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Conserved domains on  [gi|767521683|gb|AJT49371|]
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cytochrome c oxidase subunit I, partial (mitochondrion) [Termitinae sp. MG-ENT-329]

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 ...
 1-331 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: 673.89  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683   1 QIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLTSSTVESGVGTGWTVYPP 80
Cdd:MTH00153  50 QIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPP 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683  81 LASGIAHAGASVDLAIFSLHLAGVSSILGAVNFITTTINMKPKNMKPERIPLFVWSIAITALLLLLSLPVLAGAITMLLT 160
Cdd:MTH00153 130 LSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLT 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683 161 DRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIICHESGKKEAFGNLGMIFAMLAIGLLGFVVWAHH 240
Cdd:MTH00153 210 DRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHH 289

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683 241 MFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATMYGTRMTYSAACLWALGFVFLFTMGGLTGVVLANSSIDIVLHDTY 320
Cdd:MTH00153 290 MFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTY 369

                        330
                 ....*....|.
gi 767521683 321 YVVAHFHYVLS 331
Cdd:MTH00153 370 YVVAHFHYVLS 380
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-331 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 673.89  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683   1 QIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLTSSTVESGVGTGWTVYPP 80
Cdd:MTH00153  50 QIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPP 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683  81 LASGIAHAGASVDLAIFSLHLAGVSSILGAVNFITTTINMKPKNMKPERIPLFVWSIAITALLLLLSLPVLAGAITMLLT 160
Cdd:MTH00153 130 LSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLT 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683 161 DRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIICHESGKKEAFGNLGMIFAMLAIGLLGFVVWAHH 240
Cdd:MTH00153 210 DRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHH 289

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683 241 MFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATMYGTRMTYSAACLWALGFVFLFTMGGLTGVVLANSSIDIVLHDTY 320
Cdd:MTH00153 290 MFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTY 369

                        330
                 ....*....|.
gi 767521683 321 YVVAHFHYVLS 331
Cdd:MTH00153 370 YVVAHFHYVLS 380
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-331 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: 612.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683   1 QIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLTSSTVESGVGTGWTVYPP 80
Cdd:cd01663   43 QLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPP 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683  81 LASGIAHAGASVDLAIFSLHLAGVSSILGAVNFITTTINMKPKNMKPERIPLFVWSIAITALLLLLSLPVLAGAITMLLT 160
Cdd:cd01663  123 LSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLT 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683 161 DRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIICHESGKKEAFGNLGMIFAMLAIGLLGFVVWAHH 240
Cdd:cd01663  203 DRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHH 282

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683 241 MFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATMYGTRMTYSAACLWALGFVFLFTMGGLTGVVLANSSIDIVLHDTY 320
Cdd:cd01663  283 MFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTY 362

                        330
                 ....*....|.
gi 767521683 321 YVVAHFHYVLS 331
Cdd:cd01663  363 YVVAHFHYVLS 373
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
3-330 2.15e-138

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 402.58  E-value: 2.15e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683   3 YNVIVTAHAFVMIFFMVMPiMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLTSSTVESGVGTGWTVYPPLA 82
Cdd:COG0843   57 YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLS 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683  83 SGIAHAGASVDLAIFSLHLAGVSSILGAVNFITTTINMKPKNMKPERIPLFVWSIAITALLLLLSLPVLAGAITMLLTDR 162
Cdd:COG0843  136 GLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDR 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683 163 NLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIICHESGKKeAFGNLGMIFAMLAIGLLGFVVWAHHMF 242
Cdd:COG0843  216 SLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMF 294

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683 243 TVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATMYGTRMTYSAACLWALGFVFLFTMGGLTGVVLANSSIDIVLHDTYYV 322
Cdd:COG0843  295 TPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFV 374


                 ....*...
gi 767521683 323 VAHFHYVL 330
Cdd:COG0843  375 VAHFHYVL 382
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 3-330 5.63e-137

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: 397.75  E-value: 5.63e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683    3 YNVIVTAHAFVMIFFMVMPIMiGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLTSSTVESGVGTGWTVYPPLA 82
Cdd:TIGR02891  48 YNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLS 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683   83 SGIAHAGASVDLAIFSLHLAGVSSILGAVNFITTTINMKPKNMKPERIPLFVWSIAITALLLLLSLPVLAGAITMLLTDR 162
Cdd:TIGR02891 127 STSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDR 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683  163 NLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIICHESGKKeAFGNLGMIFAMLAIGLLGFVVWAHHMF 242
Cdd:TIGR02891 207 LFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMF 285

