NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1557928044|gb|QAA08179|]
View 

cytochrome oxidase subunit 1, partial (mitochondrion) [Ichneumonidae sp. INDOBIOSYS-CCDB24682-F06]

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 ...
 1-205 9.98e-129

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: 371.89  E-value: 9.98e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557928044   1 AGMIGASLSLLIRLELGNPGFLINNDQIYNSIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLL 80
Cdd:MTH00153   24 SGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557928044  81 PPSIFFLLCSSIINQGVGTGWTVYPPLSLNINHEGMSVDMAIFSLHLAGMSSIMGAINFISTIFNLRPNNVKMDQISLFS 160
Cdd:MTH00153  104 PPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFV 183

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1557928044 161 WSIKITTILLLLAVPVLAGAITMLLTDRNLNTSFFDPSGGGDPIL 205
Cdd:MTH00153  184 WSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPIL 228
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-205 9.98e-129

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 371.89  E-value: 9.98e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557928044   1 AGMIGASLSLLIRLELGNPGFLINNDQIYNSIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLL 80
Cdd:MTH00153   24 SGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557928044  81 PPSIFFLLCSSIINQGVGTGWTVYPPLSLNINHEGMSVDMAIFSLHLAGMSSIMGAINFISTIFNLRPNNVKMDQISLFS 160
Cdd:MTH00153  104 PPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFV 183

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1557928044 161 WSIKITTILLLLAVPVLAGAITMLLTDRNLNTSFFDPSGGGDPIL 205
Cdd:MTH00153  184 WSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPIL 228
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-205 2.41e-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: 349.86  E-value: 2.41e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557928044   1 AGMIGASLSLLIRLELGNPGFLINNDQIYNSIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLL 80
Cdd:cd01663    17 SGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLL 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557928044  81 PPSIFFLLCSSIINQGVGTGWTVYPPLSLNINHEGMSVDMAIFSLHLAGMSSIMGAINFISTIFNLRPNNVKMDQISLFS 160
Cdd:cd01663    97 PPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFV 176

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1557928044 161 WSIKITTILLLLAVPVLAGAITMLLTDRNLNTSFFDPSGGGDPIL 205
Cdd:cd01663   177 WSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPIL 221
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-205 1.32e-63

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 205.36  E-value: 1.32e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557928044   1 AGMIGASLSLLIRLELGNPGFLINNDQIYNSIVTAHAFIMIFFMVMPiMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLL 80
Cdd:COG0843    29 FLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLY 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557928044  81 PPSIFFLLCSSIINQGVGTGWTVYPPLSLNINHEGMSVDMAIFSLHLAGMSSIMGAINFISTIFNLRPNNVKMDQISLFS 160
Cdd:COG0843   108 LFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFT 187

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1557928044 161 WSIKITTILLLLAVPVLAGAITMLLTDRNLNTSFFDPSGGGDPIL 205
Cdd:COG0843   188 WAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLL 232
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-205 1.15e-38

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: 137.70  E-value: 1.15e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557928044   1 AGMIGASLSLLIRLELGNPGFLINNDQIYNSIVTAHAFIMIFFMVMPiMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLL 80
Cdd:pfam00115  13 WFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557928044  81 PPSIFFLLCSSiinQGVGTGWTVYPPLslninhegMSVDMAIFSLHLAGMSSIMGAINFISTIFNLRPNNVKMdQISLFS 160
Cdd:pfam00115  92 VLGAVLLLASF---GGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFV 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1557928044 161 WSIKITTILLLLAVPVLAGAITMLLTDRNLNTsffdpsGGGDPIL 205
Cdd:pfam00115 160 WAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLL 198
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 5-205 2.65e-32

