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Conserved domains on  [gi|62461922|gb|AAX83094|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Sarcophaga formosensis]

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 ...
 11-183 3.73e-123

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: 356.87  E-value: 3.73e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62461922   11 VSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSSGITFDRMPLFVWSVVITAL 90
Cdd:MTH00153 112 SSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAI 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62461922   91 LLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGSLGM 170
Cdd:MTH00153 192 LLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGM 271

                        170
                 ....*....|...
gi 62461922  171 IYAMLAIGLLGFI 183
Cdd:MTH00153 272 IYAMLAIGLLGFI 284
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 11-183 3.73e-123

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 356.87  E-value: 3.73e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62461922   11 VSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSSGITFDRMPLFVWSVVITAL 90
Cdd:MTH00153 112 SSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAI 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62461922   91 LLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGSLGM 170
Cdd:MTH00153 192 LLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGM 271

                        170
                 ....*....|...
gi 62461922  171 IYAMLAIGLLGFI 183
Cdd:MTH00153 272 IYAMLAIGLLGFI 284
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 12-183 2.62e-108

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: 318.27  E-value: 2.62e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62461922  12 SSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSSGITFDRMPLFVWSVVITALL 91
Cdd:cd01663 106 SALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFL 185

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62461922  92 LLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGSLGMI 171
Cdd:cd01663 186 LLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMV 265

                       170
                ....*....|..
gi 62461922 172 YAMLAIGLLGFI 183
Cdd:cd01663 266 YAMLSIGILGFI 277
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 18-183 1.13e-65

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: 209.00  E-value: 1.13e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62461922    18 GAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSSGITFDRMPLFVWSVVITALLLLLSLP 97
Cdd:TIGR02891 114 APDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFP 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62461922    98 VLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKeTFGSLGMIYAMLAI 177
Cdd:TIGR02891 194 VLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKP-IFGYRAMVYATVAI 272


                  ....*.
gi 62461922   178 GLLGFI 183
Cdd:TIGR02891 273 GFLSFG 278
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
18-183 2.46e-65

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 208.83  E-value: 2.46e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62461922  18 GAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSSGITFDRMPLFVWSVVITALLLLLSLP 97
Cdd:COG0843 123 AADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFP 202

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62461922  98 VLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKeTFGSLGMIYAMLAI 177
Cdd:COG0843 203 VLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAI 281


                ....*.
gi 62461922 178 GLLGFI 183
Cdd:COG0843 282 AFLSFL 287
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 17-184 4.69e-38

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: 135.01  E-value: 4.69e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62461922    17 NGAGTGWTVYPPLssniahggASVDLAIFSLHLAGISSILGAVNFITTVINMRSSGITFdRMPLFVWSVVITALLLLLSL 96
Cdd:pfam00115 103 GGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAF 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62461922    97 PVLAGAITMLLTDRNINtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKeTFGSLGMIYAMLA 176
Cdd:pfam00115 174 PVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWL 246


                  ....*...
gi 62461922   177 IGLLGFIA 184
Cdd:pfam00115 247 IAFLGFLV 254
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 11-183 3.73e-123

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 356.87  E-value: 3.73e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62461922   11 VSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSSGITFDRMPLFVWSVVITAL 90
Cdd:MTH00153 112 SSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAI 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62461922   91 LLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGSLGM 170
Cdd:MTH00153 192 LLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGM 271

                        170
                 ....*....|...
gi 62461922  171 IYAMLAIGLLGFI 183
Cdd:MTH00153 272 IYAMLAIGLLGFI 284
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 12-183 2.62e-108

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: 318.27  E-value: 2.62e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62461922  12 SSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSSGITFDRMPLFVWSVVITALL 91
Cdd:cd01663 106 SALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFL 185

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62461922  92 LLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGSLGMI 171
Cdd:cd01663 186 LLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMV 265

                       170
                ....*....|..
gi 62461922 172 YAMLAIGLLGFI 183
Cdd:cd01663 266 YAMLSIGILGFI 277
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 11-183 1.88e-101

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 301.51  E-value: 1.88e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62461922   11 VSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSSGITFDRMPLFVWSVVITAL 90
Cdd:MTH00223 111 SSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTAF 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62461922   91 LLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGSLGM 170
Cdd:MTH00223 191 LLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKEVFGTLGM 270

                        170
                 ....*....|...
gi 62461922  171 IYAMLAIGLLGFI 183
Cdd:MTH00223 271 IYAMLSIGVLGFI 283
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 11-183 1.43e-99

