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Conserved domains on  [gi|963775086|gb|ALT10224|]
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cytochrome c oxidase subunit I, partial (mitochondrion) [Filarioidea sp. 961MG]

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 ...
 1-215 4.78e-101

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 MTH00079:

Pssm-ID: 469701  Cd Length: 508  Bit Score: 301.60  E-value: 4.78e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775086   1 WVLPLMLTAPEMAFPRLNALSFWFTLVALFMVYHSFFVGMGAGGSWTFYPPLNTEGLPELSTDTMILSLHTVGFGSLLGA 80
Cdd:MTH00079  82 WMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLSTLGHPGSSVDLAIFSLHCAGISSILGG 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775086  81 INFMATVQNMRATSVTLDQMSMFVWTLYLTSLLLLLSVPVLAGALLFLLMDRNFNCSFYDTKTGGNPLLYQHLFWFFGHP 160
Cdd:MTH00079 162 INFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHP 241

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 963775086 161 EVYIIILPAFGIISESVLFLTDKERLFGQTSMTFASIWIAVLGLSVWGHHMYTAG 215
Cdd:MTH00079 242 EVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVG 296
 
Name Accession Description Interval E-value
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-215 4.78e-101

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 301.60  E-value: 4.78e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775086   1 WVLPLMLTAPEMAFPRLNALSFWFTLVALFMVYHSFFVGMGAGGSWTFYPPLNTEGLPELSTDTMILSLHTVGFGSLLGA 80
Cdd:MTH00079  82 WMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLSTLGHPGSSVDLAIFSLHCAGISSILGG 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775086  81 INFMATVQNMRATSVTLDQMSMFVWTLYLTSLLLLLSVPVLAGALLFLLMDRNFNCSFYDTKTGGNPLLYQHLFWFFGHP 160
Cdd:MTH00079 162 INFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHP 241

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 963775086 161 EVYIIILPAFGIISESVLFLTDKERLFGQTSMTFASIWIAVLGLSVWGHHMYTAG 215
Cdd:MTH00079 242 EVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVG 296
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-215 6.55e-91

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: 275.13  E-value: 6.55e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775086   1 WVLPLMLTAPEMAFPRLNALSFWFTLVALFMVYHSFFVGMGAGGSWTFYPPL-NTEGLPELSTDTMILSLHTVGFGSLLG 79
Cdd:cd01663   72 WLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLsSILAHSGPSVDLAIFSLHLAGISSILG 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775086  80 AINFMATVQNMRATSVTLDQMSMFVWTLYLTSLLLLLSVPVLAGALLFLLMDRNFNCSFYDTKTGGNPLLYQHLFWFFGH 159
Cdd:cd01663  152 AINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGH 231

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 963775086 160 PEVYIIILPAFGIISESVLFLTDKERLFGQTSMTFASIWIAVLGLSVWGHHMYTAG 215
Cdd:cd01663  232 PEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVG 287
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-215 1.02e-69

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 221.54  E-value: 1.02e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775086   1 WVLPLMLTAPEMAFPRLNALSFWFTLVALFMVYHSFFVGMGAGGSWTFYPPLNT-EGLPELSTDTMILSLHTVGFGSLLG 79
Cdd:COG0843   83 YLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGlEASPGVGVDLWLLGLALFGVGSILG 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775086  80 AINFMATVQNMRATSVTLDQMSMFVWTLYLTSLLLLLSVPVLAGALLFLLMDRNFNCSFYDTKTGGNPLLYQHLFWFFGH 159
Cdd:COG0843  163 GVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGH 242

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 963775086 160 PEVYIIILPAFGIISEsVLFLTDKERLFGQTSMTFASIWIAVLGLSVWGHHMYTAG 215
Cdd:COG0843  243 PEVYILILPAFGIVSE-IIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPG 297
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-215 7.64e-68

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: 215.94  E-value: 7.64e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775086    1 WVLPLMLTAPEMAFPRLNALSFWFTLVALFMVYHSFFVGMGAGGSWTFYPPL-NTEGLPELSTDTMILSLHTVGFGSLLG 79
Cdd:TIGR02891  74 YLLPLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLsSTSGSPGVGVDLWLLGLHLLGISSILG 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775086   80 AINFMATVQNMRATSVTLDQMSMFVWTLYLTSLLLLLSVPVLAGALLFLLMDRNFNCSFYDTKTGGNPLLYQHLFWFFGH 159
Cdd:TIGR02891 154 AVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGH 233