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: 122.66  E-value: 2.65e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557928044   5 GASLSLLIRLELGNPGFLINNDQIYNSIVTAHAFIMIFFMVMPIMIGgFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPSI 84
Cdd:TIGR02882  68 GGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGA 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557928044  85 FFLLCSSIINQGVGTGWTVYPPLSLNINHEGMSVDMAIFSLHLAGMSSIMGAINFISTIFNLRPNNVKMDQISLFSWSIK 164
Cdd:TIGR02882 147 MLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTL 226

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1557928044 165 ITTILLLLAVPVLAGAITMLLTDRNLNTSFFDPSGGGDPIL 205
Cdd:TIGR02882 227 ITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPML 267
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-205 9.98e-129

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 371.89  E-value: 9.98e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557928044   1 AGMIGASLSLLIRLELGNPGFLINNDQIYNSIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLL 80
Cdd:MTH00153   24 SGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557928044  81 PPSIFFLLCSSIINQGVGTGWTVYPPLSLNINHEGMSVDMAIFSLHLAGMSSIMGAINFISTIFNLRPNNVKMDQISLFS 160
Cdd:MTH00153  104 PPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFV 183

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1557928044 161 WSIKITTILLLLAVPVLAGAITMLLTDRNLNTSFFDPSGGGDPIL 205
Cdd:MTH00153  184 WSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPIL 228
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-205 2.41e-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: 349.86  E-value: 2.41e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557928044   1 AGMIGASLSLLIRLELGNPGFLINNDQIYNSIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLL 80
Cdd:cd01663    17 SGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLL 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557928044  81 PPSIFFLLCSSIINQGVGTGWTVYPPLSLNINHEGMSVDMAIFSLHLAGMSSIMGAINFISTIFNLRPNNVKMDQISLFS 160
Cdd:cd01663    97 PPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFV 176

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1557928044 161 WSIKITTILLLLAVPVLAGAITMLLTDRNLNTSFFDPSGGGDPIL 205
Cdd:cd01663   177 WSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPIL 221
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-205 4.91e-114

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 334.34  E-value: 4.91e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557928044   1 AGMIGASLSLLIRLELGNPGFLINNDQIYNSIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLL 80
Cdd:MTH00167   26 AGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557928044  81 PPSIFFLLCSSIINQGVGTGWTVYPPLSLNINHEGMSVDMAIFSLHLAGMSSIMGAINFISTIFNLRPNNVKMDQISLFS 160
Cdd:MTH00167  106 PPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFV 185

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1557928044 161 WSIKITTILLLLAVPVLAGAITMLLTDRNLNTSFFDPSGGGDPIL 205
Cdd:MTH00167  186 WSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPIL 230
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-205 5.38e-111

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 326.55  E-value: 5.38e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557928044   1 AGMIGASLSLLIRLELGNPGFLINNDQIYNSIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLL 80
Cdd:MTH00223   23 SGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLL 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557928044  81 PPSIFFLLCSSIINQGVGTGWTVYPPLSLNINHEGMSVDMAIFSLHLAGMSSIMGAINFISTIFNLRPNNVKMDQISLFS 160
Cdd:MTH00223  103 PPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFV 182

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1557928044 161 WSIKITTILLLLAVPVLAGAITMLLTDRNLNTSFFDPSGGGDPIL 205
Cdd:MTH00223  183 WSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPIL 227
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-205 6.51e-110

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 323.97  E-value: 6.51e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557928044   1 AGMIGASLSLLIRLELGNPGFLINNDQIYNSIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLL 80
Cdd:MTH00116   26 AGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557928044  81 PPSIFFLLCSSIINQGVGTGWTVYPPLSLNINHEGMSVDMAIFSLHLAGMSSIMGAINFISTIFNLRPNNVKMDQISLFS 160
Cdd:MTH00116  106 PPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFV 185

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1557928044 161 WSIKITTILLLLAVPVLAGAITMLLTDRNLNTSFFDPSGGGDPIL 205
Cdd:MTH00116  186 WSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPIL 230
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-205 4.11e-107

