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Conserved domains on  [gi|1573757531|gb|QBC75055|]
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cytochrome oxidase subunit 1, partial (mitochondrion) [Rhytimorpha coccinea]

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 ...
 2-163 1.38e-90

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: 272.51  E-value: 1.38e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573757531   2 SMSIIIRLELSMPGKLLNNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGNWLIPLMLGAPDMAFPRMNNMSFWIIVPSLMM 81
Cdd:MTH00153   30 SLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTL 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573757531  82 MLLSSFINIGAGTGWTIYPPLSANLSHSGMSMDLVIFSLHLAGISSILGSINFMTTIMNMRLFFYKMDQLTLLFWSIFIT 161
Cdd:MTH00153  110 LLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLIT 189


                  ..
gi 1573757531 162 TI 163
Cdd:MTH00153  190 AI 191
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 2-163 1.38e-90

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 272.51  E-value: 1.38e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573757531   2 SMSIIIRLELSMPGKLLNNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGNWLIPLMLGAPDMAFPRMNNMSFWIIVPSLMM 81
Cdd:MTH00153   30 SLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTL 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573757531  82 MLLSSFINIGAGTGWTIYPPLSANLSHSGMSMDLVIFSLHLAGISSILGSINFMTTIMNMRLFFYKMDQLTLLFWSIFIT 161
Cdd:MTH00153  110 LLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLIT 189


                  ..
gi 1573757531 162 TI 163
Cdd:MTH00153  190 AI 191
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-163 2.40e-87

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: 263.57  E-value: 2.40e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573757531   1 LSMSIIIRLELSMPGKLLNNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGNWLIPLMLGAPDMAFPRMNNMSFWIIVPSLM 80
Cdd:cd01663    22 TSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLL 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573757531  81 MMLLSSFINIGAGTGWTIYPPLSANLSHSGMSMDLVIFSLHLAGISSILGSINFMTTIMNMRLFFYKMDQLTLLFWSIFI 160
Cdd:cd01663   102 LLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLI 181


                  ...
gi 1573757531 161 TTI 163
Cdd:cd01663   182 TAF 184
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
3-163 1.22e-46

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 158.75  E-value: 1.22e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573757531   3 MSIIIRLELSMPGKLLNNDQIYNSIVTSHAFIMIFFMVMPiMLGGFGNWLIPLMLGAPDMAFPRMNNMSFWIIVPSLMMM 82
Cdd:COG0843    36 LALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573757531  83 LLSSFINIGAGTGWTIYPPLSANLSHSGMSMDLVIFSLHLAGISSILGSINFMTTIMNMRLFFYKMDQLTLLFWSIFITT 162
Cdd:COG0843   115 LISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTS 194


                  .
gi 1573757531 163 I 163
Cdd:COG0843   195 I 195
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 3-163 5.55e-27

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: 104.58  E-value: 5.55e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573757531   3 MSIIIRLELSMPGKLLNNDQIYNSIVTSHAFIMIFFMVMPIMlGGFGNWLIPLMLGAPDMAFPRMNNMSFWIIVPSLMMM 82
Cdd:pfam00115  20 LGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPFL-FGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573757531  83 LLSSfinIGAGTGWTIYPPLSAnlshsgmsMDLVIFSLHLAGISSILGSINFMTTIMNMRLFFYKMdQLTLLFWSIFITT 162
Cdd:pfam00115  99 LASF---GGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATA 166


                  .
gi 1573757531 163 I 163
Cdd:pfam00115 167 I 167
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 4-163 4.01e-26

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: 103.40  E-value: 4.01e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573757531   4 SIIIRLELSMPGKLLNNDQIYNSIVTSHAFIMIFFMVMPIMLGgFGNWLIPLMLGAPDMAFPRMNNMSFWIIVPSLMMML 83
Cdd:TIGR02882  72 ALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFN 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573757531  84 LSSFINIGAGTGWTIYPPLSANLSHSGMSMDLVIFSLHLAGISSILGSINFMTTIMNMRLFFYKMDQLTLLFWSIFITTI 163
Cdd:TIGR02882 151 ISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTL 230
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 2-163 1.38e-90

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 272.51  E-value: 1.38e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573757531   2 SMSIIIRLELSMPGKLLNNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGNWLIPLMLGAPDMAFPRMNNMSFWIIVPSLMM 81
Cdd:MTH00153   30 SLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTL 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573757531  82 MLLSSFINIGAGTGWTIYPPLSANLSHSGMSMDLVIFSLHLAGISSILGSINFMTTIMNMRLFFYKMDQLTLLFWSIFIT 161
Cdd:MTH00153  110 LLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLIT 189


