NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|323328809|gb|ADX38387|]
View 

cytochrome oxidase subunit 1, partial (mitochondrion) [Chirothrips meridionalis]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 1-218 4.01e-124

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: 360.72  E-value: 4.01e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809   1 ILYFLFGFWSGILGLSLSMLIRLNLRTPmKLFISNDQFYNSVVTAHAFIMIFFTVMPIMIGGFGNWLVPLMLGAPDMAFP 80
Cdd:MTH00153  15 TLYFIFGAWSGMVGTSLSLLIRAELGQP-GSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFP 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809  81 RLNNMSFWLLPPSIILLIMGLSKE-GAGTGWTVYPPLSTF-YHSGMSVDLTIFSLHLAGISSILGALNFITTIINLKTKN 158
Cdd:MTH00153  94 RMNNMSFWLLPPSLTLLLSSSMVEsGAGTGWTVYPPLSSNiAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKG 173

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809 159 LSSNKMSLFIWSVILTAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPVLYQHLF 218
Cdd:MTH00153 174 MTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 233
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-218 4.01e-124

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 360.72  E-value: 4.01e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809   1 ILYFLFGFWSGILGLSLSMLIRLNLRTPmKLFISNDQFYNSVVTAHAFIMIFFTVMPIMIGGFGNWLVPLMLGAPDMAFP 80
Cdd:MTH00153  15 TLYFIFGAWSGMVGTSLSLLIRAELGQP-GSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFP 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809  81 RLNNMSFWLLPPSIILLIMGLSKE-GAGTGWTVYPPLSTF-YHSGMSVDLTIFSLHLAGISSILGALNFITTIINLKTKN 158
Cdd:MTH00153  94 RMNNMSFWLLPPSLTLLLSSSMVEsGAGTGWTVYPPLSSNiAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKG 173

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809 159 LSSNKMSLFIWSVILTAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPVLYQHLF 218
Cdd:MTH00153 174 MTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 233
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-218 8.66e-120

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: 348.70  E-value: 8.66e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809   1 ILYFLFGFWSGILGLSLSMLIRLNLRTPmKLFISNDQFYNSVVTAHAFIMIFFTVMPIMIGGFGNWLVPLMLGAPDMAFP 80
Cdd:cd01663    8 TLYLIFGLWSGLVGTSLSLLIRLELSQP-GSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFP 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809  81 RLNNMSFWLLPPSIILLIMGLSKE-GAGTGWTVYPPLSTF-YHSGMSVDLTIFSLHLAGISSILGALNFITTIINLKTKN 158
Cdd:cd01663   87 RLNNLSFWLLPPSLLLLLLSALVEgGAGTGWTVYPPLSSIlAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPG 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809 159 LSSNKMSLFIWSVILTAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPVLYQHLF 218
Cdd:cd01663  167 MTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 226
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-218 4.06e-69

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 220.38  E-value: 4.06e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809   1 ILYFLFGFWSGILGLSLSMLIRLNLRTPMKLFISNDQfYNSVVTAHAFIMIFFTVMPiMIGGFGNWLVPLMLGAPDMAFP 80
Cdd:COG0843   20 IMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPET-YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFP 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809  81 RLNNMSFWLLPPSIILLIMGL-SKEGAGTGWTVYPPLSTF-YHSGMSVDLTIFSLHLAGISSILGALNFITTIINLKTKN 158
Cdd:COG0843   98 RLNALSFWLYLFGGLLLLISLfVGGAADVGWTFYPPLSGLeASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPG 177

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809 159 LSSNKMSLFIWSVILTAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPVLYQHLF 218
Cdd:COG0843  178 MTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLF 237
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-218 9.51e-44

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: 151.57  E-value: 9.51e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809    1 ILYFLFGFWSGILGLSLSMLIRLNLRTPMKLFISNdQFYNSVVTAHAFIMIFFTVMPiMIGGFGNWLVPLMLGAPDMAFP 80
Cdd:pfam00115   4 LLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSP-LTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809   81 RLNNMSFWLLPPSIILLIMGLskEGAGTGWTVYPPLstfyhsgMSVDLTIFSLHLAGISSILGALNFITTIINLKTKNLs 160
Cdd:pfam00115  82 RLNALSFWLVVLGAVLLLASF--GGATTGWTEYPPL-------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGM- 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 323328809  161 SNKMSLFIWSVILTAILLLLSLPVLAGAITMLLTDRNLNTsffdpsGGGDPVLYQHLF 218
Cdd:pfam00115 152 TLRMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLF 203
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-218 4.01e-124

