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Conserved domains on  [gi|1839330978|gb|QJQ72129|]
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cytochrome c oxidase I, partial (mitochondrion) [Polyarthra cf. major TW-2020]

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 ...
 1-217 6.78e-133

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: 383.06  E-value: 6.78e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839330978   1 AGFIGLSMSLLIRMELGVVGAFLGDEHLYNVLVTAHAFVMIFFMVMPISMGGFGNWLIPLMLGVADMAFPRMNNLSFWLL 80
Cdd:MTH00153   24 SGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839330978  81 VPSFMFLLLSSILDAGVGTGWTVYPPLADAKYHSGISVDLAIFSLHLAGVSSILGSINFLTTIICSRTTKlISMDRLPLL 160
Cdd:MTH00153  104 PPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKG-MTLDRMPLF 182

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1839330978 161 LWAISVTAVLLITSLPVLAGAITMLLTDRNFNTSFFDPSGGGNPILYQHLFWFFGHP 217
Cdd:MTH00153  183 VWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHP 239
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-217 6.78e-133

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 383.06  E-value: 6.78e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839330978   1 AGFIGLSMSLLIRMELGVVGAFLGDEHLYNVLVTAHAFVMIFFMVMPISMGGFGNWLIPLMLGVADMAFPRMNNLSFWLL 80
Cdd:MTH00153   24 SGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839330978  81 VPSFMFLLLSSILDAGVGTGWTVYPPLADAKYHSGISVDLAIFSLHLAGVSSILGSINFLTTIICSRTTKlISMDRLPLL 160
Cdd:MTH00153  104 PPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKG-MTLDRMPLF 182

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1839330978 161 LWAISVTAVLLITSLPVLAGAITMLLTDRNFNTSFFDPSGGGNPILYQHLFWFFGHP 217
Cdd:MTH00153  183 VWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHP 239
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-217 2.53e-129

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: 373.36  E-value: 2.53e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839330978   1 AGFIGLSMSLLIRMELGVVGAFLGDEHLYNVLVTAHAFVMIFFMVMPISMGGFGNWLIPLMLGVADMAFPRMNNLSFWLL 80
Cdd:cd01663    17 SGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLL 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839330978  81 VPSFMFLLLSSILDAGVGTGWTVYPPLADAKYHSGISVDLAIFSLHLAGVSSILGSINFLTTIICSRTTKlISMDRLPLL 160
Cdd:cd01663    97 PPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPG-MTLEKMPLF 175

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1839330978 161 LWAISVTAVLLITSLPVLAGAITMLLTDRNFNTSFFDPSGGGNPILYQHLFWFFGHP 217
Cdd:cd01663   176 VWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHP 232
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-217 4.44e-77

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 240.80  E-value: 4.44e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839330978   1 AGFIGLSMSLLIRMELGVVGAFLGDEHLYNVLVTAHAFVMIFFMVMPIsMGGFGNWLIPLMLGVADMAFPRMNNLSFWLL 80
Cdd:COG0843    29 FLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPF-LAGFGNYLVPLQIGARDMAFPRLNALSFWLY 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839330978  81 VPSFMFLLLSSILDAGVGTGWTVYPPLADAKYHSGISVDLAIFSLHLAGVSSILGSINFLTTIICSRtTKLISMDRLPLL 160
Cdd:COG0843   108 LFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMR-APGMTLMRMPLF 186

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1839330978 161 LWAISVTAVLLITSLPVLAGAITMLLTDRNFNTSFFDPSGGGNPILYQHLFWFFGHP 217
Cdd:COG0843   187 TWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHP 243
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-217 4.97e-77

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: 239.82  E-value: 4.97e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839330978   1 AGFIGLSMSLLIRMELGVVGAFLGDEHLYNVLVTAHAFVMIFFMVMPIsMGGFGNWLIPLMLGVADMAFPRMNNLSFWLL 80
Cdd:TIGR02891  20 FFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPI-LAGFGNYLLPLMIGARDMAFPRLNAFSYWLY 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839330978  81 VPSFMFLLLSSILDAGVGTGWTVYPPLADAKYHSGISVDLAIFSLHLAGVSSILGSINFLTTIICSRTtKLISMDRLPLL 160
Cdd:TIGR02891  99 LFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRA-PGMTLMRMPLF 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1839330978 161 LWAISVTAVLLITSLPVLAGAITMLLTDRNFNTSFFDPSGGGNPILYQHLFWFFGHP 217
Cdd:TIGR02891 178 VWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHP 234
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-217 8.67e-46

