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Conserved domains on  [gi|254681564|gb|ACT78990|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Stenobothrus rubicundulus]

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 ...
 1-333 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: 684.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564   1 VMPIMIGGFGNWLVPLMIGAPD*AFPRMNNMSFWLLPPSLTLLIASSMMDSGAGT*WTIYPPLAGAIAHGGSSVDLAIFS 80
Cdd:MTH00153  68 VMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFS 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564  81 LHLAGVSSILGAVNFITTAINMRSESMTL*QTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRBLNTSFFDPAGGGDPI 160
Cdd:MTH00153 148 LHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPI 227

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564 161 LYQHLFWFFGHPEVYILILPGFGIISHIVYQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSAT 240
Cdd:MTH00153 228 LYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSAT 307

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564 241 MIIAVPTGIKVFSWLATLYGTKFNFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAI 320
Cdd:MTH00153 308 MIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAI 387

                        330
                 ....*....|...
gi 254681564 321 MGGIIQWYPLFTG 333
Cdd:MTH00153 388 MGGFIHWFPLFTG 400
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-333 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 684.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564   1 VMPIMIGGFGNWLVPLMIGAPD*AFPRMNNMSFWLLPPSLTLLIASSMMDSGAGT*WTIYPPLAGAIAHGGSSVDLAIFS 80
Cdd:MTH00153  68 VMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFS 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564  81 LHLAGVSSILGAVNFITTAINMRSESMTL*QTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRBLNTSFFDPAGGGDPI 160
Cdd:MTH00153 148 LHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPI 227

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564 161 LYQHLFWFFGHPEVYILILPGFGIISHIVYQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSAT 240
Cdd:MTH00153 228 LYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSAT 307

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564 241 MIIAVPTGIKVFSWLATLYGTKFNFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAI 320
Cdd:MTH00153 308 MIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAI 387

                        330
                 ....*....|...
gi 254681564 321 MGGIIQWYPLFTG 333
Cdd:MTH00153 388 MGGFIHWFPLFTG 400
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-333 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: 613.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564   1 VMPIMIGGFGNWLVPLMIGAPD*AFPRMNNMSFWLLPPSLTLLIASSMMDSGAGT*WTIYPPLAGAIAHGGSSVDLAIFS 80
Cdd:cd01663   61 VMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFS 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564  81 LHLAGVSSILGAVNFITTAINMRSESMTL*QTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRBLNTSFFDPAGGGDPI 160
Cdd:cd01663  141 LHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPI 220

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564 161 LYQHLFWFFGHPEVYILILPGFGIISHIVYQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSAT 240
Cdd:cd01663  221 LYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAAT 300

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564 241 MIIAVPTGIKVFSWLATLYGTKFNFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAI 320
Cdd:cd01663  301 MIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAI 380

                        330
                 ....*....|...
gi 254681564 321 MGGIIQWYPLFTG 333
Cdd:cd01663  381 FAGFYYWFPKITG 393
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
5-333 3.23e-139

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 404.89  E-value: 3.23e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564   5 MIGGFGNWLVPLMIGAPD*AFPRMNNMSFWLLPPSLTLLIASSMMDSGAGT*WTIYPPLAGAIAHGGSSVDLAIFSLHLA 84
Cdd:COG0843   76 FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALF 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564  85 GVSSILGAVNFITTAINMRSESMTL*QTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRBLNTSFFDPAGGGDPILYQH 164
Cdd:COG0843  156 GVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQH 235

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564 165 LFWFFGHPEVYILILPGFGIISHIVYQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIA 244
Cdd:COG0843  236 LFWFFGHPEVYILILPAFGIVSEIIPTFSRK-PLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIA 314

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564 245 VPTGIKVFSWLATLYGTKFNFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGI 324
Cdd:COG0843  315 VPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGL 394


                 ....*....
gi 254681564 325 IQWYPLFTG 333
Cdd:COG0843  395 YYWFPKMTG 403
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 5-333 5.27e-139

