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Conserved domains on  [gi|1194587614|gb|ARR97113|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Arthroleptis stenodactylus]

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 ...
 1-284 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: 544.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614   1 WSVLITAILLLLSLPVLAASITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVTFYSNKK 80
Cdd:MTH00153  184 WSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKK 263

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614  81 EPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGIIKWETPMLWALGFI 160
Cdd:MTH00153  264 ETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFV 343

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614 161 FLFTIGGLTGIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGFMLHKTWTKIHFTVMFVGVNITF 240
Cdd:MTH00153  344 FLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTF 423

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1194587614 241 FPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVVM*M 284
Cdd:MTH00153  424 FPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFI 467
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-284 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 544.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614   1 WSVLITAILLLLSLPVLAASITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVTFYSNKK 80
Cdd:MTH00153  184 WSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKK 263

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614  81 EPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGIIKWETPMLWALGFI 160
Cdd:MTH00153  264 ETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFV 343

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614 161 FLFTIGGLTGIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGFMLHKTWTKIHFTVMFVGVNITF 240
Cdd:MTH00153  344 FLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTF 423

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1194587614 241 FPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVVM*M 284
Cdd:MTH00153  424 FPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFI 467
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-284 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: 536.68  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614   1 WSVLITAILLLLSLPVLAASITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVTFYSNKK 80
Cdd:cd01663   177 WSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKK 256

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614  81 EPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGIIKWETPMLWALGFI 160
Cdd:cd01663   257 PVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFI 336

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614 161 FLFTIGGLTGIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGFMLHKTWTKIHFTVMFVGVNITF 240
Cdd:cd01663   337 FLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTF 416

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1194587614 241 FPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVVM*M 284
Cdd:cd01663   417 FPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFL 460
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-282 2.08e-126

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 370.23  E-value: 2.08e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614   1 WSVLITAILLLLSLPVLAASITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVTFYSnKK 80
Cdd:COG0843   188 WAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFS-RK 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614  81 EPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGIIKWETPMLWALGFI 160
Cdd:COG0843   267 PLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFI 346

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614 161 FLFTIGGLTGIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGFMLHKTWTKIHFTVMFVGVNITF 240
Cdd:COG0843   347 ILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTF 426

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1194587614 241 FPQHFLGLAGMPRRYSDYP--DAYTLWNTVSSIGSLISLVAVVM 282
Cdd:COG0843   427 FPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLL 470
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-282 4.56e-123

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: 360.39  E-value: 4.56e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614   1 WSVLITAILLLLSLPVLAASITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVTFYSnKK 80
Cdd:TIGR02891 179 WGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFA-RK 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614  81 EPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGIIKWETPMLWALGFI 160
Cdd:TIGR02891 258 PIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFI 337

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614 161 FLFTIGGLTGIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGFMLHKTWTKIHFTVMFVGVNITF 240
Cdd:TIGR02891 338 FLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTF 417

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1194587614 241 FPQHFLGLAGMPRRYSDYPDA--YTLWNTVSSIGSLISLVAVVM 282
Cdd:TIGR02891 418 FPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLV 461
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-275 7.77e-85

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: 260.58  E-value: 7.77e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614   1 WSVLITAILLLLSLPVLAASITMLLTDRNLNttffdpAGGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVTFYSNKK 80
Cdd:pfam00115 160 WAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614  81 ePFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGIIKW-ETPMLWALGF 159
Cdd:pfam00115 234 -LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrTTPMLFFLGF 312

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614 160 IFLFTIGGLTGIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGFMLHKTWTKIHFTVMFVGVNIT 239
Cdd:pfam00115 313 AFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLT 392

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1194587614 240 FFPQHFLGLAGMPRRYS----DYPDAYTLWNTVSSIGSLI 275
Cdd:pfam00115 393 FFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-284 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 544.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614   1 WSVLITAILLLLSLPVLAASITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVTFYSNKK 80
Cdd:MTH00153  184 WSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKK 263

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614  81 EPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGIIKWETPMLWALGFI 160
Cdd:MTH00153  264 ETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFV 343

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614 161 FLFTIGGLTGIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGFMLHKTWTKIHFTVMFVGVNITF 240
Cdd:MTH00153  344 FLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTF 423