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 963775086  160 PEVYIIILPAFGIISESVLFLTDKeRLFGQTSMTFASIWIAVLGLSVWGHHMYTAG 215
Cdd:TIGR02891 234 PEVYIIFLPAFGIISEILPTFARK-PIFGYRAMVYATVAIGFLSFGVWAHHMFTTG 288
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-215 6.81e-42

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: 146.56  E-value: 6.81e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775086    1 WVLPLMLTAPEMAFPRLNALSFWFTLVALFMVYHSFfvgMGAGGSWTFYPPLnteglpeLSTDTMILSLHTVGFGSLLGA 80
Cdd:pfam00115  67 YLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPL-------VGVDLWYIGLLLAGVSSLLGA 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775086   81 INFMATVQNMRATSVTLdQMSMFVWTLYLTSLLLLLSVPVLAGALLFLLMDRNFNcsfydtKTGGNPLLYQHLFWFFGHP 160
Cdd:pfam00115 137 INFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHP 209

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 963775086  161 EVYIIILPAFGIISESVLFLTDKeRLFGQTSMTFASIWIAVLGLSVWGHHMYTAG 215
Cdd:pfam00115 210 EVYILILPAFGIIYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTG 263
 
Name Accession Description Interval E-value
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-215 4.78e-101

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 301.60  E-value: 4.78e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775086   1 WVLPLMLTAPEMAFPRLNALSFWFTLVALFMVYHSFFVGMGAGGSWTFYPPLNTEGLPELSTDTMILSLHTVGFGSLLGA 80
Cdd:MTH00079  82 WMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLSTLGHPGSSVDLAIFSLHCAGISSILGG 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775086  81 INFMATVQNMRATSVTLDQMSMFVWTLYLTSLLLLLSVPVLAGALLFLLMDRNFNCSFYDTKTGGNPLLYQHLFWFFGHP 160
Cdd:MTH00079 162 INFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHP 241

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 963775086 161 EVYIIILPAFGIISESVLFLTDKERLFGQTSMTFASIWIAVLGLSVWGHHMYTAG 215
Cdd:MTH00079 242 EVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVG 296
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-215 6.55e-91

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: 275.13  E-value: 6.55e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775086   1 WVLPLMLTAPEMAFPRLNALSFWFTLVALFMVYHSFFVGMGAGGSWTFYPPL-NTEGLPELSTDTMILSLHTVGFGSLLG 79
Cdd:cd01663   72 WLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLsSILAHSGPSVDLAIFSLHLAGISSILG 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775086  80 AINFMATVQNMRATSVTLDQMSMFVWTLYLTSLLLLLSVPVLAGALLFLLMDRNFNCSFYDTKTGGNPLLYQHLFWFFGH 159
Cdd:cd01663  152 AINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGH 231

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 963775086 160 PEVYIIILPAFGIISESVLFLTDKERLFGQTSMTFASIWIAVLGLSVWGHHMYTAG 215
Cdd:cd01663  232 PEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVG 287
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-215 6.89e-75

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 234.38  E-value: 6.89e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775086   1 WVLPLMLTAPEMAFPRLNALSFWFTLVALFMVYHSFFVGMGAGGSWTFYPPL-NTEGLPELSTDTMILSLHTVGFGSLLG 79
Cdd:MTH00153  79 WLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLsSNIAHSGASVDLAIFSLHLAGISSILG 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775086  80 AINFMATVQNMRATSVTLDQMSMFVWTLYLTSLLLLLSVPVLAGALLFLLMDRNFNCSFYDTKTGGNPLLYQHLFWFFGH 159
Cdd:MTH00153 159 AINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 238

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 963775086 160 PEVYIIILPAFGIISESVLFLTDKERLFGQTSMTFASIWIAVLGLSVWGHHMYTAG 215
Cdd:MTH00153 239 PEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVG 294
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-215 2.53e-74