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: 403.14  E-value: 5.27e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564    5 MIGGFGNWLVPLMIGAPD*AFPRMNNMSFWLLPPSLTLLIASSMMDSGAGT*WTIYPPLAGAIAHGGSSVDLAIFSLHLA 84
Cdd:TIGR02891  67 ILAGFGNYLLPLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLL 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564   85 GVSSILGAVNFITTAINMRSESMTL*QTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRBLNTSFFDPAGGGDPILYQH 164
Cdd:TIGR02891 147 GISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQH 226

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564  165 LFWFFGHPEVYILILPGFGIISHIVYQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIA 244
Cdd:TIGR02891 227 LFWFFGHPEVYIIFLPAFGIISEILPTFARK-PIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIA 305

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564  245 VPTGIKVFSWLATLYGTKFNFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGI 324
Cdd:TIGR02891 306 VPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAI 385


                  ....*....
gi 254681564  325 IQWYPLFTG 333
Cdd:TIGR02891 386 YYWFPKVTG 394
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 5-333 1.39e-92

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: 282.15  E-value: 1.39e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564    5 MIGGFGNWLVPLMIGAPD*AFPRMNNMSFWLLPPSLTLLIASSMmdsGAGT*WTIYPPLAGaiahggssVDLAIFSLHLA 84
Cdd:pfam00115  60 FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLA 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564   85 GVSSILGAVNFITTAINMRSESMTL*QTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRBLNtsffdpAGGGDPILYQH 164
Cdd:pfam00115 129 GVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQH 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564  165 LFWFFGHPEVYILILPGFGIISHIVYQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIA 244
Cdd:pfam00115 202 LFWWFGHPEVYILILPAFGIIYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIA 280

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564  245 VPTGIKVFSWLATLYGTKFNFN-PPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGG 323
Cdd:pfam00115 281 VPSGVKVFNWLATLWGGWIRFRtTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGG 360

                         330
                  ....*....|
gi 254681564  324 IIQWYPLFTG 333
Cdd:pfam00115 361 IYYWLPKLTG 370
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-333 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 684.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564   1 VMPIMIGGFGNWLVPLMIGAPD*AFPRMNNMSFWLLPPSLTLLIASSMMDSGAGT*WTIYPPLAGAIAHGGSSVDLAIFS 80
Cdd:MTH00153  68 VMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFS 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564  81 LHLAGVSSILGAVNFITTAINMRSESMTL*QTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRBLNTSFFDPAGGGDPI 160
Cdd:MTH00153 148 LHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPI 227

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564 161 LYQHLFWFFGHPEVYILILPGFGIISHIVYQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSAT 240
Cdd:MTH00153 228 LYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSAT 307

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564 241 MIIAVPTGIKVFSWLATLYGTKFNFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAI 320
Cdd:MTH00153 308 MIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAI 387

                        330
                 ....*....|...
gi 254681564 321 MGGIIQWYPLFTG 333
Cdd:MTH00153 388 MGGFIHWFPLFTG 400
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-333 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: 613.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564   1 VMPIMIGGFGNWLVPLMIGAPD*AFPRMNNMSFWLLPPSLTLLIASSMMDSGAGT*WTIYPPLAGAIAHGGSSVDLAIFS 80
Cdd:cd01663   61 VMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFS 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564  81 LHLAGVSSILGAVNFITTAINMRSESMTL*QTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRBLNTSFFDPAGGGDPI 160
Cdd:cd01663  141 LHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPI 220

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564 161 LYQHLFWFFGHPEVYILILPGFGIISHIVYQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSAT 240
Cdd:cd01663  221 LYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAAT 300

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564 241 MIIAVPTGIKVFSWLATLYGTKFNFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAI 320
Cdd:cd01663  301 MIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAI 380