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1194587614 241 FPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVVM*M 284
Cdd:MTH00153  424 FPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFI 467
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-284 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 541.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614   1 WSVLITAILLLLSLPVLAASITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVTFYSNKK 80
Cdd:MTH00116  186 WSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAGKK 265

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614  81 EPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGIIKWETPMLWALGFI 160
Cdd:MTH00116  266 EPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFI 345

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614 161 FLFTIGGLTGIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGFMLHKTWTKIHFTVMFVGVNITF 240
Cdd:MTH00116  346 FLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWTKAQFGVMFTGVNLTF 425

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1194587614 241 FPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVVM*M 284
Cdd:MTH00116  426 FPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLM 469
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-284 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: 536.68  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614   1 WSVLITAILLLLSLPVLAASITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVTFYSNKK 80
Cdd:cd01663   177 WSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKK 256

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614  81 EPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGIIKWETPMLWALGFI 160
Cdd:cd01663   257 PVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFI 336

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614 161 FLFTIGGLTGIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGFMLHKTWTKIHFTVMFVGVNITF 240
Cdd:cd01663   337 FLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTF 416

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1194587614 241 FPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVVM*M 284
Cdd:cd01663   417 FPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFL 460
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-284 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 524.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614   1 WSVLITAILLLLSLPVLAASITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVTFYSNKK 80
Cdd:MTH00167  186 WSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSGKK 265

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614  81 EPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGIIKWETPMLWALGFI 160
Cdd:MTH00167  266 EPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWETPMLWALGFI 345

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614 161 FLFTIGGLTGIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGFMLHKTWTKIHFTVMFVGVNITF 240
Cdd:MTH00167  346 FLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETWTKIHFFVMFIGVNLTF 425

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1194587614 241 FPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVVM*M 284
Cdd:MTH00167  426 FPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFL 469
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-284 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 510.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614   1 WSVLITAILLLLSLPVLAASITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVTFYSNKK 80
Cdd:MTH00077  186 WSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYYSAKK 265

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614  81 EPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGIIKWETPMLWALGFI 160
Cdd:MTH00077  266 EPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDAAMLWALGFI 345

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614 161 FLFTIGGLTGIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGFMLHKTWTKIHFTVMFVGVNITF 240
Cdd:MTH00077  346 FLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWSKIHFGVMFIGVNLTF 425

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1194587614 241 FPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVVM*M 284
Cdd:MTH00077  426 FPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMM 469
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-284 2.91e-173

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 488.72  E-value: 2.91e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614   1 WSVLITAILLLLSLPVLAASITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVTFYSNKK 80
Cdd:MTH00223  183 WSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKK 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614  81 EPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGIIKWETPMLWALGFI 160
Cdd:MTH00223  263 EVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEAPMLWALGFI 342

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614 161 FLFTIGGLTGIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGFMLHKTWTKIHFTVMFVGVNITF 240
Cdd:MTH00223  343 FLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRRWAKAHFFLMFLGVNLTF 422

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1194587614 241 FPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVVM*M 284
Cdd:MTH00223  423 FPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFM 466
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-284 4.53e-172

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 485.58  E-value: 4.53e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614   1 WSVLITAILLLLSLPVLAASITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVTFYSNKK 80
Cdd:MTH00183  186 WAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSGKK 265

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614  81 EPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGIIKWETPMLWALGFI 160
Cdd:MTH00183  266 EPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFI 345

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614 161 FLFTIGGLTGIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGFMLHKTWTKIHFTVMFVGVNITF 240
Cdd:MTH00183  346 FLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWTKIHFGVMFVGVNLTF 425

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1194587614 241 FPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVVM*M 284
Cdd:MTH00183  426 FPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFL 469
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-284 8.60e-170

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 479.60  E-value: 8.60e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614   1 WSVLITAILLLLSLPVLAASITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVTFYSNKK 80
Cdd:MTH00142  184 WSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHYSGKK 263

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614  81 EPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGIIKWETPMLWALGFI 160
Cdd:MTH00142  264 EVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEPPMLWALGFI 343

