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Conserved domains on  [gi|300684753|gb|ADK27793|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Agolohymena aspidocauda]

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 ...
 145-267 4.97e-30

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 cd00919:

Pssm-ID: 469701  Cd Length: 463  Bit Score: 116.86  E-value: 4.97e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300684753 145 AGWTFITPFSSNVKYTGVGSqDILILSVVFAGISTTISFTNLLITRRTLAMPGIRHRRilMPFITIATFLALRMLATITP 224
Cdd:cd00919  112 TGWTFYPPLSTLSYSSGVGV-DLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDK--MPLFVWSVLVTAILLLLALP 188

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 300684753 225 VLGAAVIMMAFDRHWQTTFFEYAYGGDPILSQHLFWFFGHPEV 267
Cdd:cd00919  189 VLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEV 231
 
Name Accession Description Interval E-value
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 145-267 4.97e-30

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: 116.86  E-value: 4.97e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300684753 145 AGWTFITPFSSNVKYTGVGSqDILILSVVFAGISTTISFTNLLITRRTLAMPGIRHRRilMPFITIATFLALRMLATITP 224
Cdd:cd00919  112 TGWTFYPPLSTLSYSSGVGV-DLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDK--MPLFVWSVLVTAILLLLALP 188

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 300684753 225 VLGAAVIMMAFDRHWQTTFFEYAYGGDPILSQHLFWFFGHPEV 267
Cdd:cd00919  189 VLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEV 231
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 144-267 1.28e-27

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: 110.78  E-value: 1.28e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300684753  144 TAGWTFITPFSSNVKYTGVGSqDILILSVVFAGISTTISFTNLLITRRTLAMPGIRHRRilMPFITIATFLALRMLATIT 223
Cdd:TIGR02891 116 DTGWTMYPPLSSTSGSPGVGV-DLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMR--MPLFVWGILVTSILILLAF 192

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 300684753  224 PVLGAAVIMMAFDRHWQTTFFEYAYGGDPILSQHLFWFFGHPEV 267
Cdd:TIGR02891 193 PVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEV 236
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
144-267 2.10e-27

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 110.22  E-value: 2.10e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300684753 144 TAGWTFITPFSSNVKYTGVGsQDILILSVVFAGISTTISFTNLLITRRTLAMPGIRHRRilMPFITIATFLALRMLATIT 223
Cdd:COG0843  125 DVGWTFYPPLSGLEASPGVG-VDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMR--MPLFTWAALVTSILILLAF 201

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 300684753 224 PVLGAAVIMMAFDRHWQTTFFEYAYGGDPILSQHLFWFFGHPEV 267
Cdd:COG0843  202 PVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEV 245
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 145-267 7.92e-25

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 102.75  E-value: 7.92e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300684753 145 AGWTFITPFSSNVKYTGVgSQDILILSVVFAGISTTISFTNLLITRRTLAMPGIRHRRiLMPF---ITIATFLALRMLat 221
Cdd:MTH00223 121 TGWTVYPPLSSNLAHAGP-SVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLER-LPLFvwsVKVTAFLLLLSL-- 196

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 300684753 222 itPVLGAAVIMMAFDRHWQTTFFEYAYGGDPILSQHLFWFFGHPEV 267
Cdd:MTH00223 197 --PVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEV 240
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 144-267 1.36e-14

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: 72.99  E-value: 1.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300684753  144 TAGWTFitpfssnvkYTGVGSQDILILSVVFAGISTTISFTNLLITRRTLAMPGIRHRRILMPFITIATFLalrMLATIT 223
Cdd:pfam00115 106 TTGWTE---------YPPLVGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTLRMPLFVWAILATAI---LILLAF 173

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 300684753  224 PVLGAAVIMMAFDRHWQttffeyAYGGDPILSQHLFWFFGHPEV 267
Cdd:pfam00115 174 PVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEV 211
 
Name Accession Description Interval E-value
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 145-267 4.97e-30

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: 116.86  E-value: 4.97e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300684753 145 AGWTFITPFSSNVKYTGVGSqDILILSVVFAGISTTISFTNLLITRRTLAMPGIRHRRilMPFITIATFLALRMLATITP 224
Cdd:cd00919  112 TGWTFYPPLSTLSYSSGVGV-DLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDK--MPLFVWSVLVTAILLLLALP 188