                        330
                 ....*....|...
gi 254681564 321 MGGIIQWYPLFTG 333
Cdd:cd01663  381 FAGFYYWFPKITG 393
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-333 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 589.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564   1 VMPIMIGGFGNWLVPLMIGAPD*AFPRMNNMSFWLLPPSLTLLIASSMMDSGAGT*WTIYPPLAGAIAHGGSSVDLAIFS 80
Cdd:MTH00116  70 VMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFS 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564  81 LHLAGVSSILGAVNFITTAINMRSESMTL*QTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRBLNTSFFDPAGGGDPI 160
Cdd:MTH00116 150 LHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPI 229

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564 161 LYQHLFWFFGHPEVYILILPGFGIISHIVYQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSAT 240
Cdd:MTH00116 230 LYQHLFWFFGHPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSAT 309

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564 241 MIIAVPTGIKVFSWLATLYGTKFNFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAI 320
Cdd:MTH00116 310 MIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAI 389

                        330
                 ....*....|...
gi 254681564 321 MGGIIQWYPLFTG 333
Cdd:MTH00116 390 MAGFTHWFPLFTG 402
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-333 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 584.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564   1 VMPIMIGGFGNWLVPLMIGAPD*AFPRMNNMSFWLLPPSLTLLIASSMMDSGAGT*WTIYPPLAGAIAHGGSSVDLAIFS 80
Cdd:MTH00167  70 VMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFS 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564  81 LHLAGVSSILGAVNFITTAINMRSESMTL*QTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRBLNTSFFDPAGGGDPI 160
Cdd:MTH00167 150 LHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPI 229

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564 161 LYQHLFWFFGHPEVYILILPGFGIISHIVYQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSAT 240
Cdd:MTH00167 230 LYQHLFWFFGHPEVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSAT 309

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564 241 MIIAVPTGIKVFSWLATLYGTKFNFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAI 320
Cdd:MTH00167 310 MIIAVPTGIKVFSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAI 389

                        330
                 ....*....|...
gi 254681564 321 MGGIIQWYPLFTG 333
Cdd:MTH00167 390 MAGFTHWFPLFTG 402
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-333 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 581.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564   1 VMPIMIGGFGNWLVPLMIGAPD*AFPRMNNMSFWLLPPSLTLLIASSMMDSGAGT*WTIYPPLAGAIAHGGSSVDLAIFS 80
Cdd:MTH00223  67 VMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFS 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564  81 LHLAGVSSILGAVNFITTAINMRSESMTL*QTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRBLNTSFFDPAGGGDPI 160
Cdd:MTH00223 147 LHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPI 226

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564 161 LYQHLFWFFGHPEVYILILPGFGIISHIVYQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSAT 240
Cdd:MTH00223 227 LYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAAT 306

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564 241 MIIAVPTGIKVFSWLATLYGTKFNFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAI 320
Cdd:MTH00223 307 MIIAVPTGIKVFSWLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFAL 386

                        330
                 ....*....|...
gi 254681564 321 MGGIIQWYPLFTG 333
Cdd:MTH00223 387 FAGFNHWFPLFTG 399
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-333 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 570.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564   1 VMPIMIGGFGNWLVPLMIGAPD*AFPRMNNMSFWLLPPSLTLLIASSMMDSGAGT*WTIYPPLAGAIAHGGSSVDLAIFS 80
Cdd:MTH00142  68 VMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFS 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564  81 LHLAGVSSILGAVNFITTAINMRSESMTL*QTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRBLNTSFFDPAGGGDPI 160
Cdd:MTH00142 148 LHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPI 227

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564 161 LYQHLFWFFGHPEVYILILPGFGIISHIVYQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSAT 240
Cdd:MTH00142 228 LYQHLFWFFGHPEVYILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAAT 307

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564 241 MIIAVPTGIKVFSWLATLYGTKFNFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAI 320
Cdd:MTH00142 308 MVIAVPTGIKVFSWLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAL 387

                        330
                 ....*....|...
gi 254681564 321 MGGIIQWYPLFTG 333
Cdd:MTH00142 388 FAGFIHWFPLFTG 400
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-333 0e+00

