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Conserved domains on  [gi|1194587596|gb|ARR97105|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Arthroleptides yakusini]

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 ...
 1-285 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: 541.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596   1 LFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAFYS 80
Cdd:MTH00153  181 LFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQES 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596  81 NKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGIINWEAPMLWAL 160
Cdd:MTH00153  261 GKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWAL 340

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596 161 GFIFLFTVGGLTGIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLFTGFTLHKSWTKIHFGVMFAGVN 240
Cdd:MTH00153  341 GFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVN 420

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1194587596 241 LTFFPQHFLGLAGMPRRYSDYPDAYTLWNTLSSIGSLISLAAVVM 285
Cdd:MTH00153  421 LTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILF 465
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-285 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 541.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596   1 LFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAFYS 80
Cdd:MTH00153  181 LFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQES 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596  81 NKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGIINWEAPMLWAL 160
Cdd:MTH00153  261 GKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWAL 340

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596 161 GFIFLFTVGGLTGIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLFTGFTLHKSWTKIHFGVMFAGVN 240
Cdd:MTH00153  341 GFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVN 420

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1194587596 241 LTFFPQHFLGLAGMPRRYSDYPDAYTLWNTLSSIGSLISLAAVVM 285
Cdd:MTH00153  421 LTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILF 465
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-285 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: 528.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596   1 LFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAFYS 80
Cdd:cd01663   174 LFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFS 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596  81 NKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGIINWEAPMLWAL 160
Cdd:cd01663   254 GKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWAL 333

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596 161 GFIFLFTVGGLTGIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLFTGFTLHKSWTKIHFGVMFAGVN 240
Cdd:cd01663   334 GFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVN 413

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1194587596 241 LTFFPQHFLGLAGMPRRYSDYPDAYTLWNTLSSIGSLISLAAVVM 285
Cdd:cd01663   414 LTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLL 458
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-285 3.10e-123

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 362.14  E-value: 3.10e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596   1 LFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAFYS 80
Cdd:COG0843   185 LFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFS 264

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596  81 nKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGIINWEAPMLWAL 160
Cdd:COG0843   265 -RKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFAL 343

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596 161 GFIFLFTVGGLTGIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLFTGFTLHKSWTKIHFGVMFAGVN 240
Cdd:COG0843   344 GFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFN 423

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1194587596 241 LTFFPQHFLGLAGMPRRYSDYP--DAYTLWNTLSSIGSLISLAAVVM 285
Cdd:COG0843   424 LTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLL 470
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-285 1.46e-120

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: 354.22  E-value: 1.46e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596   1 LFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAFYS 80
Cdd:TIGR02891 176 LFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFA 255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596  81 nKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGIINWEAPMLWAL 160
Cdd:TIGR02891 256 -RKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFAL 334

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596 161 GFIFLFTVGGLTGIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLFTGFTLHKSWTKIHFGVMFAGVN 240
Cdd:TIGR02891 335 GFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFN 414

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1194587596 241 LTFFPQHFLGLAGMPRRYSDYPDA--YTLWNTLSSIGSLISLAAVVM 285
Cdd:TIGR02891 415 LTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLV 461
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-278 6.98e-83

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: 255.58  E-value: 6.98e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596   1 LFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNttffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAFYS 80
Cdd:pfam00115 157 LFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFA 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596  81 NKKePFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGIINW-EAPMLWA 159
Cdd:pfam00115 231 GRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrTTPMLFF 309

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596 160 LGFIFLFTVGGLTGIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLFTGFTLHKSWTKIHFGVMFAGV 239
Cdd:pfam00115 310 LGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGF 389

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1194587596 240 NLTFFPQHFLGLAGMPRRYS----DYPDAYTLWNTLSSIGSLI 278
Cdd:pfam00115 390 NLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-285 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 541.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596   1 LFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAFYS 80
Cdd:MTH00153  181 LFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQES 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596  81 NKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGIINWEAPMLWAL 160
Cdd:MTH00153  261 GKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWAL 340

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596 161 GFIFLFTVGGLTGIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLFTGFTLHKSWTKIHFGVMFAGVN 240
Cdd:MTH00153  341 GFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVN 420

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1194587596 241 LTFFPQHFLGLAGMPRRYSDYPDAYTLWNTLSSIGSLISLAAVVM 285
Cdd:MTH00153  421 LTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILF 465
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-285 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 538.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596   1 LFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAFYS 80
Cdd:MTH00116  183 LFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYA 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596  81 NKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGIINWEAPMLWAL 160
Cdd:MTH00116  263 GKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWAL 342

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596 161 GFIFLFTVGGLTGIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLFTGFTLHKSWTKIHFGVMFAGVN 240
Cdd:MTH00116  343 GFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWTKAQFGVMFTGVN 422

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1194587596 241 LTFFPQHFLGLAGMPRRYSDYPDAYTLWNTLSSIGSLISLAAVVM 285
Cdd:MTH00116  423 LTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIM 467
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-285 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: 528.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596   1 LFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAFYS 80
Cdd:cd01663   174 LFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFS 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596  81 NKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGIINWEAPMLWAL 160
Cdd:cd01663   254 GKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWAL 333

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596 161 GFIFLFTVGGLTGIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLFTGFTLHKSWTKIHFGVMFAGVN 240
Cdd:cd01663   334 GFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVN 413

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1194587596 241 LTFFPQHFLGLAGMPRRYSDYPDAYTLWNTLSSIGSLISLAAVVM 285
Cdd:cd01663   414 LTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLL 458
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-285 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 518.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596   1 LFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAFYS 80
Cdd:MTH00167  183 LFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYS 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596  81 NKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGIINWEAPMLWAL 160
Cdd:MTH00167  263 GKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWETPMLWAL 342

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596 161 GFIFLFTVGGLTGIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLFTGFTLHKSWTKIHFGVMFAGVN 240
Cdd:MTH00167  343 GFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETWTKIHFFVMFIGVN 422

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1194587596 241 LTFFPQHFLGLAGMPRRYSDYPDAYTLWNTLSSIGSLISLAAVVM 285
Cdd:MTH00167  423 LTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVIL 467
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-285 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 509.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596   1 LFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAFYS 80
Cdd:MTH00077  183 LFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYYS 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596  81 NKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGIINWEAPMLWAL 160
Cdd:MTH00077  263 AKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDAAMLWAL 342

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596 161 GFIFLFTVGGLTGIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLFTGFTLHKSWTKIHFGVMFAGVN 240
Cdd:MTH00077  343 GFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWSKIHFGVMFIGVN 422

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1194587596 241 LTFFPQHFLGLAGMPRRYSDYPDAYTLWNTLSSIGSLISLAAVVM 285
Cdd:MTH00077  423 LTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIM 467
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-285 1.53e-172

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 487.12  E-value: 1.53e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596   1 LFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAFYS 80
Cdd:MTH00183  183 LFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYS 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596  81 NKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGIINWEAPMLWAL 160
Cdd:MTH00183  263 GKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWAL 342

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596 161 GFIFLFTVGGLTGIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLFTGFTLHKSWTKIHFGVMFAGVN 240
Cdd:MTH00183  343 GFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWTKIHFGVMFVGVN 422

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1194587596 241 LTFFPQHFLGLAGMPRRYSDYPDAYTLWNTLSSIGSLISLAAVVM 285
Cdd:MTH00183  423 LTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIM 467
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-285 7.27e-172

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 484.87  E-value: 7.27e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596   1 LFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAFYS 80
Cdd:MTH00223  180 LFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYS 259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596  81 NKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGIINWEAPMLWAL 160
Cdd:MTH00223  260 SKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEAPMLWAL 339

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596 161 GFIFLFTVGGLTGIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLFTGFTLHKSWTKIHFGVMFAGVN 240
Cdd:MTH00223  340 GFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRRWAKAHFFLMFLGVN 419

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1194587596 241 LTFFPQHFLGLAGMPRRYSDYPDAYTLWNTLSSIGSLISLAAVVM 285
Cdd:MTH00223  420 LTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLF 464
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-285 1.37e-169

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 479.22  E-value: 1.37e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596   1 LFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAFYS 80
Cdd:MTH00142  181 LFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHYS 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596  81 NKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGIINWEAPMLWAL 160
Cdd:MTH00142  261 GKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEPPMLWAL 340

