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Conserved domains on  [gi|565337723|gb|AHC06369|]
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cytochrome oxidase subunit 1, partial (mitochondrion) [Opius (Bellopius) sp. D MC-2013]

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 ...
 1-203 2.74e-109

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: 322.20  E-value: 2.74e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565337723   1 LELGMPGSLLLNDQIYNSMVTMHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLIPSLILLILSSIL 80
Cdd:MTH00153  37 AELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMV 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565337723  81 NVGVGTGWTIYPPLSSLVGHGGVSVDLAIFSLHLAGISSIMGAINFISTILNMNFYMMKMDQLVLFIWSILITAILLLLS 160
Cdd:MTH00153 117 ESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLS 196

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 565337723 161 LPVLAGAITMLLTDRNLNTSFFDFSGGGDPILFQHLFWFFGHP 203
Cdd:MTH00153 197 LPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHP 239
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-203 2.74e-109

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 322.20  E-value: 2.74e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565337723   1 LELGMPGSLLLNDQIYNSMVTMHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLIPSLILLILSSIL 80
Cdd:MTH00153  37 AELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMV 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565337723  81 NVGVGTGWTIYPPLSSLVGHGGVSVDLAIFSLHLAGISSIMGAINFISTILNMNFYMMKMDQLVLFIWSILITAILLLLS 160
Cdd:MTH00153 117 ESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLS 196

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 565337723 161 LPVLAGAITMLLTDRNLNTSFFDFSGGGDPILFQHLFWFFGHP 203
Cdd:MTH00153 197 LPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHP 239
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-203 7.05e-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: 302.48  E-value: 7.05e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565337723   1 LELGMPGSLLLNDQIYNSMVTMHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLIPSLILLILSSIL 80
Cdd:cd01663   30 LELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALV 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565337723  81 NVGVGTGWTIYPPLSSLVGHGGVSVDLAIFSLHLAGISSIMGAINFISTILNMNFYMMKMDQLVLFIWSILITAILLLLS 160
Cdd:cd01663  110 EGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLS 189

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 565337723 161 LPVLAGAITMLLTDRNLNTSFFDFSGGGDPILFQHLFWFFGHP 203
Cdd:cd01663  190 LPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHP 232
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-203 3.90e-64

cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) of cytochrome c oxidases of bacterial origin. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits I-III form the functional core of the enzyme complex. Subunit I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit II and heme a of subunit I to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. In the bacilli an apparent split (paralogism) has created a sister clade (TIGR02882) encoding subunits (QoxA) of the aa3-type quinone oxidase complex which reacts directly with quinones, bypassing the interaction with soluble cytochrome c. This model attempts to exclude these sequences, placing them between the trusted and noise cutoffs. These families, as well as archaeal and eukaryotic cytochrome c subunit I's are included within the superfamily model, pfam00115. [Energy metabolism, Electron transport]


Pssm-ID: 213748  Cd Length: 499  Bit Score: 205.92  E-value: 3.90e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565337723    1 LELGMPGSLLLNDQIYNSMVTMHAFVMIFFMVMPIMiGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLIPSLILLILSSIL 80
Cdd:TIGR02891  33 AQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFT 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565337723   81 NVGVGTGWTIYPPLSSLVGHGGVSVDLAIFSLHLAGISSIMGAINFISTILNMNFYMMKMDQLVLFIWSILITAILLLLS 160
Cdd:TIGR02891 112 GGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLA 191

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 565337723  161 LPVLAGAITMLLTDRNLNTSFFDFSGGGDPILFQHLFWFFGHP 203
Cdd:TIGR02891 192 FPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHP 234
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-203 2.52e-60

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 196.50  E-value: 2.52e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565337723   1 LELGMPGSLLLNDQIYNSMVTMHAFVMIFFMVMPiMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLIPSLILLILSSIL 80
Cdd:COG0843   42 LQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFV 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565337723  81 NVGVGTGWTIYPPLSSLVGHGGVSVDLAIFSLHLAGISSIMGAINFISTILNMNFYMMKMDQLVLFIWSILITAILLLLS 160
Cdd:COG0843  121 GGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLA 200

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 565337723 161 LPVLAGAITMLLTDRNLNTSFFDFSGGGDPILFQHLFWFFGHP 203
Cdd:COG0843  201 FPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHP 243
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-203 4.32e-33

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: 122.68  E-value: 4.32e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565337723    1 LELGMPGSLLLNDQIYNSMVTMHAFVMIFFMVMPiMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLIPSLILLILSSIl 80
Cdd:pfam00115  26 LQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASFG- 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565337723   81 nvGVGTGWTIYPPLsslvghggVSVDLAIFSLHLAGISSIMGAINFISTILNMNFYMMKMdQLVLFIWSILITAILLLLS 160
Cdd:pfam00115 104 --GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLA 172

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 565337723  161 LPVLAGAITMLLTDRNLNTsffdfsGGGDPILFQHLFWFFGHP 203
Cdd:pfam00115 173 FPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHP 209
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-203 2.74e-109

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 322.20  E-value: 2.74e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565337723   1 LELGMPGSLLLNDQIYNSMVTMHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLIPSLILLILSSIL 80
Cdd:MTH00153  37 AELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMV 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565337723  81 NVGVGTGWTIYPPLSSLVGHGGVSVDLAIFSLHLAGISSIMGAINFISTILNMNFYMMKMDQLVLFIWSILITAILLLLS 160
Cdd:MTH00153 117 ESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLS 196

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 565337723 161 LPVLAGAITMLLTDRNLNTSFFDFSGGGDPILFQHLFWFFGHP 203
Cdd:MTH00153 197 LPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHP 239
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-203 7.05e-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: 302.48  E-value: 7.05e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565337723   1 LELGMPGSLLLNDQIYNSMVTMHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLIPSLILLILSSIL 80
Cdd:cd01663   30 LELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALV 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565337723  81 NVGVGTGWTIYPPLSSLVGHGGVSVDLAIFSLHLAGISSIMGAINFISTILNMNFYMMKMDQLVLFIWSILITAILLLLS 160
Cdd:cd01663  110 EGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLS 189

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 565337723 161 LPVLAGAITMLLTDRNLNTSFFDFSGGGDPILFQHLFWFFGHP 203
Cdd:cd01663  190 LPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHP 232
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-203 3.61e-94

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 283.49  E-value: 3.61e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565337723   1 LELGMPGSLLLNDQIYNSMVTMHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLIPSLILLILSSIL 80
Cdd:MTH00167  39 AELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGV 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565337723  81 NVGVGTGWTIYPPLSSLVGHGGVSVDLAIFSLHLAGISSIMGAINFISTILNMNFYMMKMDQLVLFIWSILITAILLLLS 160
Cdd:MTH00167 119 EAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLS 198

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 565337723 161 LPVLAGAITMLLTDRNLNTSFFDFSGGGDPILFQHLFWFFGHP 203
Cdd:MTH00167 199 LPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 241
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 2-203 4.86e-94

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 283.52  E-value: 4.86e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565337723   2 ELGMPGSLLLNDQIYNSMVTMHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLIPSLILLILSSILN 81
Cdd:MTH00116  40 ELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVE 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565337723  82 VGVGTGWTIYPPLSSLVGHGGVSVDLAIFSLHLAGISSIMGAINFISTILNMNFYMMKMDQLVLFIWSILITAILLLLSL 161
Cdd:MTH00116 120 AGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSL 199

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 565337723 162 PVLAGAITMLLTDRNLNTSFFDFSGGGDPILFQHLFWFFGHP 203
Cdd:MTH00116 200 PVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 241
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-203 7.31e-94

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 282.64  E-value: 7.31e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565337723   1 LELGMPGSLLLNDQIYNSMVTMHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLIPSLILLILSSIL 80
Cdd:MTH00223  36 AELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAV 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565337723  81 NVGVGTGWTIYPPLSSLVGHGGVSVDLAIFSLHLAGISSIMGAINFISTILNMNFYMMKMDQLVLFIWSILITAILLLLS 160
Cdd:MTH00223 116 ESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLS 195

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 565337723 161 LPVLAGAITMLLTDRNLNTSFFDFSGGGDPILFQHLFWFFGHP 203
Cdd:MTH00223 196 LPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHP 238
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-203 6.57e-92

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 277.76  E-value: 6.57e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565337723   1 LELGMPGSLLLNDQIYNSMVTMHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLIPSLILLILSSIL 80
Cdd:MTH00142  37 AELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAV 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565337723  81 NVGVGTGWTIYPPLSSLVGHGGVSVDLAIFSLHLAGISSIMGAINFISTILNMNFYMMKMDQLVLFIWSILITAILLLLS 160
Cdd:MTH00142 117 ESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKITAILLLLS 196

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 565337723 161 LPVLAGAITMLLTDRNLNTSFFDFSGGGDPILFQHLFWFFGHP 203
Cdd:MTH00142 197 LPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHP 239
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 2-203 4.71e-85

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 260.53  E-value: 4.71e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565337723   2 ELGMPGSLLLNDQIYNSMVTMHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLIPSLILLILSSILN 81
Cdd:MTH00037  40 ELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVE 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565337723  82 VGVGTGWTIYPPLSSLVGHGGVSVDLAIFSLHLAGISSIMGAINFISTILNMNFYMMKMDQLVLFIWSILITAILLLLSL 161
Cdd:MTH00037 120 SGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSL 199

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 565337723 162 PVLAGAITMLLTDRNLNTSFFDFSGGGDPILFQHLFWFFGHP 203
Cdd:MTH00037 200 PVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHP 241
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-203 1.31e-83

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 256.37  E-value: 1.31e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565337723   1 LELGMPGSLLLNDQIYNSMVTMHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLIPSLILLILSSIL 80
Cdd:MTH00007  36 IELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAV 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565337723  81 NVGVGTGWTIYPPLSSLVGHGGVSVDLAIFSLHLAGISSIMGAINFISTILNMNFYMMKMDQLVLFIWSILITAILLLLS 160
Cdd:MTH00007 116 EKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVITVVLLLLS 195

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 565337723 161 LPVLAGAITMLLTDRNLNTSFFDFSGGGDPILFQHLFWFFGHP 203
Cdd:MTH00007 196 LPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHP 238
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 2-203 1.55e-82

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 253.65  E-value: 1.55e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565337723   2 ELGMPGSLLLNDQIYNSMVTMHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLIPSLILLILSSILN 81
Cdd:MTH00103  40 ELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVE 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565337723  82 VGVGTGWTIYPPLSSLVGHGGVSVDLAIFSLHLAGISSIMGAINFISTILNMNFYMMKMDQLVLFIWSILITAILLLLSL 161
Cdd:MTH00103 120 AGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSL 199

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 565337723 162 PVLAGAITMLLTDRNLNTSFFDFSGGGDPILFQHLFWFFGHP 203
Cdd:MTH00103 200 PVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 241
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 2-203 1.91e-82

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 253.69  E-value: 1.91e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565337723   2 ELGMPGSLLLNDQIYNSMVTMHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLIPSLILLILSSILN 81
Cdd:MTH00183  40 ELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVE 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565337723  82 VGVGTGWTIYPPLSSLVGHGGVSVDLAIFSLHLAGISSIMGAINFISTILNMNFYMMKMDQLVLFIWSILITAILLLLSL 161
Cdd:MTH00183 120 AGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSL 199

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 565337723 162 PVLAGAITMLLTDRNLNTSFFDFSGGGDPILFQHLFWFFGHP 203
Cdd:MTH00183 200 PVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 241
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 2-203 3.35e-82

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 252.94  E-value: 3.35e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565337723   2 ELGMPGSLLLNDQIYNSMVTMHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLIPSLILLILSSILN 81
Cdd:MTH00077  40 ELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVE 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565337723  82 VGVGTGWTIYPPLSSLVGHGGVSVDLAIFSLHLAGISSIMGAINFISTILNMNFYMMKMDQLVLFIWSILITAILLLLSL 161
Cdd:MTH00077 120 AGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSL 199

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 565337723 162 PVLAGAITMLLTDRNLNTSFFDFSGGGDPILFQHLFWFFGHP 203
Cdd:MTH00077 200 PVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHP 241
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-203 3.45e-79

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 244.98  E-value: 3.45e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565337723   1 LELGMPGSLLLNDQIYNSMVTMHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLIPSLILLILSSIL 80
Cdd:MTH00079  40 LELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFV 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565337723  81 NVGVGTGWTIYPPLSSLvGHGGVSVDLAIFSLHLAGISSIMGAINFISTILNMNFYMMKMDQLVLFIWSILITAILLLLS 160
Cdd:MTH00079 120 DMGPGTSWTVYPPLSTL-GHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLS 198

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 565337723 161 LPVLAGAITMLLTDRNLNTSFFDFSGGGDPILFQHLFWFFGHP 203
Cdd:MTH00079 199 LPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHP 241
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-203 7.23e-79

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 244.35  E-value: 7.23e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565337723   1 LELGMPGSLLLNDQIYNSMVTMHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLIPSLILLILSSIL 80
Cdd:MTH00184  41 LELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFV 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565337723  81 NVGVGTGWTIYPPLSSLVGHGGVSVDLAIFSLHLAGISSIMGAINFISTILNMNFYMMKMDQLVLFIWSILITAILLLLS 160
Cdd:MTH00184 121 EQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLS 200

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 565337723 161 LPVLAGAITMLLTDRNLNTSFFDFSGGGDPILFQHLFWFFGHP 203
Cdd:MTH00184 201 LPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHP 243
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-203 1.14e-77

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 241.65  E-value: 1.14e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565337723   1 LELGMPGSLLLNDQIYNSMVTMHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLIPSLILLILSSIL 80
Cdd:MTH00182  41 LELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFV 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565337723  81 NVGVGTGWTIYPPLSSLVGHGGVSVDLAIFSLHLAGISSIMGAINFISTILNMNFYMMKMDQLVLFIWSILITAILLLLS 160
Cdd:MTH00182 121 EQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLS 200

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 565337723 161 LPVLAGAITMLLTDRNLNTSFFDFSGGGDPILFQHLFWFFGHP 203
Cdd:MTH00182 201 LPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHP 243
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-203 8.79e-71

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 224.12  E-value: 8.79e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565337723   1 LELGMPGSLLLNDQIYNSMVTMHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLIPSLILLILSSIL 80
Cdd:MTH00026  40 LELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLV 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565337723  81 NVGVGTGWTIYPPLSSLVGHGGVSVDLAIFSLHLAGISSIMGAINFISTILNMNFYMMKMDQLVLFIWSILITAILLLLS 160
Cdd:MTH00026 120 EQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLS 199

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 565337723 161 LPVLAGAITMLLTDRNLNTSFFDFSGGGDPILFQHLFWFFGHP 203
Cdd:MTH00026 200 LPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHP 242
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-203 3.90e-64

cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) of cytochrome c oxidases of bacterial origin. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits I-III form the functional core of the enzyme complex. Subunit I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit II and heme a of subunit I to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. In the bacilli an apparent split (paralogism) has created a sister clade (TIGR02882) encoding subunits (QoxA) of the aa3-type quinone oxidase complex which reacts directly with quinones, bypassing the interaction with soluble cytochrome c. This model attempts to exclude these sequences, placing them between the trusted and noise cutoffs. These families, as well as archaeal and eukaryotic cytochrome c subunit I's are included within the superfamily model, pfam00115. [Energy metabolism, Electron transport]


Pssm-ID: 213748  Cd Length: 499  Bit Score: 205.92  E-value: 3.90e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565337723    1 LELGMPGSLLLNDQIYNSMVTMHAFVMIFFMVMPIMiGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLIPSLILLILSSIL 80
Cdd:TIGR02891  33 AQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFT 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565337723   81 NVGVGTGWTIYPPLSSLVGHGGVSVDLAIFSLHLAGISSIMGAINFISTILNMNFYMMKMDQLVLFIWSILITAILLLLS 160
Cdd:TIGR02891 112 GGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLA 191

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 565337723  161 LPVLAGAITMLLTDRNLNTSFFDFSGGGDPILFQHLFWFFGHP 203
Cdd:TIGR02891 192 FPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHP 234
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-203 7.12e-64

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: 204.30  E-value: 7.12e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565337723   1 LELGMPGSLLLNDQIYNSMVTMHAFVMIFFMVMPIMIGGFGNWLVPlMLGAPDMAFPRMNNMSFWLLIPSLILLILSSIL 80
Cdd:cd00919   28 LELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWLFPPGLLLLLSSVLV 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565337723  81 NVGVGTGWTIYPPLSSLVGHGGVSVDLAIFSLHLAGISSIMGAINFISTILNMNFYMMKMDQLVLFIWSILITAILLLLS 160
Cdd:cd00919  107 GGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTAILLLLA 186

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 565337723 161 LPVLAGAITMLLTDRNLNTSFFDFSGGGDPILFQHLFWFFGHP 203
Cdd:cd00919  187 LPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHP 229
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-203 2.52e-60

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 196.50  E-value: 2.52e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565337723   1 LELGMPGSLLLNDQIYNSMVTMHAFVMIFFMVMPiMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLIPSLILLILSSIL 80
Cdd:COG0843   42 LQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFV 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565337723  81 NVGVGTGWTIYPPLSSLVGHGGVSVDLAIFSLHLAGISSIMGAINFISTILNMNFYMMKMDQLVLFIWSILITAILLLLS 160
Cdd:COG0843  121 GGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLA 200

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 565337723 161 LPVLAGAITMLLTDRNLNTSFFDFSGGGDPILFQHLFWFFGHP 203
Cdd:COG0843  201 FPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHP 243
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 15-203 1.08e-53

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 178.72  E-value: 1.08e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565337723  15 IYNSMVTMHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLIPSLILLILSSILnvGVGTGWTIYPPL 94
Cdd:MTH00048  54 VYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPL 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565337723  95 SSLVGHGGVSVDLAIFSLHLAGISSIMGAINFISTILNMnFYMMKMDQLVLFIWSILITAILLLLSLPVLAGAITMLLTD 174
Cdd:MTH00048 132 SSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSA-FMTNVFSRTSIILWSYLFTSILLLLSLPVLAAAITMLLFD 210

                        170       180
                 ....*....|....*....|....*....
gi 565337723 175 RNLNTSFFDFSGGGDPILFQHLFWFFGHP 203
Cdd:MTH00048 211 RNFGSAFFDPLGGGDPVLFQHMFWFFGHP 239
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-203 1.31e-49

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: 167.76  E-value: 1.31e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565337723   1 LELGMPGSLLLNDQIYNSMVTMHAFVMIFFMVMPIMIGgFGNWLVPLMLGAPDMAFPRMNNMSFWLLIPSLILLILSSIL 80
Cdd:cd01662   34 TQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLI 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565337723  81 NVGVGTGWTIYPPLSSLVGHGGVSVDLAIFSLHLAGISSIMGAINFISTILNMNFYMMKMDQLVLFIWSILITAILLLLS 160
Cdd:cd01662  113 GGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFA 192

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 565337723 161 LPVLAGAITMLLTDRNLNTSFFDFSGGGDPILFQHLFWFFGHP 203
Cdd:cd01662  193 FPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHP 235
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-203 4.32e-33

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: 122.68  E-value: 4.32e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565337723    1 LELGMPGSLLLNDQIYNSMVTMHAFVMIFFMVMPiMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLIPSLILLILSSIl 80
Cdd:pfam00115  26 LQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASFG- 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565337723   81 nvGVGTGWTIYPPLsslvghggVSVDLAIFSLHLAGISSIMGAINFISTILNMNFYMMKMdQLVLFIWSILITAILLLLS 160
Cdd:pfam00115 104 --GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLA 172

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 565337723  161 LPVLAGAITMLLTDRNLNTsffdfsGGGDPILFQHLFWFFGHP 203
Cdd:pfam00115 173 FPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHP 209
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 1-203 8.73e-30

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: 115.34  E-value: 8.73e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565337723    1 LELGMPGSLLLNDQIYNSMVTMHAFVMIFFMVMPIMIGgFGNWLVPLMLGAPDMAFPRMNNMSFWLLIPSLILLILSSIL 80
Cdd:TIGR02882  77 AQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVI 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565337723   81 NVGVGTGWTIYPPLSSLVGHGGVSVDLAIFSLHLAGISSIMGAINFISTILNMNFYMMKMDQLVLFIWSILITAILLLLS 160
Cdd:TIGR02882 156 GGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFA 235

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 565337723  161 LPVLAGAITMLLTDRNLNTSFFDFSGGGDPILFQHLFWFFGHP 203
Cdd:TIGR02882 236 FPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHP 278
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 16-203 1.35e-29

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 114.65  E-value: 1.35e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565337723  16 YNSMVTMHAFVMIFFMVMPIMIGgFGNWLVPLMLGAPDMAFPRMNNMSFWLLIPSLILLILSSILNVGVGTGWTIYPPLS 95
Cdd:PRK15017  99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565337723  96 SLVGHGGVSVDLAIFSLHLAGISSIMGAINFISTILNMNFYMMKMDQLVLFIWSILITAILLLLSLPVLAGAITMLLTDR 175
Cdd:PRK15017 178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257

                        170       180
                 ....*....|....*....|....*...
gi 565337723 176 NLNTSFFDFSGGGDPILFQHLFWFFGHP 203
Cdd:PRK15017 258 YLGTHFFTNDMGGNMMMYINLIWAWGHP 285
 
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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