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 525.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564   1 VMPIMIGGFGNWLVPLMIGAPD*AFPRMNNMSFWLLPPSLTLLIASSMMDSGAGT*WTIYPPLAGAIAHGGSSVDLAIFS 80
Cdd:MTH00103  70 VMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFS 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564  81 LHLAGVSSILGAVNFITTAINMRSESMTL*QTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRBLNTSFFDPAGGGDPI 160
Cdd:MTH00103 150 LHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPI 229

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564 161 LYQHLFWFFGHPEVYILILPGFGIISHIVYQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSAT 240
Cdd:MTH00103 230 LYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSAT 309

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564 241 MIIAVPTGIKVFSWLATLYGTKFNFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAI 320
Cdd:MTH00103 310 MIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAI 389

                        330
                 ....*....|...
gi 254681564 321 MGGIIQWYPLFTG 333
Cdd:MTH00103 390 MGGFVHWFPLFSG 402
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-333 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 516.78  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564   1 VMPIMIGGFGNWLVPLMIGAPD*AFPRMNNMSFWLLPPSLTLLIASSMMDSGAGT*WTIYPPLAGAIAHGGSSVDLAIFS 80
Cdd:MTH00183  70 VMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFS 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564  81 LHLAGVSSILGAVNFITTAINMRSESMTL*QTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRBLNTSFFDPAGGGDPI 160
Cdd:MTH00183 150 LHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPI 229

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564 161 LYQHLFWFFGHPEVYILILPGFGIISHIVYQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSAT 240
Cdd:MTH00183 230 LYQHLFWFFGHPEVYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSAT 309

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564 241 MIIAVPTGIKVFSWLATLYGTKFNFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAI 320
Cdd:MTH00183 310 MIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAI 389

                        330
                 ....*....|...
gi 254681564 321 MGGIIQWYPLFTG 333
Cdd:MTH00183 390 MAAFVHWFPLFSG 402
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-333 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 516.42  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564   1 VMPIMIGGFGNWLVPLMIGAPD*AFPRMNNMSFWLLPPSLTLLIASSMMDSGAGT*WTIYPPLAGAIAHGGSSVDLAIFS 80
Cdd:MTH00077  70 VMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFS 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564  81 LHLAGVSSILGAVNFITTAINMRSESMTL*QTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRBLNTSFFDPAGGGDPI 160
Cdd:MTH00077 150 LHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPV 229

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564 161 LYQHLFWFFGHPEVYILILPGFGIISHIVYQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSAT 240
Cdd:MTH00077 230 LYQHLFWFFGHPEVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSAT 309

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564 241 MIIAVPTGIKVFSWLATLYGTKFNFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAI 320
Cdd:MTH00077 310 MIIAIPTGVKVFSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAI 389

                        330
                 ....*....|...
gi 254681564 321 MGGIIQWYPLFTG 333
Cdd:MTH00077 390 MGGFVHWFPLFSG 402
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-333 0e+00

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 514.07  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564   1 VMPIMIGGFGNWLVPLMIGAPD*AFPRMNNMSFWLLPPSLTLLIASSMMDSGAGT*WTIYPPLAGAIAHGGSSVDLAIFS 80
Cdd:MTH00007  67 VMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFS 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564  81 LHLAGVSSILGAVNFITTAINMRSESMTL*QTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRBLNTSFFDPAGGGDPI 160
Cdd:MTH00007 147 LHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPI 226

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564 161 LYQHLFWFFGHPEVYILILPGFGIISHIVYQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSAT 240
Cdd:MTH00007 227 LYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAAT 306

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564 241 MIIAVPTGIKVFSWLATLYGTKFNFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAI 320
Cdd:MTH00007 307 MIIAVPTGIKVFSWLATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAI 386