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 316.67  E-value: 4.11e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557928044   1 AGMIGASLSLLIRLELGNPGFLINNDQIYNSIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLL 80
Cdd:MTH00142   24 AGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557928044  81 PPSIFFLLCSSIINQGVGTGWTVYPPLSLNINHEGMSVDMAIFSLHLAGMSSIMGAINFISTIFNLRPNNVKMDQISLFS 160
Cdd:MTH00142  104 PPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFV 183

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1557928044 161 WSIKITTILLLLAVPVLAGAITMLLTDRNLNTSFFDPSGGGDPIL 205
Cdd:MTH00142  184 WSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPIL 228
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-205 1.48e-97

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 292.19  E-value: 1.48e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557928044   1 AGMIGASLSLLIRLELGNPGFLINNDQIYNSIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLL 80
Cdd:MTH00007   23 GGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLL 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557928044  81 PPSIFFLLCSSIINQGVGTGWTVYPPLSLNINHEGMSVDMAIFSLHLAGMSSIMGAINFISTIFNLRPNNVKMDQISLFS 160
Cdd:MTH00007  103 PPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFV 182

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1557928044 161 WSIKITTILLLLAVPVLAGAITMLLTDRNLNTSFFDPSGGGDPIL 205
Cdd:MTH00007  183 WAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPIL 227
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-205 1.59e-97

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 292.60  E-value: 1.59e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557928044   1 AGMIGASLSLLIRLELGNPGFLINNDQIYNSIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLL 80
Cdd:MTH00183   26 AGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557928044  81 PPSIFFLLCSSIINQGVGTGWTVYPPLSLNINHEGMSVDMAIFSLHLAGMSSIMGAINFISTIFNLRPNNVKMDQISLFS 160
Cdd:MTH00183  106 PPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFV 185

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1557928044 161 WSIKITTILLLLAVPVLAGAITMLLTDRNLNTSFFDPSGGGDPIL 205
Cdd:MTH00183  186 WAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPIL 230
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-205 2.39e-97

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 291.84  E-value: 2.39e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557928044   1 AGMIGASLSLLIRLELGNPGFLINNDQIYNSIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLL 80
Cdd:MTH00077   26 AGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557928044  81 PPSIFFLLCSSIINQGVGTGWTVYPPLSLNINHEGMSVDMAIFSLHLAGMSSIMGAINFISTIFNLRPNNVKMDQISLFS 160
Cdd:MTH00077  106 PPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFV 185

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1557928044 161 WSIKITTILLLLAVPVLAGAITMLLTDRNLNTSFFDPSGGGDPIL 205
Cdd:MTH00077  186 WSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVL 230
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-205 5.57e-97

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 291.02  E-value: 5.57e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557928044   1 AGMIGASLSLLIRLELGNPGFLINNDQIYNSIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLL 80
Cdd:MTH00103   26 AGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557928044  81 PPSIFFLLCSSIINQGVGTGWTVYPPLSLNINHEGMSVDMAIFSLHLAGMSSIMGAINFISTIFNLRPNNVKMDQISLFS 160
Cdd:MTH00103  106 PPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFV 185

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1557928044 161 WSIKITTILLLLAVPVLAGAITMLLTDRNLNTSFFDPSGGGDPIL 205
Cdd:MTH00103  186 WSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPIL 230
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-205 2.42e-94

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 284.41  E-value: 2.42e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557928044   1 AGMIGASLSLLIRLELGNPGFLINNDQIYNSIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLL 80
Cdd:MTH00037   26 AGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLI 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557928044  81 PPSIFFLLCSSIINQGVGTGWTVYPPLSLNINHEGMSVDMAIFSLHLAGMSSIMGAINFISTIFNLRPNNVKMDQISLFS 160
Cdd:MTH00037  106 PPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFV 185

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1557928044 161 WSIKITTILLLLAVPVLAGAITMLLTDRNLNTSFFDPSGGGDPIL 205
Cdd:MTH00037  186 WSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPIL 230
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-205 6.68e-92

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 278.24  E-value: 6.68e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557928044   1 AGMIGASLSLLIRLELGNPGFLINNDQIYNSIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLL 80
Cdd:MTH00182   28 AGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLL 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557928044  81 PPSIFFLLCSSIINQGVGTGWTVYPPLSLNINHEGMSVDMAIFSLHLAGMSSIMGAINFISTIFNLRPNNVKMDQISLFS 160
Cdd:MTH00182  108 PPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFV 187

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1557928044 161 WSIKITTILLLLAVPVLAGAITMLLTDRNLNTSFFDPSGGGDPIL 205
Cdd:MTH00182  188 WSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPIL 232
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-205 1.52e-91

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 277.09  E-value: 1.52e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557928044   1 AGMIGASLSLLIRLELGNPGFLINNDQIYNSIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLL 80
Cdd:MTH00184   28 AGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLL 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557928044  81 PPSIFFLLCSSIINQGVGTGWTVYPPLSLNINHEGMSVDMAIFSLHLAGMSSIMGAINFISTIFNLRPNNVKMDQISLFS 160
Cdd:MTH00184  108 PPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFV 187

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1557928044 161 WSIKITTILLLLAVPVLAGAITMLLTDRNLNTSFFDPSGGGDPIL 205
Cdd:MTH00184  188 WSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPIL 232
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-205 2.85e-88

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 268.47  E-value: 2.85e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557928044   1 AGMIGASLSLLIRLELGNPGFLINNDQIYNSIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLL 80
Cdd:MTH00079   27 SGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557928044  81 PPSIFFLLCSSIINQGVGTGWTVYPPLSlNINHEGMSVDMAIFSLHLAGMSSIMGAINFISTIFNLRPNNVKMDQISLFS 160
Cdd:MTH00079  107 PTSLFLILDSCFVDMGPGTSWTVYPPLS-TLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFV 185

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1557928044 161 WSIKITTILLLLAVPVLAGAITMLLTDRNLNTSFFDPSGGGDPIL 205
Cdd:MTH00079  186 WTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLL 230
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-205 3.30e-82

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 253.78  E-value: 3.30e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557928044   1 AGMIGASLSLLIRLELGNPGFLINNDQIYNSIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLL 80
Cdd:MTH00026   27 SGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557928044  81 PPSIFFLLCSSIINQGVGTGWTVYPPLSLNINHEGMSVDMAIFSLHLAGMSSIMGAINFISTIFNLRPNNVKMDQISLFS 160
Cdd:MTH00026  107 PPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFV 186

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1557928044 161 WSIKITTILLLLAVPVLAGAITMLLTDRNLNTSFFDPSGGGDPIL 205
Cdd:MTH00026  187 WSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPIL 231
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-205 3.95e-75

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: 233.19  E-value: 3.95e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557928044   1 AGMIGASLSLLIRLELGNPGFLINNDQIYNSIVTAHAFIMIFFMVMPIMIGGFGNWLIPlMLGAPDMAFPRMNNMSFWLL 80
Cdd:cd00919    15 ALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWLF 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557928044  81 PPSIFFLLCSSIINQGVGTGWTVYPPLSLNINHEGMSVDMAIFSLHLAGMSSIMGAINFISTIFNLRPNNVKMDQISLFS 160
Cdd:cd00919    94 PPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFV 173

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1557928044 161 WSIKITTILLLLAVPVLAGAITMLLTDRNLNTSFFDPSGGGDPIL 205
Cdd:cd00919   174 WSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVL 218
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-205 1.32e-63

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 205.36  E-value: 1.32e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557928044   1 AGMIGASLSLLIRLELGNPGFLINNDQIYNSIVTAHAFIMIFFMVMPiMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLL 80
Cdd:COG0843    29 FLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLY 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557928044  81 PPSIFFLLCSSIINQGVGTGWTVYPPLSLNINHEGMSVDMAIFSLHLAGMSSIMGAINFISTIFNLRPNNVKMDQISLFS 160
Cdd:COG0843   108 LFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFT 187

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1557928044 161 WSIKITTILLLLAVPVLAGAITMLLTDRNLNTSFFDPSGGGDPIL 205
Cdd:COG0843   188 WAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLL 232
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-205 1.19e-62

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 202.22  E-value: 1.19e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557928044   1 AGMIGASLSLLIRLELGNPGFLINNDQIYNSIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLL 80
Cdd:MTH00048   27 SGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557928044  81 PPSIFFLLCSSIInqGVGTGWTVYPPLSLNINHEGMSVDMAIFSLHLAGMSSIMGAINFISTIFNLRPNNVkMDQISLFS 160
Cdd:MTH00048  107 VPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNV-FSRTSIIL 183

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1557928044 161 WSIKITTILLLLAVPVLAGAITMLLTDRNLNTSFFDPSGGGDPIL 205
Cdd:MTH00048  184 WSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVL 228
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 4-205 1.79e-48

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: 165.06  E-value: 1.79e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557928044   4 IGASLSLLIRLELGNPGFLINNDQIYNSIVTAHAFIMIFFMVMPIMIGgFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPS 83
Cdd:cd01662    24 RGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFG 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557928044  84 IFFLLCSSIINQGVGTGWTVYPPLSLNINHEGMSVDMAIFSLHLAGMSSIMGAINFISTIFNLRPNNVKMDQISLFSWSI 163
Cdd:cd01662   103 GLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTT 182

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1557928044 164 KITTILLLLAVPVLAGAITMLLTDRNLNTSFFDPSGGGDPIL 205
Cdd:cd01662   183 LVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPML 224
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-205 1.15e-38

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: 137.70  E-value: 1.15e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557928044   1 AGMIGASLSLLIRLELGNPGFLINNDQIYNSIVTAHAFIMIFFMVMPiMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLL 80
Cdd:pfam00115  13 WFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557928044  81 PPSIFFLLCSSiinQGVGTGWTVYPPLslninhegMSVDMAIFSLHLAGMSSIMGAINFISTIFNLRPNNVKMdQISLFS 160
Cdd:pfam00115  92 VLGAVLLLASF---GGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFV 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1557928044 161 WSIKITTILLLLAVPVLAGAITMLLTDRNLNTsffdpsGGGDPIL 205
Cdd:pfam00115 160 WAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLL 198
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 5-205 2.65e-32

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: 122.66  E-value: 2.65e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557928044   5 GASLSLLIRLELGNPGFLINNDQIYNSIVTAHAFIMIFFMVMPIMIGgFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPSI 84
Cdd:TIGR02882  68 GGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGA 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557928044  85 FFLLCSSIINQGVGTGWTVYPPLSLNINHEGMSVDMAIFSLHLAGMSSIMGAINFISTIFNLRPNNVKMDQISLFSWSIK 164
Cdd:TIGR02882 147 MLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTL 226

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1557928044 165 ITTILLLLAVPVLAGAITMLLTDRNLNTSFFDPSGGGDPIL 205
Cdd:TIGR02882 227 ITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPML 267
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 17-205 2.35e-29

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 114.26  E-value: 2.35e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557928044  17 GNPGFLINNDqiYNSIVTAHAFIMIFFMVMPIMIGgFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPSIFFLLCSSIINQG 96
Cdd:PRK15017   89 GEAGFLPPHH--YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEF 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557928044  97 VGTGWTVYPPLSLNINHEGMSVDMAIFSLHLAGMSSIMGAINFISTIFNLRPNNVKMDQISLFSWSIKITTILLLLAVPV 176
Cdd:PRK15017  166 AQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPI 245

                         170       180
                  ....*....|....*....|....*....
gi 1557928044 177 LAGAITMLLTDRNLNTSFFDPSGGGDPIL 205
Cdd:PRK15017  246 LTVTVALLTLDRYLGTHFFTNDMGGNMMM 274
 
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