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 296.59  E-value: 1.43e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62461922   11 VSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSSGITFDRMPLFVWSVVITAL 90
Cdd:MTH00167 114 ASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTTI 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62461922   91 LLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGSLGM 170
Cdd:MTH00167 194 LLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSGKKEPFGYMGM 273

                        170
                 ....*....|...
gi 62461922  171 IYAMLAIGLLGFI 183
Cdd:MTH00167 274 VWAMMAIGLLGFI 286
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 12-183 1.88e-99

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 296.25  E-value: 1.88e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62461922   12 SSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSSGITFDRMPLFVWSVVITALL 91
Cdd:MTH00142 113 SAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKITAIL 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62461922   92 LLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGSLGMI 171
Cdd:MTH00142 193 LLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHYSGKKEVFGTLGMI 272

                        170
                 ....*....|..
gi 62461922  172 YAMLAIGLLGFI 183
Cdd:MTH00142 273 YAMLSIGLLGFI 284
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 12-183 8.55e-97

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 289.68  E-value: 8.55e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62461922   12 SSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSSGITFDRMPLFVWSVVITALL 91
Cdd:MTH00116 115 SSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVL 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62461922   92 LLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGSLGMI 171
Cdd:MTH00116 195 LLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMV 274

                        170
                 ....*....|..
gi 62461922  172 YAMLAIGLLGFI 183
Cdd:MTH00116 275 WAMLSIGFLGFI 286
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 12-183 1.46e-89

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 271.00  E-value: 1.46e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62461922   12 SSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSSGITFDRMPLFVWSVVITALL 91
Cdd:MTH00007 112 SAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVITVVL 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62461922   92 LLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGSLGMI 171
Cdd:MTH00007 192 LLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGKLEPFGTLGMI 271

                        170
                 ....*....|..
gi 62461922  172 YAMLAIGLLGFI 183
Cdd:MTH00007 272 YAMLGIGVLGFI 283
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 12-183 1.05e-87

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 266.31  E-value: 1.05e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62461922   12 SSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSSGITFDRMPLFVWSVVITALL 91
Cdd:MTH00037 115 SAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFITAFL 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62461922   92 LLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGSLGMI 171
Cdd:MTH00037 195 LLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMV 274

                        170
                 ....*....|..
gi 62461922  172 YAMLAIGLLGFI 183
Cdd:MTH00037 275 YAMIAIGILGFL 286
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 12-183 4.31e-85

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 259.47  E-value: 4.31e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62461922   12 SSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSSGITFDRMPLFVWSVVITALL 91
Cdd:MTH00183 115 SSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVL 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62461922   92 LLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGSLGMI 171
Cdd:MTH00183 195 LLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSGKKEPFGYMGMV 274

                        170
                 ....*....|..
gi 62461922  172 YAMLAIGLLGFI 183
Cdd:MTH00183 275 WAMMAIGLLGFI 286
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 11-183 1.18e-84

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 258.27  E-value: 1.18e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62461922   11 VSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSSGITFDRMPLFVWSVVITAL 90
Cdd:MTH00103 114 ASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAV 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62461922   91 LLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGSLGM 170
Cdd:MTH00103 194 LLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGM 273

                        170
                 ....*....|...
gi 62461922  171 IYAMLAIGLLGFI 183
Cdd:MTH00103 274 VWAMMSIGFLGFI 286
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 12-183 3.77e-84

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 257.18  E-value: 3.77e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62461922   12 SSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSSGITFDRMPLFVWSVVITALL 91
Cdd:MTH00077 115 SSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVL 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62461922   92 LLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGSLGMI 171
Cdd:MTH00077 195 LLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYYSAKKEPFGYMGMV 274

                        170
                 ....*....|..
gi 62461922  172 YAMLAIGLLGFI 183
Cdd:MTH00077 275 WAMMSIGLLGFI 286
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 12-183 1.43e-83

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 255.90  E-value: 1.43e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62461922   12 SSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSSGITFDRMPLFVWSVVITALL 91
Cdd:MTH00182 117 SAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFL 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62461922   92 LLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGSLGMI 171
Cdd:MTH00182 197 LLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFVAKKQIFGYLGMV 276

                        170
                 ....*....|..
gi 62461922  172 YAMLAIGLLGFI 183
Cdd:MTH00182 277 YAMLSIGILGFI 288
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 12-183 2.12e-82

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 252.83  E-value: 2.12e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62461922   12 SSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSSGITFDRMPLFVWSVVITALL 91
Cdd:MTH00184 117 SAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFL 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62461922   92 LLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGSLGMI 171
Cdd:MTH00184 197 LLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMV 276

                        170
                 ....*....|..
gi 62461922  172 YAMLAIGLLGFI 183
Cdd:MTH00184 277 YAMVSIGILGFI 288
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 12-181 8.76e-81