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683  243 TVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATMYGTRMTYSAACLWALGFVFLFTMGGLTGVVLANSSIDIVLHDTYYV 322
Cdd:TIGR02891 286 TTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFV 365


                  ....*...
gi 767521683  323 VAHFHYVL 330
Cdd:TIGR02891 366 VAHFHYVL 373
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-330 2.20e-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: 281.77  E-value: 2.20e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683    1 QIYNVIVTAHAFVMIFFMVMPiMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLTSSTvesGVGTGWTVYPP 80
Cdd:pfam00115  39 LTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPP 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683   81 LASgiahagasVDLAIFSLHLAGVSSILGAVNFITTTINMKPKNMKpERIPLFVWSIAITALLLLLSLPVLAGAITMLLT 160
Cdd:pfam00115 115 LVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMT-LRMPLFVWAILATAILILLAFPVLAAALLLLLL 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683  161 DRNLNtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIICHESGKKeAFGNLGMIFAMLAIGLLGFVVWAHH 240
Cdd:pfam00115 186 DRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHH 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683  241 MFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATMYGTRMT-YSAACLWALGFVFLFTMGGLTGVVLANSSIDIVLHDT 319
Cdd:pfam00115 259 LFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRfRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDT 338

                         330
                  ....*....|.
gi 767521683  320 YYVVAHFHYVL 330
Cdd:pfam00115 339 YFVVAHFHYVL 349
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-331 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 673.89  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683   1 QIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLTSSTVESGVGTGWTVYPP 80
Cdd:MTH00153  50 QIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPP 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683  81 LASGIAHAGASVDLAIFSLHLAGVSSILGAVNFITTTINMKPKNMKPERIPLFVWSIAITALLLLLSLPVLAGAITMLLT 160
Cdd:MTH00153 130 LSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLT 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683 161 DRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIICHESGKKEAFGNLGMIFAMLAIGLLGFVVWAHH 240
Cdd:MTH00153 210 DRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHH 289

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683 241 MFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATMYGTRMTYSAACLWALGFVFLFTMGGLTGVVLANSSIDIVLHDTY 320
Cdd:MTH00153 290 MFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTY 369

                        330
                 ....*....|.
gi 767521683 321 YVVAHFHYVLS 331
Cdd:MTH00153 370 YVVAHFHYVLS 380
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-331 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: 612.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683   1 QIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLTSSTVESGVGTGWTVYPP 80
Cdd:cd01663   43 QLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPP 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683  81 LASGIAHAGASVDLAIFSLHLAGVSSILGAVNFITTTINMKPKNMKPERIPLFVWSIAITALLLLLSLPVLAGAITMLLT 160
Cdd:cd01663  123 LSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLT 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683 161 DRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIICHESGKKEAFGNLGMIFAMLAIGLLGFVVWAHH 240
Cdd:cd01663  203 DRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHH 282

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683 241 MFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATMYGTRMTYSAACLWALGFVFLFTMGGLTGVVLANSSIDIVLHDTY 320
Cdd:cd01663  283 MFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTY 362

                        330
                 ....*....|.
gi 767521683 321 YVVAHFHYVLS 331
Cdd:cd01663  363 YVVAHFHYVLS 373
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-331 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 579.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683   1 QIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLTSSTVESGVGTGWTVYPP 80
Cdd:MTH00167  52 QIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPP 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683  81 LASGIAHAGASVDLAIFSLHLAGVSSILGAVNFITTTINMKPKNMKPERIPLFVWSIAITALLLLLSLPVLAGAITMLLT 160
Cdd:MTH00167 132 LAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLT 211

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683 161 DRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIICHESGKKEAFGNLGMIFAMLAIGLLGFVVWAHH 240
Cdd:MTH00167 212 DRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHH 291

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683 241 MFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATMYGTRMTYSAACLWALGFVFLFTMGGLTGVVLANSSIDIVLHDTY 320
Cdd:MTH00167 292 MFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTY 371