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: 156.96  E-value: 8.67e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839330978   1 AGFIGLSMSLLIRMELGVVGAFLGDEHLYNVLVTAHAFVMIFFMVMPIsMGGFGNWLIPLMLGVADMAFPRMNNLSFWLL 80
Cdd:pfam00115  13 WFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRLNALSFWLV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839330978  81 VPSFMFLLLSsilDAGVGTGWTVYPPLadakyhsgISVDLAIFSLHLAGVSSILGSINFLTTIICSRTTKLisMDRLPLL 160
Cdd:pfam00115  92 VLGAVLLLAS---FGGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGM--TLRMPLF 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1839330978 161 LWAISVTAVLLITSLPVLAGAITMLLTDRNFNTsffdpsGGGNPILYQHLFWFFGHP 217
Cdd:pfam00115 159 VWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHP 209
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-217 6.78e-133

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 383.06  E-value: 6.78e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839330978   1 AGFIGLSMSLLIRMELGVVGAFLGDEHLYNVLVTAHAFVMIFFMVMPISMGGFGNWLIPLMLGVADMAFPRMNNLSFWLL 80
Cdd:MTH00153   24 SGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839330978  81 VPSFMFLLLSSILDAGVGTGWTVYPPLADAKYHSGISVDLAIFSLHLAGVSSILGSINFLTTIICSRTTKlISMDRLPLL 160
Cdd:MTH00153  104 PPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKG-MTLDRMPLF 182

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1839330978 161 LWAISVTAVLLITSLPVLAGAITMLLTDRNFNTSFFDPSGGGNPILYQHLFWFFGHP 217
Cdd:MTH00153  183 VWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHP 239
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-217 2.53e-129

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: 373.36  E-value: 2.53e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839330978   1 AGFIGLSMSLLIRMELGVVGAFLGDEHLYNVLVTAHAFVMIFFMVMPISMGGFGNWLIPLMLGVADMAFPRMNNLSFWLL 80
Cdd:cd01663    17 SGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLL 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839330978  81 VPSFMFLLLSSILDAGVGTGWTVYPPLADAKYHSGISVDLAIFSLHLAGVSSILGSINFLTTIICSRTTKlISMDRLPLL 160
Cdd:cd01663    97 PPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPG-MTLEKMPLF 175

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1839330978 161 LWAISVTAVLLITSLPVLAGAITMLLTDRNFNTSFFDPSGGGNPILYQHLFWFFGHP 217
Cdd:cd01663   176 VWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHP 232
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-217 1.44e-120

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 351.59  E-value: 1.44e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839330978   1 AGFIGLSMSLLIRMELGVVGAFLGDEHLYNVLVTAHAFVMIFFMVMPISMGGFGNWLIPLMLGVADMAFPRMNNLSFWLL 80
Cdd:MTH00223   23 SGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLL 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839330978  81 VPSFMFLLLSSILDAGVGTGWTVYPPLADAKYHSGISVDLAIFSLHLAGVSSILGSINFLTTIICSRtTKLISMDRLPLL 160
Cdd:MTH00223  103 PPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMR-SPGMQLERLPLF 181

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1839330978 161 LWAISVTAVLLITSLPVLAGAITMLLTDRNFNTSFFDPSGGGNPILYQHLFWFFGHP 217
Cdd:MTH00223  182 VWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHP 238
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-217 9.11e-119

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 347.05  E-value: 9.11e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839330978   1 AGFIGLSMSLLIRMELGVVGAFLGDEHLYNVLVTAHAFVMIFFMVMPISMGGFGNWLIPLMLGVADMAFPRMNNLSFWLL 80
Cdd:MTH00167   26 AGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839330978  81 VPSFMFLLLSSILDAGVGTGWTVYPPLADAKYHSGISVDLAIFSLHLAGVSSILGSINFLTTIICSRtTKLISMDRLPLL 160
Cdd:MTH00167  106 PPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMK-PPGITQYQTPLF 184