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 248.44  E-value: 8.76e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62461922   12 SSMVENGAGTGWTVYPPLSSnIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSSGITFDRMPLFVWSVVITALL 91
Cdd:MTH00079 116 SCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFL 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62461922   92 LLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGSLGMI 171
Cdd:MTH00079 195 LVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTGKKEVFGSLGMV 274

                        170
                 ....*....|
gi 62461922  172 YAMLAIGLLG 181
Cdd:MTH00079 275 YAILSIGLIG 284
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 12-183 3.86e-75

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 234.52  E-value: 3.86e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62461922   12 SSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSSGITFDRMPLFVWSVVITALL 91
Cdd:MTH00026 116 SSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAIL 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62461922   92 LLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGSLGMI 171
Cdd:MTH00026 196 LLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLFSYKKQIFGYLGMV 275

                        170
                 ....*....|..
gi 62461922  172 YAMLAIGLLGFI 183
Cdd:MTH00026 276 YAMLAIGVLGFI 287
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 11-184 2.28e-70

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: 220.09  E-value: 2.28e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62461922  11 VSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSSGITFDRMPLFVWSVVITAL 90
Cdd:cd00919 102 SSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTAI 181

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62461922  91 LLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKeTFGSLGM 170
Cdd:cd00919 182 LLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFSGKP-LFGYKLM 260

                       170
                ....*....|....
gi 62461922 171 IYAMLAIGLLGFIA 184
Cdd:cd00919 261 VYAFLAIGFLSFLV 274
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 18-183 1.13e-65

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: 209.00  E-value: 1.13e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62461922    18 GAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSSGITFDRMPLFVWSVVITALLLLLSLP 97
Cdd:TIGR02891 114 APDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFP 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62461922    98 VLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKeTFGSLGMIYAMLAI 177
Cdd:TIGR02891 194 VLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKP-IFGYRAMVYATVAI 272


                  ....*.
gi 62461922   178 GLLGFI 183
Cdd:TIGR02891 273 GFLSFG 278
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
18-183 2.46e-65

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 208.83  E-value: 2.46e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62461922  18 GAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSSGITFDRMPLFVWSVVITALLLLLSLP 97
Cdd:COG0843 123 AADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFP 202

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62461922  98 VLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKeTFGSLGMIYAMLAI 177
Cdd:COG0843 203 VLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAI 281


                ....*.
gi 62461922 178 GLLGFI 183
Cdd:COG0843 282 AFLSFL 287
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 18-183 3.42e-59

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 192.59  E-value: 3.42e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62461922   18 GAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSSGITFdRMPLFVWSVVITALLLLLSLP 97
Cdd:MTH00048 120 GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFS-RTSIILWSYLFTSILLLLSLP 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62461922   98 VLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGSLGMIYAMLAI 177
Cdd:MTH00048 199 VLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSI 278


                 ....*.
gi 62461922  178 GLLGFI 183
Cdd:MTH00048 279 VCLGSV 284
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 11-183 1.86e-54

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: 179.70  E-value: 1.86e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62461922  11 VSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSSGITFDRMPLFVWSVVITAL 90
Cdd:cd01662 108 ASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSI 187

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62461922  91 LLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKeTFGSLGM 170
Cdd:cd01662 188 LILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFSRKP-LFGYRSM 266

                       170
                ....*....|...
gi 62461922 171 IYAMLAIGLLGFI 183
Cdd:cd01662 267 VYATVAIGFLSFG 279
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 17-184 4.69e-38

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: 135.01  E-value: 4.69e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62461922    17 NGAGTGWTVYPPLssniahggASVDLAIFSLHLAGISSILGAVNFITTVINMRSSGITFdRMPLFVWSVVITALLLLLSL 96
Cdd:pfam00115 103 GGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAF 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62461922    97 PVLAGAITMLLTDRNINtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKeTFGSLGMIYAMLA 176
Cdd:pfam00115 174 PVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWL 246


                  ....*...
gi 62461922   177 IGLLGFIA 184
Cdd:pfam00115 247 IAFLGFLV 254
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 19-183 1.02e-32

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 122.74  E-value: 1.02e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62461922   19 AGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSSGITFDRMPLFVWSVVITALLLLLSLPV 98
Cdd:PRK15017 166 AQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPI 245

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62461922   99 LAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESgKKETFGSLGMIYAMLAIG 178
Cdd:PRK15017 246 LTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCIT 324


                 ....*
gi 62461922  179 LLGFI 183
Cdd:PRK15017 325 VLSFI 329
 
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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