                        330
                 ....*....|...
gi 254681564 321 MGGIIQWYPLFTG 333
Cdd:MTH00007 387 FAAFNHWFPLFTG 399
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-333 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 513.61  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564   1 VMPIMIGGFGNWLVPLMIGAPD*AFPRMNNMSFWLLPPSLTLLIASSMMDSGAGT*WTIYPPLAGAIAHGGSSVDLAIFS 80
Cdd:MTH00037  70 VMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFS 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564  81 LHLAGVSSILGAVNFITTAINMRSESMTL*QTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRBLNTSFFDPAGGGDPI 160
Cdd:MTH00037 150 LHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPI 229

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564 161 LYQHLFWFFGHPEVYILILPGFGIISHIVYQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSAT 240
Cdd:MTH00037 230 LFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAAT 309

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564 241 MIIAVPTGIKVFSWLATLYGTKFNFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAI 320
Cdd:MTH00037 310 MIIAVPTGIKVFSWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAI 389

                        330
                 ....*....|...
gi 254681564 321 MGGIIQWYPLFTG 333
Cdd:MTH00037 390 FAGFTHWFPLFSG 402
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-333 3.46e-175

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 495.35  E-value: 3.46e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564   1 VMPIMIGGFGNWLVPLMIGAPD*AFPRMNNMSFWLLPPSLTLLIASSMMDSGAGT*WTIYPPLAgAIAHGGSSVDLAIFS 80
Cdd:MTH00079  71 VMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLS-TLGHPGSSVDLAIFS 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564  81 LHLAGVSSILGAVNFITTAINMRSESMTL*QTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRBLNTSFFDPAGGGDPI 160
Cdd:MTH00079 150 LHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPL 229

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564 161 LYQHLFWFFGHPEVYILILPGFGIISHIVYQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSAT 240
Cdd:MTH00079 230 LYQHLFWFFGHPEVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAAT 309

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564 241 MIIAVPTGIKVFSWLATLYGTKFNFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAI 320
Cdd:MTH00079 310 MVIAVPTGVKVFSWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGI 389

                        330
                 ....*....|...
gi 254681564 321 MGGIIQWYPLFTG 333
Cdd:MTH00079 390 FTGISLWWPFMTG 402
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-333 3.24e-170

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 483.55  E-value: 3.24e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564   1 VMPIMIGGFGNWLVPLMIGAPD*AFPRMNNMSFWLLPPSLTLLIASSMMDSGAGT*WTIYPPLAGAIAHGGSSVDLAIFS 80
Cdd:MTH00182  72 VMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFS 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564  81 LHLAGVSSILGAVNFITTAINMRSESMTL*QTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRBLNTSFFDPAGGGDPI 160
Cdd:MTH00182 152 LHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPI 231

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564 161 LYQHLFWFFGHPEVYILILPGFGIISHIVYQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSAT 240
Cdd:MTH00182 232 LFQHLFWFFGHPEVYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAAT 311

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564 241 MIIAVPTGIKVFSWLATLYGTKFNFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAI 320
Cdd:MTH00182 312 MIIAVPTGIKVFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAI 391

                        330
                 ....*....|...
gi 254681564 321 MGGIIQWYPLFTG 333
Cdd:MTH00182 392 FGGFYYWFGKITG 404
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-333 3.96e-166

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 472.77  E-value: 3.96e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564   1 VMPIMIGGFGNWLVPLMIGAPD*AFPRMNNMSFWLLPPSLTLLIASSMMDSGAGT*WTIYPPLAGAIAHGGSSVDLAIFS 80
Cdd:MTH00184  72 VMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFS 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564  81 LHLAGVSSILGAVNFITTAINMRSESMTL*QTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRBLNTSFFDPAGGGDPI 160
Cdd:MTH00184 152 LHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPI 231

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564 161 LYQHLFWFFGHPEVYILILPGFGIISHIVYQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSAT 240
Cdd:MTH00184 232 LYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAAT 311

