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Conserved domains on  [gi|254681554|gb|ACT78985|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Stenobothrus clavatus]

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 ...
 1-319 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: 673.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554   1 PLMIGAPDMAFPRMNNMSFWLLPPSLTLLIASSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGVSSILGAVN 80
Cdd:MTH00153  82 PLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAIN 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554  81 FITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 160
Cdd:MTH00153 162 FITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 241

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554 161 YILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 240
Cdd:MTH00153 242 YILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSW 321

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254681554 241 LATLYGTKFNFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTG 319
Cdd:MTH00153 322 LATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTG 400
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-319 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 673.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554   1 PLMIGAPDMAFPRMNNMSFWLLPPSLTLLIASSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGVSSILGAVN 80
Cdd:MTH00153  82 PLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAIN 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554  81 FITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 160
Cdd:MTH00153 162 FITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 241

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554 161 YILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 240
Cdd:MTH00153 242 YILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSW 321

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254681554 241 LATLYGTKFNFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTG 319
Cdd:MTH00153 322 LATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTG 400
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-319 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: 602.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554   1 PLMIGAPDMAFPRMNNMSFWLLPPSLTLLIASSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGVSSILGAVN 80
Cdd:cd01663   75 PLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAIN 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554  81 FITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 160
Cdd:cd01663  155 FITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEV 234

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554 161 YILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 240
Cdd:cd01663  235 YILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSW 314

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254681554 241 LATLYGTKFNFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTG 319
Cdd:cd01663  315 LATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITG 393
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-319 5.02e-140

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: 405.07  E-value: 5.02e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554    1 PLMIGAPDMAFPRMNNMSFWLLPPSLTLLIASSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGVSSILGAVN 80
Cdd:TIGR02891  77 PLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVN 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554   81 FITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 160
Cdd:TIGR02891 157 FIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEV 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554  161 YILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 240
Cdd:TIGR02891 237 YIIFLPAFGIISEILPTFARK-PIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNW 315

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254681554  241 LATLYGTKFNFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTG 319
Cdd:TIGR02891 316 IATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTG 394
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-319 2.26e-139

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 404.51  E-value: 2.26e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554   1 PLMIGAPDMAFPRMNNMSFWLLPPSLTLLIASSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGVSSILGAVN 80
Cdd:COG0843   86 PLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVN 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554  81 FITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 160
Cdd:COG0843  166 FIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEV 245

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554 161 YILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 240
Cdd:COG0843  246 YILILPAFGIVSEIIPTFSRK-PLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNW 324

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254681554 241 LATLYGTKFNFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTG 319
Cdd:COG0843  325 IATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTG 403
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-319 6.52e-94

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: 285.24  E-value: 6.52e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554    1 PLMIGAPDMAFPRMNNMSFWLLPPSLTLLIASSMvdsGAGTGWTVYPPLAGaiahggssVDLAIFSLHLAGVSSILGAVN 80
Cdd:pfam00115  70 PLMIGARDMAFPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAIN 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554   81 FITTAINMRSESMTLdQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLFWFFGHPEV 160
Cdd:pfam00115 139 FIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEV 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554  161 YILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 240
Cdd:pfam00115 212 YILILPAFGIIYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNW 290

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554  241 LATLYGTKFNFN-PPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTG 319
Cdd:pfam00115 291 LATLWGGWIRFRtTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTG 370
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-319 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 673.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554   1 PLMIGAPDMAFPRMNNMSFWLLPPSLTLLIASSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGVSSILGAVN 80
Cdd:MTH00153  82 PLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAIN 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554  81 FITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 160
Cdd:MTH00153 162 FITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 241

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554 161 YILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 240
Cdd:MTH00153 242 YILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSW 321

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254681554 241 LATLYGTKFNFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTG 319
Cdd:MTH00153 322 LATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTG 400
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-319 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: 602.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554   1 PLMIGAPDMAFPRMNNMSFWLLPPSLTLLIASSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGVSSILGAVN 80
Cdd:cd01663   75 PLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAIN 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554  81 FITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 160
Cdd:cd01663  155 FITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEV 234

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554 161 YILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 240
Cdd:cd01663  235 YILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSW 314

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254681554 241 LATLYGTKFNFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTG 319
Cdd:cd01663  315 LATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITG 393
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-319 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 571.27  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554   1 PLMIGAPDMAFPRMNNMSFWLLPPSLTLLIASSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGVSSILGAVN 80
Cdd:MTH00116  84 PLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAIN 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554  81 FITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 160
Cdd:MTH00116 164 FITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEV 243

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554 161 YILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 240
Cdd:MTH00116 244 YILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSW 323

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254681554 241 LATLYGTKFNFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTG 319
Cdd:MTH00116 324 LATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTG 402
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-319 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 570.08  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554   1 PLMIGAPDMAFPRMNNMSFWLLPPSLTLLIASSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGVSSILGAVN 80
Cdd:MTH00167  84 PLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSIN 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554  81 FITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 160
Cdd:MTH00167 164 FITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEV 243

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554 161 YILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 240
Cdd:MTH00167 244 YILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 323

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254681554 241 LATLYGTKFNFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTG 319
Cdd:MTH00167 324 LATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTG 402
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-319 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 566.91  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554   1 PLMIGAPDMAFPRMNNMSFWLLPPSLTLLIASSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGVSSILGAVN 80
Cdd:MTH00223  81 PLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAIN 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554  81 FITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 160
Cdd:MTH00223 161 FITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEV 240

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554 161 YILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 240
Cdd:MTH00223 241 YILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSW 320

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254681554 241 LATLYGTKFNFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTG 319
Cdd:MTH00223 321 LATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTG 399
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-319 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 555.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554   1 PLMIGAPDMAFPRMNNMSFWLLPPSLTLLIASSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGVSSILGAVN 80
Cdd:MTH00142  82 PLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAIN 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554  81 FITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 160
Cdd:MTH00142 162 FITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEV 241

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554 161 YILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 240
Cdd:MTH00142 242 YILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSW 321

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254681554 241 LATLYGTKFNFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTG 319
Cdd:MTH00142 322 LATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTG 400
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-319 0e+00

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 510.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554   1 PLMIGAPDMAFPRMNNMSFWLLPPSLTLLIASSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGVSSILGAVN 80
Cdd:MTH00103  84 PLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAIN 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554  81 FITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 160
Cdd:MTH00103 164 FITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEV 243

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554 161 YILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 240
Cdd:MTH00103 244 YILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSW 323

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254681554 241 LATLYGTKFNFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTG 319
Cdd:MTH00103 324 LATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSG 402
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-319 1.36e-178

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 503.67  E-value: 1.36e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554   1 PLMIGAPDMAFPRMNNMSFWLLPPSLTLLIASSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGVSSILGAVN 80
Cdd:MTH00007  81 PLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAIN 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554  81 FITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 160
Cdd:MTH00007 161 FITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 240

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554 161 YILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 240
Cdd:MTH00007 241 YILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSW 320

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254681554 241 LATLYGTKFNFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTG 319
Cdd:MTH00007 321 LATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTG 399
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-319 5.22e-178

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 502.53  E-value: 5.22e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554   1 PLMIGAPDMAFPRMNNMSFWLLPPSLTLLIASSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGVSSILGAVN 80
Cdd:MTH00183  84 PLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAIN 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554  81 FITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 160
Cdd:MTH00183 164 FITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEV 243

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554 161 YILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 240
Cdd:MTH00183 244 YILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSW 323

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254681554 241 LATLYGTKFNFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTG 319
Cdd:MTH00183 324 LATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSG 402
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-319 6.54e-178

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 502.16  E-value: 6.54e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554   1 PLMIGAPDMAFPRMNNMSFWLLPPSLTLLIASSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGVSSILGAVN 80
Cdd:MTH00077  84 PLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAIN 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554  81 FITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 160
Cdd:MTH00077 164 FITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEV 243

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554 161 YILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 240
Cdd:MTH00077 244 YILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSW 323

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254681554 241 LATLYGTKFNFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTG 319
Cdd:MTH00077 324 LATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSG 402
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-319 4.39e-177

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 500.13  E-value: 4.39e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554   1 PLMIGAPDMAFPRMNNMSFWLLPPSLTLLIASSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGVSSILGAVN 80
Cdd:MTH00037  84 PLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASIN 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554  81 FITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 160
Cdd:MTH00037 164 FITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEV 243

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554 161 YILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 240
Cdd:MTH00037 244 YILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSW 323

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254681554 241 LATLYGTKFNFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTG 319
Cdd:MTH00037 324 MATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSG 402
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-319 6.62e-171

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 483.80  E-value: 6.62e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554   1 PLMIGAPDMAFPRMNNMSFWLLPPSLTLLIASSMVDSGAGTGWTVYPPLAgAIAHGGSSVDLAIFSLHLAGVSSILGAVN 80
Cdd:MTH00079  85 PLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLS-TLGHPGSSVDLAIFSLHCAGISSILGGIN 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554  81 FITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 160
Cdd:MTH00079 164 FMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEV 243

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554 161 YILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 240
Cdd:MTH00079 244 YILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSW 323

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254681554 241 LATLYGTKFNFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTG 319
Cdd:MTH00079 324 LATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTG 402
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-319 4.80e-166

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 472.38  E-value: 4.80e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554   1 PLMIGAPDMAFPRMNNMSFWLLPPSLTLLIASSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGVSSILGAVN 80
Cdd:MTH00182  86 PLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAIN 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554  81 FITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 160
Cdd:MTH00182 166 FITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEV 245

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554 161 YILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 240
Cdd:MTH00182 246 YILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSW 325

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254681554 241 LATLYGTKFNFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTG 319
Cdd:MTH00182 326 LATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITG 404
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-319 3.11e-162

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 462.37  E-value: 3.11e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554   1 PLMIGAPDMAFPRMNNMSFWLLPPSLTLLIASSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGVSSILGAVN 80
Cdd:MTH00184  86 PLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMN 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554  81 FITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 160
Cdd:MTH00184 166 FITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEV 245

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554 161 YILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 240
Cdd:MTH00184 246 YILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSW 325

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254681554 241 LATLYGTKFNFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTG 319
Cdd:MTH00184 326 IATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITG 404
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-319 8.87e-147

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 423.66  E-value: 8.87e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554   1 PLMIGAPDMAFPRMNNMSFWLLPPSLTLLIASSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGVSSILGAVN 80
Cdd:MTH00026  85 PLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMN 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554  81 FITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 160
Cdd:MTH00026 165 FITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEV 244

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554 161 YILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 240
Cdd:MTH00026 245 YILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSW 324

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554 241 LATLYGTKFN--FNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFT 318
Cdd:MTH00026 325 LATVSGSGRNliFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKIT 404


                 .
gi 254681554 319 G 319
Cdd:MTH00026 405 G 405
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-319 2.81e-146

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: 419.63  E-value: 2.81e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554   1 PLMIGAPDMAFPRMNNMSFWLLPPSLTLLIASSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGVSSILGAVN 80
Cdd:cd00919   72 PPLIGARDLAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAIN 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554  81 FITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 160
Cdd:cd00919  152 FITTILNMRAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEV 231

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554 161 YILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 240
Cdd:cd00919  232 YILILPAFGAISEIIPTFSGK-PLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNW 310

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254681554 241 LATLYGTKFNFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTG 319
Cdd:cd00919  311 LATLWGGRIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTG 389
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-319 5.02e-140

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: 405.07  E-value: 5.02e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554    1 PLMIGAPDMAFPRMNNMSFWLLPPSLTLLIASSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGVSSILGAVN 80
Cdd:TIGR02891  77 PLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVN 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554   81 FITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 160
Cdd:TIGR02891 157 FIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEV 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554  161 YILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 240
Cdd:TIGR02891 237 YIIFLPAFGIISEILPTFARK-PIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNW 315

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254681554  241 LATLYGTKFNFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTG 319
Cdd:TIGR02891 316 IATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTG 394
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-319 2.26e-139

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 404.51  E-value: 2.26e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554   1 PLMIGAPDMAFPRMNNMSFWLLPPSLTLLIASSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGVSSILGAVN 80
Cdd:COG0843   86 PLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVN 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554  81 FITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 160
Cdd:COG0843  166 FIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEV 245

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554 161 YILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 240
Cdd:COG0843  246 YILILPAFGIVSEIIPTFSRK-PLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNW 324

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254681554 241 LATLYGTKFNFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTG 319
Cdd:COG0843  325 IATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTG 403
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-319 9.68e-124

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 364.00  E-value: 9.68e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554   1 PLMIGAPDMAFPRMNNMSFWLLPPSLTLLIASSMVdsGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGVSSILGAVN 80
Cdd:MTH00048  85 PLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSIN 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554  81 FITTAINMRSESMTLdQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 160
Cdd:MTH00048 163 FICTIYSAFMTNVFS-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEV 241

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554 161 YILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 240
Cdd:MTH00048 242 YVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSW 321

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554 241 LATLYGTKFNFNPPLL-WALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTG 319
Cdd:MTH00048 322 LYMLLNSRVRKSDPVVwWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITG 401
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-319 6.61e-121

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: 356.51  E-value: 6.61e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554   1 PLMIGAPDMAFPRMNNMSFWLLPPSLTLLIASSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGVSSILGAVN 80
Cdd:cd01662   78 PLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAIN 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554  81 FITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 160
Cdd:cd01662  158 FIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEV 237

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554 161 YILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 240
Cdd:cd01662  238 YILILPAFGIFSEIVPTFSRK-PLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNW 316

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254681554 241 LATLYGTKFNFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTG 319
Cdd:cd01662  317 LFTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFG 395
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-319 6.52e-94

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: 285.24  E-value: 6.52e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554    1 PLMIGAPDMAFPRMNNMSFWLLPPSLTLLIASSMvdsGAGTGWTVYPPLAGaiahggssVDLAIFSLHLAGVSSILGAVN 80
Cdd:pfam00115  70 PLMIGARDMAFPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAIN 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554   81 FITTAINMRSESMTLdQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLFWFFGHPEV 160
Cdd:pfam00115 139 FIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEV 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554  161 YILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 240
Cdd:pfam00115 212 YILILPAFGIIYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNW 290

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554  241 LATLYGTKFNFN-PPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTG 319
Cdd:pfam00115 291 LATLWGGWIRFRtTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTG 370
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 1-319 5.97e-80

cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]


Pssm-ID: 131928  Cd Length: 643  Bit Score: 255.16  E-value: 5.97e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554    1 PLMIGAPDMAFPRMNNMSFWLLPPSLTLLIASSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGVSSILGAVN 80
Cdd:TIGR02882 121 PLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGIN 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554   81 FITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 160
Cdd:TIGR02882 201 FFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEV 280

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554  161 YILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 240
Cdd:TIGR02882 281 YIVILPAFGIYSEIISTFAQK-RLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNW 359

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254681554  241 LATLYGTKFNFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTG 319
Cdd:TIGR02882 360 LLTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFG 438
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 1-315 4.86e-79

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 253.32  E-value: 4.86e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554   1 PLMIGAPDMAFPRMNNMSFWLLPPSLTLLIASSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGVSSILGAVN 80
Cdd:PRK15017 128 PLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGIN 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554  81 FITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 160
Cdd:PRK15017 208 FFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEV 287

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554 161 YILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 240
Cdd:PRK15017 288 YILILPVFGVFSEIAATFSRK-RLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNW 366

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254681554 241 LATLYGTKFNFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYP 315
Cdd:PRK15017 367 LFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWP 441
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 144-307 1.79e-08

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: 55.37  E-value: 1.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554 144 DPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIgLMGFIVWAHHMFT-VGMDVDTRAYF 222
Cdd:cd01660  200 DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKLFSDPLARLAFILFL-LFSTPVGFHHQFAdPGIGPGWKFIH 278

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681554 223 TSATMIIAVPTGIKVFSWLAT------------LYG--TKFNFNPPLLWALGF-IFLFTIGGLTGLVLANSSLDIVLHDT 287
Cdd:cd01660  279 MVLTFMVALPSLLTAFTVFASleiagrlrggkgLFGwiRALPWGDPMFLALFLaMLMFIPGGAGGIINASYQLNYVVHNT 358

                        170       180
                 ....*....|....*....|
gi 254681554 288 YYVVAHFHyvLSMGAVFAIM 307
Cdd:cd01660  359 AWVPGHFH--LTVGGAVALT 376
 
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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