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1839330978 161 LWAISVTAVLLITSLPVLAGAITMLLTDRNFNTSFFDPSGGGNPILYQHLFWFFGHP 217
Cdd:MTH00167  185 VWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 241
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-217 3.00e-113

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 333.21  E-value: 3.00e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839330978   1 AGFIGLSMSLLIRMELGVVGAFLGDEHLYNVLVTAHAFVMIFFMVMPISMGGFGNWLIPLMLGVADMAFPRMNNLSFWLL 80
Cdd:MTH00116   26 AGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839330978  81 VPSFMFLLLSSILDAGVGTGWTVYPPLADAKYHSGISVDLAIFSLHLAGVSSILGSINFLTTIIcSRTTKLISMDRLPLL 160
Cdd:MTH00116  106 PPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCI-NMKPPAMSQYQTPLF 184

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1839330978 161 LWAISVTAVLLITSLPVLAGAITMLLTDRNFNTSFFDPSGGGNPILYQHLFWFFGHP 217
Cdd:MTH00116  185 VWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 241
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-217 6.91e-111

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 327.07  E-value: 6.91e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839330978   1 AGFIGLSMSLLIRMELGVVGAFLGDEHLYNVLVTAHAFVMIFFMVMPISMGGFGNWLIPLMLGVADMAFPRMNNLSFWLL 80
Cdd:MTH00142   24 AGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839330978  81 VPSFMFLLLSSILDAGVGTGWTVYPPLADAKYHSGISVDLAIFSLHLAGVSSILGSINFLTTIICSRtTKLISMDRLPLL 160
Cdd:MTH00142  104 PPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMR-AGGMKFERVPLF 182

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1839330978 161 LWAISVTAVLLITSLPVLAGAITMLLTDRNFNTSFFDPSGGGNPILYQHLFWFFGHP 217
Cdd:MTH00142  183 VWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHP 239
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-217 1.74e-101

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 302.96  E-value: 1.74e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839330978   1 AGFIGLSMSLLIRMELGVVGAFLGDEHLYNVLVTAHAFVMIFFMVMPISMGGFGNWLIPLMLGVADMAFPRMNNLSFWLL 80
Cdd:MTH00103   26 AGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839330978  81 VPSFMFLLLSSILDAGVGTGWTVYPPLADAKYHSGISVDLAIFSLHLAGVSSILGSINFLTTIICSRTTKLiSMDRLPLL 160
Cdd:MTH00103  106 PPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAM-SQYQTPLF 184

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1839330978 161 LWAISVTAVLLITSLPVLAGAITMLLTDRNFNTSFFDPSGGGNPILYQHLFWFFGHP 217
Cdd:MTH00103  185 VWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 241
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-217 7.38e-101

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 301.44  E-value: 7.38e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839330978   1 AGFIGLSMSLLIRMELGVVGAFLGDEHLYNVLVTAHAFVMIFFMVMPISMGGFGNWLIPLMLGVADMAFPRMNNLSFWLL 80
Cdd:MTH00007   23 GGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLL 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839330978  81 VPSFMFLLLSSILDAGVGTGWTVYPPLADAKYHSGISVDLAIFSLHLAGVSSILGSINFLTTIICSRTTKLiSMDRLPLL 160
Cdd:MTH00007  103 PPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGL-RLERIPLF 181

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1839330978 161 LWAISVTAVLLITSLPVLAGAITMLLTDRNFNTSFFDPSGGGNPILYQHLFWFFGHP 217
Cdd:MTH00007  182 VWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHP 238
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-217 9.98e-100

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 298.76  E-value: 9.98e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839330978   1 AGFIGLSMSLLIRMELGVVGAFLGDEHLYNVLVTAHAFVMIFFMVMPISMGGFGNWLIPLMLGVADMAFPRMNNLSFWLL 80
Cdd:MTH00183   26 AGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839330978  81 VPSFMFLLLSSILDAGVGTGWTVYPPLADAKYHSGISVDLAIFSLHLAGVSSILGSINFLTTIICSRTTKlISMDRLPLL 160
Cdd:MTH00183  106 PPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPA-ISQYQTPLF 184

