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Conserved domains on  [gi|1511240158|gb|AYU74984|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Oecanthus similator]

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 ...
 1-219 1.56e-141

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: 405.02  E-value: 1.56e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511240158   1 ILYFIFGFWSGMVGTSLSMIIRMELGQPGFFIGDDQTYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:MTH00153   15 TLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511240158  81 MNNMSFWLLPPSLMLLMSSSMVESGAGTGWTVYPPLSSGIAHGGASVDLAIFSLHLAGISSILGAVNFITTMMNMRSPNM 160
Cdd:MTH00153   95 MNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGM 174

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1511240158 161 SLDQTPLFVWAVSITALLLLLSLPVLAGAITMLLCDRNLNTSFFDPAGGGDPILYQHLF 219
Cdd:MTH00153  175 TLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 233
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-219 1.56e-141

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 405.02  E-value: 1.56e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511240158   1 ILYFIFGFWSGMVGTSLSMIIRMELGQPGFFIGDDQTYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:MTH00153   15 TLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511240158  81 MNNMSFWLLPPSLMLLMSSSMVESGAGTGWTVYPPLSSGIAHGGASVDLAIFSLHLAGISSILGAVNFITTMMNMRSPNM 160
Cdd:MTH00153   95 MNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGM 174

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1511240158 161 SLDQTPLFVWAVSITALLLLLSLPVLAGAITMLLCDRNLNTSFFDPAGGGDPILYQHLF 219
Cdd:MTH00153  175 TLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 233
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-219 3.44e-127

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: 367.58  E-value: 3.44e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511240158   1 ILYFIFGFWSGMVGTSLSMIIRMELGQPGFFIGDDQTYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:cd01663     8 TLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPR 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511240158  81 MNNMSFWLLPPSLMLLMSSSMVESGAGTGWTVYPPLSSGIAHGGASVDLAIFSLHLAGISSILGAVNFITTMMNMRSPNM 160
Cdd:cd01663    88 LNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGM 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1511240158 161 SLDQTPLFVWAVSITALLLLLSLPVLAGAITMLLCDRNLNTSFFDPAGGGDPILYQHLF 219
Cdd:cd01663   168 TLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 226
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-219 9.43e-71

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 224.62  E-value: 9.43e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511240158   1 ILYFIFGFWSGMVGTSLSMIIRMELGQPGFFIGDDQTYNVIVTAHAFIMIFFMVMPiMIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:COG0843    20 IMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPR 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511240158  81 MNNMSFWLLPPSLMLLMSSSMVESGAGTGWTVYPPLSSGIAHGGASVDLAIFSLHLAGISSILGAVNFITTMMNMRSPNM 160
Cdd:COG0843    99 LNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGM 178

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1511240158 161 SLDQTPLFVWAVSITALLLLLSLPVLAGAITMLLCDRNLNTSFFDPAGGGDPILYQHLF 219
Cdd:COG0843   179 TLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLF 237
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-219 9.03e-43

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: 148.88  E-value: 9.03e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511240158   1 ILYFIFGFWSGMVGTSLSMIIRMELGQPGFFIGDDQTYNVIVTAHAFIMIFFMVMPiMIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:pfam00115   4 LLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511240158  81 MNNMSFWLLPPSLMLLMSSSMvesGAGTGWTVYPPLssgiahggASVDLAIFSLHLAGISSILGAVNFITTMMNMRSPNM 160
Cdd:pfam00115  83 LNALSFWLVVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGM 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1511240158 161 SLdQTPLFVWAVSITALLLLLSLPVLAGAITMLLCDRNLNtsffdpAGGGDPILYQHLF 219
Cdd:pfam00115 152 TL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLF 203
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 1-219 1.44e-31

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: 121.11  E-value: 1.44e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511240158   1 ILYFIFGFWSGMVGTSLSMIIRMELGQPGFFIGDDQTYNVIVTAHAFIMIFFMVMPIMIGgFGNWLVPLMLGAPDMAFPR 80
Cdd:TIGR02882  55 VMYIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPV 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511240158  81 MNNMSFWLLPPSLMLLMSSSMVESGAGTGWTVYPPLSSGIAHGGASVDLAIFSLHLAGISSILGAVNFITTMMNMRSPNM 160
Cdd:TIGR02882 134 LNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGM 213

