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Conserved domains on  [gi|1402364108|gb|AWU57067|]
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cytochrome c oxidase subunit I, partial (mitochondrion) [Arthropoda sp. KSA_1489]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Heme_Cu_Oxidase_I super family cl00275
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
1-219 1.94e-140

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: 412277  Cd Length: 511  Bit Score: 402.32  E-value: 1.94e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402364108   1 TLYFIFGAWSGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:MTH00153   15 TLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402364108  81 MNNMSFWLLPPSLTLLLMSGMVESGVGTGWTVYPPLAAAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTVINMRSFGM 160
Cdd:MTH00153   95 MNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGM 174
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1402364108 161 SMDQMPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLF 219
Cdd:MTH00153  175 TLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 233
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
1-219 1.94e-140

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 402.32  E-value: 1.94e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402364108   1 TLYFIFGAWSGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:MTH00153   15 TLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402364108  81 MNNMSFWLLPPSLTLLLMSGMVESGVGTGWTVYPPLAAAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTVINMRSFGM 160
Cdd:MTH00153   95 MNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGM 174
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1402364108 161 SMDQMPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLF 219
Cdd:MTH00153  175 TLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 233
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
1-219 1.04e-125

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: 363.73  E-value: 1.04e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402364108   1 TLYFIFGAWSGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:cd01663     8 TLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPR 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402364108  81 MNNMSFWLLPPSLTLLLMSGMVESGVGTGWTVYPPLAAAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTVINMRSFGM 160
Cdd:cd01663    88 LNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGM 167
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1402364108 161 SMDQMPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLF 219
Cdd:cd01663   168 TLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 226
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-219 1.74e-66

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


Pssm-ID: 223913  Cd Length: 566  Bit Score: 214.08  E-value: 1.74e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402364108   1 TLYFIFGAWSGMVGTSLSLIIRAELGQPGTL-IGNDQIYNVVVTAHAFVMIFFMVMPiMIGGFGNWLVPLMLGAPDMAFP 79
Cdd:COG0843    21 ILYLILAIFFLLVGGALALLMRLELATPSGSqFLDPQLYNQILTLHGVIMIFFFAMP-AIGGFANYLVPLMIGARDVAFP 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402364108  80 RMNNMSFWLLPPSLTLLLMSGMVESGVG-TGWTVYPPLAAAIAHAGaSVDLGIFSLHLAGVSSILGAVNFMTTVINMRSF 158
Cdd:COG0843   100 RLNAISFWLLVVGAILLVTSFFVPGGAAdTGWTAYPPLSAISYSGP-GVDLFILGLHLLGIGSLLGAINFIVTILNMRAP 178
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1402364108 159 GMSMDQMPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLF 219
Cdd:COG0843   179 GMTMMKMPLFTWSILITAILILLAFPVLAAALTMLLLDRNFGTSFFTPAGGGDPLLYQHLF 239
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I;
2-219 8.51e-42

Cytochrome C and Quinol oxidase polypeptide I;


Pssm-ID: 395065  Cd Length: 434  Bit Score: 146.56  E-value: 8.51e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402364108   2 LYFIFGAWSGMVGTSLSLIIRAELGQPGTLigndQIYNVVVTAHAFVMIFFMVMPiMIGGFGNWLVPLMLGAPDMAFPRM 81
Cdd:pfam00115   5 LYLVTALVWFLVGGLLGLLIRLQLAFPLDP----LTYNQLRTLHGNLMIFGFATP-FIFGFGNYLVPLMIGARDMAFPRL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402364108  82 NNMSFWLLPPSLTLLLMSGMveSGVGTGWTVYPPLAaaiahagaSVDLGIFSLHLAGVSSILGAVNFMTTVINMRSFGMS 161
Cdd:pfam00115  80 NALSFWLVVLGAVLLLASFF--GGATTGWTEYPPLT--------GVDLWYLGLLLAGVGSLLGAINFIVTILKRRAPGMY 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1402364108 162 MDQMPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPaggGDPVLYQHLF 219
Cdd:pfam00115 150 LSRMPLFVWAILATAILILLAFPVLAAALLLLLLDRSFGTHFFDP---GDPLLDQHLF 204
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
1-219 1.94e-140