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1839330978 161 LWAISVTAVLLITSLPVLAGAITMLLTDRNFNTSFFDPSGGGNPILYQHLFWFFGHP 217
Cdd:MTH00183  185 VWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 241
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-217 2.44e-99

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 297.90  E-value: 2.44e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839330978   1 AGFIGLSMSLLIRMELGVVGAFLGDEHLYNVLVTAHAFVMIFFMVMPISMGGFGNWLIPLMLGVADMAFPRMNNLSFWLL 80
Cdd:MTH00037   26 AGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLI 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839330978  81 VPSFMFLLLSSILDAGVGTGWTVYPPLADAKYHSGISVDLAIFSLHLAGVSSILGSINFLTTIICSRTTKlISMDRLPLL 160
Cdd:MTH00037  106 PPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPG-MTFDRLPLF 184

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1839330978 161 LWAISVTAVLLITSLPVLAGAITMLLTDRNFNTSFFDPSGGGNPILYQHLFWFFGHP 217
Cdd:MTH00037  185 VWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHP 241
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-217 3.61e-99

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 297.24  E-value: 3.61e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839330978   1 AGFIGLSMSLLIRMELGVVGAFLGDEHLYNVLVTAHAFVMIFFMVMPISMGGFGNWLIPLMLGVADMAFPRMNNLSFWLL 80
Cdd:MTH00077   26 AGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839330978  81 VPSFMFLLLSSILDAGVGTGWTVYPPLADAKYHSGISVDLAIFSLHLAGVSSILGSINFLTTIICSRTTKlISMDRLPLL 160
Cdd:MTH00077  106 PPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPS-MSQYQTPLF 184

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1839330978 161 LWAISVTAVLLITSLPVLAGAITMLLTDRNFNTSFFDPSGGGNPILYQHLFWFFGHP 217
Cdd:MTH00077  185 VWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHP 241
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-217 3.42e-98

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 295.19  E-value: 3.42e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839330978   1 AGFIGLSMSLLIRMELGVVGAFLGDEHLYNVLVTAHAFVMIFFMVMPISMGGFGNWLIPLMLGVADMAFPRMNNLSFWLL 80
Cdd:MTH00182   28 AGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLL 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839330978  81 VPSFMFLLLSSILDAGVGTGWTVYPPLADAKYHSGISVDLAIFSLHLAGVSSILGSINFLTTIICSRTTKlISMDRLPLL 160
Cdd:MTH00182  108 PPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPG-VTFNRLPLF 186

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1839330978 161 LWAISVTAVLLITSLPVLAGAITMLLTDRNFNTSFFDPSGGGNPILYQHLFWFFGHP 217
Cdd:MTH00182  187 VWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHP 243
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-217 5.77e-98

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 294.43  E-value: 5.77e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839330978   1 AGFIGLSMSLLIRMELGVVGAFLGDEHLYNVLVTAHAFVMIFFMVMPISMGGFGNWLIPLMLGVADMAFPRMNNLSFWLL 80
Cdd:MTH00184   28 AGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLL 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839330978  81 VPSFMFLLLSSILDAGVGTGWTVYPPLADAKYHSGISVDLAIFSLHLAGVSSILGSINFLTTIICSRTTKlISMDRLPLL 160
Cdd:MTH00184  108 PPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPG-ITMDRMPLF 186

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1839330978 161 LWAISVTAVLLITSLPVLAGAITMLLTDRNFNTSFFDPSGGGNPILYQHLFWFFGHP 217
Cdd:MTH00184  187 VWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHP 243
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-217 9.56e-94

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 283.11  E-value: 9.56e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839330978   1 AGFIGLSMSLLIRMELGVVGAFLGDEHLYNVLVTAHAFVMIFFMVMPISMGGFGNWLIPLMLGVADMAFPRMNNLSFWLL 80
Cdd:MTH00079   27 SGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839330978  81 VPSFMFLLLSSILDAGVGTGWTVYPPLAdAKYHSGISVDLAIFSLHLAGVSSILGSINFLTTIICSRtTKLISMDRLPLL 160
Cdd:MTH00079  107 PTSLFLILDSCFVDMGPGTSWTVYPPLS-TLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLR-SSSISLEHMSLF 184

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1839330978 161 LWAISVTAVLLITSLPVLAGAITMLLTDRNFNTSFFDPSGGGNPILYQHLFWFFGHP 217
Cdd:MTH00079  185 VWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHP 241
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-217 1.28e-88

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 270.73  E-value: 1.28e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839330978   1 AGFIGLSMSLLIRMELGVVGAFLGDEHLYNVLVTAHAFVMIFFMVMPISMGGFGNWLIPLMLGVADMAFPRMNNLSFWLL 80
Cdd:MTH00026   27 SGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839330978  81 VPSFMFLLLSSILDAGVGTGWTVYPPLADAKYHSGISVDLAIFSLHLAGVSSILGSINFLTTIICSRTTKLiSMDRLPLL 160
Cdd:MTH00026  107 PPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGM-TMSRIPLF 185

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1839330978 161 LWAISVTAVLLITSLPVLAGAITMLLTDRNFNTSFFDPSGGGNPILYQHLFWFFGHP 217
Cdd:MTH00026  186 VWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHP 242
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-217 3.49e-82

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: 252.07  E-value: 3.49e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839330978   1 AGFIGLSMSLLIRMELGVVGAFLGDEHLYNVLVTAHAFVMIFFMVMPISMGGFGNWLIPlMLGVADMAFPRMNNLSFWLL 80
Cdd:cd00919    15 ALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWLF 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839330978  81 VPSFMFLLLSSILDAGVGTGWTVYPPLADAKYHSGISVDLAIFSLHLAGVSSILGSINFLTTIICSRtTKLISMDRLPLL 160
Cdd:cd00919    94 PPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMR-APGMTLDKMPLF 172

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1839330978 161 LWAISVTAVLLITSLPVLAGAITMLLTDRNFNTSFFDPSGGGNPILYQHLFWFFGHP 217
Cdd:cd00919   173 VWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHP 229
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-217 4.44e-77

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 240.80  E-value: 4.44e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839330978   1 AGFIGLSMSLLIRMELGVVGAFLGDEHLYNVLVTAHAFVMIFFMVMPIsMGGFGNWLIPLMLGVADMAFPRMNNLSFWLL 80
Cdd:COG0843    29 FLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPF-LAGFGNYLVPLQIGARDMAFPRLNALSFWLY 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839330978  81 VPSFMFLLLSSILDAGVGTGWTVYPPLADAKYHSGISVDLAIFSLHLAGVSSILGSINFLTTIICSRtTKLISMDRLPLL 160
Cdd:COG0843   108 LFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMR-APGMTLMRMPLF 186

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1839330978 161 LWAISVTAVLLITSLPVLAGAITMLLTDRNFNTSFFDPSGGGNPILYQHLFWFFGHP 217
Cdd:COG0843   187 TWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHP 243
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-217 4.86e-77

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 240.35  E-value: 4.86e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839330978   1 AGFIGLSMSLLIRMELGVVGAFLGDEHLYNVLVTAHAFVMIFFMVMPISMGGFGNWLIPLMLGVADMAFPRMNNLSFWLL 80
Cdd:MTH00048   27 SGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839330978  81 VPSFMFLLLSSILdaGVGTGWTVYPPLADAKYHSGISVDLAIFSLHLAGVSSILGSINFLTTIICSRTTKLISmdRLPLL 160
Cdd:MTH00048  107 VPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFS--RTSII 182

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1839330978 161 LWAISVTAVLLITSLPVLAGAITMLLTDRNFNTSFFDPSGGGNPILYQHLFWFFGHP 217
Cdd:MTH00048  183 LWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHP 239
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-217 4.97e-77

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: 239.82  E-value: 4.97e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839330978   1 AGFIGLSMSLLIRMELGVVGAFLGDEHLYNVLVTAHAFVMIFFMVMPIsMGGFGNWLIPLMLGVADMAFPRMNNLSFWLL 80
Cdd:TIGR02891  20 FFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPI-LAGFGNYLLPLMIGARDMAFPRLNAFSYWLY 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839330978  81 VPSFMFLLLSSILDAGVGTGWTVYPPLADAKYHSGISVDLAIFSLHLAGVSSILGSINFLTTIICSRTtKLISMDRLPLL 160
Cdd:TIGR02891  99 LFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRA-PGMTLMRMPLF 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1839330978 161 LWAISVTAVLLITSLPVLAGAITMLLTDRNFNTSFFDPSGGGNPILYQHLFWFFGHP 217
Cdd:TIGR02891 178 VWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHP 234
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 3-217 1.27e-62

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: 202.43  E-value: 1.27e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839330978   3 FIGLSMSLLIRMELGVVGAFLGDEHLYNVLVTAHAFVMIFFMVMPIsMGGFGNWLIPLMLGVADMAFPRMNNLSFWLLVP 82
Cdd:cd01662    23 LRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPL-VFGLMNYLVPLQIGARDVAFPRLNALSFWLFLF 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839330978  83 SFMFLLLSSILDAGVGTGWTVYPPLADAKYHSGISVDLAIFSLHLAGVSSILGSINFLTTIICSRtTKLISMDRLPLLLW 162
Cdd:cd01662   102 GGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMR-APGMTLMRMPIFTW 180

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1839330978 163 AISVTAVLLITSLPVLAGAITMLLTDRNFNTSFFDPSGGGNPILYQHLFWFFGHP 217
Cdd:cd01662   181 TTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHP 235
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-217 8.67e-46

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: 156.96  E-value: 8.67e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839330978   1 AGFIGLSMSLLIRMELGVVGAFLGDEHLYNVLVTAHAFVMIFFMVMPIsMGGFGNWLIPLMLGVADMAFPRMNNLSFWLL 80
Cdd:pfam00115  13 WFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRLNALSFWLV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839330978  81 VPSFMFLLLSsilDAGVGTGWTVYPPLadakyhsgISVDLAIFSLHLAGVSSILGSINFLTTIICSRTTKLisMDRLPLL 160
Cdd:pfam00115  92 VLGAVLLLAS---FGGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGM--TLRMPLF 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1839330978 161 LWAISVTAVLLITSLPVLAGAITMLLTDRNFNTsffdpsGGGNPILYQHLFWFFGHP 217
Cdd:pfam00115 159 VWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHP 209
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 27-217 4.53e-39

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 142.00  E-value: 4.53e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839330978  27 HLYNVLVTAHAFVMIFFMVMPISMGgFGNWLIPLMLGVADMAFPRMNNLSFWLLVPSFMFLLLSSILDAGVGTGWTVYPP 106
Cdd:PRK15017   97 HHYDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPP 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839330978 107 LADAKYHSGISVDLAIFSLHLAGVSSILGSINFLTTIICSRTTKLiSMDRLPLLLWAISVTAVLLITSLPVLAGAITMLL 186
Cdd:PRK15017  176 LSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGM-TMFKMPVFTWASLCANVLIIASFPILTVTVALLT 254

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1839330978 187 TDRNFNTSFFDPSGGGNPILYQHLFWFFGHP 217
Cdd:PRK15017  255 LDRYLGTHFFTNDMGGNMMMYINLIWAWGHP 285
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 9-217 3.20e-38

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: 139.60  E-value: 3.20e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839330978   9 SLLIRMELGVVGAFLGDEHLYNVLVTAHAFVMIFFMVMPISMGgFGNWLIPLMLGVADMAFPRMNNLSFWLLVPSFMFLL 88
Cdd:TIGR02882  72 ALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFN 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839330978  89 LSSILDAGVGTGWTVYPPLADAKYHSGISVDLAIFSLHLAGVSSILGSINFLTTIICSRTTKLISMdRLPLLLWAISVTA 168
Cdd:TIGR02882 151 ISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLM-QMPMFTWTTLITT 229

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1839330978 169 VLLITSLPVLAGAITMLLTDRNFNTSFFDPSGGGNPILYQHLFWFFGHP 217
Cdd:TIGR02882 230 LIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHP 278
 
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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