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 232.95  E-value: 2.53e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775086   1 WVLPLMLTAPEMAFPRLNALSFWFTLVALFMVYHSFFVGMGAGGSWTFYPPLNTE-GLPELSTDTMILSLHTVGFGSLLG 79
Cdd:MTH00223  78 WLVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNlAHAGPSVDLAIFSLHLAGVSSILG 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775086  80 AINFMATVQNMRATSVTLDQMSMFVWTLYLTSLLLLLSVPVLAGALLFLLMDRNFNCSFYDTKTGGNPLLYQHLFWFFGH 159
Cdd:MTH00223 158 AINFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGH 237

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 963775086 160 PEVYIIILPAFGIISESVLFLTDKERLFGQTSMTFASIWIAVLGLSVWGHHMYTAG 215
Cdd:MTH00223 238 PEVYILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVG 293
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-215 3.50e-70

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 222.24  E-value: 3.50e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775086   1 WVLPLMLTAPEMAFPRLNALSFWFTLVALFMVYHSFFVGMGAGGSWTFYPPL-NTEGLPELSTDTMILSLHTVGFGSLLG 79
Cdd:MTH00167  81 WLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLaGNLAHAGASVDLAIFSLHLAGVSSILG 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775086  80 AINFMATVQNMRATSVTLDQMSMFVWTLYLTSLLLLLSVPVLAGALLFLLMDRNFNCSFYDTKTGGNPLLYQHLFWFFGH 159
Cdd:MTH00167 161 SINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGH 240

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 963775086 160 PEVYIIILPAFGIISESVLFLTDKERLFGQTSMTFASIWIAVLGLSVWGHHMYTAG 215
Cdd:MTH00167 241 PEVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVG 296
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-215 1.02e-69

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 221.54  E-value: 1.02e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775086   1 WVLPLMLTAPEMAFPRLNALSFWFTLVALFMVYHSFFVGMGAGGSWTFYPPLNT-EGLPELSTDTMILSLHTVGFGSLLG 79
Cdd:COG0843   83 YLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGlEASPGVGVDLWLLGLALFGVGSILG 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775086  80 AINFMATVQNMRATSVTLDQMSMFVWTLYLTSLLLLLSVPVLAGALLFLLMDRNFNCSFYDTKTGGNPLLYQHLFWFFGH 159
Cdd:COG0843  163 GVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGH 242

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 963775086 160 PEVYIIILPAFGIISEsVLFLTDKERLFGQTSMTFASIWIAVLGLSVWGHHMYTAG 215
Cdd:COG0843  243 PEVYILILPAFGIVSE-IIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPG 297
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-215 7.64e-68

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: 215.94  E-value: 7.64e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775086    1 WVLPLMLTAPEMAFPRLNALSFWFTLVALFMVYHSFFVGMGAGGSWTFYPPL-NTEGLPELSTDTMILSLHTVGFGSLLG 79
Cdd:TIGR02891  74 YLLPLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLsSTSGSPGVGVDLWLLGLHLLGISSILG 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775086   80 AINFMATVQNMRATSVTLDQMSMFVWTLYLTSLLLLLSVPVLAGALLFLLMDRNFNCSFYDTKTGGNPLLYQHLFWFFGH 159
Cdd:TIGR02891 154 AVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGH 233

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 963775086  160 PEVYIIILPAFGIISESVLFLTDKeRLFGQTSMTFASIWIAVLGLSVWGHHMYTAG 215
Cdd:TIGR02891 234 PEVYIIFLPAFGIISEILPTFARK-PIFGYRAMVYATVAIGFLSFGVWAHHMFTTG 288
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-215 3.75e-67

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 214.59  E-value: 3.75e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775086   1 WVLPLMLTAPEMAFPRLNALSFWFTLVALFMVYHSFFVGMGAGGSWTFYPPLNTEGLPE-LSTDTMILSLHTVGFGSLLG 79
Cdd:MTH00142  79 WLVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSgGSVDLAIFSLHLAGVSSILG 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775086  80 AINFMATVQNMRATSVTLDQMSMFVWTLYLTSLLLLLSVPVLAGALLFLLMDRNFNCSFYDTKTGGNPLLYQHLFWFFGH 159
Cdd:MTH00142 159 AINFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGH 238