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1511240158 161 SLDQTPLFVWAVSITALLLLLSLPVLAGAITMLLCDRNLNTSFFDPAGGGDPILYQHLF 219
Cdd:TIGR02882 214 KLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLF 272
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-219 1.56e-141

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 405.02  E-value: 1.56e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511240158   1 ILYFIFGFWSGMVGTSLSMIIRMELGQPGFFIGDDQTYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:MTH00153   15 TLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511240158  81 MNNMSFWLLPPSLMLLMSSSMVESGAGTGWTVYPPLSSGIAHGGASVDLAIFSLHLAGISSILGAVNFITTMMNMRSPNM 160
Cdd:MTH00153   95 MNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGM 174

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1511240158 161 SLDQTPLFVWAVSITALLLLLSLPVLAGAITMLLCDRNLNTSFFDPAGGGDPILYQHLF 219
Cdd:MTH00153  175 TLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 233
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-219 3.44e-127

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: 367.58  E-value: 3.44e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511240158   1 ILYFIFGFWSGMVGTSLSMIIRMELGQPGFFIGDDQTYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:cd01663     8 TLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPR 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511240158  81 MNNMSFWLLPPSLMLLMSSSMVESGAGTGWTVYPPLSSGIAHGGASVDLAIFSLHLAGISSILGAVNFITTMMNMRSPNM 160
Cdd:cd01663    88 LNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGM 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1511240158 161 SLDQTPLFVWAVSITALLLLLSLPVLAGAITMLLCDRNLNTSFFDPAGGGDPILYQHLF 219
Cdd:cd01663   168 TLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 226
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 2-219 5.21e-121

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 352.83  E-value: 5.21e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511240158   2 LYFIFGFWSGMVGTSLSMIIRMELGQPGFFIGDDQTYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRM 81
Cdd:MTH00167   18 LYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRM 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511240158  82 NNMSFWLLPPSLMLLMSSSMVESGAGTGWTVYPPLSSGIAHGGASVDLAIFSLHLAGISSILGAVNFITTMMNMRSPNMS 161
Cdd:MTH00167   98 NNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGIT 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1511240158 162 LDQTPLFVWAVSITALLLLLSLPVLAGAITMLLCDRNLNTSFFDPAGGGDPILYQHLF 219
Cdd:MTH00167  178 QYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 2-219 1.97e-119

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 349.01  E-value: 1.97e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511240158   2 LYFIFGFWSGMVGTSLSMIIRMELGQPGFFIGDDQTYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRM 81
Cdd:MTH00116   18 LYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRM 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511240158  82 NNMSFWLLPPSLMLLMSSSMVESGAGTGWTVYPPLSSGIAHGGASVDLAIFSLHLAGISSILGAVNFITTMMNMRSPNMS 161
Cdd:MTH00116   98 NNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMS 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1511240158 162 LDQTPLFVWAVSITALLLLLSLPVLAGAITMLLCDRNLNTSFFDPAGGGDPILYQHLF 219
Cdd:MTH00116  178 QYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 2-219 2.80e-118

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 345.81  E-value: 2.80e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511240158   2 LYFIFGFWSGMVGTSLSMIIRMELGQPGFFIGDDQTYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRM 81
Cdd:MTH00223   15 LYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRL 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511240158  82 NNMSFWLLPPSLMLLMSSSMVESGAGTGWTVYPPLSSGIAHGGASVDLAIFSLHLAGISSILGAVNFITTMMNMRSPNMS 161
Cdd:MTH00223   95 NNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQ 174

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1511240158 162 LDQTPLFVWAVSITALLLLLSLPVLAGAITMLLCDRNLNTSFFDPAGGGDPILYQHLF 219
Cdd:MTH00223  175 LERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 232
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 2-219 7.06e-117