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564 241 MIIAVPTGIKVFSWLATLYGTKFNFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAI 320
Cdd:MTH00184 312 MIIAVPTGIKIFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAI 391

                        330
                 ....*....|...
gi 254681564 321 MGGIIQWYPLFTG 333
Cdd:MTH00184 392 FGGFYYWFGKITG 404
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-333 6.13e-151

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 434.83  E-value: 6.13e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564   1 VMPIMIGGFGNWLVPLMIGAPD*AFPRMNNMSFWLLPPSLTLLIASSMMDSGAGT*WTIYPPLAGAIAHGGSSVDLAIFS 80
Cdd:MTH00026  71 VMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFS 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564  81 LHLAGVSSILGAVNFITTAINMRSESMTL*QTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRBLNTSFFDPAGGGDPI 160
Cdd:MTH00026 151 LHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPI 230

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564 161 LYQHLFWFFGHPEVYILILPGFGIISHIVYQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSAT 240
Cdd:MTH00026 231 LYQHLFWFFGHPEVYILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAAT 310

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564 241 MIIAVPTGIKVFSWLATLYGTKFN--FNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVF 318
Cdd:MTH00026 311 MIIAVPTGIKIFSWLATVSGSGRNliFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVF 390

                        330
                 ....*....|....*
gi 254681564 319 AIMGGIIQWYPLFTG 333
Cdd:MTH00026 391 AIFGGFYLWFGKITG 405
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-333 4.15e-144

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: 414.62  E-value: 4.15e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564   1 VMPIMIGGFGNWLVPlMIGAPD*AFPRMNNMSFWLLPPSLTLLIASSMMDSGAGT*WTIYPPLAGAIAHGGSSVDLAIFS 80
Cdd:cd00919   59 VMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILG 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564  81 LHLAGVSSILGAVNFITTAINMRSESMTL*QTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRBLNTSFFDPAGGGDPI 160
Cdd:cd00919  138 LHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPV 217

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564 161 LYQHLFWFFGHPEVYILILPGFGIISHIVYQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSAT 240
Cdd:cd00919  218 LYQHLFWFFGHPEVYILILPAFGAISEIIPTFSGK-PLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAAT 296

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564 241 MIIAVPTGIKVFSWLATLYGTKFNFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAI 320
Cdd:cd00919  297 MIIAVPTGIKVFNWLATLWGGRIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAI 376

                        330
                 ....*....|...
gi 254681564 321 MGGIIQWYPLFTG 333
Cdd:cd00919  377 FAGLYYWFPKMTG 389
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
5-333 3.23e-139

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 404.89  E-value: 3.23e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564   5 MIGGFGNWLVPLMIGAPD*AFPRMNNMSFWLLPPSLTLLIASSMMDSGAGT*WTIYPPLAGAIAHGGSSVDLAIFSLHLA 84
Cdd:COG0843   76 FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALF 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564  85 GVSSILGAVNFITTAINMRSESMTL*QTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRBLNTSFFDPAGGGDPILYQH 164
Cdd:COG0843  156 GVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQH 235

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564 165 LFWFFGHPEVYILILPGFGIISHIVYQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIA 244
Cdd:COG0843  236 LFWFFGHPEVYILILPAFGIVSEIIPTFSRK-PLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIA 314

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564 245 VPTGIKVFSWLATLYGTKFNFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGI 324
Cdd:COG0843  315 VPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGL 394


                 ....*....
gi 254681564 325 IQWYPLFTG 333
Cdd:COG0843  395 YYWFPKMTG 403
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 5-333 5.27e-139

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: 403.14  E-value: 5.27e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564    5 MIGGFGNWLVPLMIGAPD*AFPRMNNMSFWLLPPSLTLLIASSMMDSGAGT*WTIYPPLAGAIAHGGSSVDLAIFSLHLA 84
Cdd:TIGR02891  67 ILAGFGNYLLPLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLL 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564   85 GVSSILGAVNFITTAINMRSESMTL*QTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRBLNTSFFDPAGGGDPILYQH 164
Cdd:TIGR02891 147 GISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQH 226

