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Conserved domains on  [gi|1034218643|gb|ANI25046|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Coptera occidentalis]

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 ...
 1-174 3.58e-79

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 cd01663:

Pssm-ID: 469701  Cd Length: 488  Bit Score: 243.16  E-value: 3.58e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034218643   1 DQIYNMIVTMHAFIMIFFFIMPMMMGGFGNWLIPMMMLLPDMSYPRLNNMSFWLLPPSIIMLLSTMFISNGSGTGWTMYP 80
Cdd:cd01663    42 DQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYP 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034218643  81 PLSNKIYHNDLSMDLTIFSLHIAGISSIVGSMNFINTIIFMRHFMMNLFLISLFSWSMLLTTILLLLSLPVLAGALTMLL 160
Cdd:cd01663   122 PLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLL 201

                         170
                  ....*....|....
gi 1034218643 161 FDRNFNTSFFDPIG 174
Cdd:cd01663   202 TDRNFNTSFFDPAG 215
 
Name Accession Description Interval E-value
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-174 3.58e-79

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: 243.16  E-value: 3.58e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034218643   1 DQIYNMIVTMHAFIMIFFFIMPMMMGGFGNWLIPMMMLLPDMSYPRLNNMSFWLLPPSIIMLLSTMFISNGSGTGWTMYP 80
Cdd:cd01663    42 DQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYP 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034218643  81 PLSNKIYHNDLSMDLTIFSLHIAGISSIVGSMNFINTIIFMRHFMMNLFLISLFSWSMLLTTILLLLSLPVLAGALTMLL 160
Cdd:cd01663   122 PLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLL 201

                         170
                  ....*....|....
gi 1034218643 161 FDRNFNTSFFDPIG 174
Cdd:cd01663   202 TDRNFNTSFFDPAG 215
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-174 1.28e-76

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 237.07  E-value: 1.28e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034218643   1 DQIYNMIVTMHAFIMIFFFIMPMMMGGFGNWLIPMMMLLPDMSYPRLNNMSFWLLPPSIIMLLSTMFISNGSGTGWTMYP 80
Cdd:MTH00153   49 DQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYP 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034218643  81 PLSNKIYHNDLSMDLTIFSLHIAGISSIVGSMNFINTIIFMRHFMMNLFLISLFSWSMLLTTILLLLSLPVLAGALTMLL 160
Cdd:MTH00153  129 PLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLL 208

                         170
                  ....*....|....
gi 1034218643 161 FDRNFNTSFFDPIG 174
Cdd:MTH00153  209 TDRNLNTSFFDPAG 222
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
4-172 1.12e-44

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 154.13  E-value: 1.12e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034218643   4 YNMIVTMHAFIMIFFFIMPMMmGGFGNWLIPMMMLLPDMSYPRLNNMSFWLLPPSIIMLLSTMFISNGSGTGWTMYPPLS 83
Cdd:COG0843    57 YNQLFTMHGTIMIFFFATPFL-AGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLS 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034218643  84 NKIYHNDLSMDLTIFSLHIAGISSIVGSMNFINTIIFMRHFMMNLFLISLFSWSMLLTTILLLLSLPVLAGALTMLLFDR 163
Cdd:COG0843   136 GLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDR 215


                  ....*....
gi 1034218643 164 NFNTSFFDP 172
Cdd:COG0843   216 SLGTHFFDP 224
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 2-173 2.71e-25

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: 100.34  E-value: 2.71e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034218643   2 QIYNMIVTMHAFIMIFFFIMPMMMGgFGNWLIPMMMLLPDMSYPRLNNMSFWLLPPSIIMLLSTMfisNGSGTGWTMYPP 81
Cdd:pfam00115  39 LTYNQLRTLHGNLMIFWFATPFLFG-FGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPP 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034218643  82 LSNkiyhndlsMDLTIFSLHIAGISSIVGSMNFINTIIFMRHFMMNLfLISLFSWSMLLTTILLLLSLPVLAGALTMLLF 161
Cdd:pfam00115 115 LVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLL 185

                         170
                  ....*....|..
gi 1034218643 162 DRNFNTSFFDPI 173
Cdd:pfam00115 186 DRSLGAGGGDPL 197
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 2-170 2.81e-19

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: 84.14  E-value: 2.81e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034218643   2 QIYNMIVTMHAFIMIFFFIMPMMMGgFGNWLIPMMMLLPDMSYPRLNNMSFWLLPPSIIMLLSTMFISNGSGTGWTMYPP 81
Cdd:TIGR02882  90 QHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAP 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034218643  82 LSNKIYHNDLSMDLTIFSLHIAGISSIVGSMNFINTIIFMRHFMMNLFLISLFSWSMLLTTILLLLSLPVLAGALTMLLF 161
Cdd:TIGR02882 169 LAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTT 248


                  ....*....
gi 1034218643 162 DRNFNTSFF 170
Cdd:TIGR02882 249 DRIFDTAFF 257
 
Name Accession Description Interval E-value
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-174 3.58e-79

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: 243.16  E-value: 3.58e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034218643   1 DQIYNMIVTMHAFIMIFFFIMPMMMGGFGNWLIPMMMLLPDMSYPRLNNMSFWLLPPSIIMLLSTMFISNGSGTGWTMYP 80
Cdd:cd01663    42 DQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYP 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034218643  81 PLSNKIYHNDLSMDLTIFSLHIAGISSIVGSMNFINTIIFMRHFMMNLFLISLFSWSMLLTTILLLLSLPVLAGALTMLL 160
Cdd:cd01663   122 PLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLL 201

                         170
                  ....*....|....
gi 1034218643 161 FDRNFNTSFFDPIG 174
Cdd:cd01663   202 TDRNFNTSFFDPAG 215
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-174 1.28e-76

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 237.07  E-value: 1.28e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034218643   1 DQIYNMIVTMHAFIMIFFFIMPMMMGGFGNWLIPMMMLLPDMSYPRLNNMSFWLLPPSIIMLLSTMFISNGSGTGWTMYP 80
Cdd:MTH00153   49 DQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYP 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034218643  81 PLSNKIYHNDLSMDLTIFSLHIAGISSIVGSMNFINTIIFMRHFMMNLFLISLFSWSMLLTTILLLLSLPVLAGALTMLL 160
Cdd:MTH00153  129 PLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLL 208

                         170
                  ....*....|....
gi 1034218643 161 FDRNFNTSFFDPIG 174
Cdd:MTH00153  209 TDRNLNTSFFDPAG 222
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-174 1.73e-72

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 226.40  E-value: 1.73e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034218643   1 DQIYNMIVTMHAFIMIFFFIMPMMMGGFGNWLIPMMMLLPDMSYPRLNNMSFWLLPPSIIMLLSTMFISNGSGTGWTMYP 80
Cdd:MTH00223   48 DQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYP 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034218643  81 PLSNKIYHNDLSMDLTIFSLHIAGISSIVGSMNFINTIIFMRHFMMNLFLISLFSWSMLLTTILLLLSLPVLAGALTMLL 160
Cdd:MTH00223  128 PLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLL 207

                         170
                  ....*....|....
gi 1034218643 161 FDRNFNTSFFDPIG 174
Cdd:MTH00223  208 TDRNFNTSFFDPAG 221
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-174 4.36e-72

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 225.33  E-value: 4.36e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034218643   1 DQIYNMIVTMHAFIMIFFFIMPMMMGGFGNWLIPMMMLLPDMSYPRLNNMSFWLLPPSIIMLLSTMFISNGSGTGWTMYP 80
Cdd:MTH00167   51 DQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYP 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034218643  81 PLSNKIYHNDLSMDLTIFSLHIAGISSIVGSMNFINTIIFMRHFMMNLFLISLFSWSMLLTTILLLLSLPVLAGALTMLL 160
Cdd:MTH00167  131 PLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLL 210

                         170
                  ....*....|....
gi 1034218643 161 FDRNFNTSFFDPIG 174
Cdd:MTH00167  211 TDRNLNTTFFDPAG 224
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-174 9.51e-68

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 214.19  E-value: 9.51e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034218643   1 DQIYNMIVTMHAFIMIFFFIMPMMMGGFGNWLIPMMMLLPDMSYPRLNNMSFWLLPPSIIMLLSTMFISNGSGTGWTMYP 80
Cdd:MTH00116   51 DQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYP 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034218643  81 PLSNKIYHNDLSMDLTIFSLHIAGISSIVGSMNFINTIIFMRHFMMNLFLISLFSWSMLLTTILLLLSLPVLAGALTMLL 160
Cdd:MTH00116  131 PLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLL 210

                         170
                  ....*....|....
gi 1034218643 161 FDRNFNTSFFDPIG 174
Cdd:MTH00116  211 TDRNLNTTFFDPAG 224
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-174 2.27e-65