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 342.47  E-value: 7.06e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511240158   2 LYFIFGFWSGMVGTSLSMIIRMELGQPGFFIGDDQTYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRM 81
Cdd:MTH00142   16 LYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRM 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511240158  82 NNMSFWLLPPSLMLLMSSSMVESGAGTGWTVYPPLSSGIAHGGASVDLAIFSLHLAGISSILGAVNFITTMMNMRSPNMS 161
Cdd:MTH00142   96 NNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMK 175

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1511240158 162 LDQTPLFVWAVSITALLLLLSLPVLAGAITMLLCDRNLNTSFFDPAGGGDPILYQHLF 219
Cdd:MTH00142  176 FERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 233
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 2-219 1.42e-106

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 316.39  E-value: 1.42e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511240158   2 LYFIFGFWSGMVGTSLSMIIRMELGQPGFFIGDDQTYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRM 81
Cdd:MTH00037   18 LYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRM 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511240158  82 NNMSFWLLPPSLMLLMSSSMVESGAGTGWTVYPPLSSGIAHGGASVDLAIFSLHLAGISSILGAVNFITTMMNMRSPNMS 161
Cdd:MTH00037   98 NNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMT 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1511240158 162 LDQTPLFVWAVSITALLLLLSLPVLAGAITMLLCDRNLNTSFFDPAGGGDPILYQHLF 219
Cdd:MTH00037  178 FDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLF 235
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 2-219 1.15e-105

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 313.78  E-value: 1.15e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511240158   2 LYFIFGFWSGMVGTSLSMIIRMELGQPGFFIGDDQTYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRM 81
Cdd:MTH00183   18 LYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRM 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511240158  82 NNMSFWLLPPSLMLLMSSSMVESGAGTGWTVYPPLSSGIAHGGASVDLAIFSLHLAGISSILGAVNFITTMMNMRSPNMS 161
Cdd:MTH00183   98 NNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAIS 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1511240158 162 LDQTPLFVWAVSITALLLLLSLPVLAGAITMLLCDRNLNTSFFDPAGGGDPILYQHLF 219
Cdd:MTH00183  178 QYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 2-219 1.61e-105

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 313.36  E-value: 1.61e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511240158   2 LYFIFGFWSGMVGTSLSMIIRMELGQPGFFIGDDQTYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRM 81
Cdd:MTH00103   18 LYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRM 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511240158  82 NNMSFWLLPPSLMLLMSSSMVESGAGTGWTVYPPLSSGIAHGGASVDLAIFSLHLAGISSILGAVNFITTMMNMRSPNMS 161
Cdd:MTH00103   98 NNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMS 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1511240158 162 LDQTPLFVWAVSITALLLLLSLPVLAGAITMLLCDRNLNTSFFDPAGGGDPILYQHLF 219
Cdd:MTH00103  178 QYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 2-219 2.92e-105

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 312.65  E-value: 2.92e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511240158   2 LYFIFGFWSGMVGTSLSMIIRMELGQPGFFIGDDQTYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRM 81
Cdd:MTH00077   18 LYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRM 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511240158  82 NNMSFWLLPPSLMLLMSSSMVESGAGTGWTVYPPLSSGIAHGGASVDLAIFSLHLAGISSILGAVNFITTMMNMRSPNMS 161
Cdd:MTH00077   98 NNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMS 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1511240158 162 LDQTPLFVWAVSITALLLLLSLPVLAGAITMLLCDRNLNTSFFDPAGGGDPILYQHLF 219
Cdd:MTH00077  178 QYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLF 235
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 2-219 8.68e-105

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 311.45  E-value: 8.68e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511240158   2 LYFIFGFWSGMVGTSLSMIIRMELGQPGFFIGDDQTYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRM 81
Cdd:MTH00007   15 LYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRL 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511240158  82 NNMSFWLLPPSLMLLMSSSMVESGAGTGWTVYPPLSSGIAHGGASVDLAIFSLHLAGISSILGAVNFITTMMNMRSPNMS 161
Cdd:MTH00007   95 NNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLR 174

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1511240158 162 LDQTPLFVWAVSITALLLLLSLPVLAGAITMLLCDRNLNTSFFDPAGGGDPILYQHLF 219
Cdd:MTH00007  175 LERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 232
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 2-219 2.12e-97

