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Conserved domains on  [gi|984291148|gb|AMB48983|]
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cytochrome oxidase subunit 1, partial (mitochondrion) [Megachile ligniseca]

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 ...
 1-213 1.24e-106

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: 316.04  E-value: 1.24e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984291148   1 HKDIGILYMIFALWSGMVGSSMSMIIRMELSVPGAWIKNDQIYNSIVTAHAFLMIFFLVMPFMIGGFGNWLMPLMIGAPD 80
Cdd:MTH00153  10 HKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPD 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984291148  81 MAFPRMNNVSFWLLPPSLILLLSSNLINPSPGTGWTVYPPLSLYMFHPSPSVDMTIFSLHLSGISSIIGSLNFMVTILMM 160
Cdd:MTH00153  90 MAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINM 169

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 984291148 161 KNFSLNYSKVTLFPWSVFITTVLLLLSLPVLAGAITMLLFDRNLNTSFFDPMG 213
Cdd:MTH00153 170 RSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAG 222
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-213 1.24e-106

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 316.04  E-value: 1.24e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984291148   1 HKDIGILYMIFALWSGMVGSSMSMIIRMELSVPGAWIKNDQIYNSIVTAHAFLMIFFLVMPFMIGGFGNWLMPLMIGAPD 80
Cdd:MTH00153  10 HKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPD 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984291148  81 MAFPRMNNVSFWLLPPSLILLLSSNLINPSPGTGWTVYPPLSLYMFHPSPSVDMTIFSLHLSGISSIIGSLNFMVTILMM 160
Cdd:MTH00153  90 MAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINM 169

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 984291148 161 KNFSLNYSKVTLFPWSVFITTVLLLLSLPVLAGAITMLLFDRNLNTSFFDPMG 213
Cdd:MTH00153 170 RSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAG 222
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-213 5.31e-105

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: 310.95  E-value: 5.31e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984291148   1 HKDIGILYMIFALWSGMVGSSMSMIIRMELSVPGAWIKNDQIYNSIVTAHAFLMIFFLVMPFMIGGFGNWLMPLMIGAPD 80
Cdd:cd01663    3 HKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984291148  81 MAFPRMNNVSFWLLPPSLILLLSSNLINPSPGTGWTVYPPLSLYMFHPSPSVDMTIFSLHLSGISSIIGSLNFMVTILMM 160
Cdd:cd01663   83 MAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNM 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 984291148 161 KNFSLNYSKVTLFPWSVFITTVLLLLSLPVLAGAITMLLFDRNLNTSFFDPMG 213
Cdd:cd01663  163 RAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAG 215
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-211 1.97e-56

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 186.87  E-value: 1.97e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984291148   1 HKDIGILYMIFALWSGMVGSSMSMIIRMELSVPGAWIKNDQIYNSIVTAHAFLMIFFLVMPFmIGGFGNWLMPLMIGAPD 80
Cdd:COG0843   15 HKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPF-LAGFGNYLVPLQIGARD 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984291148  81 MAFPRMNNVSFWLLPPSLILLLSSNLINPSPGTGWTVYPPLSLYMFHPSPSVDMTIFSLHLSGISSIIGSLNFMVTILMM 160
Cdd:COG0843   94 MAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKM 173

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 984291148 161 KNFSLNYSKVTLFPWSVFITTVLLLLSLPVLAGAITMLLFDRNLNTSFFDP 211
Cdd:COG0843  174 RAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDP 224
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 1-209 9.48e-35

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: 129.59  E-value: 9.48e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984291148    1 HKDIGILYMIFALWSGMVGSSMSMIIRMELSVPGAWIKNDQIYNSIVTAHAFLMIFFLVMPFMIGgFGNWLMPLMIGAPD 80
Cdd:TIGR02882  50 HKKIGVMYIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARD 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984291148   81 MAFPRMNNVSFWLLPPSLILLLSSNLINPSPGTGWTVYPPLSLYMFHPSPSVDMTIFSLHLSGISSIIGSLNFMVTILMM 160
Cdd:TIGR02882 129 VAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKM 208

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 984291148  161 KNFSLNYSKVTLFPWSVFITTVLLLLSLPVLAGAITMLLFDRNLNTSFF 209
Cdd:TIGR02882 209 RAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFF 257
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 3-212 1.79e-34

