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Conserved domains on  [gi|1246340381|gb|ATE51232|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Trimerotropis sp. C12C]

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 ...
 1-194 2.25e-141

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: 403.48  E-value: 2.25e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246340381   1 VDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSDSMTMDQTPLFVWSVAITALLLLL 80
Cdd:MTH00153  116 VESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLL 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246340381  81 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAM 160
Cdd:MTH00153  196 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAM 275

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1246340381 161 LSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMI 194
Cdd:MTH00153  276 LAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMI 309
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-194 2.25e-141

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 403.48  E-value: 2.25e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246340381   1 VDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSDSMTMDQTPLFVWSVAITALLLLL 80
Cdd:MTH00153  116 VESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLL 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246340381  81 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAM 160
Cdd:MTH00153  196 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAM 275

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1246340381 161 LSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMI 194
Cdd:MTH00153  276 LAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMI 309
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-194 2.65e-126

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: 364.50  E-value: 2.65e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246340381   1 VDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSDSMTMDQTPLFVWSVAITALLLLL 80
Cdd:cd01663   109 VEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLL 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246340381  81 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAM 160
Cdd:cd01663   189 SLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAM 268

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1246340381 161 LSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMI 194
Cdd:cd01663   269 LSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMI 302
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-194 7.12e-76

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: 235.58  E-value: 7.12e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246340381   1 VDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSDSMTMDQTPLFVWSVAITALLLLL 80
Cdd:TIGR02891 111 TGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILL 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246340381  81 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAM 160
Cdd:TIGR02891 191 AFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARK-PIFGYRAMVYAT 269

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1246340381 161 LSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMI 194
Cdd:TIGR02891 270 VAIGFLSFGVWAHHMFTTGMPPLALAFFSAATML 303
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-194 2.28e-74

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 232.71  E-value: 2.28e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246340381   1 VDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSDSMTMDQTPLFVWSVAITALLLLL 80
Cdd:COG0843   120 VGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILL 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246340381  81 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAM 160
Cdd:COG0843   200 AFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRK-PLFGYKAMVLAT 278

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1246340381 161 LSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMI 194
Cdd:COG0843   279 VAIAFLSFLVWAHHMFTPGISPLVKAFFSIATML 312
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 4-194 1.36e-47

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: 160.82  E-value: 1.36e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246340381   4 GAGTGWTVYPPLAGaiahggasVDLAIFSLHLAGISSILGAVNFITTAINMRSDSMTMdQTPLFVWSVAITALLLLLSLP 83
Cdd:pfam00115 104 GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFP 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246340381  84 VLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSI 163
Cdd:pfam00115 175 VLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGR-PLFGYKLSVLAFWLI 247

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1246340381 164 GLMGFIVWAHHMFTVGMDVDTRAYFTSATMI 194
Cdd:pfam00115 248 AFLGFLVWAHHLFTTGLPPWLQALFSVFSML 278
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-194 2.25e-141

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 403.48  E-value: 2.25e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246340381   1 VDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSDSMTMDQTPLFVWSVAITALLLLL 80
Cdd:MTH00153  116 VESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLL 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246340381  81 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAM 160
Cdd:MTH00153  196 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAM 275

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1246340381 161 LSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMI 194
Cdd:MTH00153  276 LAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMI 309
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-194 2.65e-126

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: 364.50  E-value: 2.65e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246340381   1 VDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSDSMTMDQTPLFVWSVAITALLLLL 80
Cdd:cd01663   109 VEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLL 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246340381  81 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAM 160
Cdd:cd01663   189 SLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAM 268

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1246340381 161 LSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMI 194
Cdd:cd01663   269 LSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMI 302
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-194 2.89e-118

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 344.65  E-value: 2.89e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246340381   1 VDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSDSMTMDQTPLFVWSVAITALLLLL 80
Cdd:MTH00223  115 VESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLL 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246340381  81 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAM 160
Cdd:MTH00223  195 SLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKEVFGTLGMIYAM 274

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1246340381 161 LSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMI 194
Cdd:MTH00223  275 LSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMI 308
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-194 4.76e-117