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 292.35  E-value: 2.12e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511240158   2 LYFIFGFWSGMVGTSLSMIIRMELGQPGFFIGDDQTYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRM 81
Cdd:MTH00079   19 LYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511240158  82 NNMSFWLLPPSLMLLMSSSMVESGAGTGWTVYPPLSSgIAHGGASVDLAIFSLHLAGISSILGAVNFITTMMNMRSPNMS 161
Cdd:MTH00079   99 NNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSIS 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1511240158 162 LDQTPLFVWAVSITALLLLLSLPVLAGAITMLLCDRNLNTSFFDPAGGGDPILYQHLF 219
Cdd:MTH00079  178 LEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLF 235
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 2-219 1.15e-96

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 290.95  E-value: 1.15e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511240158   2 LYFIFGFWSGMVGTSLSMIIRMELGQPGFFIGDDQTYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRM 81
Cdd:MTH00182   20 LYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511240158  82 NNMSFWLLPPSLMLLMSSSMVESGAGTGWTVYPPLSSGIAHGGASVDLAIFSLHLAGISSILGAVNFITTMMNMRSPNMS 161
Cdd:MTH00182  100 NNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVT 179

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1511240158 162 LDQTPLFVWAVSITALLLLLSLPVLAGAITMLLCDRNLNTSFFDPAGGGDPILYQHLF 219
Cdd:MTH00182  180 FNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLF 237
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 2-219 3.63e-96

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 289.80  E-value: 3.63e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511240158   2 LYFIFGFWSGMVGTSLSMIIRMELGQPGFFIGDDQTYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRM 81
Cdd:MTH00184   20 LYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511240158  82 NNMSFWLLPPSLMLLMSSSMVESGAGTGWTVYPPLSSGIAHGGASVDLAIFSLHLAGISSILGAVNFITTMMNMRSPNMS 161
Cdd:MTH00184  100 NNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGIT 179

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1511240158 162 LDQTPLFVWAVSITALLLLLSLPVLAGAITMLLCDRNLNTSFFDPAGGGDPILYQHLF 219
Cdd:MTH00184  180 MDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLF 237
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 2-219 5.47e-88

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 269.19  E-value: 5.47e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511240158   2 LYFIFGFWSGMVGTSLSMIIRMELGQPGFFIGDDQTYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRM 81
Cdd:MTH00026   19 LYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511240158  82 NNMSFWLLPPSLMLLMSSSMVESGAGTGWTVYPPLSSGIAHGGASVDLAIFSLHLAGISSILGAVNFITTMMNMRSPNMS 161
Cdd:MTH00026   99 NNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMT 178

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1511240158 162 LDQTPLFVWAVSITALLLLLSLPVLAGAITMLLCDRNLNTSFFDPAGGGDPILYQHLF 219
Cdd:MTH00026  179 MSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLF 236
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-219 9.88e-80

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: 245.90  E-value: 9.88e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511240158   1 ILYFIFGFWSGMVGTSLSMIIRMELGQPGFFIGDDQTYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPlMLGAPDMAFPR 80
Cdd:cd00919     6 LLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511240158  81 MNNMSFWLLPPSLMLLMSSSMVESGAGTGWTVYPPLSSGIAHGGASVDLAIFSLHLAGISSILGAVNFITTMMNMRSPNM 160
Cdd:cd00919    85 LNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGM 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1511240158 161 SLDQTPLFVWAVSITALLLLLSLPVLAGAITMLLCDRNLNTSFFDPAGGGDPILYQHLF 219
Cdd:cd00919   165 TLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLF 223
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-219 9.43e-71

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 224.62  E-value: 9.43e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511240158   1 ILYFIFGFWSGMVGTSLSMIIRMELGQPGFFIGDDQTYNVIVTAHAFIMIFFMVMPiMIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:COG0843    20 IMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPR 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511240158  81 MNNMSFWLLPPSLMLLMSSSMVESGAGTGWTVYPPLSSGIAHGGASVDLAIFSLHLAGISSILGAVNFITTMMNMRSPNM 160
Cdd:COG0843    99 LNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGM 178

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1511240158 161 SLDQTPLFVWAVSITALLLLLSLPVLAGAITMLLCDRNLNTSFFDPAGGGDPILYQHLF 219
Cdd:COG0843   179 TLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLF 237
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-219 8.69e-65