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 963775086 160 PEVYIIILPAFGIISESVLFLTDKERLFGQTSMTFASIWIAVLGLSVWGHHMYTAG 215
Cdd:MTH00142 239 PEVYILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVG 294
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-215 1.20e-64

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 208.02  E-value: 1.20e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775086   1 WVLPLMLTAPEMAFPRLNALSFWFTLVALFMVYHSFFVGMGAGGSWTFYPPLN---TEGLPelSTDTMILSLHTVGFGSL 77
Cdd:MTH00116  81 WLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAgnlAHAGA--SVDLAIFSLHLAGVSSI 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775086  78 LGAINFMATVQNMRATSVTLDQMSMFVWTLYLTSLLLLLSVPVLAGALLFLLMDRNFNCSFYDTKTGGNPLLYQHLFWFF 157
Cdd:MTH00116 159 LGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFF 238

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 963775086 158 GHPEVYIIILPAFGIISESVLFLTDKERLFGQTSMTFASIWIAVLGLSVWGHHMYTAG 215
Cdd:MTH00116 239 GHPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVG 296
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-215 4.09e-64

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: 206.28  E-value: 4.09e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775086   1 WVLPLMLTAPEMAFPRLNALSFWFTLVALFMVYHSFFVGMGAGGSWTFYPPLNT-EGLPELSTDTMILSLHTVGFGSLLG 79
Cdd:cd01662   75 YLVPLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGlEYSPGVGVDYWILGLQFSGIGTLLG 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775086  80 AINFMATVQNMRATSVTLDQMSMFVWTLYLTSLLLLLSVPVLAGALLFLLMDRNFNCSFYDTKTGGNPLLYQHLFWFFGH 159
Cdd:cd01662  155 AINFIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGH 234

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 963775086 160 PEVYIIILPAFGIISESVLFLTDKeRLFGQTSMTFASIWIAVLGLSVWGHHMYTAG 215
Cdd:cd01662  235 PEVYILILPAFGIFSEIVPTFSRK-PLFGYRSMVYATVAIGFLSFGVWVHHMFTTG 289
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-215 1.44e-62

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: 201.22  E-value: 1.44e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775086   1 WVLPLMLTAPEMAFPRLNALSFWFTLVALFMVYHSFFVGMGAGGSWTFYPPLNTEG-LPELSTDTMILSLHTVGFGSLLG 79
Cdd:cd00919   69 NLLPPLIGARDLAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSySSGVGVDLAILGLHLAGVSSILG 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775086  80 AINFMATVQNMRATSVTLDQMSMFVWTLYLTSLLLLLSVPVLAGALLFLLMDRNFNCSFYDTKTGGNPLLYQHLFWFFGH 159
Cdd:cd00919  149 AINFITTILNMRAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGH 228

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 963775086 160 PEVYIIILPAFGIISESVLFLTDKeRLFGQTSMTFASIWIAVLGLSVWGHHMYTAG 215
Cdd:cd00919  229 PEVYILILPAFGAISEIIPTFSGK-PLFGYKLMVYAFLAIGFLSFLVWAHHMFTVG 283
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-215 1.46e-61

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 200.43  E-value: 1.46e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775086   1 WVLPLMLTAPEMAFPRLNALSFWFTLVALFMVYHSFFVGMGAGGSWTFYPPL-NTEGLPELSTDTMILSLHTVGFGSLLG 79
Cdd:MTH00182  83 WLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLsSIQAHSGGAVDMAIFSLHLAGVSSILG 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775086  80 AINFMATVQNMRATSVTLDQMSMFVWTLYLTSLLLLLSVPVLAGALLFLLMDRNFNCSFYDTKTGGNPLLYQHLFWFFGH 159
Cdd:MTH00182 163 AINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGH 242

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 963775086 160 PEVYIIILPAFGIISESVLFLTDKERLFGQTSMTFASIWIAVLGLSVWGHHMYTAG 215
Cdd:MTH00182 243 PEVYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVG 298
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-215 1.53e-61

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 200.05  E-value: 1.53e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775086   1 WVLPLMLTAPEMAFPRLNALSFWFTLVALFMVYHSFFVGMGAGGSWTFYPPLNT-EGLPELSTDTMILSLHTVGFGSLLG 79
Cdd:MTH00184  83 WFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSiQAHSGGSVDMAIFSLHLAGISSILG 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775086  80 AINFMATVQNMRATSVTLDQMSMFVWTLYLTSLLLLLSVPVLAGALLFLLMDRNFNCSFYDTKTGGNPLLYQHLFWFFGH 159
Cdd:MTH00184 163 AMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGH 242