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614 161 FLFTIGGLTGIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGFMLHKTWTKIHFTVMFVGVNITF 240
Cdd:MTH00142  344 FLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWLKAHFYTMFIGVNLTF 423

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1194587614 241 FPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVVM*M 284
Cdd:MTH00142  424 FPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFV 467
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-284 1.77e-169

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 478.99  E-value: 1.77e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614   1 WSVLITAILLLLSLPVLAASITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVTFYSNKK 80
Cdd:MTH00103  186 WSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKK 265

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614  81 EPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGIIKWETPMLWALGFI 160
Cdd:MTH00103  266 EPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFI 345

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614 161 FLFTIGGLTGIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGFMLHKTWTKIHFTVMFVGVNITF 240
Cdd:MTH00103  346 FLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHFTIMFVGVNMTF 425

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1194587614 241 FPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVVM*M 284
Cdd:MTH00103  426 FPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMI 469
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-284 2.25e-156

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 445.81  E-value: 2.25e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614   1 WSVLITAILLLLSLPVLAASITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVTFYSNKK 80
Cdd:MTH00037  186 WSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKQ 265

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614  81 EPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGIIKWETPMLWALGFI 160
Cdd:MTH00037  266 EPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWETPLLWALGFV 345

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614 161 FLFTIGGLTGIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGFMLHKTWTKIHFTVMFVGVNITF 240
Cdd:MTH00037  346 FLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLWSKVHFFLMFIGVNLTF 425

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1194587614 241 FPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVVM*M 284
Cdd:MTH00037  426 FPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFL 469
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-284 2.00e-152

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 435.87  E-value: 2.00e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614   1 WSVLITAILLLLSLPVLAASITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVTFYSNKK 80
Cdd:MTH00007  183 WAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGKL 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614  81 EPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGIIKWETPMLWALGFI 160
Cdd:MTH00007  263 EPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYETPMLWALGFI 342

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614 161 FLFTIGGLTGIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGFMLHKTWTKIHFTVMFVGVNITF 240
Cdd:MTH00007  343 FLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRWAKAHFFLMFLGVNLTF 422

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1194587614 241 FPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVVM*M 284
Cdd:MTH00007  423 FPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFI 466
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-281 6.49e-140

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 404.20  E-value: 6.49e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614   1 WSVLITAILLLLSLPVLAASITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVTFYSNKK 80
Cdd:MTH00182  188 WSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFVAKK 267

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614  81 EPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGIIKWETPMLWALGFI 160
Cdd:MTH00182  268 QIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDTPMLWAMGFV 347

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614 161 FLFTIGGLTGIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGFMLHKTWTKIHFTVMFVGVNITF 240
Cdd:MTH00182  348 FLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNELYGKIHFWLMFIGVNLTF 427

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1194587614 241 FPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVV 281
Cdd:MTH00182  428 FPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVV 468
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-282 1.80e-137

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 397.51  E-value: 1.80e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614   1 WSVLITAILLLLSLPVLAASITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVTFYSNKK 80
Cdd:MTH00079  186 WTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTGKK 265

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614  81 EPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGIIKWETPMLWALGFI 160
Cdd:MTH00079  266 EVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPLLLWVLGFI 345

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614 161 FLFTIGGLTGIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGFMLHKTWTKIHFTVMFVGVNITF 240
Cdd:MTH00079  346 FLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMMSAVFFLMFVGVNLTF 425

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1194587614 241 FPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVVM 282
Cdd:MTH00079  426 FPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFL 467
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-281 3.76e-137

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 397.27  E-value: 3.76e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614   1 WSVLITAILLLLSLPVLAASITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVTFYSNKK 80
Cdd:MTH00184  188 WSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKK 267

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614  81 EPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGIIKWETPMLWALGFI 160
Cdd:MTH00184  268 QIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDTPMLWAIGFV 347

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614 161 FLFTIGGLTGIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGFMLHKTWTKIHFTVMFVGVNITF 240
Cdd:MTH00184  348 FLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEVYGKIHFWLMFIGVNLTF 427