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 300684753 225 VLGAAVIMMAFDRHWQTTFFEYAYGGDPILSQHLFWFFGHPEV 267
Cdd:cd00919  189 VLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEV 231
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 144-267 1.28e-27

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: 110.78  E-value: 1.28e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300684753  144 TAGWTFITPFSSNVKYTGVGSqDILILSVVFAGISTTISFTNLLITRRTLAMPGIRHRRilMPFITIATFLALRMLATIT 223
Cdd:TIGR02891 116 DTGWTMYPPLSSTSGSPGVGV-DLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMR--MPLFVWGILVTSILILLAF 192

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 300684753  224 PVLGAAVIMMAFDRHWQTTFFEYAYGGDPILSQHLFWFFGHPEV 267
Cdd:TIGR02891 193 PVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEV 236
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
144-267 2.10e-27

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 110.22  E-value: 2.10e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300684753 144 TAGWTFITPFSSNVKYTGVGsQDILILSVVFAGISTTISFTNLLITRRTLAMPGIRHRRilMPFITIATFLALRMLATIT 223
Cdd:COG0843  125 DVGWTFYPPLSGLEASPGVG-VDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMR--MPLFTWAALVTSILILLAF 201

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 300684753 224 PVLGAAVIMMAFDRHWQTTFFEYAYGGDPILSQHLFWFFGHPEV 267
Cdd:COG0843  202 PVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEV 245
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 145-267 1.90e-25

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: 104.49  E-value: 1.90e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300684753 145 AGWTFITPFSSNVKYTGvGSQDILILSVVFAGISTTISFTNLLITRRTLAMPGIRHRRilMPFITIATFLALRMLATITP 224
Cdd:cd01663  115 TGWTVYPPLSSILAHSG-PSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEK--MPLFVWSVLITAFLLLLSLP 191

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 300684753 225 VLGAAVIMMAFDRHWQTTFFEYAYGGDPILSQHLFWFFGHPEV 267
Cdd:cd01663  192 VLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEV 234
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 145-267 7.92e-25

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 102.75  E-value: 7.92e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300684753 145 AGWTFITPFSSNVKYTGVgSQDILILSVVFAGISTTISFTNLLITRRTLAMPGIRHRRiLMPF---ITIATFLALRMLat 221
Cdd:MTH00223 121 TGWTVYPPLSSNLAHAGP-SVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLER-LPLFvwsVKVTAFLLLLSL-- 196

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 300684753 222 itPVLGAAVIMMAFDRHWQTTFFEYAYGGDPILSQHLFWFFGHPEV 267
Cdd:MTH00223 197 --PVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEV 240
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 145-267 1.43e-23

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: 99.19  E-value: 1.43e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300684753 145 AGWTFITPFSSNVKYTGVGSqDILILSVVFAGISTTISFTNLLITRRTLAMPGIRHRRilMPFITIATFLALRMLATITP 224
Cdd:cd01662  118 AGWFAYPPLSGLEYSPGVGV-DYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMR--MPIFTWTTLVTSILILFAFP 194

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 300684753 225 VLGAAVIMMAFDRHWQTTFFEYAYGGDPILSQHLFWFFGHPEV 267
Cdd:cd01662  195 VLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEV 237
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 146-267 3.64e-23

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 98.21  E-value: 3.64e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300684753 146 GWTFITPFSSNVKYTGvGSQDILILSVVFAGISTTISFTNLLITRRTLAMPGIRHRRilMPFITIATFLALRMLATITPV 225
Cdd:MTH00167 125 GWTVYPPLAGNLAHAG-ASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQ--TPLFVWSILVTTILLLLSLPV 201

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 300684753 226 LGAAVIMMAFDRHWQTTFFEYAYGGDPILSQHLFWFFGHPEV 267
Cdd:MTH00167 202 LAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEV 243
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 146-267 2.30e-22

