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Conserved domains on  [gi|1004168773|gb|AMP19122|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Comaster schlegelii]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Heme_Cu_Oxidase_I super family cl00275
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-203 8.61e-137

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: 392.31  E-value: 8.61e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004168773   1 SAGVESGVGTGWTIYPPLSSGIAHSGGSVDLAIFSLHIAGASSIIASINFITTIINMRSPGITFDRLSLFVWSIFITTFL 80
Cdd:MTH00153  113 SSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAIL 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004168773  81 LLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVVAHYSGKSEPFGYLGMV 160
Cdd:MTH00153  193 LLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMI 272

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1004168773 161 YAMVAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTG 203
Cdd:MTH00153  273 YAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTG 315
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-203 8.61e-137

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 392.31  E-value: 8.61e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004168773   1 SAGVESGVGTGWTIYPPLSSGIAHSGGSVDLAIFSLHIAGASSIIASINFITTIINMRSPGITFDRLSLFVWSIFITTFL 80
Cdd:MTH00153  113 SSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAIL 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004168773  81 LLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVVAHYSGKSEPFGYLGMV 160
Cdd:MTH00153  193 LLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMI 272

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1004168773 161 YAMVAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTG 203
Cdd:MTH00153  273 YAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTG 315
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-203 2.09e-132

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: 380.29  E-value: 2.09e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004168773   1 SAGVESGVGTGWTIYPPLSSGIAHSGGSVDLAIFSLHIAGASSIIASINFITTIINMRSPGITFDRLSLFVWSIFITTFL 80
Cdd:cd01663   106 SALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFL 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004168773  81 LLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVVAHYSGKSEPFGYLGMV 160
Cdd:cd01663   186 LLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMV 265

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1004168773 161 YAMVAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTG 203
Cdd:cd01663   266 YAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTG 308
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 4-203 5.24e-83

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: 254.46  E-value: 5.24e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004168773   4 VESGVGTGWTIYPPLSSGIAHSGGSVDLAIFSLHIAGASSIIASINFITTIINMRSPGITFDRLSLFVWSIFITTFLLLL 83
Cdd:TIGR02891 111 TGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILL 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004168773  84 SLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVVAHYSGKsEPFGYLGMVYAM 163
Cdd:TIGR02891 191 AFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARK-PIFGYRAMVYAT 269

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1004168773 164 VAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTG 203
Cdd:TIGR02891 270 VAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTG 309
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
7-203 3.46e-81

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 250.81  E-value: 3.46e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004168773   7 GVGTGWTIYPPLSSGIAHSGGSVDLAIFSLHIAGASSIIASINFITTIINMRSPGITFDRLSLFVWSIFITTFLLLLSLP 86
Cdd:COG0843   123 AADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFP 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004168773  87 VLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVVAHYSGKsEPFGYLGMVYAMVAI 166
Cdd:COG0843   203 VLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRK-PLFGYKAMVLATVAI 281

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1004168773 167 GILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTG 203
Cdd:COG0843   282 AFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTG 318
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 7-203 1.66e-50

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: 168.52  E-value: 1.66e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004168773   7 GVGTGWTIYPPLssgiahsgGSVDLAIFSLHIAGASSIIASINFITTIINMRSPGITFdRLSLFVWSIFITTFLLLLSLP 86
Cdd:pfam00115 104 GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFP 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004168773  87 VLAGAITMLLTDRNVNttffdpAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVVAHYSGKsEPFGYLGMVYAMVAI 166
Cdd:pfam00115 175 VLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGR-PLFGYKLSVLAFWLI 247

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1004168773 167 GILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTG 203
Cdd:pfam00115 248 AFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSG 284
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-203 8.61e-137

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 392.31  E-value: 8.61e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004168773   1 SAGVESGVGTGWTIYPPLSSGIAHSGGSVDLAIFSLHIAGASSIIASINFITTIINMRSPGITFDRLSLFVWSIFITTFL 80
Cdd:MTH00153  113 SSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAIL 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004168773  81 LLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVVAHYSGKSEPFGYLGMV 160
Cdd:MTH00153  193 LLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMI 272