                        330
                 ....*....|.
gi 767521683 321 YVVAHFHYVLS 331
Cdd:MTH00167 372 YVVAHFHYVLS 382
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-331 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 577.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683   1 QIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLTSSTVESGVGTGWTVYPP 80
Cdd:MTH00116  52 QIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPP 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683  81 LASGIAHAGASVDLAIFSLHLAGVSSILGAVNFITTTINMKPKNMKPERIPLFVWSIAITALLLLLSLPVLAGAITMLLT 160
Cdd:MTH00116 132 LAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLT 211

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683 161 DRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIICHESGKKEAFGNLGMIFAMLAIGLLGFVVWAHH 240
Cdd:MTH00116 212 DRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHH 291

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683 241 MFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATMYGTRMTYSAACLWALGFVFLFTMGGLTGVVLANSSIDIVLHDTY 320
Cdd:MTH00116 292 MFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTY 371

                        330
                 ....*....|.
gi 767521683 321 YVVAHFHYVLS 331
Cdd:MTH00116 372 YVVAHFHYVLS 382
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-331 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 576.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683   1 QIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLTSSTVESGVGTGWTVYPP 80
Cdd:MTH00223  49 QLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPP 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683  81 LASGIAHAGASVDLAIFSLHLAGVSSILGAVNFITTTINMKPKNMKPERIPLFVWSIAITALLLLLSLPVLAGAITMLLT 160
Cdd:MTH00223 129 LSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLT 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683 161 DRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIICHESGKKEAFGNLGMIFAMLAIGLLGFVVWAHH 240
Cdd:MTH00223 209 DRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHH 288

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683 241 MFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATMYGTRMTYSAACLWALGFVFLFTMGGLTGVVLANSSIDIVLHDTY 320
Cdd:MTH00223 289 MFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTY 368

                        330
                 ....*....|.
gi 767521683 321 YVVAHFHYVLS 331
Cdd:MTH00223 369 YVVAHFHYVLS 379
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-331 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 565.89  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683   1 QIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLTSSTVESGVGTGWTVYPP 80
Cdd:MTH00142  50 QLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPP 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683  81 LASGIAHAGASVDLAIFSLHLAGVSSILGAVNFITTTINMKPKNMKPERIPLFVWSIAITALLLLLSLPVLAGAITMLLT 160
Cdd:MTH00142 130 LSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLT 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683 161 DRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIICHESGKKEAFGNLGMIFAMLAIGLLGFVVWAHH 240
Cdd:MTH00142 210 DRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHH 289

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683 241 MFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATMYGTRMTYSAACLWALGFVFLFTMGGLTGVVLANSSIDIVLHDTY 320
Cdd:MTH00142 290 MFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTY 369

                        330
                 ....*....|.
gi 767521683 321 YVVAHFHYVLS 331
Cdd:MTH00142 370 YVVAHFHYVLS 380
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-331 0e+00

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 513.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683   1 QIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLTSSTVESGVGTGWTVYPP 80
Cdd:MTH00007  49 QLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPP 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683  81 LASGIAHAGASVDLAIFSLHLAGVSSILGAVNFITTTINMKPKNMKPERIPLFVWSIAITALLLLLSLPVLAGAITMLLT 160
Cdd:MTH00007 129 LASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLT 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683 161 DRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIICHESGKKEAFGNLGMIFAMLAIGLLGFVVWAHH 240
Cdd:MTH00007 209 DRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHH 288

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683 241 MFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATMYGTRMTYSAACLWALGFVFLFTMGGLTGVVLANSSIDIVLHDTY 320
Cdd:MTH00007 289 MFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTY 368

                        330
                 ....*....|.
gi 767521683 321 YVVAHFHYVLS 331
Cdd:MTH00007 369 YVVAHFHYVLS 379
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-331 0e+00

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 512.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683   1 QIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLTSSTVESGVGTGWTVYPP 80
Cdd:MTH00103  52 QIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPP 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683  81 LASGIAHAGASVDLAIFSLHLAGVSSILGAVNFITTTINMKPKNMKPERIPLFVWSIAITALLLLLSLPVLAGAITMLLT 160
Cdd:MTH00103 132 LAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLT 211

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683 161 DRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIICHESGKKEAFGNLGMIFAMLAIGLLGFVVWAHH 240
Cdd:MTH00103 212 DRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHH 291

