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Conserved domains on  [gi|807049792|gb|AKC35301|]
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cytochrome oxidase subunit 1, partial (mitochondrion) [Centroceras arcii]

Protein Classification

heme-copper oxidase family protein( domain architecture ID 14)

heme-copper oxidase family protein may catalyze the transfer of electrons from an electron donor onto molecular oxygen

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Heme_Cu_Oxidase_I super family cl00275
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-189 1.40e-102

Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. Membership in the superfamily is defined by subunit I, which contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons to the binuclear center. Only subunit I is common to the entire superfamily. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from the electron donor on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I of cytochrome c oxidase (CcO) and ubiquinol oxidase. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electron transfer occurs in two segments: from the electron donor to the low-spin heme, and from the low-spin heme to the binuclear center. The first segment can be a multi-step process and varies among the different families, while the second segment, a direct transfer, is consistent throughout the superfamily.


The actual alignment was detected with superfamily member cd01663:

Pssm-ID: 469701  Cd Length: 488  Bit Score: 303.64  E-value: 1.40e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807049792   1 CMSMLIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSL 80
Cdd:cd01663   23 SLSLLIRLELSQPGS--QLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSL 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807049792  81 CLLLLSAIVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQSMYRIPLFVWSIF 160
Cdd:cd01663  101 LLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVL 180

                        170       180
                 ....*....|....*....|....*....
gi 807049792 161 VTAFLLLLAVPVLAGAITMLLTDRNFNTA 189
Cdd:cd01663  181 ITAFLLLLSLPVLAGAITMLLTDRNFNTS 209
 
Name Accession Description Interval E-value
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-189 1.40e-102

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: 303.64  E-value: 1.40e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807049792   1 CMSMLIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSL 80
Cdd:cd01663   23 SLSLLIRLELSQPGS--QLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSL 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807049792  81 CLLLLSAIVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQSMYRIPLFVWSIF 160
Cdd:cd01663  101 LLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVL 180

                        170       180
                 ....*....|....*....|....*....
gi 807049792 161 VTAFLLLLAVPVLAGAITMLLTDRNFNTA 189
Cdd:cd01663  181 ITAFLLLLSLPVLAGAITMLLTDRNFNTS 209
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 2-188 2.50e-100

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 298.71  E-value: 2.50e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807049792   2 MSMLIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLC 81
Cdd:MTH00153  31 LSLLIRAELGQPGS--LIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLT 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807049792  82 LLLLSAIVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQSMYRIPLFVWSIFV 161
Cdd:MTH00153 109 LLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLI 188

                        170       180
                 ....*....|....*....|....*..
gi 807049792 162 TAFLLLLAVPVLAGAITMLLTDRNFNT 188
Cdd:MTH00153 189 TAILLLLSLPVLAGAITMLLTDRNLNT 215
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-188 3.89e-58

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 190.34  E-value: 3.89e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807049792   2 MSMLIRMELAQPGNHLLLGNHqvYNVLITAHAFLMIFFMVMPvMIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLC 81
Cdd:COG0843   36 LALLMRLQLAGPGLGLLSPET--YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807049792  82 LLLLSAIVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQSMYRIPLFVWSIFV 161
Cdd:COG0843  113 LLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALV 192

                        170       180
                 ....*....|....*....|....*..
gi 807049792 162 TAFLLLLAVPVLAGAITMLLTDRNFNT 188
Cdd:COG0843  193 TSILILLAFPVLAAALLLLLLDRSLGT 219
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 2-189 3.04e-36

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: 130.39  E-value: 3.04e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807049792    2 MSMLIRMELAQPGNHLLlgNHQVYNVLITAHAFLMIFFMVMPvMIGGFGNWLVPIMIGSPDMAFPRLNNISFWllpPSLC 81
Cdd:pfam00115  20 LGLLIRLQLAFPGLNFL--SPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFW---LVVL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807049792   82 LLLLSAIVEVGVGTGWTVYPPLssiqshsgAAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQSMyRIPLFVWSIFV 161
Cdd:pfam00115  94 GAVLLLASFGGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILA 164

                         170       180
                  ....*....|....*....|....*...
gi 807049792  162 TAFLLLLAVPVLAGAITMLLTDRNFNTA 189
Cdd:pfam00115 165 TAILILLAFPVLAAALLLLLLDRSLGAG 192
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 3-189 4.20e-31

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: 118.42  E-value: 4.20e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807049792    3 SMLIRMELAQPGNHLLLGNHqvYNVLITAHAFLMIFFMVMPVMIGgFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCL 82
Cdd:TIGR02882  72 ALLMRAQLTVPDNKFLDAQH--YNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAML 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807049792   83 LLLSAIVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQSMYRIPLFVWSIFVT 162
Cdd:TIGR02882 149 FNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLIT 228

                         170       180
                  ....*....|....*....|....*..
gi 807049792  163 AFLLLLAVPVLAGAITMLLTDRNFNTA 189
Cdd:TIGR02882 229 TLIIIFAFPVLTVALALMTTDRIFDTA 255
 
Name Accession Description Interval E-value
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-189 1.40e-102

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: 303.64  E-value: 1.40e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807049792   1 CMSMLIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSL 80
Cdd:cd01663   23 SLSLLIRLELSQPGS--QLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSL 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807049792  81 CLLLLSAIVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQSMYRIPLFVWSIF 160
Cdd:cd01663  101 LLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVL 180

                        170       180
                 ....*....|....*....|....*....
gi 807049792 161 VTAFLLLLAVPVLAGAITMLLTDRNFNTA 189
Cdd:cd01663  181 ITAFLLLLSLPVLAGAITMLLTDRNFNTS 209
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 2-188 2.50e-100

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 298.71  E-value: 2.50e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807049792   2 MSMLIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLC 81
Cdd:MTH00153  31 LSLLIRAELGQPGS--LIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLT 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807049792  82 LLLLSAIVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQSMYRIPLFVWSIFV 161
Cdd:MTH00153 109 LLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLI 188

                        170       180
                 ....*....|....*....|....*..
gi 807049792 162 TAFLLLLAVPVLAGAITMLLTDRNFNT 188
Cdd:MTH00153 189 TAILLLLSLPVLAGAITMLLTDRNLNT 215
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 2-188 3.84e-90

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 272.71  E-value: 3.84e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807049792   2 MSMLIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLC 81
Cdd:MTH00167  33 LSLLIRAELSQPGS--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLL 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807049792  82 LLLLSAIVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQSMYRIPLFVWSIFV 161
Cdd:MTH00167 111 LLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILV 190

                        170       180
                 ....*....|....*....|....*..
gi 807049792 162 TAFLLLLAVPVLAGAITMLLTDRNFNT 188
Cdd:MTH00167 191 TTILLLLSLPVLAAAITMLLTDRNLNT 217
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 2-188 1.76e-87

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 265.69  E-value: 1.76e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807049792   2 MSMLIRMELAQPGnhLLLGNHQVYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLC 81
Cdd:MTH00223  30 LSLLIRAELGQPG--ALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLY 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807049792  82 LLLLSAIVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQSMYRIPLFVWSIFV 161
Cdd:MTH00223 108 LLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKV 187

                        170       180
                 ....*....|....*....|....*..
gi 807049792 162 TAFLLLLAVPVLAGAITMLLTDRNFNT 188
Cdd:MTH00223 188 TAFLLLLSLPVLAGAITMLLTDRNFNT 214
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-189 2.56e-87

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 265.42  E-value: 2.56e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807049792   1 CMSMLIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSL 80
Cdd:MTH00116  32 ALSLLIRAELGQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSF 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807049792  81 CLLLLSAIVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQSMYRIPLFVWSIF 160
Cdd:MTH00116 110 LLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVL 189

                        170       180
                 ....*....|....*....|....*....
gi 807049792 161 VTAFLLLLAVPVLAGAITMLLTDRNFNTA 189
Cdd:MTH00116 190 ITAVLLLLSLPVLAAGITMLLTDRNLNTT 218
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 2-189 2.46e-85

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 260.43  E-value: 2.46e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807049792   2 MSMLIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLC 81
Cdd:MTH00142  31 LSLLIRAELGQPGS--LLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALL 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807049792  82 LLLLSAIVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQSMYRIPLFVWSIFV 161
Cdd:MTH00142 109 LLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKI 188

                        170       180
                 ....*....|....*....|....*...
gi 807049792 162 TAFLLLLAVPVLAGAITMLLTDRNFNTA 189
Cdd:MTH00142 189 TAILLLLSLPVLAGAITMLLTDRNFNTS 216
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 2-188 2.42e-81

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 250.51  E-value: 2.42e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807049792   2 MSMLIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLC 81
Cdd:MTH00182  35 FSMLIRLELSAPGA--MLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALI 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807049792  82 LLLLSAIVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQSMYRIPLFVWSIFV 161
Cdd:MTH00182 113 LLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILI 192

                        170       180
                 ....*....|....*....|....*..
gi 807049792 162 TAFLLLLAVPVLAGAITMLLTDRNFNT 188
Cdd:MTH00182 193 TAFLLLLSLPVLAGAITMLLTDRNFNT 219
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 2-189 3.09e-79

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 244.74  E-value: 3.09e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807049792   2 MSMLIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLC 81
Cdd:MTH00184  35 FSMLIRLELSAPGS--MLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPALT 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807049792  82 LLLLSAIVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQSMYRIPLFVWSIFV 161
Cdd:MTH00184 113 LLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILV 192

                        170       180
                 ....*....|....*....|....*...
gi 807049792 162 TAFLLLLAVPVLAGAITMLLTDRNFNTA 189
Cdd:MTH00184 193 TTFLLLLSLPVLAGAITMLLTDRNFNTT 220
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 2-188 7.63e-79

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 243.58  E-value: 7.63e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807049792   2 MSMLIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLC 81
Cdd:MTH00037  33 MSVIIRTELAQPGS--LLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFL 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807049792  82 LLLLSAIVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQSMYRIPLFVWSIFV 161
Cdd:MTH00037 111 LLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFI 190

                        170       180
                 ....*....|....*....|....*..
gi 807049792 162 TAFLLLLAVPVLAGAITMLLTDRNFNT 188
Cdd:MTH00037 191 TAFLLLLSLPVLAGAITMLLTDRNINT 217
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 2-188 5.47e-77

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 239.01  E-value: 5.47e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807049792   2 MSMLIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLC 81
Cdd:MTH00103  33 LSLLIRAELGQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFL 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807049792  82 LLLLSAIVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQSMYRIPLFVWSIFV 161
Cdd:MTH00103 111 LLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLI 190

                        170       180
                 ....*....|....*....|....*..
gi 807049792 162 TAFLLLLAVPVLAGAITMLLTDRNFNT 188
Cdd:MTH00103 191 TAVLLLLSLPVLAAGITMLLTDRNLNT 217
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 2-188 7.85e-76

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 235.97  E-value: 7.85e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807049792   2 MSMLIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLC 81
Cdd:MTH00183  33 LSLLIRAELSQPGA--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFL 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807049792  82 LLLLSAIVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQSMYRIPLFVWSIFV 161
Cdd:MTH00183 111 LLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLI 190

                        170       180
                 ....*....|....*....|....*..
gi 807049792 162 TAFLLLLAVPVLAGAITMLLTDRNFNT 188
Cdd:MTH00183 191 TAVLLLLSLPVLAAGITMLLTDRNLNT 217
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 2-189 1.18e-75

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 235.57  E-value: 1.18e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807049792   2 MSMLIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLC 81
Cdd:MTH00007  30 MSLLIRIELGQPGA--FLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPALI 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807049792  82 LLLLSAIVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQSMYRIPLFVWSIFV 161
Cdd:MTH00007 108 LLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVI 187

                        170       180
                 ....*....|....*....|....*...
gi 807049792 162 TAFLLLLAVPVLAGAITMLLTDRNFNTA 189
Cdd:MTH00007 188 TVVLLLLSLPVLAGAITMLLTDRNLNTS 215
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 2-188 1.71e-75

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 235.22  E-value: 1.71e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807049792   2 MSMLIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLC 81
Cdd:MTH00077  33 LSLLIRAELSQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFL 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807049792  82 LLLLSAIVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQSMYRIPLFVWSIFV 161
Cdd:MTH00077 111 LLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLI 190

                        170       180
                 ....*....|....*....|....*..
gi 807049792 162 TAFLLLLAVPVLAGAITMLLTDRNFNT 188
Cdd:MTH00077 191 TAVLLLLSLPVLAAGITMLLTDRNLNT 217
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 3-188 4.61e-72

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 226.82  E-value: 4.61e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807049792   3 SMLIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCL 82
Cdd:MTH00026  35 SMLIRLELSSPGS--MLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPALFL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807049792  83 LLLSAIVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQSMYRIPLFVWSIFVT 162
Cdd:MTH00026 113 LLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFIT 192

                        170       180
                 ....*....|....*....|....*.
gi 807049792 163 AFLLLLAVPVLAGAITMLLTDRNFNT 188
Cdd:MTH00026 193 AILLLLSLPVLAGAITMLLTDRNFNT 218
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 2-189 1.03e-71

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 224.94  E-value: 1.03e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807049792   2 MSMLIRMELAQPGnhLLLGNHQVYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLC 81
Cdd:MTH00079  34 LSLIIRLELSKPG--LLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLF 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807049792  82 LLLLSAIVEVGVGTGWTVYPPLSSiQSHSGAAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQSMYRIPLFVWSIFV 161
Cdd:MTH00079 112 LILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFV 190

                        170       180
                 ....*....|....*....|....*...
gi 807049792 162 TAFLLLLAVPVLAGAITMLLTDRNFNTA 189
Cdd:MTH00079 191 TVFLLVLSLPVLAGAITMLLTDRNLNTS 218
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 2-188 7.94e-63

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: 200.83  E-value: 7.94e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807049792   2 MSMLIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPiMIGSPDMAFPRLNNISFWLLPPSLC 81
Cdd:cd00919   22 LALLIRLELATPGS--LFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWLFPPGLL 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807049792  82 LLLLSAIVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQSMYRIPLFVWSIFV 161
Cdd:cd00919   99 LLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLV 178

                        170       180
                 ....*....|....*....|....*..
gi 807049792 162 TAFLLLLAVPVLAGAITMLLTDRNFNT 188
Cdd:cd00919  179 TAILLLLALPVLAAALVMLLLDRNFGT 205
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-188 3.89e-58

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 190.34  E-value: 3.89e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807049792   2 MSMLIRMELAQPGNHLLLGNHqvYNVLITAHAFLMIFFMVMPvMIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLC 81
Cdd:COG0843   36 LALLMRLQLAGPGLGLLSPET--YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807049792  82 LLLLSAIVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQSMYRIPLFVWSIFV 161
Cdd:COG0843  113 LLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALV 192

                        170       180
                 ....*....|....*....|....*..
gi 807049792 162 TAFLLLLAVPVLAGAITMLLTDRNFNT 188
Cdd:COG0843  193 TSILILLAFPVLAAALLLLLLDRSLGT 219
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 2-189 1.71e-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: 164.29  E-value: 1.71e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807049792   2 MSMLIRMELAQPGNHLLLGNHqvYNVLITAHAFLMIFFMVMPVMIGgFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLC 81
Cdd:cd01662   28 DALLMRTQLALPGNDFLSPEH--YNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGGL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807049792  82 LLLLSAIVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQSMYRIPLFVWSIFV 161
Cdd:cd01662  105 LLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLV 184

                        170       180
                 ....*....|....*....|....*...
gi 807049792 162 TAFLLLLAVPVLAGAITMLLTDRNFNTA 189
Cdd:cd01662  185 TSILILFAFPVLTAALALLELDRYFGTH 212
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 2-189 1.42e-42

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 148.67  E-value: 1.42e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807049792   2 MSMLIRMELAQPGNHLLlgNHQVYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLC 81
Cdd:MTH00048  34 LSLLIRLNFLDPYYNVI--SLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIV 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807049792  82 LLLLSAIveVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQSmYRIPLFVWSIFV 161
Cdd:MTH00048 112 FLLLSMC--LGAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVF-SRTSIILWSYLF 188

                        170       180
                 ....*....|....*....|....*...
gi 807049792 162 TAFLLLLAVPVLAGAITMLLTDRNFNTA 189
Cdd:MTH00048 189 TSILLLLSLPVLAAAITMLLFDRNFGSA 216
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 2-189 3.04e-36

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: 130.39  E-value: 3.04e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807049792    2 MSMLIRMELAQPGNHLLlgNHQVYNVLITAHAFLMIFFMVMPvMIGGFGNWLVPIMIGSPDMAFPRLNNISFWllpPSLC 81
Cdd:pfam00115  20 LGLLIRLQLAFPGLNFL--SPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFW---LVVL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807049792   82 LLLLSAIVEVGVGTGWTVYPPLssiqshsgAAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQSMyRIPLFVWSIFV 161
Cdd:pfam00115  94 GAVLLLASFGGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILA 164

                         170       180
                  ....*....|....*....|....*...
gi 807049792  162 TAFLLLLAVPVLAGAITMLLTDRNFNTA 189
Cdd:pfam00115 165 TAILILLAFPVLAAALLLLLLDRSLGAG 192
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 3-189 4.20e-31

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: 118.42  E-value: 4.20e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807049792    3 SMLIRMELAQPGNHLLLGNHqvYNVLITAHAFLMIFFMVMPVMIGgFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCL 82
Cdd:TIGR02882  72 ALLMRAQLTVPDNKFLDAQH--YNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAML 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807049792   83 LLLSAIVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQSMYRIPLFVWSIFVT 162
Cdd:TIGR02882 149 FNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLIT 228

                         170       180
                  ....*....|....*....|....*..
gi 807049792  163 AFLLLLAVPVLAGAITMLLTDRNFNTA 189
Cdd:TIGR02882 229 TLIIIFAFPVLTVALALMTTDRIFDTA 255
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 4-188 1.99e-30

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 116.57  E-value: 1.99e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807049792   4 MLIRMELAQPGNHLLLGNHQvYNVLITAHAFLMIFFMVMPVMIGgFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCLL 83
Cdd:PRK15017  79 MRSQQALASAGEAGFLPPHH-YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILV 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807049792  84 LlsaiVEVGVG----TGWTVYPPLSSIQSHSGAAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQSMYRIPLFVWSI 159
Cdd:PRK15017 157 N----VSLGVGefaqTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWAS 232

                        170       180
                 ....*....|....*....|....*....
gi 807049792 160 FVTAFLLLLAVPVLAGAITMLLTDRNFNT 188
Cdd:PRK15017 233 LCANVLIIASFPILTVTVALLTLDRYLGT 261
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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