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1004168773 161 YAMVAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTG 203
Cdd:MTH00153  273 YAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTG 315
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-203 2.09e-132

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: 380.29  E-value: 2.09e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004168773   1 SAGVESGVGTGWTIYPPLSSGIAHSGGSVDLAIFSLHIAGASSIIASINFITTIINMRSPGITFDRLSLFVWSIFITTFL 80
Cdd:cd01663   106 SALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFL 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004168773  81 LLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVVAHYSGKSEPFGYLGMV 160
Cdd:cd01663   186 LLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMV 265

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1004168773 161 YAMVAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTG 203
Cdd:cd01663   266 YAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTG 308
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-203 5.13e-125

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 362.46  E-value: 5.13e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004168773   1 SAGVESGVGTGWTIYPPLSSGIAHSGGSVDLAIFSLHIAGASSIIASINFITTIINMRSPGITFDRLSLFVWSIFITTFL 80
Cdd:MTH00167  115 SSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTTIL 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004168773  81 LLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVVAHYSGKSEPFGYLGMV 160
Cdd:MTH00167  195 LLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSGKKEPFGYMGMV 274

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1004168773 161 YAMVAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTG 203
Cdd:MTH00167  275 WAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTG 317
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-203 2.69e-124

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 360.68  E-value: 2.69e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004168773   1 SAGVESGVGTGWTIYPPLSSGIAHSGGSVDLAIFSLHIAGASSIIASINFITTIINMRSPGITFDRLSLFVWSIFITTFL 80
Cdd:MTH00037  115 SAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFITAFL 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004168773  81 LLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVVAHYSGKSEPFGYLGMV 160
Cdd:MTH00037  195 LLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMV 274

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1004168773 161 YAMVAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTG 203
Cdd:MTH00037  275 YAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTG 317
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-203 5.65e-124

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 359.68  E-value: 5.65e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004168773   1 SAGVESGVGTGWTIYPPLSSGIAHSGGSVDLAIFSLHIAGASSIIASINFITTIINMRSPGITFDRLSLFVWSIFITTFL 80
Cdd:MTH00223  112 SSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTAFL 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004168773  81 LLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVVAHYSGKSEPFGYLGMV 160
Cdd:MTH00223  192 LLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKEVFGTLGMI 271

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1004168773 161 YAMVAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTG 203
Cdd:MTH00223  272 YAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTG 314
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-203 4.26e-120

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 349.79  E-value: 4.26e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004168773   1 SAGVESGVGTGWTIYPPLSSGIAHSGGSVDLAIFSLHIAGASSIIASINFITTIINMRSPGITFDRLSLFVWSIFITTFL 80
Cdd:MTH00142  113 SAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKITAIL 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004168773  81 LLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVVAHYSGKSEPFGYLGMV 160
Cdd:MTH00142  193 LLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHYSGKKEVFGTLGMI 272

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1004168773 161 YAMVAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTG 203
Cdd:MTH00142  273 YAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTG 315
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-203 1.70e-119

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 348.24  E-value: 1.70e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004168773   1 SAGVESGVGTGWTIYPPLSSGIAHSGGSVDLAIFSLHIAGASSIIASINFITTIINMRSPGITFDRLSLFVWSIFITTFL 80
Cdd:MTH00116  115 SSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVL 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004168773  81 LLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVVAHYSGKSEPFGYLGMV 160
Cdd:MTH00116  195 LLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMV 274

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1004168773 161 YAMVAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTG 203
Cdd:MTH00116  275 WAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTG 317
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-203 2.34e-106

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 315.22  E-value: 2.34e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004168773   1 SAGVESGVGTGWTIYPPLSSGIAHSGGSVDLAIFSLHIAGASSIIASINFITTIINMRSPGITFDRLSLFVWSIFITTFL 80
Cdd:MTH00182  117 SAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFL 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004168773  81 LLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVVAHYSGKSEPFGYLGMV 160
Cdd:MTH00182  197 LLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFVAKKQIFGYLGMV 276

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1004168773 161 YAMVAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTG 203
Cdd:MTH00182  277 YAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTG 319
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-203 6.70e-106