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 402.32  E-value: 1.94e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402364108   1 TLYFIFGAWSGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:MTH00153   15 TLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402364108  81 MNNMSFWLLPPSLTLLLMSGMVESGVGTGWTVYPPLAAAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTVINMRSFGM 160
Cdd:MTH00153   95 MNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGM 174
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1402364108 161 SMDQMPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLF 219
Cdd:MTH00153  175 TLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 233
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
1-219 1.04e-125

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: 363.73  E-value: 1.04e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402364108   1 TLYFIFGAWSGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:cd01663     8 TLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPR 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402364108  81 MNNMSFWLLPPSLTLLLMSGMVESGVGTGWTVYPPLAAAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTVINMRSFGM 160
Cdd:cd01663    88 LNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGM 167
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1402364108 161 SMDQMPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLF 219
Cdd:cd01663   168 TLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 226
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
1-219 1.97e-122

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 356.29  E-value: 1.97e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402364108   1 TLYFIFGAWSGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:MTH00167   17 TLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPR 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402364108  81 MNNMSFWLLPPSLTLLLMSGMVESGVGTGWTVYPPLAAAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTVINMRSFGM 160
Cdd:MTH00167   97 MNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGI 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1402364108 161 SMDQMPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLF 219
Cdd:MTH00167  177 TQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
1-219 3.05e-118

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 345.56  E-value: 3.05e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402364108   1 TLYFIFGAWSGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:MTH00142   15 TLYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPR 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402364108  81 MNNMSFWLLPPSLTLLLMSGMVESGVGTGWTVYPPLAAAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTVINMRSFGM 160
Cdd:MTH00142   95 MNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGM 174
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1402364108 161 SMDQMPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLF 219
Cdd:MTH00142  175 KFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 233
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
1-219 5.04e-118

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 345.15  E-value: 5.04e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402364108   1 TLYFIFGAWSGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:MTH00116   17 TLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPR 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402364108  81 MNNMSFWLLPPSLTLLLMSGMVESGVGTGWTVYPPLAAAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTVINMRSFGM 160
Cdd:MTH00116   97 MNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAM 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1402364108 161 SMDQMPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLF 219
Cdd:MTH00116  177 SQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
1-219 3.00e-114

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 335.41  E-value: 3.00e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402364108   1 TLYFIFGAWSGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:MTH00223   14 TLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPR 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402364108  81 MNNMSFWLLPPSLTLLLMSGMVESGVGTGWTVYPPLAAAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTVINMRSFGM 160
Cdd:MTH00223   94 LNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGM 173
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1402364108 161 SMDQMPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLF 219
Cdd:MTH00223  174 QLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 232
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
1-219 5.30e-105

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 312.20  E-value: 5.30e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402364108   1 TLYFIFGAWSGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:MTH00103   17 TLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPR 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402364108  81 MNNMSFWLLPPSLTLLLMSGMVESGVGTGWTVYPPLAAAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTVINMRSFGM 160
Cdd:MTH00103   97 MNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAM 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1402364108 161 SMDQMPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLF 219
Cdd:MTH00103  177 SQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
1-219 5.53e-105

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 312.15  E-value: 5.53e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402364108   1 TLYFIFGAWSGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:MTH00037   17 TLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPR 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402364108  81 MNNMSFWLLPPSLTLLLMSGMVESGVGTGWTVYPPLAAAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTVINMRSFGM 160
Cdd:MTH00037   97 MNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGM 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1402364108 161 SMDQMPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLF 219
Cdd:MTH00037  177 TFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLF 235
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
1-219 1.76e-104