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 360.72  E-value: 4.01e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809   1 ILYFLFGFWSGILGLSLSMLIRLNLRTPmKLFISNDQFYNSVVTAHAFIMIFFTVMPIMIGGFGNWLVPLMLGAPDMAFP 80
Cdd:MTH00153  15 TLYFIFGAWSGMVGTSLSLLIRAELGQP-GSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFP 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809  81 RLNNMSFWLLPPSIILLIMGLSKE-GAGTGWTVYPPLSTF-YHSGMSVDLTIFSLHLAGISSILGALNFITTIINLKTKN 158
Cdd:MTH00153  94 RMNNMSFWLLPPSLTLLLSSSMVEsGAGTGWTVYPPLSSNiAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKG 173

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809 159 LSSNKMSLFIWSVILTAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPVLYQHLF 218
Cdd:MTH00153 174 MTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 233
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-218 8.66e-120

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: 348.70  E-value: 8.66e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809   1 ILYFLFGFWSGILGLSLSMLIRLNLRTPmKLFISNDQFYNSVVTAHAFIMIFFTVMPIMIGGFGNWLVPLMLGAPDMAFP 80
Cdd:cd01663    8 TLYLIFGLWSGLVGTSLSLLIRLELSQP-GSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFP 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809  81 RLNNMSFWLLPPSIILLIMGLSKE-GAGTGWTVYPPLSTF-YHSGMSVDLTIFSLHLAGISSILGALNFITTIINLKTKN 158
Cdd:cd01663   87 RLNNLSFWLLPPSLLLLLLSALVEgGAGTGWTVYPPLSSIlAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPG 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809 159 LSSNKMSLFIWSVILTAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPVLYQHLF 218
Cdd:cd01663  167 MTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 226
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 2-218 3.56e-110

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 325.09  E-value: 3.56e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809   2 LYFLFGFWSGILGLSLSMLIRLNLRTPMKLfISNDQFYNSVVTAHAFIMIFFTVMPIMIGGFGNWLVPLMLGAPDMAFPR 81
Cdd:MTH00167  18 LYFIFGAWAGMVGTALSLLIRAELSQPGSL-LGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPR 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809  82 LNNMSFWLLPPSIILLIM-GLSKEGAGTGWTVYPPLS-TFYHSGMSVDLTIFSLHLAGISSILGALNFITTIINLKTKNL 159
Cdd:MTH00167  97 MNNMSFWLLPPSLLLLLAsSGVEAGAGTGWTVYPPLAgNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGI 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 323328809 160 SSNKMSLFIWSVILTAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPVLYQHLF 218
Cdd:MTH00167 177 TQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 2-218 1.98e-108

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 320.77  E-value: 1.98e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809   2 LYFLFGFWSGILGLSLSMLIRLNLRTPMKLFiSNDQFYNSVVTAHAFIMIFFTVMPIMIGGFGNWLVPLMLGAPDMAFPR 81
Cdd:MTH00223  15 LYLIFGMWSGLVGTSLSLLIRAELGQPGALL-GDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPR 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809  82 LNNMSFWLLPPSIILLIM-GLSKEGAGTGWTVYPPLS-TFYHSGMSVDLTIFSLHLAGISSILGALNFITTIINLKTKNL 159
Cdd:MTH00223  94 LNNMSFWLLPPSLYLLLSsSAVESGVGTGWTVYPPLSsNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGM 173

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 323328809 160 SSNKMSLFIWSVILTAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPVLYQHLF 218
Cdd:MTH00223 174 QLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 232
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 2-218 6.08e-107

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 317.03  E-value: 6.08e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809   2 LYFLFGFWSGILGLSLSMLIRLNLRTPMKLFiSNDQFYNSVVTAHAFIMIFFTVMPIMIGGFGNWLVPLMLGAPDMAFPR 81
Cdd:MTH00116  18 LYLIFGAWAGMVGTALSLLIRAELGQPGTLL-GDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPR 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809  82 LNNMSFWLLPPSIILLIMGLSKE-GAGTGWTVYPPLS-TFYHSGMSVDLTIFSLHLAGISSILGALNFITTIINLKTKNL 159
Cdd:MTH00116  97 MNNMSFWLLPPSFLLLLASSTVEaGAGTGWTVYPPLAgNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAM 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 323328809 160 SSNKMSLFIWSVILTAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPVLYQHLF 218
Cdd:MTH00116 177 SQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 2-218 1.11e-103