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 313.76  E-value: 6.70e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004168773   1 SAGVESGVGTGWTIYPPLSSGIAHSGGSVDLAIFSLHIAGASSIIASINFITTIINMRSPGITFDRLSLFVWSIFITTFL 80
Cdd:MTH00007  112 SAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVITVVL 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004168773  81 LLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVVAHYSGKSEPFGYLGMV 160
Cdd:MTH00007  192 LLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGKLEPFGTLGMI 271

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1004168773 161 YAMVAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTG 203
Cdd:MTH00007  272 YAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTG 314
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-203 1.32e-104

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 310.32  E-value: 1.32e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004168773   1 SAGVESGVGTGWTIYPPLSSGIAHSGGSVDLAIFSLHIAGASSIIASINFITTIINMRSPGITFDRLSLFVWSIFITTFL 80
Cdd:MTH00183  115 SSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVL 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004168773  81 LLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVVAHYSGKSEPFGYLGMV 160
Cdd:MTH00183  195 LLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSGKKEPFGYMGMV 274

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1004168773 161 YAMVAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTG 203
Cdd:MTH00183  275 WAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTG 317
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-203 1.85e-104

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 310.22  E-value: 1.85e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004168773   1 SAGVESGVGTGWTIYPPLSSGIAHSGGSVDLAIFSLHIAGASSIIASINFITTIINMRSPGITFDRLSLFVWSIFITTFL 80
Cdd:MTH00184  117 SAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFL 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004168773  81 LLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVVAHYSGKSEPFGYLGMV 160
Cdd:MTH00184  197 LLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMV 276

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1004168773 161 YAMVAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTG 203
Cdd:MTH00184  277 YAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTG 319
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-203 2.53e-102

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 304.50  E-value: 2.53e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004168773   1 SAGVESGVGTGWTIYPPLSSGIAHSGGSVDLAIFSLHIAGASSIIASINFITTIINMRSPGITFDRLSLFVWSIFITTFL 80
Cdd:MTH00103  115 SSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVL 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004168773  81 LLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVVAHYSGKSEPFGYLGMV 160
Cdd:MTH00103  195 LLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMV 274

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1004168773 161 YAMVAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTG 203
Cdd:MTH00103  275 WAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTG 317
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-203 1.25e-100

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 300.32  E-value: 1.25e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004168773   1 SAGVESGVGTGWTIYPPLSSGIAHSGGSVDLAIFSLHIAGASSIIASINFITTIINMRSPGITFDRLSLFVWSIFITTFL 80
Cdd:MTH00077  115 SSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVL 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004168773  81 LLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVVAHYSGKSEPFGYLGMV 160
Cdd:MTH00077  195 LLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYYSAKKEPFGYMGMV 274

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1004168773 161 YAMVAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTG 203
Cdd:MTH00077  275 WAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTG 317
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 4-203 3.61e-100

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 298.90  E-value: 3.61e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004168773   4 VESGVGTGWTIYPPLSSgIAHSGGSVDLAIFSLHIAGASSIIASINFITTIINMRSPGITFDRLSLFVWSIFITTFLLLL 83
Cdd:MTH00079  119 VDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVL 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004168773  84 SLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVVAHYSGKSEPFGYLGMVYAM 163
Cdd:MTH00079  198 SLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAI 277

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1004168773 164 VAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTG 203
Cdd:MTH00079  278 LSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTG 317
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-203 3.61e-89

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 271.50  E-value: 3.61e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004168773   1 SAGVESGVGTGWTIYPPLSSGIAHSGGSVDLAIFSLHIAGASSIIASINFITTIINMRSPGITFDRLSLFVWSIFITTFL 80
Cdd:MTH00026  116 SSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAIL 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004168773  81 LLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVVAHYSGKSEPFGYLGMV 160
Cdd:MTH00026  196 LLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLFSYKKQIFGYLGMV 275

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1004168773 161 YAMVAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTG 203
Cdd:MTH00026  276 YAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTG 318
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-203 4.35e-87