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683 241 MFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATMYGTRMTYSAACLWALGFVFLFTMGGLTGVVLANSSIDIVLHDTY 320
Cdd:MTH00103 292 MFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTY 371

                        330
                 ....*....|.
gi 767521683 321 YVVAHFHYVLS 331
Cdd:MTH00103 372 YVVAHFHYVLS 382
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-331 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 511.01  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683   1 QIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLTSSTVESGVGTGWTVYPP 80
Cdd:MTH00183  52 QIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPP 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683  81 LASGIAHAGASVDLAIFSLHLAGVSSILGAVNFITTTINMKPKNMKPERIPLFVWSIAITALLLLLSLPVLAGAITMLLT 160
Cdd:MTH00183 132 LAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLT 211

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683 161 DRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIICHESGKKEAFGNLGMIFAMLAIGLLGFVVWAHH 240
Cdd:MTH00183 212 DRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHH 291

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683 241 MFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATMYGTRMTYSAACLWALGFVFLFTMGGLTGVVLANSSIDIVLHDTY 320
Cdd:MTH00183 292 MFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTY 371

                        330
                 ....*....|.
gi 767521683 321 YVVAHFHYVLS 331
Cdd:MTH00183 372 YVVAHFHYVLS 382
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-331 1.07e-180

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 509.48  E-value: 1.07e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683   1 QIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLTSSTVESGVGTGWTVYPP 80
Cdd:MTH00077  52 QIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPP 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683  81 LASGIAHAGASVDLAIFSLHLAGVSSILGAVNFITTTINMKPKNMKPERIPLFVWSIAITALLLLLSLPVLAGAITMLLT 160
Cdd:MTH00077 132 LAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLT 211

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683 161 DRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIICHESGKKEAFGNLGMIFAMLAIGLLGFVVWAHH 240
Cdd:MTH00077 212 DRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHH 291

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683 241 MFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATMYGTRMTYSAACLWALGFVFLFTMGGLTGVVLANSSIDIVLHDTY 320
Cdd:MTH00077 292 MFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTY 371

                        330
                 ....*....|.
gi 767521683 321 YVVAHFHYVLS 331
Cdd:MTH00077 372 YVVAHFHYVLS 382
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-331 2.32e-180

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 508.99  E-value: 2.32e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683   1 QIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLTSSTVESGVGTGWTVYPP 80
Cdd:MTH00037  52 QIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPP 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683  81 LASGIAHAGASVDLAIFSLHLAGVSSILGAVNFITTTINMKPKNMKPERIPLFVWSIAITALLLLLSLPVLAGAITMLLT 160
Cdd:MTH00037 132 LSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLT 211

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683 161 DRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIICHESGKKEAFGNLGMIFAMLAIGLLGFVVWAHH 240
Cdd:MTH00037 212 DRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHH 291

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683 241 MFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATMYGTRMTYSAACLWALGFVFLFTMGGLTGVVLANSSIDIVLHDTY 320
Cdd:MTH00037 292 MFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTY 371

                        330
                 ....*....|.
gi 767521683 321 YVVAHFHYVLS 331
Cdd:MTH00037 372 YVVAHFHYVLS 382
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-331 6.04e-174

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 492.27  E-value: 6.04e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683   1 QIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLTSSTVESGVGTGWTVYPP 80
Cdd:MTH00079  53 QLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPP 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683  81 LaSGIAHAGASVDLAIFSLHLAGVSSILGAVNFITTTINMKPKNMKPERIPLFVWSIAITALLLLLSLPVLAGAITMLLT 160
Cdd:MTH00079 133 L-STLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLT 211

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683 161 DRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIICHESGKKEAFGNLGMIFAMLAIGLLGFVVWAHH 240
Cdd:MTH00079 212 DRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHH 291

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683 241 MFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATMYGTRMTYSAACLWALGFVFLFTMGGLTGVVLANSSIDIVLHDTY 320
Cdd:MTH00079 292 MYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTY 371

                        330
                 ....*....|.
gi 767521683 321 YVVAHFHYVLS 331
Cdd:MTH00079 372 YVVSHFHYVLS 382
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-331 1.94e-169