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 963775086 160 PEVYIIILPAFGIISESVLFLTDKERLFGQTSMTFASIWIAVLGLSVWGHHMYTAG 215
Cdd:MTH00184 243 PEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVG 298
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-215 8.67e-61

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 197.82  E-value: 8.67e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775086   1 WVLPLMLTAPEMAFPRLNALSFWFTLVALFMVYHSFFVGMGAGGSWTFYPPLNTE-GLPELSTDTMILSLHTVGFGSLLG 79
Cdd:MTH00007  78 WLVPLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNlAHAGPSVDLAIFSLHLAGVSSILG 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775086  80 AINFMATVQNMRATSVTLDQMSMFVWTLYLTSLLLLLSVPVLAGALLFLLMDRNFNCSFYDTKTGGNPLLYQHLFWFFGH 159
Cdd:MTH00007 158 AINFITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 237

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 963775086 160 PEVYIIILPAFGIISESVLFLTDKERLFGQTSMTFASIWIAVLGLSVWGHHMYTAG 215
Cdd:MTH00007 238 PEVYILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVG 293
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-215 6.25e-58

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 190.99  E-value: 6.25e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775086   1 WVLPLMLTAPEMAFPRLNALSFWFTLVALFMVYHSFFVGMGAGGSWTFYPPL-NTEGLPELSTDTMILSLHTVGFGSLLG 79
Cdd:MTH00026  82 WFVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLaSIQAHSGGSVDMAIFSLHLAGLSSILG 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775086  80 AINFMATVQNMRATSVTLDQMSMFVWTLYLTSLLLLLSVPVLAGALLFLLMDRNFNCSFYDTKTGGNPLLYQHLFWFFGH 159
Cdd:MTH00026 162 AMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGH 241

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 963775086 160 PEVYIIILPAFGIISESVLFLTDKERLFGQTSMTFASIWIAVLGLSVWGHHMYTAG 215
Cdd:MTH00026 242 PEVYILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVG 297
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-215 9.39e-58

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 190.15  E-value: 9.39e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775086   1 WVLPLMLTAPEMAFPRLNALSFWFTLVALFMVYHSFFVGMGAGGSWTFYPPL-NTEGLPELSTDTMILSLHTVGFGSLLG 79
Cdd:MTH00077  81 WLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLaGNLAHAGASVDLTIFSLHLAGVSSILG 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775086  80 AINFMATVQNMRATSVTLDQMSMFVWTLYLTSLLLLLSVPVLAGALLFLLMDRNFNCSFYDTKTGGNPLLYQHLFWFFGH 159
Cdd:MTH00077 161 AINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGH 240

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 963775086 160 PEVYIIILPAFGIISESVLFLTDKERLFGQTSMTFASIWIAVLGLSVWGHHMYTAG 215
Cdd:MTH00077 241 PEVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVD 296
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-215 6.86e-57

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 187.78  E-value: 6.86e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775086   1 WVLPLMLTAPEMAFPRLNALSFWFTLVALFMVYHSFFVGMGAGGSWTFYPPL-NTEGLPELSTDTMILSLHTVGFGSLLG 79
Cdd:MTH00103  81 WLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLaGNLAHAGASVDLTIFSLHLAGVSSILG 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775086  80 AINFMATVQNMRATSVTLDQMSMFVWTLYLTSLLLLLSVPVLAGALLFLLMDRNFNCSFYDTKTGGNPLLYQHLFWFFGH 159
Cdd:MTH00103 161 AINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGH 240

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 963775086 160 PEVYIIILPAFGIISESVLFLTDKERLFGQTSMTFASIWIAVLGLSVWGHHMYTAG 215
Cdd:MTH00103 241 PEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVG 296
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-215 1.03e-56