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 208.04  E-value: 2.27e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034218643   1 DQIYNMIVTMHAFIMIFFFIMPMMMGGFGNWLIPMMMLLPDMSYPRLNNMSFWLLPPSIIMLLSTMFISNGSGTGWTMYP 80
Cdd:MTH00142   49 DQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYP 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034218643  81 PLSNKIYHNDLSMDLTIFSLHIAGISSIVGSMNFINTIIFMRHFMMNLFLISLFSWSMLLTTILLLLSLPVLAGALTMLL 160
Cdd:MTH00142  129 PLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLL 208

                         170
                  ....*....|....
gi 1034218643 161 FDRNFNTSFFDPIG 174
Cdd:MTH00142  209 TDRNFNTSFFDPAG 222
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-174 1.08e-60

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 195.91  E-value: 1.08e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034218643   1 DQIYNMIVTMHAFIMIFFFIMPMMMGGFGNWLIPMMMLLPDMSYPRLNNMSFWLLPPSIIMLLSTMFISNGSGTGWTMYP 80
Cdd:MTH00183   51 DQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYP 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034218643  81 PLSNKIYHNDLSMDLTIFSLHIAGISSIVGSMNFINTIIFMRHFMMNLFLISLFSWSMLLTTILLLLSLPVLAGALTMLL 160
Cdd:MTH00183  131 PLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLL 210

                         170
                  ....*....|....
gi 1034218643 161 FDRNFNTSFFDPIG 174
Cdd:MTH00183  211 TDRNLNTTFFDPAG 224
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-174 1.35e-60

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 195.51  E-value: 1.35e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034218643   1 DQIYNMIVTMHAFIMIFFFIMPMMMGGFGNWLIPMMMLLPDMSYPRLNNMSFWLLPPSIIMLLSTMFISNGSGTGWTMYP 80
Cdd:MTH00007   48 DQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYP 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034218643  81 PLSNKIYHNDLSMDLTIFSLHIAGISSIVGSMNFINTIIFMRHFMMNLFLISLFSWSMLLTTILLLLSLPVLAGALTMLL 160
Cdd:MTH00007  128 PLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLL 207

                         170
                  ....*....|....
gi 1034218643 161 FDRNFNTSFFDPIG 174
Cdd:MTH00007  208 TDRNLNTSFFDPAG 221
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-174 2.17e-59

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 192.40  E-value: 2.17e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034218643   1 DQIYNMIVTMHAFIMIFFFIMPMMMGGFGNWLIPMMMLLPDMSYPRLNNMSFWLLPPSIIMLLSTMFISNGSGTGWTMYP 80
Cdd:MTH00103   51 DQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYP 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034218643  81 PLSNKIYHNDLSMDLTIFSLHIAGISSIVGSMNFINTIIFMRHFMMNLFLISLFSWSMLLTTILLLLSLPVLAGALTMLL 160
Cdd:MTH00103  131 PLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLL 210

                         170
                  ....*....|....
gi 1034218643 161 FDRNFNTSFFDPIG 174
Cdd:MTH00103  211 TDRNLNTTFFDPAG 224
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-174 4.14e-59

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 192.08  E-value: 4.14e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034218643   1 DQIYNMIVTMHAFIMIFFFIMPMMMGGFGNWLIPMMMLLPDMSYPRLNNMSFWLLPPSIIMLLSTMFISNGSGTGWTMYP 80
Cdd:MTH00077   51 DQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYP 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034218643  81 PLSNKIYHNDLSMDLTIFSLHIAGISSIVGSMNFINTIIFMRHFMMNLFLISLFSWSMLLTTILLLLSLPVLAGALTMLL 160
Cdd:MTH00077  131 PLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLL 210

                         170
                  ....*....|....
gi 1034218643 161 FDRNFNTSFFDPIG 174
Cdd:MTH00077  211 TDRNLNTTFFDPAG 224
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-174 4.64e-59

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 191.96  E-value: 4.64e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034218643   1 DQIYNMIVTMHAFIMIFFFIMPMMMGGFGNWLIPMMMLLPDMSYPRLNNMSFWLLPPSIIMLLSTMFISNGSGTGWTMYP 80
Cdd:MTH00184   53 DHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYP 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034218643  81 PLSNKIYHNDLSMDLTIFSLHIAGISSIVGSMNFINTIIFMRHFMMNLFLISLFSWSMLLTTILLLLSLPVLAGALTMLL 160
Cdd:MTH00184  133 PLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLL 212

                         170
                  ....*....|....
gi 1034218643 161 FDRNFNTSFFDPIG 174
Cdd:MTH00184  213 TDRNFNTTFFDPAG 226
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-174 5.69e-59

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 191.57  E-value: 5.69e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034218643   1 DQIYNMIVTMHAFIMIFFFIMPMMMGGFGNWLIPMMMLLPDMSYPRLNNMSFWLLPPSIIMLLSTMFISNGSGTGWTMYP 80
Cdd:MTH00182   53 DHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYP 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034218643  81 PLSNKIYHNDLSMDLTIFSLHIAGISSIVGSMNFINTIIFMRHFMMNLFLISLFSWSMLLTTILLLLSLPVLAGALTMLL 160
Cdd:MTH00182  133 PLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLL 212

                         170
                  ....*....|....
gi 1034218643 161 FDRNFNTSFFDPIG 174
Cdd:MTH00182  213 TDRNFNTTFFDPAG 226
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-174 8.15e-59

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 191.20  E-value: 8.15e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034218643   1 DQIYNMIVTMHAFIMIFFFIMPMMMGGFGNWLIPMMMLLPDMSYPRLNNMSFWLLPPSIIMLLSTMFISNGSGTGWTMYP 80
Cdd:MTH00037   51 DQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYP 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034218643  81 PLSNKIYHNDLSMDLTIFSLHIAGISSIVGSMNFINTIIFMRHFMMNLFLISLFSWSMLLTTILLLLSLPVLAGALTMLL 160
Cdd:MTH00037  131 PLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLL 210

                         170
                  ....*....|....
gi 1034218643 161 FDRNFNTSFFDPIG 174
Cdd:MTH00037  211 TDRNINTTFFDPAG 224
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 2-174 7.36e-56

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 183.34  E-value: 7.36e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034218643   2 QIYNMIVTMHAFIMIFFFIMPMMMGGFGNWLIPMMMLLPDMSYPRLNNMSFWLLPPSIIMLLSTMFISNGSGTGWTMYPP 81
Cdd:MTH00079   53 QLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPP 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034218643  82 LSNKiYHNDLSMDLTIFSLHIAGISSIVGSMNFINTIIFMRHFMMNLFLISLFSWSMLLTTILLLLSLPVLAGALTMLLF 161
Cdd:MTH00079  133 LSTL-GHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLT 211

                         170
                  ....*....|...
gi 1034218643 162 DRNFNTSFFDPIG 174
Cdd:MTH00079  212 DRNLNTSFFDPST 224
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-174 2.90e-53

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 177.13  E-value: 2.90e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034218643   1 DQIYNMIVTMHAFIMIFFFIMPMMMGGFGNWLIPMMMLLPDMSYPRLNNMSFWLLPPSIIMLLSTMFISNGSGTGWTMYP 80
Cdd:MTH00026   52 DHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYP 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034218643  81 PLSNKIYHNDLSMDLTIFSLHIAGISSIVGSMNFINTIIFMRHFMMNLFLISLFSWSMLLTTILLLLSLPVLAGALTMLL 160
Cdd:MTH00026  132 PLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLL 211

                         170
                  ....*....|....
gi 1034218643 161 FDRNFNTSFFDPIG 174
Cdd:MTH00026  212 TDRNFNTTFFDPAG 225
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-174 8.20e-48

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: 161.16  E-value: 8.20e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034218643   1 DQIYNMIVTMHAFIMIFFFIMPMMMGGFGNWLIPMMmLLPDMSYPRLNNMSFWLLPPSIIMLLSTMFISNGSGTGWTMYP 80
Cdd:cd00919    40 PQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPPLI-GARDLAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYP 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034218643  81 PLSNKIYHNDLSMDLTIFSLHIAGISSIVGSMNFINTIIFMRHFMMNLFLISLFSWSMLLTTILLLLSLPVLAGALTMLL 160
Cdd:cd00919   119 PLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLL 198

                         170
                  ....*....|....
gi 1034218643 161 FDRNFNTSFFDPIG 174
Cdd:cd00919   199 LDRNFGTSFFDPAG 212
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 3-174 3.08e-46