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 341.66  E-value: 4.76e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246340381   1 VDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSDSMTMDQTPLFVWSVAITALLLLL 80
Cdd:MTH00167  118 VEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTTILLLL 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246340381  81 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAM 160
Cdd:MTH00167  198 SLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAM 277

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1246340381 161 LSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMI 194
Cdd:MTH00167  278 MAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMI 311
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-194 3.27e-116

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 339.76  E-value: 3.27e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246340381   1 VDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSDSMTMDQTPLFVWSVAITALLLLL 80
Cdd:MTH00116  118 VEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLL 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246340381  81 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAM 160
Cdd:MTH00116  198 SLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAM 277

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1246340381 161 LSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMI 194
Cdd:MTH00116  278 LSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMI 311
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-194 3.42e-115

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 337.08  E-value: 3.42e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246340381   1 VDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSDSMTMDQTPLFVWSVAITALLLLL 80
Cdd:MTH00142  116 VESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKITAILLLL 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246340381  81 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAM 160
Cdd:MTH00142  196 SLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHYSGKKEVFGTLGMIYAM 275

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1246340381 161 LSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMI 194
Cdd:MTH00142  276 LSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMV 309
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-194 4.60e-104

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 308.37  E-value: 4.60e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246340381   1 VDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSDSMTMDQTPLFVWSVAITALLLLL 80
Cdd:MTH00007  115 VEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVITVVLLLL 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246340381  81 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAM 160
Cdd:MTH00007  195 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGKLEPFGTLGMIYAM 274

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1246340381 161 LSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMI 194
Cdd:MTH00007  275 LGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMI 308
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-194 4.87e-103

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 306.04  E-value: 4.87e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246340381   1 VDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSDSMTMDQTPLFVWSVAITALLLLL 80
Cdd:MTH00103  118 VEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLL 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246340381  81 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAM 160
Cdd:MTH00103  198 SLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAM 277

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1246340381 161 LSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMI 194
Cdd:MTH00103  278 MSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMI 311
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-194 1.27e-101

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 302.24  E-value: 1.27e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246340381   1 VDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSDSMTMDQTPLFVWSVAITALLLLL 80
Cdd:MTH00077  118 VEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLL 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246340381  81 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAM 160
Cdd:MTH00077  198 SLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAM 277

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1246340381 161 LSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMI 194
Cdd:MTH00077  278 MSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMI 311
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-194 1.37e-101

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 302.52  E-value: 1.37e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246340381   1 VDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSDSMTMDQTPLFVWSVAITALLLLL 80
Cdd:MTH00037  118 VESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLL 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246340381  81 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAM 160
Cdd:MTH00037  198 SLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAM 277

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1246340381 161 LSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMI 194
Cdd:MTH00037  278 IAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMI 311
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-194 1.63e-101

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 302.23  E-value: 1.63e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246340381   1 VDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSDSMTMDQTPLFVWSVAITALLLLL 80
Cdd:MTH00183  118 VEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLL 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246340381  81 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAM 160
Cdd:MTH00183  198 SLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAM 277

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1246340381 161 LSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMI 194
Cdd:MTH00183  278 MAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMI 311
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-194 2.21e-98

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 293.90  E-value: 2.21e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246340381   1 VDSGAGTGWTVYPPLAgAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSDSMTMDQTPLFVWSVAITALLLLL 80
Cdd:MTH00079  119 VDMGPGTSWTVYPPLS-TLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVL 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246340381  81 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAM 160
Cdd:MTH00079  198 SLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAI 277

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1246340381 161 LSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMI 194
Cdd:MTH00079  278 LSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMV 311
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-194 1.20e-96

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 289.80  E-value: 1.20e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246340381   1 VDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSDSMTMDQTPLFVWSVAITALLLLL 80
Cdd:MTH00182  120 VEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLL 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246340381  81 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAM 160
Cdd:MTH00182  200 SLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAM 279

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1246340381 161 LSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMI 194
Cdd:MTH00182  280 LSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMI 313
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-194 3.27e-96

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 288.65  E-value: 3.27e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246340381   1 VDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSDSMTMDQTPLFVWSVAITALLLLL 80
Cdd:MTH00184  120 VEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLL 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246340381  81 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAM 160
Cdd:MTH00184  200 SLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAM 279

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1246340381 161 LSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMI 194
Cdd:MTH00184  280 VSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMI 313
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-194 2.57e-86

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 263.80  E-value: 2.57e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246340381   1 VDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSDSMTMDQTPLFVWSVAITALLLLL 80
Cdd:MTH00026  119 VEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLL 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246340381  81 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAM 160
Cdd:MTH00026  199 SLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLFSYKKQIFGYLGMVYAM 278

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1246340381 161 LSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMI 194
Cdd:MTH00026  279 LAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMI 312
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-194 2.73e-82

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: 251.30  E-value: 2.73e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246340381   1 VDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSDSMTMDQTPLFVWSVAITALLLLL 80
Cdd:cd00919   106 VGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTAILLLL 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246340381  81 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAM 160
Cdd:cd00919   186 ALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFSGK-PLFGYKLMVYAF 264

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1246340381 161 LSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMI 194
Cdd:cd00919   265 LAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMI 298
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-194 7.12e-76

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: 235.58  E-value: 7.12e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246340381   1 VDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSDSMTMDQTPLFVWSVAITALLLLL 80
Cdd:TIGR02891 111 TGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILL 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246340381  81 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAM 160
Cdd:TIGR02891 191 AFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARK-PIFGYRAMVYAT 269

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1246340381 161 LSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMI 194
Cdd:TIGR02891 270 VAIGFLSFGVWAHHMFTTGMPPLALAFFSAATML 303
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 4-194 1.54e-74

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 232.65  E-value: 1.54e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246340381   4 GAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSDSMTMdQTPLFVWSVAITALLLLLSLP 83
Cdd:MTH00048  120 GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFS-RTSIILWSYLFTSILLLLSLP 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246340381  84 VLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSI 163
Cdd:MTH00048  199 VLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSI 278

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1246340381 164 GLMGFIVWAHHMFTVGMDVDTRAYFTSATMI 194
Cdd:MTH00048  279 VCLGSVVWAHHMFTVGLDVKTAVFFSSVTMI 309
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-194 2.28e-74

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 232.71  E-value: 2.28e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246340381   1 VDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSDSMTMDQTPLFVWSVAITALLLLL 80
Cdd:COG0843   120 VGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILL 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246340381  81 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAM 160
Cdd:COG0843   200 AFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRK-PLFGYKAMVLAT 278

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1246340381 161 LSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMI 194
Cdd:COG0843   279 VAIAFLSFLVWAHHMFTPGISPLVKAFFSIATML 312
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-194 4.01e-63

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: 202.81  E-value: 4.01e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246340381   1 VDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSDSMTMDQTPLFVWSVAITALLLLL 80
Cdd:cd01662   112 IGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSILILF 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246340381  81 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAM 160
Cdd:cd01662   192 AFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFSRK-PLFGYRSMVYAT 270

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1246340381 161 LSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMI 194
Cdd:cd01662   271 VAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMI 304
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 4-194 1.36e-47

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: 160.82  E-value: 1.36e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246340381   4 GAGTGWTVYPPLAGaiahggasVDLAIFSLHLAGISSILGAVNFITTAINMRSDSMTMdQTPLFVWSVAITALLLLLSLP 83
Cdd:pfam00115 104 GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFP 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246340381  84 VLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSI 163
Cdd:pfam00115 175 VLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGR-PLFGYKLSVLAFWLI 247

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1246340381 164 GLMGFIVWAHHMFTVGMDVDTRAYFTSATMI 194
Cdd:pfam00115 248 AFLGFLVWAHHLFTTGLPPWLQALFSVFSML 278
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 5-194 5.75e-40

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 143.54  E-value: 5.75e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246340381   5 AGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSDSMTMDQTPLFVWSVAITALLLLLSLPV 84
Cdd:PRK15017  166 AQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPI 245

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246340381  85 LAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIG 164
Cdd:PRK15017  246 LTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFSRK-RLFGYTSLVWATVCIT 324

                         170       180       190
                  ....*....|....*....|....*....|
gi 1246340381 165 LMGFIVWAHHMFTVGMDVDTRAYFTSATMI 194
Cdd:PRK15017  325 VLSFIVWLHHFFTMGAGANVNAFFGITTMI 354
 
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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