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 481.24  E-value: 1.94e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683   1 QIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLTSSTVESGVGTGWTVYPP 80
Cdd:MTH00182  54 HLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPP 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683  81 LASGIAHAGASVDLAIFSLHLAGVSSILGAVNFITTTINMKPKNMKPERIPLFVWSIAITALLLLLSLPVLAGAITMLLT 160
Cdd:MTH00182 134 LSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLT 213

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683 161 DRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIICHESGKKEAFGNLGMIFAMLAIGLLGFVVWAHH 240
Cdd:MTH00182 214 DRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHH 293

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683 241 MFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATMYGTRMTYSAACLWALGFVFLFTMGGLTGVVLANSSIDIVLHDTY 320
Cdd:MTH00182 294 MFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTY 373

                        330
                 ....*....|.
gi 767521683 321 YVVAHFHYVLS 331
Cdd:MTH00182 374 YVVAHFHYVLS 384
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-331 9.78e-167

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 474.31  E-value: 9.78e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683   1 QIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLTSSTVESGVGTGWTVYPP 80
Cdd:MTH00184  54 HLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPP 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683  81 LASGIAHAGASVDLAIFSLHLAGVSSILGAVNFITTTINMKPKNMKPERIPLFVWSIAITALLLLLSLPVLAGAITMLLT 160
Cdd:MTH00184 134 LSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLT 213

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683 161 DRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIICHESGKKEAFGNLGMIFAMLAIGLLGFVVWAHH 240
Cdd:MTH00184 214 DRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHH 293

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683 241 MFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATMYGTRMTYSAACLWALGFVFLFTMGGLTGVVLANSSIDIVLHDTY 320
Cdd:MTH00184 294 MFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTY 373

                        330
                 ....*....|.
gi 767521683 321 YVVAHFHYVLS 331
Cdd:MTH00184 374 YVVAHFHYVLS 384
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-331 1.03e-149

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 431.74  E-value: 1.03e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683   1 QIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLTSSTVESGVGTGWTVYPP 80
Cdd:MTH00026  53 HLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPP 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683  81 LASGIAHAGASVDLAIFSLHLAGVSSILGAVNFITTTINMKPKNMKPERIPLFVWSIAITALLLLLSLPVLAGAITMLLT 160
Cdd:MTH00026 133 LASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLT 212

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683 161 DRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIICHESGKKEAFGNLGMIFAMLAIGLLGFVVWAHH 240
Cdd:MTH00026 213 DRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHH 292

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683 241 MFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATMYGT--RMTYSAACLWALGFVFLFTMGGLTGVVLANSSIDIVLHD 318
Cdd:MTH00026 293 MYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSgrNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHD 372

                        330
                 ....*....|...
gi 767521683 319 TYYVVAHFHYVLS 331
Cdd:MTH00026 373 TYYVVAHFHFVLS 385
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-331 1.01e-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: 416.16  E-value: 1.01e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683   1 QIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPlMLGAPDMAFPRMNNMSFWLLPPSLTLLLTSSTVESGVGTGWTVYPP 80
Cdd:cd00919   41 QLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPP 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683  81 LASGIAHAGASVDLAIFSLHLAGVSSILGAVNFITTTINMKPKNMKPERIPLFVWSIAITALLLLLSLPVLAGAITMLLT 160
Cdd:cd00919  120 LSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLL 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683 161 DRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIICHESGKKeAFGNLGMIFAMLAIGLLGFVVWAHH 240
Cdd:cd00919  200 DRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFSGKP-LFGYKLMVYAFLAIGFLSFLVWAHH 278

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683 241 MFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATMYGTRMTYSAACLWALGFVFLFTMGGLTGVVLANSSIDIVLHDTY 320
Cdd:cd00919  279 MFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTY 358

                        330
                 ....*....|.
gi 767521683 321 YVVAHFHYVLS 331
Cdd:cd00919  359 YVVAHFHYVLS 369
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
3-330 2.15e-138

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 402.58  E-value: 2.15e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683   3 YNVIVTAHAFVMIFFMVMPiMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLTSSTVESGVGTGWTVYPPLA 82
Cdd:COG0843   57 YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLS 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683  83 SGIAHAGASVDLAIFSLHLAGVSSILGAVNFITTTINMKPKNMKPERIPLFVWSIAITALLLLLSLPVLAGAITMLLTDR 162
Cdd:COG0843  136 GLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDR 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683 163 NLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIICHESGKKeAFGNLGMIFAMLAIGLLGFVVWAHHMF 242
Cdd:COG0843  216 SLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMF 294

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683 243 TVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATMYGTRMTYSAACLWALGFVFLFTMGGLTGVVLANSSIDIVLHDTYYV 322
Cdd:COG0843  295 TPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFV 374


                 ....*...
gi 767521683 323 VAHFHYVL 330
Cdd:COG0843  375 VAHFHYVL 382
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 3-330 5.63e-137

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: 397.75  E-value: 5.63e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683    3 YNVIVTAHAFVMIFFMVMPIMiGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLTSSTVESGVGTGWTVYPPLA 82
Cdd:TIGR02891  48 YNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLS 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683   83 SGIAHAGASVDLAIFSLHLAGVSSILGAVNFITTTINMKPKNMKPERIPLFVWSIAITALLLLLSLPVLAGAITMLLTDR 162
Cdd:TIGR02891 127 STSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDR 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683  163 NLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIICHESGKKeAFGNLGMIFAMLAIGLLGFVVWAHHMF 242
Cdd:TIGR02891 207 LFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMF 285

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683  243 TVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATMYGTRMTYSAACLWALGFVFLFTMGGLTGVVLANSSIDIVLHDTYYV 322
Cdd:TIGR02891 286 TTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFV 365


                  ....*...
gi 767521683  323 VAHFHYVL 330
Cdd:TIGR02891 366 VAHFHYVL 373
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 2-331 4.67e-129

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 378.25  E-value: 4.67e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683   2 IYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLTSSTVesGVGTGWTVYPPL 81
Cdd:MTH00048  54 VYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPL 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683  82 ASGIAHAGASVDLAIFSLHLAGVSSILGAVNFITTTINMKPKNMKpERIPLFVWSIAITALLLLLSLPVLAGAITMLLTD 161
Cdd:MTH00048 132 SSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVF-SRTSIILWSYLFTSILLLLSLPVLAAAITMLLFD 210

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683 162 RNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIICHESGKKEAFGNLGMIFAMLAIGLLGFVVWAHHM 241
Cdd:MTH00048 211 RNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHM 290

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683 242 FTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATMYGTRMTYSAACL-WALGFVFLFTMGGLTGVVLANSSIDIVLHDTY 320
Cdd:MTH00048 291 FTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKSDPVVwWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTW 370

                        330
                 ....*....|.
gi 767521683 321 YVVAHFHYVLS 331
Cdd:MTH00048 371 FVVAHFHYVLS 381
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 3-330 5.99e-120

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: 354.58  E-value: 5.99e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683   3 YNVIVTAHAFVMIFFMVMPIMIGgFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLTSSTVESGVGTGWTVYPPLA 82
Cdd:cd01662   49 YNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLS 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683  83 SGIAHAGASVDLAIFSLHLAGVSSILGAVNFITTTINMKPKNMKPERIPLFVWSIAITALLLLLSLPVLAGAITMLLTDR 162
Cdd:cd01662  128 GLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDR 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683 163 NLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIICHESGKKeAFGNLGMIFAMLAIGLLGFVVWAHHMF 242
Cdd:cd01662  208 YFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFSRKP-LFGYRSMVYATVAIGFLSFGVWVHHMF 286

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683 243 TVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATMYGTRMTYSAACLWALGFVFLFTMGGLTGVVLANSSIDIVLHDTYYV 322
Cdd:cd01662  287 TTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFV 366


                 ....*...
gi 767521683 323 VAHFHYVL 330
Cdd:cd01662  367 VAHFHYVL 374
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-330 2.20e-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: 281.77  E-value: 2.20e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683    1 QIYNVIVTAHAFVMIFFMVMPiMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLTSSTvesGVGTGWTVYPP 80
Cdd:pfam00115  39 LTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPP 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683   81 LASgiahagasVDLAIFSLHLAGVSSILGAVNFITTTINMKPKNMKpERIPLFVWSIAITALLLLLSLPVLAGAITMLLT 160
Cdd:pfam00115 115 LVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMT-LRMPLFVWAILATAILILLAFPVLAAALLLLLL 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683  161 DRNLNtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIICHESGKKeAFGNLGMIFAMLAIGLLGFVVWAHH 240
Cdd:pfam00115 186 DRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHH 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683  241 MFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATMYGTRMT-YSAACLWALGFVFLFTMGGLTGVVLANSSIDIVLHDT 319
Cdd:pfam00115 259 LFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRfRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDT 338