                  ..
gi 1573757531 162 TI 163
Cdd:MTH00153  190 AI 191
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-163 2.40e-87

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: 263.57  E-value: 2.40e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573757531   1 LSMSIIIRLELSMPGKLLNNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGNWLIPLMLGAPDMAFPRMNNMSFWIIVPSLM 80
Cdd:cd01663    22 TSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLL 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573757531  81 MMLLSSFINIGAGTGWTIYPPLSANLSHSGMSMDLVIFSLHLAGISSILGSINFMTTIMNMRLFFYKMDQLTLLFWSIFI 160
Cdd:cd01663   102 LLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLI 181


                  ...
gi 1573757531 161 TTI 163
Cdd:cd01663   182 TAF 184
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 2-163 1.02e-82

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 252.29  E-value: 1.02e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573757531   2 SMSIIIRLELSMPGKLLNNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGNWLIPLMLGAPDMAFPRMNNMSFWIIVPSLMM 81
Cdd:MTH00167   32 ALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLL 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573757531  82 MLLSSFINIGAGTGWTIYPPLSANLSHSGMSMDLVIFSLHLAGISSILGSINFMTTIMNMRLFFYKMDQLTLLFWSIFIT 161
Cdd:MTH00167  112 LLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVT 191


                  ..
gi 1573757531 162 TI 163
Cdd:MTH00167  192 TI 193
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-161 5.47e-79

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 242.96  E-value: 5.47e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573757531   1 LSMSIIIRLELSMPGKLLNNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGNWLIPLMLGAPDMAFPRMNNMSFWIIVPSLM 80
Cdd:MTH00223   28 TSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLY 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573757531  81 MMLLSSFINIGAGTGWTIYPPLSANLSHSGMSMDLVIFSLHLAGISSILGSINFMTTIMNMRLFFYKMDQLTLLFWSIFI 160
Cdd:MTH00223  108 LLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKV 187


                  .
gi 1573757531 161 T 161
Cdd:MTH00223  188 T 188
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 2-163 1.61e-77

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 239.22  E-value: 1.61e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573757531   2 SMSIIIRLELSMPGKLLNNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGNWLIPLMLGAPDMAFPRMNNMSFWIIVPSLMM 81
Cdd:MTH00116   32 ALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLL 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573757531  82 MLLSSFINIGAGTGWTIYPPLSANLSHSGMSMDLVIFSLHLAGISSILGSINFMTTIMNMRLFFYKMDQLTLLFWSIFIT 161
Cdd:MTH00116  112 LLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLIT 191


                  ..
gi 1573757531 162 TI 163
Cdd:MTH00116  192 AV 193
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-163 9.74e-76

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 234.62  E-value: 9.74e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573757531   1 LSMSIIIRLELSMPGKLLNNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGNWLIPLMLGAPDMAFPRMNNMSFWIIVPSLM 80
Cdd:MTH00142   29 TGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALL 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573757531  81 MMLLSSFINIGAGTGWTIYPPLSANLSHSGMSMDLVIFSLHLAGISSILGSINFMTTIMNMRLFFYKMDQLTLLFWSIFI 160
Cdd:MTH00142  109 LLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKI 188


                  ...
gi 1573757531 161 TTI 163
Cdd:MTH00142  189 TAI 191
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 2-163 2.74e-70

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 220.47  E-value: 2.74e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573757531   2 SMSIIIRLELSMPGKLLNNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGNWLIPLMLGAPDMAFPRMNNMSFWIIVPSLMM 81
Cdd:MTH00037   32 AMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLL 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573757531  82 MLLSSFINIGAGTGWTIYPPLSANLSHSGMSMDLVIFSLHLAGISSILGSINFMTTIMNMRLFFYKMDQLTLLFWSIFIT 161
Cdd:MTH00037  112 LLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFIT 191


                  ..
gi 1573757531 162 TI 163
Cdd:MTH00037  192 AF 193
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 2-163 4.57e-69

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 217.48  E-value: 4.57e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573757531   2 SMSIIIRLELSMPGKLLNNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGNWLIPLMLGAPDMAFPRMNNMSFWIIVPSLMM 81
Cdd:MTH00183   32 ALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLL 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573757531  82 MLLSSFINIGAGTGWTIYPPLSANLSHSGMSMDLVIFSLHLAGISSILGSINFMTTIMNMRLFFYKMDQLTLLFWSIFIT 161
Cdd:MTH00183  112 LLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLIT 191


