTVGGLTGIVL 159
Cdd:pfam00115 247 IAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrTTPMLFFLGFAFLFIIGGLTGVML 326

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590 160 ANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLTLHSTWVKIHFVVMFVGVNLTFFPQHFLGLAGMPR 239
Cdd:pfam00115 327 ALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPR 406

                         250       260
                  ....*....|....*....|....*.
gi 1194587590 240 RYS----DYPDAYTLWNSVSSIGSLI 261
Cdd:pfam00115 407 RYAppfiETVPAFQPLNWIRTIGGVL 432
CyoB TIGR02843
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ...
 1-261 1.88e-78

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: 249.20  E-value: 1.88e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590   1 PVLAAGITMLLTDR*LNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVAYYSnKKEPFGYMGMVWAMLS 80
Cdd:TIGR02843 243 PILTVTLALLTLDRYLGMHFFTNEAGGNPMMYVNLIWAWGHPEVYILILPAFGIFSEVVATFS-RKRLFGYTSMVWATIA 321

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590  81 IGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATIHGGTIKWETPMLWALGFIFLFTVGGLTGIVLA 160
Cdd:TIGR02843 322 ITVLSFIVWLHHFFTMGAGANVNAFFGIATMIIAIPTGVKIFNWLFTMYKGRIRFETPMLWTIGFMVTFSIGGMTGVLLA 401

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590 161 NSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLTLHSTWVKIHFVVMFVGVNLTFFPQHFLGLAGMPRR 240
Cdd:TIGR02843 402 VPPADFVLHNSLFLIAHFHNVIIGGVVFGCFAGLTYWFPKAFGFKLNEKLGKRSFWCWFIGFYLAFMPLYILGFMGMTRR 481

                         250       260
                  ....*....|....*....|..
gi 1194587590 241 YSDYPD-AYTLWNSVSSIGSLI 261
Cdd:TIGR02843 482 LNHYDNpEWHPMLIIAAFGAFL 503
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 1-246 3.20e-66

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 217.50  E-value: 3.20e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590   1 PVLAAGITMLLTDR*LNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVAYYSnKKEPFGYMGMVWAMLS 80
Cdd:PRK15017  244 PILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVC 322

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590  81 IGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATIHGGTIKWETPMLWALGFIFLFTVGGLTGIVLA 160
Cdd:PRK15017  323 ITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLA 402

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590 161 NSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLTLHSTWVKIHFVVMFVGVNLTFFPQHFLGLAGMPRR 240
Cdd:PRK15017  403 VPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRR 482


                  ....*.
gi 1194587590 241 YSDYPD 246
Cdd:PRK15017  483 LSQQID 488
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 28-269 3.55e-17

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: 80.79  E-value: 3.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590  28 DPILYQHLFWFFGHPEVYILILPGFGIISHIVAYYSNKKEPFGYMGMVWAMLSIgLLGFIVWAHHMFtTDLNVDTRAYF- 106
Cdd:cd01660   200 DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKLFSDPLARLAFILFL-LFSTPVGFHHQF-ADPGIGPGWKFi 277

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590 107 -TSATMIIAIPTGVKVFSWLATI-HGGTIK-------------WETPMLWALGF-IFLFTVGGLTGIVLANSSIDIVLHD 170
Cdd:cd01660   278 hMVLTFMVALPSLLTAFTVFASLeIAGRLRggkglfgwiralpWGDPMFLALFLaMLMFIPGGAGGIINASYQLNYVVHN 357

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587590 171 TYYVVAHFHyvLSMGAVFAIMA-GFVHWF-PLFTGLTLHSTWV-KIHFVVMFVGVNLTFFPQHFLGLAGMPRR--YSDYP 245
Cdd:cd01660   358 TAWVPGHFH--LTVGGAVALTFmAVAYWLvPHLTGRELAAKRLaLAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYG 435

                         250       260
                  ....*....|....*....|....*....
gi 1194587590 246 DAY-----TLWNSVSSIGSLISLVAVIMM 269
Cdd:cd01660   436 GLPaagewAPYQQLMAIGGTILFVSGALF 464
 
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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