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 157.92  E-value: 3.08e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034218643   3 IYNMIVTMHAFIMIFFFIMPMMMGGFGNWLIPMMMLLPDMSYPRLNNMSFWLLPPSIIMLLSTMFIsnGSGTGWTMYPPL 82
Cdd:MTH00048   54 VYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPL 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034218643  83 SNKIYHNDLSMDLTIFSLHIAGISSIVGSMNFINTIIFMrhFMMNLFL-ISLFSWSMLLTTILLLLSLPVLAGALTMLLF 161
Cdd:MTH00048  132 SSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSA--FMTNVFSrTSIILWSYLFTSILLLLSLPVLAAAITMLLF 209

                         170
                  ....*....|...
gi 1034218643 162 DRNFNTSFFDPIG 174
Cdd:MTH00048  210 DRNFGSAFFDPLG 222
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
4-172 1.12e-44

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 154.13  E-value: 1.12e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034218643   4 YNMIVTMHAFIMIFFFIMPMMmGGFGNWLIPMMMLLPDMSYPRLNNMSFWLLPPSIIMLLSTMFISNGSGTGWTMYPPLS 83
Cdd:COG0843    57 YNQLFTMHGTIMIFFFATPFL-AGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLS 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034218643  84 NKIYHNDLSMDLTIFSLHIAGISSIVGSMNFINTIIFMRHFMMNLFLISLFSWSMLLTTILLLLSLPVLAGALTMLLFDR 163
Cdd:COG0843   136 GLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDR 215


                  ....*....
gi 1034218643 164 NFNTSFFDP 172
Cdd:COG0843   216 SLGTHFFDP 224
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 4-172 3.75e-35

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: 128.08  E-value: 3.75e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034218643   4 YNMIVTMHAFIMIFFFIMPMMMGgFGNWLIPMMMLLPDMSYPRLNNMSFWLLPPSIIMLLSTMFISNGSGTGWTMYPPLS 83
Cdd:cd01662    49 YNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLS 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034218643  84 NKIYHNDLSMDLTIFSLHIAGISSIVGSMNFINTIIFMRHFMMNLFLISLFSWSMLLTTILLLLSLPVLAGALTMLLFDR 163
Cdd:cd01662   128 GLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDR 207


                  ....*....
gi 1034218643 164 NFNTSFFDP 172
Cdd:cd01662   208 YFGTHFFTN 216
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 2-173 2.71e-25

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: 100.34  E-value: 2.71e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034218643   2 QIYNMIVTMHAFIMIFFFIMPMMMGgFGNWLIPMMMLLPDMSYPRLNNMSFWLLPPSIIMLLSTMfisNGSGTGWTMYPP 81
Cdd:pfam00115  39 LTYNQLRTLHGNLMIFWFATPFLFG-FGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPP 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034218643  82 LSNkiyhndlsMDLTIFSLHIAGISSIVGSMNFINTIIFMRHFMMNLfLISLFSWSMLLTTILLLLSLPVLAGALTMLLF 161
Cdd:pfam00115 115 LVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLL 185

                         170
                  ....*....|..
gi 1034218643 162 DRNFNTSFFDPI 173
Cdd:pfam00115 186 DRSLGAGGGDPL 197
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 4-170 6.52e-23

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 94.62  E-value: 6.52e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034218643   4 YNMIVTMHAFIMIFFFIMPMMMGgFGNWLIPMMMLLPDMSYPRLNNMSFWLLPPSIIMLLSTMFISNGSGTGWTMYPPLS 83
Cdd:PRK15017   99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034218643  84 NKIYHNDLSMDLTIFSLHIAGISSIVGSMNFINTIIFMRHFMMNLFLISLFSWSMLLTTILLLLSLPVLAGALTMLLFDR 163
Cdd:PRK15017  178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257


                  ....*..
gi 1034218643 164 NFNTSFF 170
Cdd:PRK15017  258 YLGTHFF 264
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 2-170 2.81e-19

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: 84.14  E-value: 2.81e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034218643   2 QIYNMIVTMHAFIMIFFFIMPMMMGgFGNWLIPMMMLLPDMSYPRLNNMSFWLLPPSIIMLLSTMFISNGSGTGWTMYPP 81
Cdd:TIGR02882  90 QHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAP 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034218643  82 LSNKIYHNDLSMDLTIFSLHIAGISSIVGSMNFINTIIFMRHFMMNLFLISLFSWSMLLTTILLLLSLPVLAGALTMLLF 161
Cdd:TIGR02882 169 LAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTT 248


                  ....*....
gi 1034218643 162 DRNFNTSFF 170
Cdd:TIGR02882 249 DRIFDTAFF 257
 
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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