                  ..
gi 1573757531 162 TI 163
Cdd:MTH00183  192 AV 193
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 2-163 3.94e-68

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 214.75  E-value: 3.94e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573757531   2 SMSIIIRLELSMPGKLLNNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGNWLIPLMLGAPDMAFPRMNNMSFWIIVPSLMM 81
Cdd:MTH00103   32 ALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLL 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573757531  82 MLLSSFINIGAGTGWTIYPPLSANLSHSGMSMDLVIFSLHLAGISSILGSINFMTTIMNMRLFFYKMDQLTLLFWSIFIT 161
Cdd:MTH00103  112 LLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLIT 191


                  ..
gi 1573757531 162 TI 163
Cdd:MTH00103  192 AV 193
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 2-163 7.11e-68

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 214.03  E-value: 7.11e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573757531   2 SMSIIIRLELSMPGKLLNNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGNWLIPLMLGAPDMAFPRMNNMSFWIIVPSLMM 81
Cdd:MTH00077   32 ALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLL 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573757531  82 MLLSSFINIGAGTGWTIYPPLSANLSHSGMSMDLVIFSLHLAGISSILGSINFMTTIMNMRLFFYKMDQLTLLFWSIFIT 161
Cdd:MTH00077  112 LLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLIT 191


                  ..
gi 1573757531 162 TI 163
Cdd:MTH00077  192 AV 193
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 2-163 2.14e-67

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 212.84  E-value: 2.14e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573757531   2 SMSIIIRLELSMPGKLLNNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGNWLIPLMLGAPDMAFPRMNNMSFWIIVPSLMM 81
Cdd:MTH00007   29 SMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPALIL 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573757531  82 MLLSSFINIGAGTGWTIYPPLSANLSHSGMSMDLVIFSLHLAGISSILGSINFMTTIMNMRLFFYKMDQLTLLFWSIFIT 161
Cdd:MTH00007  109 LVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVIT 188


                  ..
gi 1573757531 162 TI 163
Cdd:MTH00007  189 VV 190
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-163 7.45e-65

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 206.60  E-value: 7.45e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573757531   1 LSMSIIIRLELSMPGKLLNNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGNWLIPLMLGAPDMAFPRMNNMSFWIIVPSLM 80
Cdd:MTH00184   33 TAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPALT 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573757531  81 MMLLSSFINIGAGTGWTIYPPLSANLSHSGMSMDLVIFSLHLAGISSILGSINFMTTIMNMRLFFYKMDQLTLLFWSIFI 160
Cdd:MTH00184  113 LLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILV 192


                  ...
gi 1573757531 161 TTI 163
Cdd:MTH00184  193 TTF 195
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 2-163 8.11e-64

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 203.90  E-value: 8.11e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573757531   2 SMSIIIRLELSMPGKLLNNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGNWLIPLMLGAPDMAFPRMNNMSFWIIVPSLMM 81
Cdd:MTH00182   34 AFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALIL 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573757531  82 MLLSSFINIGAGTGWTIYPPLSANLSHSGMSMDLVIFSLHLAGISSILGSINFMTTIMNMRLFFYKMDQLTLLFWSIFIT 161
Cdd:MTH00182  114 LLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILIT 193


                  ..
gi 1573757531 162 TI 163
Cdd:MTH00182  194 AF 195
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-161 4.90e-62

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 198.75  E-value: 4.90e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573757531   1 LSMSIIIRLELSMPGKLLNNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGNWLIPLMLGAPDMAFPRMNNMSFWIIVPSLM 80
Cdd:MTH00079   32 TSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLF 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573757531  81 MMLLSSFINIGAGTGWTIYPPLSaNLSHSGMSMDLVIFSLHLAGISSILGSINFMTTIMNMRLFFYKMDQLTLLFWSIFI 160
Cdd:MTH00079  112 LILDSCFVDMGPGTSWTVYPPLS-TLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFV 190


                  .
gi 1573757531 161 T 161
Cdd:MTH00079  191 T 191
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 2-163 8.91e-57

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 185.60  E-value: 8.91e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573757531   2 SMSIIIRLELSMPGKLLNNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGNWLIPLMLGAPDMAFPRMNNMSFWIIVPSLMM 81
Cdd:MTH00026   33 AFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPALFL 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573757531  82 MLLSSFINIGAGTGWTIYPPLSANLSHSGMSMDLVIFSLHLAGISSILGSINFMTTIMNMRLFFYKMDQLTLLFWSIFIT 161
Cdd:MTH00026  113 LLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFIT 192