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: 126.53  E-value: 1.79e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984291148    3 DIGILYMIFALWSGMVGSSMSMIIRMELSVPGAWIKNDQIYNSIVTAHAFLMIFFLVMPFmIGGFGNWLMPLMIGAPDMA 82
Cdd:pfam00115   1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984291148   83 FPRMNNVSFWLLPPSLILLLSSNLinpSPGTGWTVYPPLslymfhpsPSVDMTIFSLHLSGISSIIGSLNFMVTILMMKN 162
Cdd:pfam00115  80 FPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 984291148  163 fSLNYSKVTLFPWSVFITTVLLLLSLPVLAGAITMLLFDRNLNTSFFDPM 212
Cdd:pfam00115 149 -PGMTLRMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGAGGGDPL 197
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-213 1.24e-106

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 316.04  E-value: 1.24e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984291148   1 HKDIGILYMIFALWSGMVGSSMSMIIRMELSVPGAWIKNDQIYNSIVTAHAFLMIFFLVMPFMIGGFGNWLMPLMIGAPD 80
Cdd:MTH00153  10 HKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPD 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984291148  81 MAFPRMNNVSFWLLPPSLILLLSSNLINPSPGTGWTVYPPLSLYMFHPSPSVDMTIFSLHLSGISSIIGSLNFMVTILMM 160
Cdd:MTH00153  90 MAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINM 169

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 984291148 161 KNFSLNYSKVTLFPWSVFITTVLLLLSLPVLAGAITMLLFDRNLNTSFFDPMG 213
Cdd:MTH00153 170 RSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAG 222
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-213 5.31e-105

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: 310.95  E-value: 5.31e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984291148   1 HKDIGILYMIFALWSGMVGSSMSMIIRMELSVPGAWIKNDQIYNSIVTAHAFLMIFFLVMPFMIGGFGNWLMPLMIGAPD 80
Cdd:cd01663    3 HKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984291148  81 MAFPRMNNVSFWLLPPSLILLLSSNLINPSPGTGWTVYPPLSLYMFHPSPSVDMTIFSLHLSGISSIIGSLNFMVTILMM 160
Cdd:cd01663   83 MAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNM 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 984291148 161 KNFSLNYSKVTLFPWSVFITTVLLLLSLPVLAGAITMLLFDRNLNTSFFDPMG 213
Cdd:cd01663  163 RAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAG 215
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-213 1.87e-94

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 284.65  E-value: 1.87e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984291148   1 HKDIGILYMIFALWSGMVGSSMSMIIRMELSVPGAWIKNDQIYNSIVTAHAFLMIFFLVMPFMIGGFGNWLMPLMIGAPD 80
Cdd:MTH00167  12 HKDIGTLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPD 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984291148  81 MAFPRMNNVSFWLLPPSLILLLSSNLINPSPGTGWTVYPPLSLYMFHPSPSVDMTIFSLHLSGISSIIGSLNFMVTILMM 160
Cdd:MTH00167  92 MAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINM 171

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 984291148 161 KNFSLNYSKVTLFPWSVFITTVLLLLSLPVLAGAITMLLFDRNLNTSFFDPMG 213
Cdd:MTH00167 172 KPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAG 224
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-213 1.71e-89

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 271.85  E-value: 1.71e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984291148   1 HKDIGILYMIFALWSGMVGSSMSMIIRMELSVPGAWIKNDQIYNSIVTAHAFLMIFFLVMPFMIGGFGNWLMPLMIGAPD 80
Cdd:MTH00223   9 HKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPD 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984291148  81 MAFPRMNNVSFWLLPPSLILLLSSNLINPSPGTGWTVYPPLSLYMFHPSPSVDMTIFSLHLSGISSIIGSLNFMVTILMM 160
Cdd:MTH00223  89 MAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINM 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 984291148 161 KNFSLNYSKVTLFPWSVFITTVLLLLSLPVLAGAITMLLFDRNLNTSFFDPMG 213
Cdd:MTH00223 169 RSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAG 221
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-213 8.43e-87

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 265.03  E-value: 8.43e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984291148   1 HKDIGILYMIFALWSGMVGSSMSMIIRMELSVPGAWIKNDQIYNSIVTAHAFLMIFFLVMPFMIGGFGNWLMPLMIGAPD 80
Cdd:MTH00116  12 HKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPD 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984291148  81 MAFPRMNNVSFWLLPPSLILLLSSNLINPSPGTGWTVYPPLSLYMFHPSPSVDMTIFSLHLSGISSIIGSLNFMVTILMM 160
Cdd:MTH00116  92 MAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINM 171

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 984291148 161 KNFSLNYSKVTLFPWSVFITTVLLLLSLPVLAGAITMLLFDRNLNTSFFDPMG 213
Cdd:MTH00116 172 KPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAG 224
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-213 5.34e-86

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 263.12  E-value: 5.34e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984291148   1 HKDIGILYMIFALWSGMVGSSMSMIIRMELSVPGAWIKNDQIYNSIVTAHAFLMIFFLVMPFMIGGFGNWLMPLMIGAPD 80
Cdd:MTH00142  10 HKDIGTLYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPD 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984291148  81 MAFPRMNNVSFWLLPPSLILLLSSNLINPSPGTGWTVYPPLSLYMFHPSPSVDMTIFSLHLSGISSIIGSLNFMVTILMM 160
Cdd:MTH00142  90 MAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINM 169

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 984291148 161 KNFSLNYSKVTLFPWSVFITTVLLLLSLPVLAGAITMLLFDRNLNTSFFDPMG 213
Cdd:MTH00142 170 RAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAG 222
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-213 1.87e-79

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 246.35  E-value: 1.87e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984291148   1 HKDIGILYMIFALWSGMVGSSMSMIIRMELSVPGAWIKNDQIYNSIVTAHAFLMIFFLVMPFMIGGFGNWLMPLMIGAPD 80
Cdd:MTH00007   9 HKDIGTLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPD 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984291148  81 MAFPRMNNVSFWLLPPSLILLLSSNLINPSPGTGWTVYPPLSLYMFHPSPSVDMTIFSLHLSGISSIIGSLNFMVTILMM 160
Cdd:MTH00007  89 MAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINM 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 984291148 161 KNFSLNYSKVTLFPWSVFITTVLLLLSLPVLAGAITMLLFDRNLNTSFFDPMG 213
Cdd:MTH00007 169 RWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAG 221
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-213 1.05e-78

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 244.46  E-value: 1.05e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984291148   1 HKDIGILYMIFALWSGMVGSSMSMIIRMELSVPGAWIKNDQIYNSIVTAHAFLMIFFLVMPFMIGGFGNWLMPLMIGAPD 80
Cdd:MTH00077  12 HKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPD 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984291148  81 MAFPRMNNVSFWLLPPSLILLLSSNLINPSPGTGWTVYPPLSLYMFHPSPSVDMTIFSLHLSGISSIIGSLNFMVTILMM 160
Cdd:MTH00077  92 MAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINM 171

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 984291148 161 KNFSLNYSKVTLFPWSVFITTVLLLLSLPVLAGAITMLLFDRNLNTSFFDPMG 213
Cdd:MTH00077 172 KPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAG 224
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-213 2.55e-78

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 243.29  E-value: 2.55e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984291148   1 HKDIGILYMIFALWSGMVGSSMSMIIRMELSVPGAWIKNDQIYNSIVTAHAFLMIFFLVMPFMIGGFGNWLMPLMIGAPD 80
Cdd:MTH00183  12 HKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPD 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984291148  81 MAFPRMNNVSFWLLPPSLILLLSSNLINPSPGTGWTVYPPLSLYMFHPSPSVDMTIFSLHLSGISSIIGSLNFMVTILMM 160
Cdd:MTH00183  92 MAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINM 171

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 984291148 161 KNFSLNYSKVTLFPWSVFITTVLLLLSLPVLAGAITMLLFDRNLNTSFFDPMG 213
Cdd:MTH00183 172 KPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAG 224
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-213 4.62e-78

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 242.66  E-value: 4.62e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984291148   1 HKDIGILYMIFALWSGMVGSSMSMIIRMELSVPGAWIKNDQIYNSIVTAHAFLMIFFLVMPFMIGGFGNWLMPLMIGAPD 80
Cdd:MTH00079  13 HKDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPD 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984291148  81 MAFPRMNNVSFWLLPPSLILLLSSNLINPSPGTGWTVYPPLSLyMFHPSPSVDMTIFSLHLSGISSIIGSLNFMVTILMM 160
Cdd:MTH00079  93 MSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNL 171

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 984291148 161 KNFSLNYSKVTLFPWSVFITTVLLLLSLPVLAGAITMLLFDRNLNTSFFDPMG 213
Cdd:MTH00079 172 RSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPST 224
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-213 2.30e-77

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 240.94  E-value: 2.30e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984291148   1 HKDIGILYMIFALWSGMVGSSMSMIIRMELSVPGAWIKNDQIYNSIVTAHAFLMIFFLVMPFMIGGFGNWLMPLMIGAPD 80
Cdd:MTH00103  12 HKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPD 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984291148  81 MAFPRMNNVSFWLLPPSLILLLSSNLINPSPGTGWTVYPPLSLYMFHPSPSVDMTIFSLHLSGISSIIGSLNFMVTILMM 160
Cdd:MTH00103  92 MAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINM 171

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 984291148 161 KNFSLNYSKVTLFPWSVFITTVLLLLSLPVLAGAITMLLFDRNLNTSFFDPMG 213
Cdd:MTH00103 172 KPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAG 224
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-213 2.44e-77

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 240.89  E-value: 2.44e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984291148   1 HKDIGILYMIFALWSGMVGSSMSMIIRMELSVPGAWIKNDQIYNSIVTAHAFLMIFFLVMPFMIGGFGNWLMPLMIGAPD 80
Cdd:MTH00037  12 HKDIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPD 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984291148  81 MAFPRMNNVSFWLLPPSLILLLSSNLINPSPGTGWTVYPPLSLYMFHPSPSVDMTIFSLHLSGISSIIGSLNFMVTILMM 160
Cdd:MTH00037  92 MAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINM 171

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 984291148 161 KNFSLNYSKVTLFPWSVFITTVLLLLSLPVLAGAITMLLFDRNLNTSFFDPMG 213
Cdd:MTH00037 172 RTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAG 224
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-213 1.29e-74

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 233.95  E-value: 1.29e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984291148   1 HKDIGILYMIFALWSGMVGSSMSMIIRMELSVPGAWIKNDQIYNSIVTAHAFLMIFFLVMPFMIGGFGNWLMPLMIGAPD 80
Cdd:MTH00184  14 HKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPD 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984291148  81 MAFPRMNNVSFWLLPPSLILLLSSNLINPSPGTGWTVYPPLSLYMFHPSPSVDMTIFSLHLSGISSIIGSLNFMVTILMM 160
Cdd:MTH00184  94 MAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNM 173

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 984291148 161 KNFSLNYSKVTLFPWSVFITTVLLLLSLPVLAGAITMLLFDRNLNTSFFDPMG 213
Cdd:MTH00184 174 RAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAG 226
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-213 6.90e-74

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 232.02  E-value: 6.90e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984291148   1 HKDIGILYMIFALWSGMVGSSMSMIIRMELSVPGAWIKNDQIYNSIVTAHAFLMIFFLVMPFMIGGFGNWLMPLMIGAPD 80
Cdd:MTH00182  14 HKDIGTLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPD 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984291148  81 MAFPRMNNVSFWLLPPSLILLLSSNLINPSPGTGWTVYPPLSLYMFHPSPSVDMTIFSLHLSGISSIIGSLNFMVTILMM 160
Cdd:MTH00182  94 MAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNM 173

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 984291148 161 KNFSLNYSKVTLFPWSVFITTVLLLLSLPVLAGAITMLLFDRNLNTSFFDPMG 213
Cdd:MTH00182 174 RAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAG 226
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-213 9.09e-67

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 214.11  E-value: 9.09e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984291148   1 HKDIGILYMIFALWSGMVGSSMSMIIRMELSVPGAWIKNDQIYNSIVTAHAFLMIFFLVMPFMIGGFGNWLMPLMIGAPD 80
Cdd:MTH00026  13 HKDIGSLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPD 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984291148  81 MAFPRMNNVSFWLLPPSLILLLSSNLINPSPGTGWTVYPPLSLYMFHPSPSVDMTIFSLHLSGISSIIGSLNFMVTILMM 160
Cdd:MTH00026  93 MAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNM 172

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 984291148 161 KNFSLNYSKVTLFPWSVFITTVLLLLSLPVLAGAITMLLFDRNLNTSFFDPMG 213
Cdd:MTH00026 173 RTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAG 225
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-213 3.68e-64

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: 205.46  E-value: 3.68e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984291148   1 HKDIGILYMIFALWSGMVGSSMSMIIRMELSVPGAWIKNDQIYNSIVTAHAFLMIFFLVMPFMIGGFGNWlMPLMIGAPD 80
Cdd:cd00919    1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNL-LPPLIGARD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984291148  81 MAFPRMNNVSFWLLPPSLILLLSSNLINPSPGTGWTVYPPLSLYMFHPSPSVDMTIFSLHLSGISSIIGSLNFMVTILMM 160
Cdd:cd00919   80 LAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNM 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 984291148 161 KNFSLNYSKVTLFPWSVFITTVLLLLSLPVLAGAITMLLFDRNLNTSFFDPMG 213
Cdd:cd00919  160 RAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAG 212
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-211 1.97e-56

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 186.87  E-value: 1.97e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984291148   1 HKDIGILYMIFALWSGMVGSSMSMIIRMELSVPGAWIKNDQIYNSIVTAHAFLMIFFLVMPFmIGGFGNWLMPLMIGAPD 80
Cdd:COG0843   15 HKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPF-LAGFGNYLVPLQIGARD 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984291148  81 MAFPRMNNVSFWLLPPSLILLLSSNLINPSPGTGWTVYPPLSLYMFHPSPSVDMTIFSLHLSGISSIIGSLNFMVTILMM 160
Cdd:COG0843   94 MAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKM 173

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 984291148 161 KNFSLNYSKVTLFPWSVFITTVLLLLSLPVLAGAITMLLFDRNLNTSFFDP 211
Cdd:COG0843  174 RAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDP 224
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-213 7.50e-53

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 177.18  E-value: 7.50e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984291148   1 HKDIGILYMIFALWSGMVGSSMSMIIRMELSVPGAWIKNDQIYNSIVTAHAFLMIFFLVMPFMIGGFGNWLMPLMIGAPD 80
Cdd:MTH00048  13 HKRIGVIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSD 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984291148  81 MAFPRMNNVSFWLLPPSLILLLSSNLInpSPGTGWTVYPPLSLYMFHPSPSVDMTIFSLHLSGISSIIGSLNFMVTILMM 160
Cdd:MTH00048  93 LNLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSA 170

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 984291148 161 KNFSLNySKVTLFPWSVFITTVLLLLSLPVLAGAITMLLFDRNLNTSFFDPMG 213
Cdd:MTH00048 171 FMTNVF-SRTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLG 222
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-211 1.22e-44

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: 155.05  E-value: 1.22e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984291148   1 HKDIGILYMIFALWSGMVGSSMSMIIRMELSVPGAWIKNDQIYNSIVTAHAFLMIFFLVMPFMIGgFGNWLMPLMIGAPD 80
Cdd:cd01662    7 HKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984291148  81 MAFPRMNNVSFWLLPPSLILLLSSNLINPSPGTGWTVYPPLSLYMFHPSPSVDMTIFSLHLSGISSIIGSLNFMVTILMM 160
Cdd:cd01662   86 VAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKM 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 984291148 161 KNFSLNYSKVTLFPWSVFITTVLLLLSLPVLAGAITMLLFDRNLNTSFFDP 211
Cdd:cd01662  166 RAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTN 216
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 1-209 9.48e-35

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: 129.59  E-value: 9.48e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984291148    1 HKDIGILYMIFALWSGMVGSSMSMIIRMELSVPGAWIKNDQIYNSIVTAHAFLMIFFLVMPFMIGgFGNWLMPLMIGAPD 80
Cdd:TIGR02882  50 HKKIGVMYIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARD 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984291148   81 MAFPRMNNVSFWLLPPSLILLLSSNLINPSPGTGWTVYPPLSLYMFHPSPSVDMTIFSLHLSGISSIIGSLNFMVTILMM 160
Cdd:TIGR02882 129 VAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKM 208

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 984291148  161 KNFSLNYSKVTLFPWSVFITTVLLLLSLPVLAGAITMLLFDRNLNTSFF 209
Cdd:TIGR02882 209 RAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFF 257
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 3-212 1.79e-34

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: 126.53  E-value: 1.79e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984291148    3 DIGILYMIFALWSGMVGSSMSMIIRMELSVPGAWIKNDQIYNSIVTAHAFLMIFFLVMPFmIGGFGNWLMPLMIGAPDMA 82
Cdd:pfam00115   1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984291148   83 FPRMNNVSFWLLPPSLILLLSSNLinpSPGTGWTVYPPLslymfhpsPSVDMTIFSLHLSGISSIIGSLNFMVTILMMKN 162
Cdd:pfam00115  80 FPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 984291148  163 fSLNYSKVTLFPWSVFITTVLLLLSLPVLAGAITMLLFDRNLNTSFFDPM 212
Cdd:pfam00115 149 -PGMTLRMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGAGGGDPL 197
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 1-209 4.54e-30

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 116.57  E-value: 4.54e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984291148   1 HKDIGILYMIFALWSGMVGSSMSMIIRME---LSVPGAWIKNDQIYNSIVTAHAFLMIFFLVMPFMIGgFGNWLMPLMIG 77
Cdd:PRK15017  54 HKRLGIMYIIVAIVMLLRGFADAIMMRSQqalASAGEAGFLPPHHYDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIG 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984291148  78 APDMAFPRMNNVSFWLLPPSLILLLSSNLINPSPGTGWTVYPPLSLYMFHPSPSVDMTIFSLHLSGISSIIGSLNFMVTI 157
Cdd:PRK15017 133 ARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTI 212

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 984291148 158 LMMKNFSLNYSKVTLFPWSVFITTVLLLLSLPVLAGAITMLLFDRNLNTSFF 209
Cdd:PRK15017 213 LKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFF 264
 
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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