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564  165 LFWFFGHPEVYILILPGFGIISHIVYQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIA 244
Cdd:TIGR02891 227 LFWFFGHPEVYIIFLPAFGIISEILPTFARK-PIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIA 305

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564  245 VPTGIKVFSWLATLYGTKFNFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGI 324
Cdd:TIGR02891 306 VPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAI 385


                  ....*....
gi 254681564  325 IQWYPLFTG 333
Cdd:TIGR02891 386 YYWFPKVTG 394
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 2-333 1.10e-129

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 379.79  E-value: 1.10e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564   2 MPIMIGGFGNWLVPLMIGAPD*AFPRMNNMSFWLLPPSLTLLIASsmMDSGAGT*WTIYPPLAGAIAHGGSSVDLAIFSL 81
Cdd:MTH00048  72 MPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLS--MCLGAGVGWTFYPPLSSSLFSSSWGVDFLMFSL 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564  82 HLAGVSSILGAVNFITTAINMRSESMTL*QTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRBLNTSFFDPAGGGDPIL 161
Cdd:MTH00048 150 HLAGVSSLFGSINFICTIYSAFMTNVFS-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVL 228

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564 162 YQHLFWFFGHPEVYILILPGFGIISHIVYQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATM 241
Cdd:MTH00048 229 FQHMFWFFGHPEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTM 308

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564 242 IIAVPTGIKVFSWLATLYGTKFNFNPPLL-WALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAI 320
Cdd:MTH00048 309 IIGVPTGIKVFSWLYMLLNSRVRKSDPVVwWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSV 388

                        330
                 ....*....|...
gi 254681564 321 MGGIIQWYPLFTG 333
Cdd:MTH00048 389 VIMFIWWWPLITG 401
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 2-333 7.60e-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: 356.89  E-value: 7.60e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564   2 MPIMIGgFGNWLVPLMIGAPD*AFPRMNNMSFWLLPPSLTLLIASSMMDSGAGT*WTIYPPLAGAIAHGGSSVDLAIFSL 81
Cdd:cd01662   66 MPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGL 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564  82 HLAGVSSILGAVNFITTAINMRSESMTL*QTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRBLNTSFFDPAGGGDPIL 161
Cdd:cd01662  145 QFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPML 224

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564 162 YQHLFWFFGHPEVYILILPGFGIISHIVYQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATM 241
Cdd:cd01662  225 WQHLFWIFGHPEVYILILPAFGIFSEIVPTFSRK-PLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATM 303

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564 242 IIAVPTGIKVFSWLATLYGTKFNFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIM 321
Cdd:cd01662  304 IIAVPTGVKIFNWLFTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLF 383

                        330
                 ....*....|..
gi 254681564 322 GGIIQWYPLFTG 333
Cdd:cd01662  384 AGFYYWFPKMFG 395
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 5-333 1.39e-92

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: 282.15  E-value: 1.39e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564    5 MIGGFGNWLVPLMIGAPD*AFPRMNNMSFWLLPPSLTLLIASSMmdsGAGT*WTIYPPLAGaiahggssVDLAIFSLHLA 84
Cdd:pfam00115  60 FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLA 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564   85 GVSSILGAVNFITTAINMRSESMTL*QTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRBLNtsffdpAGGGDPILYQH 164
Cdd:pfam00115 129 GVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQH 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564  165 LFWFFGHPEVYILILPGFGIISHIVYQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIA 244
Cdd:pfam00115 202 LFWWFGHPEVYILILPAFGIIYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIA 280

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564  245 VPTGIKVFSWLATLYGTKFNFN-PPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGG 323
Cdd:pfam00115 281 VPSGVKVFNWLATLWGGWIRFRtTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGG 360

                         330
                  ....*....|
gi 254681564  324 IIQWYPLFTG 333
Cdd:pfam00115 361 IYYWLPKLTG 370
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 2-333 3.05e-79