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 187.44  E-value: 1.03e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775086   1 WVLPLMLTAPEMAFPRLNALSFWFTLVALFMVYHSFFVGMGAGGSWTFYPPLNTE-GLPELSTDTMILSLHTVGFGSLLG 79
Cdd:MTH00183  81 WLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNlAHAGASVDLTIFSLHLAGVSSILG 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775086  80 AINFMATVQNMRATSVTLDQMSMFVWTLYLTSLLLLLSVPVLAGALLFLLMDRNFNCSFYDTKTGGNPLLYQHLFWFFGH 159
Cdd:MTH00183 161 AINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGH 240

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 963775086 160 PEVYIIILPAFGIISESVLFLTDKERLFGQTSMTFASIWIAVLGLSVWGHHMYTAG 215
Cdd:MTH00183 241 PEVYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVG 296
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-215 3.30e-56

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 186.19  E-value: 3.30e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775086   1 WVLPLMLTAPEMAFPRLNALSFWFTLVALFMVYHSFFVGMGAGGSWTFYPPLNTeGLPEL--STDTMILSLHTVGFGSLL 78
Cdd:MTH00037  81 WLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSS-NIAHAggSVDLAIFSLHLAGASSIL 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775086  79 GAINFMATVQNMRATSVTLDQMSMFVWTLYLTSLLLLLSVPVLAGALLFLLMDRNFNCSFYDTKTGGNPLLYQHLFWFFG 158
Cdd:MTH00037 160 ASINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFG 239

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 963775086 159 HPEVYIIILPAFGIISESVLFLTDKERLFGQTSMTFASIWIAVLGLSVWGHHMYTAG 215
Cdd:MTH00037 240 HPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVG 296
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-215 1.19e-49

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 168.70  E-value: 1.19e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775086   1 WVLPLMLTAPEMAFPRLNALSFWFTLVALFMVYHSFFVGMGAGgsWTFYPPLNT-EGLPELSTDTMILSLHTVGFGSLLG 79
Cdd:MTH00048  82 YLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCLGAGVG--WTFYPPLSSsLFSSSWGVDFLMFSLHLAGVSSLFG 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775086  80 AINFMATVQNMRATSVTLdQMSMFVWTLYLTSLLLLLSVPVLAGALLFLLMDRNFNCSFYDTKTGGNPLLYQHLFWFFGH 159
Cdd:MTH00048 160 SINFICTIYSAFMTNVFS-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGH 238

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 963775086 160 PEVYIIILPAFGIISESVLFLTDKERLFGQTSMTFASIWIAVLGLSVWGHHMYTAG 215
Cdd:MTH00048 239 PEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVG 294
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-215 6.81e-42

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: 146.56  E-value: 6.81e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775086    1 WVLPLMLTAPEMAFPRLNALSFWFTLVALFMVYHSFfvgMGAGGSWTFYPPLnteglpeLSTDTMILSLHTVGFGSLLGA 80
Cdd:pfam00115  67 YLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPL-------VGVDLWYIGLLLAGVSSLLGA 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775086   81 INFMATVQNMRATSVTLdQMSMFVWTLYLTSLLLLLSVPVLAGALLFLLMDRNFNcsfydtKTGGNPLLYQHLFWFFGHP 160
Cdd:pfam00115 137 INFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHP 209

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 963775086  161 EVYIIILPAFGIISESVLFLTDKeRLFGQTSMTFASIWIAVLGLSVWGHHMYTAG 215
Cdd:pfam00115 210 EVYILILPAFGIIYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTG 263
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 2-215 1.76e-41

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 148.55  E-value: 1.76e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775086   2 VLPLMLTAPEMAFPRLNALSFWFTLVALFMVYHSFFVGMGAGGSWTFYPPLN-TEGLPELSTDTMILSLHTVGFGSLLGA 80
Cdd:PRK15017 126 VVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSgIEYSPGVGVDYWIWSLQLSGIGTTLTG 205

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775086  81 INFMATVQNMRATSVTLDQMSMFVWTLYLTSLLLLLSVPVLAGALLFLLMDRNFNCSFYDTKTGGNPLLYQHLFWFFGHP 160
Cdd:PRK15017 206 INFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHP 285

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 963775086 161 EVYIIILPAFGIISESVLFLTdKERLFGQTSMTFASIWIAVLGLSVWGHHMYTAG 215
Cdd:PRK15017 286 EVYILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFFTMG 339
 
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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