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1194587614 241 FPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVV 281
Cdd:MTH00184  428 FPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVV 468
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-282 2.36e-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: 375.33  E-value: 2.36e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614   1 WSVLITAILLLLSLPVLAASITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVTFYSNKK 80
Cdd:cd00919   174 WSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFSGKP 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614  81 ePFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGIIKWETPMLWALGFI 160
Cdd:cd00919   254 -LFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDPPMLFALGFL 332

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614 161 FLFTIGGLTGIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGFMLHKTWTKIHFTVMFVGVNITF 240
Cdd:cd00919   333 FLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIHFWLWFIGFNLTF 412

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1194587614 241 FPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVVM 282
Cdd:cd00919   413 FPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLL 454
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-282 2.08e-126

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 370.23  E-value: 2.08e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614   1 WSVLITAILLLLSLPVLAASITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVTFYSnKK 80
Cdd:COG0843   188 WAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFS-RK 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614  81 EPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGIIKWETPMLWALGFI 160
Cdd:COG0843   267 PLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFI 346

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614 161 FLFTIGGLTGIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGFMLHKTWTKIHFTVMFVGVNITF 240
Cdd:COG0843   347 ILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTF 426

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1194587614 241 FPQHFLGLAGMPRRYSDYP--DAYTLWNTVSSIGSLISLVAVVM 282
Cdd:COG0843   427 FPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLL 470
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-282 4.56e-123

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: 360.39  E-value: 4.56e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614   1 WSVLITAILLLLSLPVLAASITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVTFYSnKK 80
Cdd:TIGR02891 179 WGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFA-RK 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614  81 EPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGIIKWETPMLWALGFI 160
Cdd:TIGR02891 258 PIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFI 337

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614 161 FLFTIGGLTGIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGFMLHKTWTKIHFTVMFVGVNITF 240
Cdd:TIGR02891 338 FLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTF 417

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1194587614 241 FPQHFLGLAGMPRRYSDYPDA--YTLWNTVSSIGSLISLVAVVM 282
Cdd:TIGR02891 418 FPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLV 461
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-281 3.95e-120

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 354.32  E-value: 3.95e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614   1 WSVLITAILLLLSLPVLAASITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVTFYSNKK 80
Cdd:MTH00026  187 WSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLFSYKK 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614  81 EPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGG--IIKWETPMLWALG 158
Cdd:MTH00026  267 QIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSgrNLIFTTPMAWALG 346

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614 159 FIFLFTIGGLTGIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGFMLHKTWTKIHFTVMFVGVNI 238
Cdd:MTH00026  347 FIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDIYGLIHFWLMFIGVNI 426

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1194587614 239 TFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVV 281
Cdd:MTH00026  427 TFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVI 469
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-282 8.17e-114

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: 336.86  E-value: 8.17e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614   1 WSVLITAILLLLSLPVLAASITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVTFYSnKK 80
Cdd:cd01662   180 WTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFS-RK 258

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614  81 EPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGIIKWETPMLWALGFI 160
Cdd:cd01662   259 PLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLWAIGFL 338

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614 161 FLFTIGGLTGIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGFMLHKTWTKIHFTVMFVGVNITF 240
Cdd:cd01662   339 VTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERLGKWSFWLWFIGFNLTF 418

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1194587614 241 FPQHFLGLAGMPRRYSDYP--DAYTLWNTVSSIGSLISLVAVVM 282
Cdd:cd01662   419 FPMHILGLMGMPRRVYTYLpgPGWDPLNLISTIGAFLIAAGVLL 462
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-284 1.74e-108

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 323.55  E-value: 1.74e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614   1 WSVLITAILLLLSLPVLAASITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVTFYSNKK 80
Cdd:MTH00048  184 WSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSLSNND 263

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614  81 EPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHG-GIIKWETPMLWALGF 159
Cdd:MTH00048  264 DPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNsRVRKSDPVVWWVVSF 343

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614 160 IFLFTIGGLTGIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGFMLHKTWTKIHFTVMFVGVNIT 239
Cdd:MTH00048  344 IVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQCHCIISMIGFNLC 423

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1194587614 240 FFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVVM*M 284
Cdd:MTH00048  424 FFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFV 468
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-275 7.77e-85