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 208.38  E-value: 8.69e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511240158   1 ILYFIFGFWSGMVGTSLSMIIRMELGQPGFFIGDDQTYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:MTH00048   18 VIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPR 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511240158  81 MNNMSFWLLPPSLMLLMSSSMVesGAGTGWTVYPPLSSGIAHGGASVDLAIFSLHLAGISSILGAVNFITTMMNMRSPNM 160
Cdd:MTH00048   98 LNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNV 175

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1511240158 161 SLdQTPLFVWAVSITALLLLLSLPVLAGAITMLLCDRNLNTSFFDPAGGGDPILYQHLF 219
Cdd:MTH00048  176 FS-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMF 233
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-219 1.81e-55

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: 183.94  E-value: 1.81e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511240158   1 ILYFIFGFWSGMVGTSLSMIIRMELGQPGFFIGDDQTYNVIVTAHAFIMIFFMVMPIMIGgFGNWLVPLMLGAPDMAFPR 80
Cdd:cd01662    12 IMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPR 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511240158  81 MNNMSFWLLPPSLMLLMSSSMVESGAGTGWTVYPPLSSGIAHGGASVDLAIFSLHLAGISSILGAVNFITTMMNMRSPNM 160
Cdd:cd01662    91 LNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGM 170

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1511240158 161 SLDQTPLFVWAVSITALLLLLSLPVLAGAITMLLCDRNLNTSFFDPAGGGDPILYQHLF 219
Cdd:cd01662   171 TLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLF 229
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-219 9.03e-43

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: 148.88  E-value: 9.03e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511240158   1 ILYFIFGFWSGMVGTSLSMIIRMELGQPGFFIGDDQTYNVIVTAHAFIMIFFMVMPiMIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:pfam00115   4 LLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511240158  81 MNNMSFWLLPPSLMLLMSSSMvesGAGTGWTVYPPLssgiahggASVDLAIFSLHLAGISSILGAVNFITTMMNMRSPNM 160
Cdd:pfam00115  83 LNALSFWLVVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGM 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1511240158 161 SLdQTPLFVWAVSITALLLLLSLPVLAGAITMLLCDRNLNtsffdpAGGGDPILYQHLF 219
Cdd:pfam00115 152 TL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLF 203
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 1-218 2.51e-33

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 125.82  E-value: 2.51e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511240158   1 ILYFIFGFWSGMVGTSLSMIIRME-----LGQPGFFigDDQTYNVIVTAHAFIMIFFMVMPIMIGgFGNWLVPLMLGAPD 75
Cdd:PRK15017   59 IMYIIVAIVMLLRGFADAIMMRSQqalasAGEAGFL--PPHHYDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARD 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511240158  76 MAFPRMNNMSFWLLPPSLMLLMSSSMVESGAGTGWTVYPPLSSGIAHGGASVDLAIFSLHLAGISSILGAVNFITTMMNM 155
Cdd:PRK15017  136 VAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKM 215

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1511240158 156 RSPNMSLDQTPLFVWAVSITALLLLLSLPVLAGAITMLLCDRNLNTSFFDPAGGGDPILYQHL 218
Cdd:PRK15017  216 RAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINL 278
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 1-219 1.44e-31

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: 121.11  E-value: 1.44e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511240158   1 ILYFIFGFWSGMVGTSLSMIIRMELGQPGFFIGDDQTYNVIVTAHAFIMIFFMVMPIMIGgFGNWLVPLMLGAPDMAFPR 80
Cdd:TIGR02882  55 VMYIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPV 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511240158  81 MNNMSFWLLPPSLMLLMSSSMVESGAGTGWTVYPPLSSGIAHGGASVDLAIFSLHLAGISSILGAVNFITTMMNMRSPNM 160
Cdd:TIGR02882 134 LNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGM 213

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1511240158 161 SLDQTPLFVWAVSITALLLLLSLPVLAGAITMLLCDRNLNTSFFDPAGGGDPILYQHLF 219
Cdd:TIGR02882 214 KLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLF 272
 
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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