                  ..
gi 1573757531 162 TI 163
Cdd:MTH00026  193 AI 194
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-163 2.04e-51

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: 170.02  E-value: 2.04e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573757531   1 LSMSIIIRLELSMPGKLLNNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGNWLIPlMLGAPDMAFPRMNNMSFWIIVPSLM 80
Cdd:cd00919    20 GLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWLFPPGLL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573757531  81 MMLLSSFINIGAGTGWTIYPPLSANLSHSGMSMDLVIFSLHLAGISSILGSINFMTTIMNMRLFFYKMDQLTLLFWSIFI 160
Cdd:cd00919    99 LLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLV 178


                  ...
gi 1573757531 161 TTI 163
Cdd:cd00919   179 TAI 181
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
3-163 1.22e-46

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 158.75  E-value: 1.22e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573757531   3 MSIIIRLELSMPGKLLNNDQIYNSIVTSHAFIMIFFMVMPiMLGGFGNWLIPLMLGAPDMAFPRMNNMSFWIIVPSLMMM 82
Cdd:COG0843    36 LALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573757531  83 LLSSFINIGAGTGWTIYPPLSANLSHSGMSMDLVIFSLHLAGISSILGSINFMTTIMNMRLFFYKMDQLTLLFWSIFITT 162
Cdd:COG0843   115 LISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTS 194


                  .
gi 1573757531 163 I 163
Cdd:COG0843   195 I 195
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-139 8.44e-41

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 142.89  E-value: 8.44e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573757531   1 LSMSIIIRLELSMPGKLLNNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGNWLIPLMLGAPDMAFPRMNNMSFWIIVPSLM 80
Cdd:MTH00048   32 LSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIV 111

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1573757531  81 MMLLSSFinIGAGTGWTIYPPLSANLSHSGMSMDLVIFSLHLAGISSILGSINFMTTIM 139
Cdd:MTH00048  112 FLLLSMC--LGAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIY 168
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 2-163 7.98e-38

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: 134.63  E-value: 7.98e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573757531   2 SMSIIIRLELSMPGKLLNNDQIYNSIVTSHAFIMIFFMVMPIMLGgFGNWLIPLMLGAPDMAFPRMNNMSFWIIVPSLMM 81
Cdd:cd01662    27 VDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGGLL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573757531  82 MLLSSFINIGAGTGWTIYPPLSANLSHSGMSMDLVIFSLHLAGISSILGSINFMTTIMNMRLFFYKMDQLTLLFWSIFIT 161
Cdd:cd01662   106 LNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVT 185


                  ..
gi 1573757531 162 TI 163
Cdd:cd01662   186 SI 187
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 3-163 5.55e-27

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: 104.58  E-value: 5.55e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573757531   3 MSIIIRLELSMPGKLLNNDQIYNSIVTSHAFIMIFFMVMPIMlGGFGNWLIPLMLGAPDMAFPRMNNMSFWIIVPSLMMM 82
Cdd:pfam00115  20 LGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPFL-FGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573757531  83 LLSSfinIGAGTGWTIYPPLSAnlshsgmsMDLVIFSLHLAGISSILGSINFMTTIMNMRLFFYKMdQLTLLFWSIFITT 162
Cdd:pfam00115  99 LASF---GGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATA 166


                  .
gi 1573757531 163 I 163
Cdd:pfam00115 167 I 167
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 4-163 4.01e-26

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: 103.40  E-value: 4.01e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573757531   4 SIIIRLELSMPGKLLNNDQIYNSIVTSHAFIMIFFMVMPIMLGgFGNWLIPLMLGAPDMAFPRMNNMSFWIIVPSLMMML 83
Cdd:TIGR02882  72 ALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFN 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573757531  84 LSSFINIGAGTGWTIYPPLSANLSHSGMSMDLVIFSLHLAGISSILGSINFMTTIMNMRLFFYKMDQLTLLFWSIFITTI 163
Cdd:TIGR02882 151 ISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTL 230
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 24-163 4.50e-25

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 100.40  E-value: 4.50e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573757531  24 YNSIVTSHAFIMIFFMVMPIMLGgFGNWLIPLMLGAPDMAFPRMNNMSFWIIVPSLMMMLLSSFINIGAGTGWTIYPPLS 103
Cdd:PRK15017   99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573757531 104 ANLSHSGMSMDLVIFSLHLAGISSILGSINFMTTIMNMRLFFYKMDQLTLLFWSIFITTI 163
Cdd:PRK15017  178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANV 237
 
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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