                         330
                  ....*....|.
gi 767521683  320 YYVVAHFHYVL 330
Cdd:pfam00115 339 YFVVAHFHYVL 349
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 3-330 1.22e-79

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 255.25  E-value: 1.22e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683   3 YNVIVTAHAFVMIFFMVMPIMIGgFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLTSSTVESGVGTGWTVYPPLA 82
Cdd:PRK15017  99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683  83 SGIAHAGASVDLAIFSLHLAGVSSILGAVNFITTTINMKPKNMKPERIPLFVWSIAITALLLLLSLPVLAGAITMLLTDR 162
Cdd:PRK15017 178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683 163 NLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIICHESgKKEAFGNLGMIFAMLAIGLLGFVVWAHHMF 242
Cdd:PRK15017 258 YLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFF 336

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683 243 TVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATMYGTRMTYSAACLWALGFVFLFTMGGLTGVVLANSSIDIVLHDTYYV 322
Cdd:PRK15017 337 TMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFL 416


                 ....*...
gi 767521683 323 VAHFHYVL 330
Cdd:PRK15017 417 IAHFHNVI 424
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 1-330 8.14e-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: 252.85  E-value: 8.14e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683    1 QIYNVIVTAHAFVMIFFMVMPIMIGgFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLTSSTVESGVGTGWTVYPP 80
Cdd:TIGR02882  90 QHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAP 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683   81 LASGIAHAGASVDLAIFSLHLAGVSSILGAVNFITTTINMKPKNMKPERIPLFVWSIAITALLLLLSLPVLAGAITMLLT 160
Cdd:TIGR02882 169 LAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTT 248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683  161 DRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIICHESgKKEAFGNLGMIFAMLAIGLLGFVVWAHH 240
Cdd:TIGR02882 249 DRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPAFGIYSEIISTFA-QKRLFGYKSMVWSTVGIAFLSFLVWVHH 327

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683  241 MFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATMYGTRMTYSAACLWALGFVFLFTMGGLTGVVLANSSIDIVLHDTY 320
Cdd:TIGR02882 328 FFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTY 407

                         330
                  ....*....|
gi 767521683  321 YVVAHFHYVL 330
Cdd:TIGR02882 408 FLVAHFHYVL 417
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 3-327 1.47e-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: 55.76  E-value: 1.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683   3 YNVIVTAHAFVM-IFFMVMPIMigGFGNWLVPLMLGAPDMAfPRMNNMSFWLLPPSLTLLLTSstVESGVGTG-WTVYPP 80
Cdd:cd01660   44 YYQGLTLHGVLLaIVFTTFFIM--GFFYAIVARALLRSLFN-RRLAWAGFWLMVIGTVMAAVP--ILLGQASVlYTFYPP 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683  81 LasgIAHAGASVDLAIFSlhlagVSSILGAVNFITTTINMKPKNmKPERIPLFVWSIAITALLLLLSLPVLAGAITMLLt 160
Cdd:cd01660  119 L---QAHPLFYIGAALVV-----VGSWISGFAMFVTLWRWKKAN-PGKKVPLATFMVVTTMILWLVASLGVALEVLFQL- 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683 161 drnLNTSFFDpAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIICHESGKKeAFGNLGMIFAMLAIGLLGFVVWAHH 240
Cdd:cd01660  189 ---LPWSLGL-VDTVDVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGK-LFSDPLARLAFILFLLFSTPVGFHH 263

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767521683 241 MFT-VGMDVDTRAYFTSATMIIAVPTGIKIFSWLATM-YGTRMTYSAACLW---------------ALGFVFlFTMGGLT 303
Cdd:cd01660  264 QFAdPGIGPGWKFIHMVLTFMVALPSLLTAFTVFASLeIAGRLRGGKGLFGwiralpwgdpmflalFLAMLM-FIPGGAG 342

                        330       340
                 ....*....|....*....|....
gi 767521683 304 GVVLANSSIDIVLHDTYYVVAHFH 327
Cdd:cd01660  343 GIINASYQLNYVVHNTAWVPGHFH 366
 
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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