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 310.72  E-value: 1.76e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402364108   1 TLYFIFGAWSGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:MTH00077   17 TLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPR 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402364108  81 MNNMSFWLLPPSLTLLLMSGMVESGVGTGWTVYPPLAAAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTVINMRSFGM 160
Cdd:MTH00077   97 MNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSM 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1402364108 161 SMDQMPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLF 219
Cdd:MTH00077  177 SQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLF 235
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
1-219 7.99e-104

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 309.16  E-value: 7.99e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402364108   1 TLYFIFGAWSGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:MTH00183   17 TLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPR 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402364108  81 MNNMSFWLLPPSLTLLLMSGMVESGVGTGWTVYPPLAAAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTVINMRSFGM 160
Cdd:MTH00183   97 MNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAI 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1402364108 161 SMDQMPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLF 219
Cdd:MTH00183  177 SQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
1-219 3.35e-103

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 307.21  E-value: 3.35e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402364108   1 TLYFIFGAWSGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:MTH00007   14 TLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPR 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402364108  81 MNNMSFWLLPPSLTLLLMSGMVESGVGTGWTVYPPLAAAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTVINMRSFGM 160
Cdd:MTH00007   94 LNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGL 173
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1402364108 161 SMDQMPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLF 219
Cdd:MTH00007  174 RLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 232
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
1-219 9.42e-97

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 290.81  E-value: 9.42e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402364108   1 TLYFIFGAWSGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:MTH00079   18 TLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPR 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402364108  81 MNNMSFWLLPPSLTLLLMSGMVESGVGTGWTVYPPLaAAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTVINMRSFGM 160
Cdd:MTH00079   98 LNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPL-STLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSI 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1402364108 161 SMDQMPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLF 219
Cdd:MTH00079  177 SLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLF 235
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
1-219 1.42e-94

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 285.56  E-value: 1.42e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402364108   1 TLYFIFGAWSGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:MTH00182   19 TLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPR 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402364108  81 MNNMSFWLLPPSLTLLLMSGMVESGVGTGWTVYPPLAAAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTVINMRSFGM 160
Cdd:MTH00182   99 LNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGV 178
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1402364108 161 SMDQMPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLF 219
Cdd:MTH00182  179 TFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLF 237
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
1-219 4.08e-94

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 284.41  E-value: 4.08e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402364108   1 TLYFIFGAWSGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:MTH00184   19 TLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPR 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402364108  81 MNNMSFWLLPPSLTLLLMSGMVESGVGTGWTVYPPLAAAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTVINMRSFGM 160
Cdd:MTH00184   99 LNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGI 178
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1402364108 161 SMDQMPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLF 219
Cdd:MTH00184  179 TMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLF 237
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
1-219 8.71e-86

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 263.41  E-value: 8.71e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402364108   1 TLYFIFGAWSGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:MTH00026   18 SLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPR 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402364108  81 MNNMSFWLLPPSLTLLLMSGMVESGVGTGWTVYPPLAAAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTVINMRSFGM 160
Cdd:MTH00026   98 LNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGM 177
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1402364108 161 SMDQMPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLF 219
Cdd:MTH00026  178 TMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLF 236
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
1-219 2.37e-76

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: 237.04  E-value: 2.37e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402364108   1 TLYFIFGAWSGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPlMLGAPDMAFPR 80
Cdd:cd00919     6 LLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPR 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402364108  81 MNNMSFWLLPPSLTLLLMSGMVESGVGTGWTVYPPLAAAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTVINMRSFGM 160
Cdd:cd00919    85 LNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGM 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1402364108 161 SMDQMPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLF 219
Cdd:cd00919   165 TLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLF 223
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-219 1.74e-66