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596 161 GFIFLFTVGGLTGIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLFTGFTLHKSWTKIHFGVMFAGVN 240
Cdd:MTH00142  341 GFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWLKAHFYTMFIGVN 420

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1194587596 241 LTFFPQHFLGLAGMPRRYSDYPDAYTLWNTLSSIGSLISLAAVVM 285
Cdd:MTH00142  421 LTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLM 465
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-285 4.14e-168

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 475.53  E-value: 4.14e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596   1 LFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAFYS 80
Cdd:MTH00103  183 LFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYS 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596  81 NKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGIINWEAPMLWAL 160
Cdd:MTH00103  263 GKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWAL 342

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596 161 GFIFLFTVGGLTGIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLFTGFTLHKSWTKIHFGVMFAGVN 240
Cdd:MTH00103  343 GFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHFTIMFVGVN 422

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1194587596 241 LTFFPQHFLGLAGMPRRYSDYPDAYTLWNTLSSIGSLISLAAVVM 285
Cdd:MTH00103  423 MTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVML 467
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-284 6.32e-155

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 442.35  E-value: 6.32e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596   1 LFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAFYS 80
Cdd:MTH00037  183 LFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYS 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596  81 NKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGIINWEAPMLWAL 160
Cdd:MTH00037  263 GKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWETPLLWAL 342

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596 161 GFIFLFTVGGLTGIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLFTGFTLHKSWTKIHFGVMFAGVN 240
Cdd:MTH00037  343 GFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLWSKVHFFLMFIGVN 422

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1194587596 241 LTFFPQHFLGLAGMPRRYSDYPDAYTLWNTLSSIGSLISLAAVV 284
Cdd:MTH00037  423 LTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATL 466
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-285 4.08e-150

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 429.71  E-value: 4.08e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596   1 LFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAFYS 80
Cdd:MTH00007  180 LFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYA 259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596  81 NKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGIINWEAPMLWAL 160
Cdd:MTH00007  260 GKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYETPMLWAL 339

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596 161 GFIFLFTVGGLTGIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLFTGFTLHKSWTKIHFGVMFAGVN 240
Cdd:MTH00007  340 GFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRWAKAHFFLMFLGVN 419

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1194587596 241 LTFFPQHFLGLAGMPRRYSDYPDAYTLWNTLSSIGSLISLAAVVM 285
Cdd:MTH00007  420 LTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLL 464
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-284 6.39e-138

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 399.20  E-value: 6.39e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596   1 LFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAFYS 80
Cdd:MTH00182  185 LFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFV 264

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596  81 NKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGIINWEAPMLWAL 160
Cdd:MTH00182  265 AKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDTPMLWAM 344

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596 161 GFIFLFTVGGLTGIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLFTGFTLHKSWTKIHFGVMFAGVN 240
Cdd:MTH00182  345 GFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNELYGKIHFWLMFIGVN 424

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1194587596 241 LTFFPQHFLGLAGMPRRYSDYPDAYTLWNTLSSIGSLISLAAVV 284
Cdd:MTH00182  425 LTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVV 468
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-285 2.46e-137

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 397.13  E-value: 2.46e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596   1 LFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAFYS 80
Cdd:MTH00079  183 LFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLT 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596  81 NKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGIINWEAPMLWAL 160
Cdd:MTH00079  263 GKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPLLLWVL 342

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596 161 GFIFLFTVGGLTGIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLFTGFTLHKSWTKIHFGVMFAGVN 240
Cdd:MTH00079  343 GFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMMSAVFFLMFVGVN 422

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1194587596 241 LTFFPQHFLGLAGMPRRYSDYPDAYTLWNTLSSIGSLISLAAVVM 285
Cdd:MTH00079  423 LTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFL 467
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-284 7.00e-136

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 393.81  E-value: 7.00e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596   1 LFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAFYS 80
Cdd:MTH00184  185 LFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFA 264

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596  81 NKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGIINWEAPMLWAL 160
Cdd:MTH00184  265 AKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDTPMLWAI 344

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596 161 GFIFLFTVGGLTGIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLFTGFTLHKSWTKIHFGVMFAGVN 240
Cdd:MTH00184  345 GFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEVYGKIHFWLMFIGVN 424

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1194587596 241 LTFFPQHFLGLAGMPRRYSDYPDAYTLWNTLSSIGSLISLAAVV 284
Cdd:MTH00184  425 LTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVV 468
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-285 3.19e-127

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: 369.94  E-value: 3.19e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596   1 LFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAFYS 80
Cdd:cd00919   171 LFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFS 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596  81 NKKePFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGIINWEAPMLWAL 160
Cdd:cd00919   251 GKP-LFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDPPMLFAL 329

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596 161 GFIFLFTVGGLTGIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLFTGFTLHKSWTKIHFGVMFAGVN 240
Cdd:cd00919   330 GFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIHFWLWFIGFN 409

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1194587596 241 LTFFPQHFLGLAGMPRRYSDYPDAYTLWNTLSSIGSLISLAAVVM 285
Cdd:cd00919   410 LTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLL 454
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-285 3.10e-123

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 362.14  E-value: 3.10e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596   1 LFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAFYS 80
Cdd:COG0843   185 LFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFS 264

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596  81 nKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGIINWEAPMLWAL 160
Cdd:COG0843   265 -RKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFAL 343

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596 161 GFIFLFTVGGLTGIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLFTGFTLHKSWTKIHFGVMFAGVN 240
Cdd:COG0843   344 GFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFN 423

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1194587596 241 LTFFPQHFLGLAGMPRRYSDYP--DAYTLWNTLSSIGSLISLAAVVM 285
Cdd:COG0843   424 LTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLL 470
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-285 1.46e-120

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: 354.22  E-value: 1.46e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596   1 LFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAFYS 80
Cdd:TIGR02891 176 LFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFA 255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596  81 nKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGIINWEAPMLWAL 160
Cdd:TIGR02891 256 -RKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFAL 334

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596 161 GFIFLFTVGGLTGIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLFTGFTLHKSWTKIHFGVMFAGVN 240
Cdd:TIGR02891 335 GFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFN 414

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1194587596 241 LTFFPQHFLGLAGMPRRYSDYPDA--YTLWNTLSSIGSLISLAAVVM 285
Cdd:TIGR02891 415 LTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLV 461
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-284 6.31e-118

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 348.54  E-value: 6.31e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596   1 LFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAFYS 80
Cdd:MTH00026  184 LFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLFS 263

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596  81 NKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGIIN--WEAPMLW 158
Cdd:MTH00026  264 YKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSGRNliFTTPMAW 343

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596 159 ALGFIFLFTVGGLTGIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLFTGFTLHKSWTKIHFGVMFAG 238
Cdd:MTH00026  344 ALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDIYGLIHFWLMFIG 423

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1194587596 239 VNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTLSSIGSLISLAAVV 284
Cdd:MTH00026  424 VNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVI 469
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-285 1.17e-112

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: 334.16  E-value: 1.17e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596   1 LFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAFYS 80
Cdd:cd01662   177 IFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFS 256

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596  81 nKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGIINWEAPMLWAL 160
Cdd:cd01662   257 -RKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLWAI 335

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596 161 GFIFLFTVGGLTGIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLFTGFTLHKSWTKIHFGVMFAGVN 240
Cdd:cd01662   336 GFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERLGKWSFWLWFIGFN 415

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1194587596 241 LTFFPQHFLGLAGMPRRYSDYP--DAYTLWNTLSSIGSLISLAAVVM 285
Cdd:cd01662   416 LTFFPMHILGLMGMPRRVYTYLpgPGWDPLNLISTIGAFLIAAGVLL 462
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 3-279 1.39e-106

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 318.93  E-value: 1.39e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596   3 VWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAFYSNK 82
Cdd:MTH00048  183 LWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSLSNN 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596  83 KEPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGIINWEAPML-WALG 161
Cdd:MTH00048  263 DDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKSDPVVwWVVS 342

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596 162 FIFLFTVGGLTGIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLFTGFTLHKSWTKIHFGVMFAGVNL 241
Cdd:MTH00048  343 FIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQCHCIISMIGFNL 422

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1194587596 242 TFFPQHFLGLAGMPRRYSDYPDAYTLWNTLSSIGSLIS 279
Cdd:MTH00048  423 CFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFIS 460
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-278 6.98e-83

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: 255.58  E-value: 6.98e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596   1 LFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNttffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAFYS 80
Cdd:pfam00115 157 LFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFA 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596  81 NKKePFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGIINW-EAPMLWA 159
Cdd:pfam00115 231 GRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrTTPMLFF 309

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596 160 LGFIFLFTVGGLTGIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLFTGFTLHKSWTKIHFGVMFAGV 239
Cdd:pfam00115 310 LGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGF 389

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1194587596 240 NLTFFPQHFLGLAGMPRRYS----DYPDAYTLWNTLSSIGSLI 278
Cdd:pfam00115 390 NLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
CyoB TIGR02843
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ...
 1-284 2.95e-77

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: 246.89  E-value: 2.95e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596   1 LFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAFYS 80
Cdd:TIGR02843 226 VFTWTSLCSNVLIIASFPILTVTLALLTLDRYLGMHFFTNEAGGNPMMYVNLIWAWGHPEVYILILPAFGIFSEVVATFS 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596  81 nKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGIINWEAPMLWAL 160
Cdd:TIGR02843 306 -RKRLFGYTSMVWATIAITVLSFIVWLHHFFTMGAGANVNAFFGIATMIIAIPTGVKIFNWLFTMYKGRIRFETPMLWTI 384

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596 161 GFIFLFTVGGLTGIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLFTGFTLHKSWTKIHFGVMFAGVN 240
Cdd:TIGR02843 385 GFMVTFSIGGMTGVLLAVPPADFVLHNSLFLIAHFHNVIIGGVVFGCFAGLTYWFPKAFGFKLNEKLGKRSFWCWFIGFY 464

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1194587596 241 LTFFPQHFLGLAGMPRRYSDYPD-AYTLWNTLSSIGSLISLAAVV 284
Cdd:TIGR02843 465 LAFMPLYILGFMGMTRRLNHYDNpEWHPMLIIAAFGAFLIACGIL 509
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 1-263 2.55e-65

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 215.96  E-value: 2.55e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596   1 LFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAFYS 80
Cdd:PRK15017  227 VFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFS 306

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596  81 nKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGIINWEAPMLWAL 160
Cdd:PRK15017  307 -RKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTI 385

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596 161 GFIFLFTVGGLTGIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLFTGFTLHKSWTKIHFGVMFAGVN 240
Cdd:PRK15017  386 GFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFF 465

                         250       260
                  ....*....|....*....|...
gi 1194587596 241 LTFFPQHFLGLAGMPRRYSDYPD 263
Cdd:PRK15017  466 VAFMPLYALGFMGMTRRLSQQID 488
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 45-285 2.67e-14

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: 72.32  E-value: 2.67e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596  45 DPILYQHLFWFFGHPEVYILILPGFGIISHVVAFYSNKKEPFGYMGMVWAMLSIgLLGFIVWAHHMFTtDLNVDTRAYF- 123
Cdd:cd01660   200 DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKLFSDPLARLAFILFL-LFSTPVGFHHQFA-DPGIGPGWKFi 277

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596 124 -TSATMIIAIPTGVKVFSWLATM--------HGGIINWEAPMLW--------ALGFIFlFTVGGLTGIVLANSSIDIVLH 186
Cdd:cd01660   278 hMVLTFMVALPSLLTAFTVFASLeiagrlrgGKGLFGWIRALPWgdpmflalFLAMLM-FIPGGAGGIINASYQLNYVVH 356

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587596 187 DTYYVVAHFHyvLSMGAVFAIMA-GFIHWF-PLFTGFTL-HKSWTKIHFGVMFAGVNLTFFPQHFLGLAGMPRR--YSDY 261
Cdd:cd01660   357 NTAWVPGHFH--LTVGGAVALTFmAVAYWLvPHLTGRELaAKRLALAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQY 434

                         250       260
                  ....*....|....*....|....*....
gi 1194587596 262 PDAY-----TLWNTLSSIGSLISLAAVVM 285
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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