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: 260.58  E-value: 7.77e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614   1 WSVLITAILLLLSLPVLAASITMLLTDRNLNttffdpAGGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVTFYSNKK 80
Cdd:pfam00115 160 WAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614  81 ePFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGIIKW-ETPMLWALGF 159
Cdd:pfam00115 234 -LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrTTPMLFFLGF 312

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614 160 IFLFTIGGLTGIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGFMLHKTWTKIHFTVMFVGVNIT 239
Cdd:pfam00115 313 AFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLT 392

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1194587614 240 FFPQHFLGLAGMPRRYS----DYPDAYTLWNTVSSIGSLI 275
Cdd:pfam00115 393 FFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
CyoB TIGR02843
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ...
 1-281 1.17e-79

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: 253.06  E-value: 1.17e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614   1 WSVLITAILLLLSLPVLAASITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVTFYSnKK 80
Cdd:TIGR02843 229 WTSLCSNVLIIASFPILTVTLALLTLDRYLGMHFFTNEAGGNPMMYVNLIWAWGHPEVYILILPAFGIFSEVVATFS-RK 307

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614  81 EPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGIIKWETPMLWALGFI 160
Cdd:TIGR02843 308 RLFGYTSMVWATIAITVLSFIVWLHHFFTMGAGANVNAFFGIATMIIAIPTGVKIFNWLFTMYKGRIRFETPMLWTIGFM 387

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614 161 FLFTIGGLTGIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGFMLHKTWTKIHFTVMFVGVNITF 240
Cdd:TIGR02843 388 VTFSIGGMTGVLLAVPPADFVLHNSLFLIAHFHNVIIGGVVFGCFAGLTYWFPKAFGFKLNEKLGKRSFWCWFIGFYLAF 467

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1194587614 241 FPQHFLGLAGMPRRYSDYPD-AYTLWNTVSSIGSLISLVAVV 281
Cdd:TIGR02843 468 MPLYILGFMGMTRRLNHYDNpEWHPMLIIAAFGAFLIACGIL 509
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 1-260 2.04e-65

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 215.96  E-value: 2.04e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614   1 WSVLITAILLLLSLPVLAASITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVTFYSnKK 80
Cdd:PRK15017  230 WASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFS-RK 308

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614  81 EPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGIIKWETPMLWALGFI 160
Cdd:PRK15017  309 RLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFI 388

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614 161 FLFTIGGLTGIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGFMLHKTWTKIHFTVMFVGVNITF 240
Cdd:PRK15017  389 VTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAF 468

                         250       260
                  ....*....|....*....|
gi 1194587614 241 FPQHFLGLAGMPRRYSDYPD 260
Cdd:PRK15017  469 MPLYALGFMGMTRRLSQQID 488
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 42-282 3.04e-16

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: 78.10  E-value: 3.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614  42 DPVLYQHLFWFFGHPEVYILILPGFGIISHVVTFYSNKKEPFGYMGMVWAMLSIgLLGFIVWAHHMFTtDLNVDTRAYF- 120
Cdd:cd01660   200 DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKLFSDPLARLAFILFL-LFSTPVGFHHQFA-DPGIGPGWKFi 277

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614 121 -TSATMIIAIPTGVKVFSWLATM--------HGGIIKWETPMLW--------ALGFIFlFTIGGLTGIVLANSSIDIVLH 183
Cdd:cd01660   278 hMVLTFMVALPSLLTAFTVFASLeiagrlrgGKGLFGWIRALPWgdpmflalFLAMLM-FIPGGAGGIINASYQLNYVVH 356

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587614 184 DTYYVVAHFHyvLSMGAVFAIMA-GFVHWF-PLFTGFML-HKTWTKIHFTVMFVGVNITFFPQHFLGLAGMPRR--YSDY 258
Cdd:cd01660   357 NTAWVPGHFH--LTVGGAVALTFmAVAYWLvPHLTGRELaAKRLALAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQY 434

                         250       260
                  ....*....|....*....|....*....
gi 1194587614 259 PDAY-----TLWNTVSSIGSLISLVAVVM 282
Cdd:cd01660   435 GGLPaagewAPYQQLMAIGGTILFVSGAL 463
 
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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