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


Pssm-ID: 223913  Cd Length: 566  Bit Score: 214.08  E-value: 1.74e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402364108   1 TLYFIFGAWSGMVGTSLSLIIRAELGQPGTL-IGNDQIYNVVVTAHAFVMIFFMVMPiMIGGFGNWLVPLMLGAPDMAFP 79
Cdd:COG0843    21 ILYLILAIFFLLVGGALALLMRLELATPSGSqFLDPQLYNQILTLHGVIMIFFFAMP-AIGGFANYLVPLMIGARDVAFP 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402364108  80 RMNNMSFWLLPPSLTLLLMSGMVESGVG-TGWTVYPPLAAAIAHAGaSVDLGIFSLHLAGVSSILGAVNFMTTVINMRSF 158
Cdd:COG0843   100 RLNAISFWLLVVGAILLVTSFFVPGGAAdTGWTAYPPLSAISYSGP-GVDLFILGLHLLGIGSLLGAINFIVTILNMRAP 178
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1402364108 159 GMSMDQMPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLF 219
Cdd:COG0843   179 GMTMMKMPLFTWSILITAILILLAFPVLAAALTMLLLDRNFGTSFFTPAGGGDPLLYQHLF 239
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
2-219 1.07e-59

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 195.28  E-value: 1.07e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402364108   2 LYFIFGAWSGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRM 81
Cdd:MTH00048   19 IYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRL 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402364108  82 NNMSFWLLPPSLTLLLMSgmVESGVGTGWTVYPPLAAAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTVINMRSFGMS 161
Cdd:MTH00048   99 NALSAWLLVPSIVFLLLS--MCLGAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVF 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1402364108 162 MdQMPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLF 219
Cdd:MTH00048  177 S-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMF 233
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
14-219 1.31e-52

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: 176.23  E-value: 1.31e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402364108  14 GTSLSLIIRAELGQP-GTLIGNDQiYNVVVTAHAFVMIFFMVMPIMIGgFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPS 92
Cdd:cd01662    25 GGVDALLMRTQLALPgNDFLSPEH-YNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFG 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402364108  93 LTLLLMSGMVESGVGTGWTVYPPLAAAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTVINMRSFGMSMDQMPLFVWSV 172
Cdd:cd01662   103 GLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTT 182
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1402364108 173 FITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLF 219
Cdd:cd01662   183 LVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLF 229
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I;
2-219 8.51e-42

Cytochrome C and Quinol oxidase polypeptide I;


Pssm-ID: 395065  Cd Length: 434  Bit Score: 146.56  E-value: 8.51e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402364108   2 LYFIFGAWSGMVGTSLSLIIRAELGQPGTLigndQIYNVVVTAHAFVMIFFMVMPiMIGGFGNWLVPLMLGAPDMAFPRM 81
Cdd:pfam00115   5 LYLVTALVWFLVGGLLGLLIRLQLAFPLDP----LTYNQLRTLHGNLMIFGFATP-FIFGFGNYLVPLMIGARDMAFPRL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402364108  82 NNMSFWLLPPSLTLLLMSGMveSGVGTGWTVYPPLAaaiahagaSVDLGIFSLHLAGVSSILGAVNFMTTVINMRSFGMS 161
Cdd:pfam00115  80 NALSFWLVVLGAVLLLASFF--GGATTGWTEYPPLT--------GVDLWYLGLLLAGVGSLLGAINFIVTILKRRAPGMY 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1402364108 162 MDQMPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPaggGDPVLYQHLF 219
Cdd:pfam00115 150 LSRMPLFVWAILATAILILLAFPVLAAALLLLLLDRSFGTHFFDP---GDPLLDQHLF 204
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
38-218 1.74e-31

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 120.81  E-value: 1.74e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402364108  38 YNVVVTAHAFVMIFFMVMPIMIGgFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLMSGMVESGVGTGWTVYPPLA 117
Cdd:PRK15017   99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402364108 118 AAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTVINMRSFGMSMDQMPLFVWSVFITAILLLLSLPVLAGAITMLLTDR 197
Cdd:PRK15017  178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257
                         170       180
                  ....*....|....*....|.
gi 1402364108 198 NLNTSFFDPAGGGDPVLYQHL 218
Cdd:PRK15017  258 YLGTHFFTNDMGGNMMMYINL 278
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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