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 95.95  E-value: 2.30e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300684753 146 GWTFITPFSSNVKYTGvGSQDILILSVVFAGISTTISFTNLLITRRTLAMPGIRHRRIlmPFITIATFLALRMLATITPV 225
Cdd:MTH00142 123 GWTVYPPLSSNLAHSG-GSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERV--PLFVWSVKITAILLLLSLPV 199

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 300684753 226 LGAAVIMMAFDRHWQTTFFEYAYGGDPILSQHLFWFFGHPEV 267
Cdd:MTH00142 200 LAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEV 241
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 146-267 1.46e-21

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 93.39  E-value: 1.46e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300684753 146 GWTFITPFSSNVKYTGvGSQDILILSVVFAGISTTISFTNLLITRRTLAMPGIRHRRilMPF----ITIATFLALRMLat 221
Cdd:MTH00153 123 GWTVYPPLSSNIAHSG-ASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDR--MPLfvwsVLITAILLLLSL-- 197

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 300684753 222 itPVLGAAVIMMAFDRHWQTTFFEYAYGGDPILSQHLFWFFGHPEV 267
Cdd:MTH00153 198 --PVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 241
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 146-267 1.67e-21

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 93.20  E-value: 1.67e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300684753 146 GWTFITPFSSNVKYTGVGSqDILILSVVFAGISTTISFTNLLITRRTLAMPGIRHRRIlmpfITIATFLALRMLATIT-P 224
Cdd:MTH00048 124 GWTFYPPLSSSLFSSSWGV-DFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFSRTS----IILWSYLFTSILLLLSlP 198

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 300684753 225 VLGAAVIMMAFDRHWQTTFFEYAYGGDPILSQHLFWFFGHPEV 267
Cdd:MTH00048 199 VLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEV 241
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 145-267 1.81e-21

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 93.35  E-value: 1.81e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300684753 145 AGWTFITPFSSNVKYTGvGSQDILILSVVFAGISTTISFTNLLITRRTLAMPGIRHRRilMPFITIATFLALRMLATITP 224
Cdd:MTH00184 126 TGWTVYPPLSSIQAHSG-GSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDR--MPLFVWSILVTTFLLLLSLP 202

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 300684753 225 VLGAAVIMMAFDRHWQTTFFEYAYGGDPILSQHLFWFFGHPEV 267
Cdd:MTH00184 203 VLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEV 245
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 146-267 1.94e-21

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 93.04  E-value: 1.94e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300684753 146 GWTFITPFSSNVKYTGvGSQDILILSVVFAGISTTISFTNLLITRRTLAMPGIRHRRilMPFITIATFLALRMLATITPV 225
Cdd:MTH00007 122 GWTVYPPLASNLAHAG-PSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLER--IPLFVWAVVITVVLLLLSLPV 198

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 300684753 226 LGAAVIMMAFDRHWQTTFFEYAYGGDPILSQHLFWFFGHPEV 267
Cdd:MTH00007 199 LAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 240
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 146-267 2.29e-21

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 92.85  E-value: 2.29e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300684753 146 GWTFITPFSSNVKYTGvGSQDILILSVVFAGISTTISFTNLLITRRTLAMPGIRHRRilMPFITIATFLALRMLATITPV 225
Cdd:MTH00116 125 GWTVYPPLAGNLAHAG-ASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQ--TPLFVWSVLITAVLLLLSLPV 201

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 300684753 226 LGAAVIMMAFDRHWQTTFFEYAYGGDPILSQHLFWFFGHPEV 267
Cdd:MTH00116 202 LAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEV 243
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 146-267 4.73e-21

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 91.81  E-value: 4.73e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300684753 146 GWTFITPFSSNVKYTGvGSQDILILSVVFAGISTTISFTNLLITRRTLAMPGIRHRRilMPFITIATFLALRMLATITPV 225
Cdd:MTH00037 125 GWTIYPPLSSNIAHAG-GSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDR--LPLFVWSVFITAFLLLLSLPV 201

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 300684753 226 LGAAVIMMAFDRHWQTTFFEYAYGGDPILSQHLFWFFGHPEV 267
Cdd:MTH00037 202 LAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEV 243
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 146-267 6.24e-21

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 91.52  E-value: 6.24e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300684753 146 GWTFITPFSSNVKYTGvGSQDILILSVVFAGISTTISFTNLLITRRTLAMPGIRHRRilMPFITIATFLALRMLATITPV 225
Cdd:MTH00183 125 GWTVYPPLAGNLAHAG-ASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQ--TPLFVWAVLITAVLLLLSLPV 201

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 300684753 226 LGAAVIMMAFDRHWQTTFFEYAYGGDPILSQHLFWFFGHPEV 267
Cdd:MTH00183 202 LAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEV 243
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 146-267 5.49e-20

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 88.92  E-value: 5.49e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300684753 146 GWTFITPFSSNVKYTGvGSQDILILSVVFAGISTTISFTNLLITRRTLAMPGIRHRRIlmPFITIATFLALRMLATITPV 225
Cdd:MTH00026 126 GWTVYPPLASIQAHSG-GSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRI--PLFVWSVFITAILLLLSLPV 202

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 300684753 226 LGAAVIMMAFDRHWQTTFFEYAYGGDPILSQHLFWFFGHPEV 267
Cdd:MTH00026 203 LAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEV 244
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 145-267 9.93e-20

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 88.34  E-value: 9.93e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300684753 145 AGWTFITPFSSNVKYTGvGSQDILILSVVFAGISTTISFTNLLITRRTLAMPGIRHRRilMPF----ITIATFLALRMLa 220
Cdd:MTH00182 126 TGWTVYPPLSSIQAHSG-GAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNR--LPLfvwsILITAFLLLLSL- 201

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 300684753 221 titPVLGAAVIMMAFDRHWQTTFFEYAYGGDPILSQHLFWFFGHPEV 267
Cdd:MTH00182 202 ---PVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEV 245
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 146-267 1.47e-19

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 87.63  E-value: 1.47e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300684753 146 GWTFITPFSSNVKYTGvGSQDILILSVVFAGISTTISFTNLLITRRTLAMPGIRHRRilMPFITIATFLALRMLATITPV 225
Cdd:MTH00103 125 GWTVYPPLAGNLAHAG-ASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQ--TPLFVWSVLITAVLLLLSLPV 201

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 300684753 226 LGAAVIMMAFDRHWQTTFFEYAYGGDPILSQHLFWFFGHPEV 267
Cdd:MTH00103 202 LAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEV 243
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 146-267 1.74e-19

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 87.30  E-value: 1.74e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300684753 146 GWTFITPFSSNVKYTGvGSQDILILSVVFAGISTTISFTNLLITRRTLAMPGIRHRRilMPFITIATFLALRMLATITPV 225
Cdd:MTH00077 125 GWTVYPPLAGNLAHAG-ASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQ--TPLFVWSVLITAVLLLLSLPV 201

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 300684753 226 LGAAVIMMAFDRHWQTTFFEYAYGGDPILSQHLFWFFGHPEV 267
Cdd:MTH00077 202 LAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEV 243
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 146-267 1.31e-18

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 84.73  E-value: 1.31e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300684753 146 GWTFITPFSSNVKYTGvgSQDILILSVVFAGISTTISFTNLLITRRTLAMPGIRHRRilMPFITIATFLALRMLATITPV 225
Cdd:MTH00079 126 SWTVYPPLSTLGHPGS--SVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEH--MSLFVWTVFVTVFLLVLSLPV 201

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 300684753 226 LGAAVIMMAFDRHWQTTFFEYAYGGDPILSQHLFWFFGHPEV 267
Cdd:MTH00079 202 LAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEV 243
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 144-267 1.36e-14

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: 72.99  E-value: 1.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300684753  144 TAGWTFitpfssnvkYTGVGSQDILILSVVFAGISTTISFTNLLITRRTLAMPGIRHRRILMPFITIATFLalrMLATIT 223
Cdd:pfam00115 106 TTGWTE---------YPPLVGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTLRMPLFVWAILATAI---LILLAF 173

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 300684753  224 PVLGAAVIMMAFDRHWQttffeyAYGGDPILSQHLFWFFGHPEV 267
Cdd:pfam00115 174 PVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEV 211
 
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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