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: 264.01  E-value: 4.35e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004168773   1 SAGVESGVGTGWTIYPPLSSGIAHSGGSVDLAIFSLHIAGASSIIASINFITTIINMRSPGITFDRLSLFVWSIFITTFL 80
Cdd:cd00919   103 SVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTAIL 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004168773  81 LLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVVAHYSGKsEPFGYLGMV 160
Cdd:cd00919   183 LLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFSGK-PLFGYKLMV 261

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1004168773 161 YAMVAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTG 203
Cdd:cd00919   262 YAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTG 304
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 4-203 5.24e-83

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: 254.46  E-value: 5.24e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004168773   4 VESGVGTGWTIYPPLSSGIAHSGGSVDLAIFSLHIAGASSIIASINFITTIINMRSPGITFDRLSLFVWSIFITTFLLLL 83
Cdd:TIGR02891 111 TGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILL 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004168773  84 SLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVVAHYSGKsEPFGYLGMVYAM 163
Cdd:TIGR02891 191 AFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARK-PIFGYRAMVYAT 269

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1004168773 164 VAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTG 203
Cdd:TIGR02891 270 VAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTG 309
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
7-203 3.46e-81

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 250.81  E-value: 3.46e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004168773   7 GVGTGWTIYPPLSSGIAHSGGSVDLAIFSLHIAGASSIIASINFITTIINMRSPGITFDRLSLFVWSIFITTFLLLLSLP 86
Cdd:COG0843   123 AADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFP 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004168773  87 VLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVVAHYSGKsEPFGYLGMVYAMVAI 166
Cdd:COG0843   203 VLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRK-PLFGYKAMVLATVAI 281

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1004168773 167 GILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTG 203
Cdd:COG0843   282 AFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTG 318
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 7-203 3.49e-80

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 247.67  E-value: 3.49e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004168773   7 GVGTGWTIYPPLSSGIAHSGGSVDLAIFSLHIAGASSIIASINFITTIINMRSPGITFdRLSLFVWSIFITTFLLLLSLP 86
Cdd:MTH00048  120 GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFS-RTSIILWSYLFTSILLLLSLP 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004168773  87 VLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVVAHYSGKSEPFGYLGMVYAMVAI 166
Cdd:MTH00048  199 VLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSI 278

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1004168773 167 GILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTG 203
Cdd:MTH00048  279 VCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTG 315
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 10-203 4.37e-70

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: 221.30  E-value: 4.37e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004168773  10 TGWTIYPPLSSGIAHSGGSVDLAIFSLHIAGASSIIASINFITTIINMRSPGITFDRLSLFVWSIFITTFLLLLSLPVLA 89
Cdd:cd01662   118 AGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLT 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004168773  90 GAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVVAHYSGKsEPFGYLGMVYAMVAIGIL 169
Cdd:cd01662   198 AALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFSRK-PLFGYRSMVYATVAIGFL 276

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1004168773 170 GFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTG 203
Cdd:cd01662   277 SFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTG 310
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 7-203 1.66e-50

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: 168.52  E-value: 1.66e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004168773   7 GVGTGWTIYPPLssgiahsgGSVDLAIFSLHIAGASSIIASINFITTIINMRSPGITFdRLSLFVWSIFITTFLLLLSLP 86
Cdd:pfam00115 104 GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFP 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004168773  87 VLAGAITMLLTDRNVNttffdpAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVVAHYSGKsEPFGYLGMVYAMVAI 166
Cdd:pfam00115 175 VLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGR-PLFGYKLSVLAFWLI 247

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1004168773 167 GILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTG 203
Cdd:pfam00115 248 AFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSG 284
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 1-203 6.49e-44

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 155.09  E-value: 6.49e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004168773   1 SAGVESGVGTGWTIYPPLSSGIAHSGGSVDLAIFSLHIAGASSIIASINFITTIINMRSPGITFDRLSLFVWSIFITTFL 80
Cdd:PRK15017  159 SLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVL 238

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004168773  81 LLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVVAHYSgKSEPFGYLGMV 160
Cdd:PRK15017  239 IIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFS-RKRLFGYTSLV 317

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1004168773 161 YAMVAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTG 203
Cdd:PRK15017  318 WATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTG 360
 
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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