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: 254.01  E-value: 3.05e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564    2 MPIMIGgFGNWLVPLMIGAPD*AFPRMNNMSFWLLPPSLTLLIASSMMDSGAGT*WTIYPPLAGAIAHGGSSVDLAIFSL 81
Cdd:TIGR02882 109 MPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIAL 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564   82 HLAGVSSILGAVNFITTAINMRSESMTL*QTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRBLNTSFFDPAGGGDPIL 161
Cdd:TIGR02882 188 QISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPML 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564  162 YQHLFWFFGHPEVYILILPGFGIISHIVYQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATM 241
Cdd:TIGR02882 268 WANLFWIWGHPEVYIVILPAFGIYSEIISTFAQK-RLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTM 346

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564  242 IIAVPTGIKVFSWLATLYGTKFNFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIM 321
Cdd:TIGR02882 347 AIAIPTGVKIFNWLLTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACL 426

                         330
                  ....*....|..
gi 254681564  322 GGIIQWYPLFTG 333
Cdd:TIGR02882 427 AGLIYWYPKMFG 438
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 2-329 3.78e-78

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 251.39  E-value: 3.78e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564   2 MPIMIGgFGNWLVPLMIGAPD*AFPRMNNMSFWLLPPSLTLLIASSMMDSGAGT*WTIYPPLAGAIAHGGSSVDLAIFSL 81
Cdd:PRK15017 116 MPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSL 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564  82 HLAGVSSILGAVNFITTAINMRSESMTL*QTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRBLNTSFFDPAGGGDPIL 161
Cdd:PRK15017 195 QLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMM 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564 162 YQHLFWFFGHPEVYILILPGFGIISHIVYQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATM 241
Cdd:PRK15017 275 YINLIWAWGHPEVYILILPVFGVFSEIAATFSRK-RLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTM 353

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564 242 IIAVPTGIKVFSWLATLYGTKFNFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIM 321
Cdd:PRK15017 354 IIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCF 433


                 ....*...
gi 254681564 322 GGIIQWYP 329
Cdd:PRK15017 434 AGMTYWWP 441
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 6-321 1.05e-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: 56.14  E-value: 1.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564   6 IGGFGNWLVPLMIGAPD*AfPRMNNMSFWLLppSLTLLIASSMMDSG-AGT*WTIYPPLagaIAHGGSSVDLAIFSLHla 84
Cdd:cd01660   64 IMGFFYAIVARALLRSLFN-RRLAWAGFWLM--VIGTVMAAVPILLGqASVLYTFYPPL---QAHPLFYIGAALVVVG-- 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564  85 gvSSILGAVNFITTAINMRSESMTL*qTPLFVWSVAITALLLLLSLPVLAGAITMLLtdrbLNTSFFDpAGGGDPILYQH 164
Cdd:cd01660  136 --SWISGFAMFVTLWRWKKANPGKK--VPLATFMVVTTMILWLVASLGVALEVLFQL----LPWSLGL-VDTVDVLLSRT 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564 165 LFWFFGHPEVYILILPGFGIISHIVYQESGKIESFGTLGMIYAMLSIgLMGFIVWAHHMFT-VGMDVDTRAYFTSATMII 243
Cdd:cd01660  207 LFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKLFSDPLARLAFILFL-LFSTPVGFHHQFAdPGIGPGWKFIHMVLTFMV 285

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254681564 244 AVPTGIKVFSWLAT------------LYG--TKFNFNPPLLWALGF-IFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHF 308
Cdd:cd01660  286 ALPSLLTAFTVFASleiagrlrggkgLFGwiRALPWGDPMFLALFLaMLMFIPGGAGGIINASYQLNYVVHNTAWVPGHF 365

                        330
                 ....*....|...
gi 254681564 309 HyvLSMGAVFAIM 321
Cdd:cd01660  366 H--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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