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 308.58  E-value: 1.11e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809   2 LYFLFGFWSGILGLSLSMLIRLNLRTPMKLfISNDQFYNSVVTAHAFIMIFFTVMPIMIGGFGNWLVPLMLGAPDMAFPR 81
Cdd:MTH00142  16 LYFLFGAWAGMVGTGLSLLIRAELGQPGSL-LGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPR 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809  82 LNNMSFWLLPPSIILLIM-GLSKEGAGTGWTVYPPLST-FYHSGMSVDLTIFSLHLAGISSILGALNFITTIINLKTKNL 159
Cdd:MTH00142  95 MNNMSFWLLPPALLLLLSsAAVESGAGTGWTVYPPLSSnLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGM 174

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 323328809 160 SSNKMSLFIWSVILTAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPVLYQHLF 218
Cdd:MTH00142 175 KFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 233
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 2-218 9.50e-95

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 285.42  E-value: 9.50e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809   2 LYFLFGFWSGILGLSLSMLIRLNLRTPMkLFISNDQFYNSVVTAHAFIMIFFTVMPIMIGGFGNWLVPLMLGAPDMAFPR 81
Cdd:MTH00079  19 LYFLFGLWSGMVGTSLSLIIRLELSKPG-LLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPR 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809  82 LNNMSFWLLPPSIILLIMGLSKE-GAGTGWTVYPPLSTFYHSGMSVDLTIFSLHLAGISSILGALNFITTIINLKTKNLS 160
Cdd:MTH00079  98 LNNLSFWLLPTSLFLILDSCFVDmGPGTSWTVYPPLSTLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSIS 177

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 323328809 161 SNKMSLFIWSVILTAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPVLYQHLF 218
Cdd:MTH00079 178 LEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLF 235
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 2-218 1.25e-94

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 285.26  E-value: 1.25e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809   2 LYFLFGFWSGILGLSLSMLIRLNLRTPMKlFISNDQFYNSVVTAHAFIMIFFTVMPIMIGGFGNWLVPLMLGAPDMAFPR 81
Cdd:MTH00007  15 LYFILGVWGGLLGTSMSLLIRIELGQPGA-FLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPR 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809  82 LNNMSFWLLPPSIILLIMGLSKE-GAGTGWTVYPPL-STFYHSGMSVDLTIFSLHLAGISSILGALNFITTIINLKTKNL 159
Cdd:MTH00007  94 LNNMSFWLLPPALILLVSSAAVEkGVGTGWTVYPPLaSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGL 173

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 323328809 160 SSNKMSLFIWSVILTAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPVLYQHLF 218
Cdd:MTH00007 174 RLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 232
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 2-218 1.70e-94

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 285.24  E-value: 1.70e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809   2 LYFLFGFWSGILGLSLSMLIRLNLRTPMKLfISNDQFYNSVVTAHAFIMIFFTVMPIMIGGFGNWLVPLMLGAPDMAFPR 81
Cdd:MTH00103  18 LYLLFGAWAGMVGTALSLLIRAELGQPGTL-LGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPR 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809  82 LNNMSFWLLPPSIILLIMGLSKE-GAGTGWTVYPPLS-TFYHSGMSVDLTIFSLHLAGISSILGALNFITTIINLKTKNL 159
Cdd:MTH00103  97 MNNMSFWLLPPSFLLLLASSMVEaGAGTGWTVYPPLAgNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAM 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 323328809 160 SSNKMSLFIWSVILTAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPVLYQHLF 218
Cdd:MTH00103 177 SQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 2-218 1.59e-93

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 282.58  E-value: 1.59e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809   2 LYFLFGFWSGILGLSLSMLIRLNLRTPMKLfISNDQFYNSVVTAHAFIMIFFTVMPIMIGGFGNWLVPLMLGAPDMAFPR 81
Cdd:MTH00183  18 LYLVFGAWAGMVGTALSLLIRAELSQPGAL-LGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPR 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809  82 LNNMSFWLLPPSIILLIMGLSKE-GAGTGWTVYPPLS-TFYHSGMSVDLTIFSLHLAGISSILGALNFITTIINLKTKNL 159
Cdd:MTH00183  97 MNNMSFWLLPPSFLLLLASSGVEaGAGTGWTVYPPLAgNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAI 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 323328809 160 SSNKMSLFIWSVILTAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPVLYQHLF 218
Cdd:MTH00183 177 SQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 2-218 5.44e-93

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 281.44  E-value: 5.44e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809   2 LYFLFGFWSGILGLSLSMLIRLNLRTPMKLfISNDQFYNSVVTAHAFIMIFFTVMPIMIGGFGNWLVPLMLGAPDMAFPR 81
Cdd:MTH00077  18 LYLVFGAWAGMVGTALSLLIRAELSQPGTL-LGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPR 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809  82 LNNMSFWLLPPSIILLIMGLSKE-GAGTGWTVYPPLS-TFYHSGMSVDLTIFSLHLAGISSILGALNFITTIINLKTKNL 159
Cdd:MTH00077  97 MNNMSFWLLPPSFLLLLASSGVEaGAGTGWTVYPPLAgNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSM 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 323328809 160 SSNKMSLFIWSVILTAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPVLYQHLF 218
Cdd:MTH00077 177 SQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLF 235
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 2-218 1.82e-89

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 272.47  E-value: 1.82e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809   2 LYFLFGFWSGILGLSLSMLIRLNLRTPMKLfISNDQFYNSVVTAHAFIMIFFTVMPIMIGGFGNWLVPLMLGAPDMAFPR 81
Cdd:MTH00037  18 LYLIFGAWAGMVGTAMSVIIRTELAQPGSL-LQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPR 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809  82 LNNMSFWLLPPSIILLIMGLSKE-GAGTGWTVYPPLST-FYHSGMSVDLTIFSLHLAGISSILGALNFITTIINLKTKNL 159
Cdd:MTH00037  97 MNNMSFWLIPPSFLLLLASAGVEsGAGTGWTIYPPLSSnIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGM 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 323328809 160 SSNKMSLFIWSVILTAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPVLYQHLF 218
Cdd:MTH00037 177 TFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLF 235
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 2-218 6.49e-89

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 271.31  E-value: 6.49e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809   2 LYFLFGFWSGILGLSLSMLIRLNLRTPMKLfISNDQFYNSVVTAHAFIMIFFTVMPIMIGGFGNWLVPLMLGAPDMAFPR 81
Cdd:MTH00182  20 LYLVFGAGAGMIGTAFSMLIRLELSAPGAM-LGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPR 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809  82 LNNMSFWLLPPSIILLI-MGLSKEGAGTGWTVYPPLSTFY-HSGMSVDLTIFSLHLAGISSILGALNFITTIINLKTKNL 159
Cdd:MTH00182  99 LNNISFWLLPPALILLLgSAFVEQGAGTGWTVYPPLSSIQaHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGV 178

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 323328809 160 SSNKMSLFIWSVILTAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPVLYQHLF 218
Cdd:MTH00182 179 TFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLF 237
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 2-218 2.50e-88

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 269.39  E-value: 2.50e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809   2 LYFLFGFWSGILGLSLSMLIRLNLRTPMKLfISNDQFYNSVVTAHAFIMIFFTVMPIMIGGFGNWLVPLMLGAPDMAFPR 81
Cdd:MTH00184  20 LYLLFGAFAGMIGTAFSMLIRLELSAPGSM-LGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPR 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809  82 LNNMSFWLLPPSIILLI-MGLSKEGAGTGWTVYPPLSTFY-HSGMSVDLTIFSLHLAGISSILGALNFITTIINLKTKNL 159
Cdd:MTH00184  99 LNNISFWLLPPALTLLLgSAFVEQGAGTGWTVYPPLSSIQaHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGI 178

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 323328809 160 SSNKMSLFIWSVILTAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPVLYQHLF 218
Cdd:MTH00184 179 TMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLF 237
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 2-218 1.15e-80

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 250.32  E-value: 1.15e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809   2 LYFLFGFWSGILGLSLSMLIRLNLRTPMKLfISNDQFYNSVVTAHAFIMIFFTVMPIMIGGFGNWLVPLMLGAPDMAFPR 81
Cdd:MTH00026  19 LYLVFGALSGAIGTAFSMLIRLELSSPGSM-LGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPR 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809  82 LNNMSFWLLPPSIILLI-MGLSKEGAGTGWTVYPPLSTFY-HSGMSVDLTIFSLHLAGISSILGALNFITTIINLKTKNL 159
Cdd:MTH00026  98 LNNISFWLLPPALFLLLgSSLVEQGAGTGWTVYPPLASIQaHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGM 177

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 323328809 160 SSNKMSLFIWSVILTAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPVLYQHLF 218
Cdd:MTH00026 178 TMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLF 236
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-218 1.31e-74

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: 232.42  E-value: 1.31e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809   1 ILYFLFGFWSGILGLSLSMLIRLNLRTPMKLFIsNDQFYNSVVTAHAFIMIFFTVMPIMIGGFGNWLVPlMLGAPDMAFP 80
Cdd:cd00919    6 LLYLIFAFVALLLGGLLALLIRLELATPGSLFL-DPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809  81 RLNNMSFWLLPPSIILLIMG-LSKEGAGTGWTVYPPLST-FYHSGMSVDLTIFSLHLAGISSILGALNFITTIINLKTKN 158
Cdd:cd00919   84 RLNNLSFWLFPPGLLLLLSSvLVGGGAGTGWTFYPPLSTlSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPG 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809 159 LSSNKMSLFIWSVILTAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPVLYQHLF 218
Cdd:cd00919  164 MTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLF 223
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-218 1.59e-72

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 228.41  E-value: 1.59e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809   1 ILYFLFGFWSGILGLSLSMLIRLNLRTPMKLFISNDqFYNSVVTAHAFIMIFFTVMPIMIGGFGNWLVPLMLGAPDMAFP 80
Cdd:MTH00048  18 VIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLD-VYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLP 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809  81 RLNNMSFWLLPPSIILLIMGLSKeGAGTGWTVYPPLSTFYHS-GMSVDLTIFSLHLAGISSILGALNFITTIINLKTKNL 159
Cdd:MTH00048  97 RLNALSAWLLVPSIVFLLLSMCL-GAGVGWTFYPPLSSSLFSsSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNV 175

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 323328809 160 SSnKMSLFIWSVILTAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPVLYQHLF 218
Cdd:MTH00048 176 FS-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMF 233
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-218 4.06e-69

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 220.38  E-value: 4.06e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809   1 ILYFLFGFWSGILGLSLSMLIRLNLRTPMKLFISNDQfYNSVVTAHAFIMIFFTVMPiMIGGFGNWLVPLMLGAPDMAFP 80
Cdd:COG0843   20 IMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPET-YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFP 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809  81 RLNNMSFWLLPPSIILLIMGL-SKEGAGTGWTVYPPLSTF-YHSGMSVDLTIFSLHLAGISSILGALNFITTIINLKTKN 158
Cdd:COG0843   98 RLNALSFWLYLFGGLLLLISLfVGGAADVGWTFYPPLSGLeASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPG 177

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809 159 LSSNKMSLFIWSVILTAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPVLYQHLF 218
Cdd:COG0843  178 MTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLF 237
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-218 8.95e-53

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: 176.62  E-value: 8.95e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809   1 ILYFLFGFWSGILGLSLSMLIRLNLRTPMKLFISNDQfYNSVVTAHAFIMIFFTVMPIMIGgFGNWLVPLMLGAPDMAFP 80
Cdd:cd01662   12 IMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEH-YNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFP 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809  81 RLNNMSFWL-LPPSIILLIMGLSKEGAGTGWTVYPPLSTFYHS-GMSVDLTIFSLHLAGISSILGALNFITTIINLKTKN 158
Cdd:cd01662   90 RLNALSFWLfLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSpGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPG 169

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809 159 LSSNKMSLFIWSVILTAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPVLYQHLF 218
Cdd:cd01662  170 MTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLF 229
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-218 9.51e-44

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: 151.57  E-value: 9.51e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809    1 ILYFLFGFWSGILGLSLSMLIRLNLRTPMKLFISNdQFYNSVVTAHAFIMIFFTVMPiMIGGFGNWLVPLMLGAPDMAFP 80
Cdd:pfam00115   4 LLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSP-LTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809   81 RLNNMSFWLLPPSIILLIMGLskEGAGTGWTVYPPLstfyhsgMSVDLTIFSLHLAGISSILGALNFITTIINLKTKNLs 160
Cdd:pfam00115  82 RLNALSFWLVVLGAVLLLASF--GGATTGWTEYPPL-------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGM- 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 323328809  161 SNKMSLFIWSVILTAILLLLSLPVLAGAITMLLTDRNLNTsffdpsGGGDPVLYQHLF 218
Cdd:pfam00115 152 TLRMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLF 203
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 39-217 1.37e-32

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 123.89  E-value: 1.37e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809  39 YNSVVTAHAFIMIFFTVMPIMIGgFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSIILLIMGLS-KEGAGTGWTVYPPLS 117
Cdd:PRK15017  99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGvGEFAQTGWLAYPPLS 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323328809 118 TF-YHSGMSVDLTIFSLHLAGISSILGALNFITTIINLKTKNLSSNKMSLFIWSVILTAILLLLSLPVLAGAITMLLTDR 196
Cdd:PRK15017 178 GIeYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257

                        170       180
                 ....*....|....*....|.
gi 323328809 197 NLNTSFFDPSGGGDPVLYQHL 217
Cdd:PRK15017 258 YLGTHFFTNDMGGNMMMYINL 278
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH