NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1812373152|gb|QID41086|]
View 

cytochrome c oxidase subunit I, partial (mitochondrion) [Dendarus messenius]

Protein Classification

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

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Heme_Cu_Oxidase_I super family cl00275
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-136 3.39e-92

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: 275.59  E-value: 3.39e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812373152   1 PPSLTLLLMSSVVENGAGTGWTVYPPLSSNIAHGGSSVDLAIFSLHLAGISSILGAVNFITTVINMRPQGMTFDRMPLFV 80
Cdd:MTH00153  104 PPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFV 183

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1812373152  81 WAVVITAVLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHP 136
Cdd:MTH00153  184 WSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHP 239
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-136 3.39e-92

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 275.59  E-value: 3.39e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812373152   1 PPSLTLLLMSSVVENGAGTGWTVYPPLSSNIAHGGSSVDLAIFSLHLAGISSILGAVNFITTVINMRPQGMTFDRMPLFV 80
Cdd:MTH00153  104 PPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFV 183

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1812373152  81 WAVVITAVLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHP 136
Cdd:MTH00153  184 WSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHP 239
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-136 1.44e-81

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: 247.40  E-value: 1.44e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812373152   1 PPSLTLLLMSSVVENGAGTGWTVYPPLSSNIAHGGSSVDLAIFSLHLAGISSILGAVNFITTVINMRPQGMTFDRMPLFV 80
Cdd:cd01663    97 PPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFV 176

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1812373152  81 WAVVITAVLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHP 136
Cdd:cd01663   177 WSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHP 232
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-136 1.79e-51

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: 169.71  E-value: 1.79e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812373152   1 PPSLTLLLMSSVVENGAGTGWTVYPPLSSNIAHGGSSVDLAIFSLHLAGISSILGAVNFITTVINMRPQGMTFDRMPLFV 80
Cdd:TIGR02891  99 LFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFV 178

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1812373152  81 WAVVITAVLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHP 136
Cdd:TIGR02891 179 WGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHP 234
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
5-136 1.67e-50

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 168.00  E-value: 1.67e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812373152   5 TLLLMSSVVENG-AGTGWTVYPPLSSNIAHGGSSVDLAIFSLHLAGISSILGAVNFITTVINMRPQGMTFDRMPLFVWAV 83
Cdd:COG0843   111 GLLLLISLFVGGaADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAA 190

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1812373152  84 VITAVLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHP 136
Cdd:COG0843   191 LVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHP 243
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 5-136 5.95e-26

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: 100.73  E-value: 5.95e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812373152   5 TLLLMSSVveNGAGTGWTVYPPLSSniahggssVDLAIFSLHLAGISSILGAVNFITTVINMRPQGMTFdRMPLFVWAVV 84
Cdd:pfam00115  95 AVLLLASF--GGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAIL 163

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1812373152  85 ITAVLLLLSLPVLAGAITMLLTDRNINtsffdpAGGGDPILYQHLFWFFGHP 136
Cdd:pfam00115 164 ATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHP 209
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-136 3.39e-92

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 275.59  E-value: 3.39e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812373152   1 PPSLTLLLMSSVVENGAGTGWTVYPPLSSNIAHGGSSVDLAIFSLHLAGISSILGAVNFITTVINMRPQGMTFDRMPLFV 80
Cdd:MTH00153  104 PPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFV 183

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1812373152  81 WAVVITAVLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHP 136
Cdd:MTH00153  184 WSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHP 239
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-136 1.44e-81

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: 247.40  E-value: 1.44e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812373152   1 PPSLTLLLMSSVVENGAGTGWTVYPPLSSNIAHGGSSVDLAIFSLHLAGISSILGAVNFITTVINMRPQGMTFDRMPLFV 80
Cdd:cd01663    97 PPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFV 176

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1812373152  81 WAVVITAVLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHP 136
Cdd:cd01663   177 WSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHP 232
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-136 2.76e-76

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 234.57  E-value: 2.76e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812373152   1 PPSLTLLLMSSVVENGAGTGWTVYPPLSSNIAHGGSSVDLAIFSLHLAGISSILGAVNFITTVINMRPQGMTFDRMPLFV 80
Cdd:MTH00167  106 PPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFV 185

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1812373152  81 WAVVITAVLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHP 136
Cdd:MTH00167  186 WSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 241
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-136 9.23e-76

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 233.33  E-value: 9.23e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812373152   1 PPSLTLLLMSSVVENGAGTGWTVYPPLSSNIAHGGSSVDLAIFSLHLAGISSILGAVNFITTVINMRPQGMTFDRMPLFV 80
Cdd:MTH00223  103 PPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFV 182

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1812373152  81 WAVVITAVLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHP 136
Cdd:MTH00223  183 WSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHP 238
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-136 1.71e-75

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 232.69  E-value: 1.71e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812373152   1 PPSLTLLLMSSVVENGAGTGWTVYPPLSSNIAHGGSSVDLAIFSLHLAGISSILGAVNFITTVINMRPQGMTFDRMPLFV 80
Cdd:MTH00142  104 PPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFV 183

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1812373152  81 WAVVITAVLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHP 136
Cdd:MTH00142  184 WSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHP 239
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-136 4.63e-73

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 226.51  E-value: 4.63e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812373152   1 PPSLTLLLMSSVVENGAGTGWTVYPPLSSNIAHGGSSVDLAIFSLHLAGISSILGAVNFITTVINMRPQGMTFDRMPLFV 80
Cdd:MTH00116  106 PPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFV 185

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1812373152  81 WAVVITAVLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHP 136
Cdd:MTH00116  186 WSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 241
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-136 9.95e-69

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 215.15  E-value: 9.95e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812373152   1 PPSLTLLLMSSVVENGAGTGWTVYPPLSSNIAHGGSSVDLAIFSLHLAGISSILGAVNFITTVINMRPQGMTFDRMPLFV 80
Cdd:MTH00007  103 PPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFV 182

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1812373152  81 WAVVITAVLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHP 136
Cdd:MTH00007  183 WAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHP 238
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-136 2.00e-65

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 206.60  E-value: 2.00e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812373152   1 PPSLTLLLMSSVVENGAGTGWTVYPPLSSNIAHGGSSVDLAIFSLHLAGISSILGAVNFITTVINMRPQGMTFDRMPLFV 80
Cdd:MTH00037  106 PPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFV 185

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1812373152  81 WAVVITAVLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHP 136
Cdd:MTH00037  186 WSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHP 241
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-136 2.31e-64

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 203.90  E-value: 2.31e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812373152   1 PPSLTLLLMSSVVENGAGTGWTVYPPLSSNIAHGGSSVDLAIFSLHLAGISSILGAVNFITTVINMRPQGMTFDRMPLFV 80
Cdd:MTH00184  108 PPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFV 187

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1812373152  81 WAVVITAVLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHP 136
Cdd:MTH00184  188 WSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHP 243
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-136 3.49e-64

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 203.62  E-value: 3.49e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812373152   1 PPSLTLLLMSSVVENGAGTGWTVYPPLSSNIAHGGSSVDLAIFSLHLAGISSILGAVNFITTVINMRPQGMTFDRMPLFV 80
Cdd:MTH00183  106 PPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFV 185

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1812373152  81 WAVVITAVLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHP 136
Cdd:MTH00183  186 WAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 241
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-136 4.70e-64

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 203.19  E-value: 4.70e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812373152   1 PPSLTLLLMSSVVENGAGTGWTVYPPLSSNIAHGGSSVDLAIFSLHLAGISSILGAVNFITTVINMRPQGMTFDRMPLFV 80
Cdd:MTH00103  106 PPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFV 185

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1812373152  81 WAVVITAVLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHP 136
Cdd:MTH00103  186 WSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 241
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-136 5.53e-64

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 203.13  E-value: 5.53e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812373152   1 PPSLTLLLMSSVVENGAGTGWTVYPPLSSNIAHGGSSVDLAIFSLHLAGISSILGAVNFITTVINMRPQGMTFDRMPLFV 80
Cdd:MTH00182  108 PPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFV 187

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1812373152  81 WAVVITAVLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHP 136
Cdd:MTH00182  188 WSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHP 243
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-136 1.35e-63

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 202.09  E-value: 1.35e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812373152   1 PPSLTLLLMSSVVENGAGTGWTVYPPLSSNIAHGGSSVDLAIFSLHLAGISSILGAVNFITTVINMRPQGMTFDRMPLFV 80
Cdd:MTH00077  106 PPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFV 185

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1812373152  81 WAVVITAVLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHP 136
Cdd:MTH00077  186 WSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHP 241
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-136 3.64e-61

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 195.28  E-value: 3.64e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812373152   1 PPSLTLLLMSSVVENGAGTGWTVYPPLSSnIAHGGSSVDLAIFSLHLAGISSILGAVNFITTVINMRPQGMTFDRMPLFV 80
Cdd:MTH00079  107 PTSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFV 185

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1812373152  81 WAVVITAVLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHP 136
Cdd:MTH00079  186 WTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHP 241
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-136 8.86e-58

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 187.14  E-value: 8.86e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812373152   1 PPSLTLLLMSSVVENGAGTGWTVYPPLSSNIAHGGSSVDLAIFSLHLAGISSILGAVNFITTVINMRPQGMTFDRMPLFV 80
Cdd:MTH00026  107 PPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFV 186

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1812373152  81 WAVVITAVLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHP 136
Cdd:MTH00026  187 WSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHP 242
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-136 4.82e-56

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: 180.80  E-value: 4.82e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812373152   1 PPSLTLLLMSSVVENGAGTGWTVYPPLSSNIAHGGSSVDLAIFSLHLAGISSILGAVNFITTVINMRPQGMTFDRMPLFV 80
Cdd:cd00919    94 PPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFV 173

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1812373152  81 WAVVITAVLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHP 136
Cdd:cd00919   174 WSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHP 229
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-136 1.79e-51

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: 169.71  E-value: 1.79e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812373152   1 PPSLTLLLMSSVVENGAGTGWTVYPPLSSNIAHGGSSVDLAIFSLHLAGISSILGAVNFITTVINMRPQGMTFDRMPLFV 80
Cdd:TIGR02891  99 LFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFV 178

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1812373152  81 WAVVITAVLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHP 136
Cdd:TIGR02891 179 WGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHP 234
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
5-136 1.67e-50

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 168.00  E-value: 1.67e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812373152   5 TLLLMSSVVENG-AGTGWTVYPPLSSNIAHGGSSVDLAIFSLHLAGISSILGAVNFITTVINMRPQGMTFDRMPLFVWAV 83
Cdd:COG0843   111 GLLLLISLFVGGaADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAA 190

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1812373152  84 VITAVLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHP 136
Cdd:COG0843   191 LVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHP 243
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 2-136 6.40e-42

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 144.82  E-value: 6.40e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812373152   2 PSLTLLLMSSVVenGAGTGWTVYPPLSSNIAHGGSSVDLAIFSLHLAGISSILGAVNFITTVINMRPQGMTFdRMPLFVW 81
Cdd:MTH00048  108 PSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFS-RTSIILW 184

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1812373152  82 AVVITAVLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHP 136
Cdd:MTH00048  185 SYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHP 239
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 6-136 2.01e-40

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: 140.41  E-value: 2.01e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812373152   6 LLLMSSVVENGAGTGWTVYPPLSSNIAHGGSSVDLAIFSLHLAGISSILGAVNFITTVINMRPQGMTFDRMPLFVWAVVI 85
Cdd:cd01662   105 LLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLV 184

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1812373152  86 TAVLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHP 136
Cdd:cd01662   185 TSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHP 235
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 5-136 5.95e-26

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: 100.73  E-value: 5.95e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812373152   5 TLLLMSSVveNGAGTGWTVYPPLSSniahggssVDLAIFSLHLAGISSILGAVNFITTVINMRPQGMTFdRMPLFVWAVV 84
Cdd:pfam00115  95 AVLLLASF--GGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAIL 163

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1812373152  85 ITAVLLLLSLPVLAGAITMLLTDRNINtsffdpAGGGDPILYQHLFWFFGHP 136
Cdd:pfam00115 164 ATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHP 209
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 17-136 7.22e-22

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 89.99  E-value: 7.22e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812373152  17 AGTGWTVYPPLSSNIAHGGSSVDLAIFSLHLAGISSILGAVNFITTVINMRPQGMTFDRMPLFVWAVVITAVLLLLSLPV 96
Cdd:PRK15017  166 AQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPI 245

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1812373152  97 LAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHP 136
Cdd:PRK15017  246 LTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHP 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH