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Conserved domains on  [gi|963775408|gb|ALT10310|]
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cytochrome c oxidase subunit I, partial (mitochondrion) [Eimeria lancasterensis]

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 ...
 3-238 7.20e-95

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 cd01663:

Pssm-ID: 469701  Cd Length: 488  Bit Score: 285.92  E-value: 7.20e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408   3 SPTSVDLIVFGLAISGISSFLSSVNFLSTIA---VLGVTNGAKPwcLFTWAIVFTAIMLIATLPILTGGLLMLVLDLHLN 79
Cdd:cd01663  130 SGPSVDLAIFSLHLAGISSILGAINFITTIFnmrAPGMTLEKMP--LFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFN 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408  80 TQFYDASFNGDPVLYQHLFWFFGHPEVYIIILPAFGVISQTLSTSAGKL-VFGGPSMILAMGCITVLGSLVWAHHMMTVG 158
Cdd:cd01663  208 TSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKpVFGYLGMVYAMLSIGILGFIVWAHHMFTVG 287

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408 159 LETDTRAYFSAITMMIAIPTGTKIFNWLSTFMGnpfSTISLD--IWYALSFIFLFTLGGTTGVVLGNSAIDVALHDTYYV 236
Cdd:cd01663  288 LDVDTRAYFTAATMIIAVPTGIKVFSWLATMWG---GSIKFEtpMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYV 364


                 ..
gi 963775408 237 IA 238
Cdd:cd01663  365 VA 366
 
Name Accession Description Interval E-value
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 3-238 7.20e-95

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: 285.92  E-value: 7.20e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408   3 SPTSVDLIVFGLAISGISSFLSSVNFLSTIA---VLGVTNGAKPwcLFTWAIVFTAIMLIATLPILTGGLLMLVLDLHLN 79
Cdd:cd01663  130 SGPSVDLAIFSLHLAGISSILGAINFITTIFnmrAPGMTLEKMP--LFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFN 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408  80 TQFYDASFNGDPVLYQHLFWFFGHPEVYIIILPAFGVISQTLSTSAGKL-VFGGPSMILAMGCITVLGSLVWAHHMMTVG 158
Cdd:cd01663  208 TSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKpVFGYLGMVYAMLSIGILGFIVWAHHMFTVG 287

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408 159 LETDTRAYFSAITMMIAIPTGTKIFNWLSTFMGnpfSTISLD--IWYALSFIFLFTLGGTTGVVLGNSAIDVALHDTYYV 236
Cdd:cd01663  288 LDVDTRAYFTAATMIIAVPTGIKVFSWLATMWG---GSIKFEtpMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYV 364


                 ..
gi 963775408 237 IA 238
Cdd:cd01663  365 VA 366
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 6-238 2.73e-88

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 269.82  E-value: 2.73e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408   6 SVDLIVFGLAISGISSFLSSVNFLSTI---AVLGVTNGAKPwcLFTWAIVFTAIMLIATLPILTGGLLMLVLDLHLNTQF 82
Cdd:MTH00153 140 SVDLAIFSLHLAGISSILGAINFITTIinmRSKGMTLDRMP--LFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSF 217

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408  83 YDASFNGDPVLYQHLFWFFGHPEVYIIILPAFGVISQTLSTSAGKL-VFGGPSMILAMGCITVLGSLVWAHHMMTVGLET 161
Cdd:MTH00153 218 FDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKeTFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDV 297

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 963775408 162 DTRAYFSAITMMIAIPTGTKIFNWLSTFMGNPFSTISLDIWyALSFIFLFTLGGTTGVVLGNSAIDVALHDTYYVIA 238
Cdd:MTH00153 298 DTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLW-ALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVA 373
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
5-238 4.54e-73

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 231.17  E-value: 4.54e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408   5 TSVDLIVFGLAISGISSFLSSVNFLSTIAVL---GVTNGAKPwcLFTWAIVFTAIMLIATLPILTGGLLMLVLDLHLNTQ 81
Cdd:COG0843  143 VGVDLWLLGLALFGVGSILGGVNFIVTILKMrapGMTLMRMP--LFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTH 220

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408  82 FYDASFNGDPVLYQHLFWFFGHPEVYIIILPAFGVISQTLSTSAGKLVFGGPSMILAMGCITVLGSLVWAHHMMTVGLET 161
Cdd:COG0843  221 FFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISP 300

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 963775408 162 DTRAYFSAITMMIAIPTGTKIFNWLSTFMGN--PFSTISLdiwYALSFIFLFTLGGTTGVVLGNSAIDVALHDTYYVIA 238
Cdd:COG0843  301 LVKAFFSIATMLIAVPTGVKVFNWIATMWRGriRFTTPML---FALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVA 376
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 5-238 2.75e-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: 217.86  E-value: 2.75e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408    5 TSVDLIVFGLAISGISSFLSSVNFLSTIAVL---GVTNGAKPwcLFTWAIVFTAIMLIATLPILTGGLLMLVLDLHLNTQ 81
Cdd:TIGR02891 134 VGVDLWLLGLHLLGISSILGAVNFIVTILNMrapGMTLMRMP--LFVWGILVTSILILLAFPVLIAALILLLLDRLFGTH 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408   82 FYDASFNGDPVLYQHLFWFFGHPEVYIIILPAFGVISQTLSTSAGKLVFGGPSMILAMGCITVLGSLVWAHHMMTVGLET 161
Cdd:TIGR02891 212 FFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPP 291

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 963775408  162 DTRAYFSAITMMIAIPTGTKIFNWLSTFM-GNPfsTISLDIWYALSFIFLFTLGGTTGVVLGNSAIDVALHDTYYVIA 238
Cdd:TIGR02891 292 LALAFFSAATMLIAVPTGVKVFNWIATLWgGSI--RFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVA 367
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 7-238 9.99e-53

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: 175.84  E-value: 9.99e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408    7 VDLIVFGLAISGISSFLSSVNFLSTIAVLGVTNGAKPWCLFTWAIVFTAIMLIATLPILTGGLLMLVLDLHLNTqfydas 86
Cdd:pfam00115 118 VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTLRMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA------ 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408   87 FNGDPVLYQHLFWFFGHPEVYIIILPAFGVISQTLSTSAGKLVFGGPSMILAMGCITVLGSLVWAHHMMTVGLETDTRAY 166
Cdd:pfam00115 192 GGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQAL 271

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 963775408  167 FSAITMMIAIPTGTKIFNWLSTFMGNPFSTISLDIWYALSFIFLFTLGGTTGVVLGNSAIDVALHDTYYVIA 238
Cdd:pfam00115 272 FSVFSMLIAVPSGVKVFNWLATLWGGWIRFRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVA 343
 
Name Accession Description Interval E-value
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 3-238 7.20e-95

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: 285.92  E-value: 7.20e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408   3 SPTSVDLIVFGLAISGISSFLSSVNFLSTIA---VLGVTNGAKPwcLFTWAIVFTAIMLIATLPILTGGLLMLVLDLHLN 79
Cdd:cd01663  130 SGPSVDLAIFSLHLAGISSILGAINFITTIFnmrAPGMTLEKMP--LFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFN 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408  80 TQFYDASFNGDPVLYQHLFWFFGHPEVYIIILPAFGVISQTLSTSAGKL-VFGGPSMILAMGCITVLGSLVWAHHMMTVG 158
Cdd:cd01663  208 TSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKpVFGYLGMVYAMLSIGILGFIVWAHHMFTVG 287

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408 159 LETDTRAYFSAITMMIAIPTGTKIFNWLSTFMGnpfSTISLD--IWYALSFIFLFTLGGTTGVVLGNSAIDVALHDTYYV 236
Cdd:cd01663  288 LDVDTRAYFTAATMIIAVPTGIKVFSWLATMWG---GSIKFEtpMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYV 364


                 ..
gi 963775408 237 IA 238
Cdd:cd01663  365 VA 366
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 6-238 2.73e-88

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 269.82  E-value: 2.73e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408   6 SVDLIVFGLAISGISSFLSSVNFLSTI---AVLGVTNGAKPwcLFTWAIVFTAIMLIATLPILTGGLLMLVLDLHLNTQF 82
Cdd:MTH00153 140 SVDLAIFSLHLAGISSILGAINFITTIinmRSKGMTLDRMP--LFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSF 217

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408  83 YDASFNGDPVLYQHLFWFFGHPEVYIIILPAFGVISQTLSTSAGKL-VFGGPSMILAMGCITVLGSLVWAHHMMTVGLET 161
Cdd:MTH00153 218 FDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKeTFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDV 297

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 963775408 162 DTRAYFSAITMMIAIPTGTKIFNWLSTFMGNPFSTISLDIWyALSFIFLFTLGGTTGVVLGNSAIDVALHDTYYVIA 238
Cdd:MTH00153 298 DTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLW-ALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVA 373
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 6-238 1.77e-83

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 257.60  E-value: 1.77e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408   6 SVDLIVFGLAISGISSFLSSVNFLSTIAVLGVTNGAKPWC-LFTWAIVFTAIMLIATLPILTGGLLMLVLDLHLNTQFYD 84
Cdd:MTH00223 139 SVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLpLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFD 218

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408  85 ASFNGDPVLYQHLFWFFGHPEVYIIILPAFGVISQTLSTSAGKL-VFGGPSMILAMGCITVLGSLVWAHHMMTVGLETDT 163
Cdd:MTH00223 219 PAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKeVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDT 298

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 963775408 164 RAYFSAITMMIAIPTGTKIFNWLSTFMGNPFSTiSLDIWYALSFIFLFTLGGTTGVVLGNSAIDVALHDTYYVIA 238
Cdd:MTH00223 299 RAYFTAATMIIAVPTGIKVFSWLATIYGSKIKY-EAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVA 372
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 3-238 1.40e-80

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 249.98  E-value: 1.40e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408   3 SPTSVDLIVFGLAISGISSFLSSVNFLSTIAVL---GVTNGAKPwcLFTWAIVFTAIMLIATLPILTGGLLMLVLDLHLN 79
Cdd:MTH00167 139 AGASVDLAIFSLHLAGVSSILGSINFITTIINMkppGITQYQTP--LFVWSILVTTILLLLSLPVLAAAITMLLTDRNLN 216

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408  80 TQFYDASFNGDPVLYQHLFWFFGHPEVYIIILPAFGVISQTLSTSAGK-LVFGGPSMILAMGCITVLGSLVWAHHMMTVG 158
Cdd:MTH00167 217 TTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSGKkEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVG 296

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408 159 LETDTRAYFSAITMMIAIPTGTKIFNWLSTFMGNPFsTISLDIWYALSFIFLFTLGGTTGVVLGNSAIDVALHDTYYVIA 238
Cdd:MTH00167 297 MDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKI-KWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVA 375
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 3-238 3.91e-78

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 243.85  E-value: 3.91e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408   3 SPTSVDLIVFGLAISGISSFLSSVNFLST-IAVLGVTNGAKPWCLFTWAIVFTAIMLIATLPILTGGLLMLVLDLHLNTQ 81
Cdd:MTH00116 139 AGASVDLAIFSLHLAGVSSILGAINFITTcINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTT 218

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408  82 FYDASFNGDPVLYQHLFWFFGHPEVYIIILPAFGVISQTLSTSAGKL-VFGGPSMILAMGCITVLGSLVWAHHMMTVGLE 160
Cdd:MTH00116 219 FFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAGKKePFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMD 298

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408 161 TDTRAYFSAITMMIAIPTGTKIFNWLSTFMGnpfSTISLD--IWYALSFIFLFTLGGTTGVVLGNSAIDVALHDTYYVIA 238
Cdd:MTH00116 299 VDTRAYFTSATMIIAIPTGIKVFSWLATLHG---GTIKWDppMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVA 375
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 6-238 3.33e-77

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 241.51  E-value: 3.33e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408   6 SVDLIVFGLAISGISSFLSSVNFLSTIAVL---GVTNGAKPwcLFTWAIVFTAIMLIATLPILTGGLLMLVLDLHLNTQF 82
Cdd:MTH00079 142 SVDLAIFSLHCAGISSILGGINFMVTTKNLrssSISLEHMS--LFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSF 219

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408  83 YDASFNGDPVLYQHLFWFFGHPEVYIIILPAFGVISQ-TLSTSAGKLVFGGPSMILAMGCITVLGSLVWAHHMMTVGLET 161
Cdd:MTH00079 220 FDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQsTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDL 299

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 963775408 162 DTRAYFSAITMMIAIPTGTKIFNWLSTFMGNPFSTISLDIWyALSFIFLFTLGGTTGVVLGNSAIDVALHDTYYVIA 238
Cdd:MTH00079 300 DSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPLLLW-VLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVS 375
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 6-238 6.94e-76

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 238.08  E-value: 6.94e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408   6 SVDLIVFGLAISGISSFLSSVNFLSTIAVL---GVTNGAKPwcLFTWAIVFTAIMLIATLPILTGGLLMLVLDLHLNTQF 82
Cdd:MTH00142 140 SVDLAIFSLHLAGVSSILGAINFITTVINMragGMKFERVP--LFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSF 217

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408  83 YDASFNGDPVLYQHLFWFFGHPEVYIIILPAFGVISQTLSTSAGKL-VFGGPSMILAMGCITVLGSLVWAHHMMTVGLET 161
Cdd:MTH00142 218 FDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHYSGKKeVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDV 297

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 963775408 162 DTRAYFSAITMMIAIPTGTKIFNWLSTFMGNPFStISLDIWYALSFIFLFTLGGTTGVVLGNSAIDVALHDTYYVIA 238
Cdd:MTH00142 298 DTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVK-YEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVA 373
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 6-238 3.97e-73

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 230.94  E-value: 3.97e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408   6 SVDLIVFGLAISGISSFLSSVNFLSTIAVL---GVTNGAKPwcLFTWAIVFTAIMLIATLPILTGGLLMLVLDLHLNTQF 82
Cdd:MTH00007 139 SVDLAIFSLHLAGVSSILGAINFITTVINMrwkGLRLERIP--LFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSF 216

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408  83 YDASFNGDPVLYQHLFWFFGHPEVYIIILPAFGVISQTLSTSAGKL-VFGGPSMILAMGCITVLGSLVWAHHMMTVGLET 161
Cdd:MTH00007 217 FDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGKLePFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDV 296

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 963775408 162 DTRAYFSAITMMIAIPTGTKIFNWLSTFMGNPFSTISLDIWyALSFIFLFTLGGTTGVVLGNSAIDVALHDTYYVIA 238
Cdd:MTH00007 297 DTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYETPMLW-ALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVA 372
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
5-238 4.54e-73

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 231.17  E-value: 4.54e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408   5 TSVDLIVFGLAISGISSFLSSVNFLSTIAVL---GVTNGAKPwcLFTWAIVFTAIMLIATLPILTGGLLMLVLDLHLNTQ 81
Cdd:COG0843  143 VGVDLWLLGLALFGVGSILGGVNFIVTILKMrapGMTLMRMP--LFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTH 220

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408  82 FYDASFNGDPVLYQHLFWFFGHPEVYIIILPAFGVISQTLSTSAGKLVFGGPSMILAMGCITVLGSLVWAHHMMTVGLET 161
Cdd:COG0843  221 FFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISP 300

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 963775408 162 DTRAYFSAITMMIAIPTGTKIFNWLSTFMGN--PFSTISLdiwYALSFIFLFTLGGTTGVVLGNSAIDVALHDTYYVIA 238
Cdd:COG0843  301 LVKAFFSIATMLIAVPTGVKVFNWIATMWRGriRFTTPML---FALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVA 376
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 3-238 4.64e-73

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: 229.34  E-value: 4.64e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408   3 SPTSVDLIVFGLAISGISSFLSSVNFLSTIAVL-GVTNGAKPWCLFTWAIVFTAIMLIATLPILTGGLLMLVLDLHLNTQ 81
Cdd:cd00919  127 SGVGVDLAILGLHLAGVSSILGAINFITTILNMrAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTS 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408  82 FYDASFNGDPVLYQHLFWFFGHPEVYIIILPAFGVISQTLSTSAGKLVFGGPSMILAMGCITVLGSLVWAHHMMTVGLET 161
Cdd:cd00919  207 FFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFSGKPLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPV 286

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 963775408 162 DTRAYFSAITMMIAIPTGTKIFNWLSTFMGNP--FSTISLdiwYALSFIFLFTLGGTTGVVLGNSAIDVALHDTYYVIA 238
Cdd:cd00919  287 DTRAYFTAATMIIAVPTGIKVFNWLATLWGGRirFDPPML---FALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVA 362
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 3-238 6.55e-71

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 225.48  E-value: 6.55e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408   3 SPTSVDLIVFGLAISGISSFLSSVNFLSTIAVL---GVTNGAKPwcLFTWAIVFTAIMLIATLPILTGGLLMLVLDLHLN 79
Cdd:MTH00184 141 SGGSVDMAIFSLHLAGISSILGAMNFITTIFNMrapGITMDRMP--LFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFN 218

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408  80 TQFYDASFNGDPVLYQHLFWFFGHPEVYIIILPAFGVISQTLST-SAGKLVFGGPSMILAMGCITVLGSLVWAHHMMTVG 158
Cdd:MTH00184 219 TTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTfAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVG 298

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408 159 LETDTRAYFSAITMMIAIPTGTKIFNWLSTFMGNPFSTISLDIWyALSFIFLFTLGGTTGVVLGNSAIDVALHDTYYVIA 238
Cdd:MTH00184 299 MDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDTPMLW-AIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVA 377
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 6-238 1.92e-70

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 223.94  E-value: 1.92e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408   6 SVDLIVFGLAISGISSFLSSVNFLSTIAVL---GVTNGAKPwcLFTWAIVFTAIMLIATLPILTGGLLMLVLDLHLNTQF 82
Cdd:MTH00037 142 SVDLAIFSLHLAGASSILASINFITTIINMrtpGMTFDRLP--LFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTF 219

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408  83 YDASFNGDPVLYQHLFWFFGHPEVYIIILPAFGVISQTLSTSAGKL-VFGGPSMILAMGCITVLGSLVWAHHMMTVGLET 161
Cdd:MTH00037 220 FDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKQePFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDV 299

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 963775408 162 DTRAYFSAITMMIAIPTGTKIFNWLSTFMGNPFsTISLDIWYALSFIFLFTLGGTTGVVLGNSAIDVALHDTYYVIA 238
Cdd:MTH00037 300 DTRAYFTAATMIIAVPTGIKVFSWMATLQGSNL-RWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVA 375
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 6-238 2.17e-70

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 224.03  E-value: 2.17e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408   6 SVDLIVFGLAISGISSFLSSVNFLSTIAVL---GVTNGAKPwcLFTWAIVFTAIMLIATLPILTGGLLMLVLDLHLNTQF 82
Cdd:MTH00183 142 SVDLTIFSLHLAGVSSILGAINFITTIINMkppAISQYQTP--LFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTF 219

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408  83 YDASFNGDPVLYQHLFWFFGHPEVYIIILPAFGVISQTLSTSAGKL-VFGGPSMILAMGCITVLGSLVWAHHMMTVGLET 161
Cdd:MTH00183 220 FDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSGKKePFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDV 299

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 963775408 162 DTRAYFSAITMMIAIPTGTKIFNWLSTFMGNPFSTISLDIWyALSFIFLFTLGGTTGVVLGNSAIDVALHDTYYVIA 238
Cdd:MTH00183 300 DTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLW-ALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVA 375
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 6-238 1.54e-69

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 221.68  E-value: 1.54e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408   6 SVDLIVFGLAISGISSFLSSVNFLSTIAVL---GVTNGAKPwcLFTWAIVFTAIMLIATLPILTGGLLMLVLDLHLNTQF 82
Cdd:MTH00103 142 SVDLTIFSLHLAGVSSILGAINFITTIINMkppAMSQYQTP--LFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTF 219

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408  83 YDASFNGDPVLYQHLFWFFGHPEVYIIILPAFGVISQTLSTSAGKL-VFGGPSMILAMGCITVLGSLVWAHHMMTVGLET 161
Cdd:MTH00103 220 FDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKePFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDV 299

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 963775408 162 DTRAYFSAITMMIAIPTGTKIFNWLSTFMGNPFSTISLDIWyALSFIFLFTLGGTTGVVLGNSAIDVALHDTYYVIA 238
Cdd:MTH00103 300 DTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLW-ALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVA 375
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 6-238 4.40e-69

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 220.58  E-value: 4.40e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408   6 SVDLIVFGLAISGISSFLSSVNFLSTIAVL---GVTNGAKPwcLFTWAIVFTAIMLIATLPILTGGLLMLVLDLHLNTQF 82
Cdd:MTH00077 142 SVDLTIFSLHLAGVSSILGAINFITTSINMkppSMSQYQTP--LFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTF 219

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408  83 YDASFNGDPVLYQHLFWFFGHPEVYIIILPAFGVISQTLS-TSAGKLVFGGPSMILAMGCITVLGSLVWAHHMMTVGLET 161
Cdd:MTH00077 220 FDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTyYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNV 299

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 963775408 162 DTRAYFSAITMMIAIPTGTKIFNWLSTFMGNPFSTISLDIWyALSFIFLFTLGGTTGVVLGNSAIDVALHDTYYVIA 238
Cdd:MTH00077 300 DTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDAAMLW-ALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVA 375
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 3-238 7.11e-69

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 220.08  E-value: 7.11e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408   3 SPTSVDLIVFGLAISGISSFLSSVNFLSTIAVL---GVTNGAKPwcLFTWAIVFTAIMLIATLPILTGGLLMLVLDLHLN 79
Cdd:MTH00182 141 SGGAVDMAIFSLHLAGVSSILGAINFITTIFNMrapGVTFNRLP--LFVWSILITAFLLLLSLPVLAGAITMLLTDRNFN 218

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408  80 TQFYDASFNGDPVLYQHLFWFFGHPEVYIIILPAFGVISQTLST-SAGKLVFGGPSMILAMGCITVLGSLVWAHHMMTVG 158
Cdd:MTH00182 219 TTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTfVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVG 298

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408 159 LETDTRAYFSAITMMIAIPTGTKIFNWLSTFMGNPFSTISLDIWyALSFIFLFTLGGTTGVVLGNSAIDVALHDTYYVIA 238
Cdd:MTH00182 299 MDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDTPMLW-AMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVA 377
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 5-238 2.75e-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: 217.86  E-value: 2.75e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408    5 TSVDLIVFGLAISGISSFLSSVNFLSTIAVL---GVTNGAKPwcLFTWAIVFTAIMLIATLPILTGGLLMLVLDLHLNTQ 81
Cdd:TIGR02891 134 VGVDLWLLGLHLLGISSILGAVNFIVTILNMrapGMTLMRMP--LFVWGILVTSILILLAFPVLIAALILLLLDRLFGTH 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408   82 FYDASFNGDPVLYQHLFWFFGHPEVYIIILPAFGVISQTLSTSAGKLVFGGPSMILAMGCITVLGSLVWAHHMMTVGLET 161
Cdd:TIGR02891 212 FFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPP 291

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 963775408  162 DTRAYFSAITMMIAIPTGTKIFNWLSTFM-GNPfsTISLDIWYALSFIFLFTLGGTTGVVLGNSAIDVALHDTYYVIA 238
Cdd:TIGR02891 292 LALAFFSAATMLIAVPTGVKVFNWIATLWgGSI--RFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVA 367
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 7-238 2.88e-67

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 215.70  E-value: 2.88e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408   7 VDLIVFGLAISGISSFLSSVNFLSTIAVLGVTNGAKPWCLFTWAIVFTAIMLIATLPILTGGLLMLVLDLHLNTQFYDAS 86
Cdd:MTH00048 142 VDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFSRTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPL 221

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408  87 FNGDPVLYQHLFWFFGHPEVYIIILPAFGVISQT-LSTSAGKLVFGGPSMILAMGCITVLGSLVWAHHMMTVGLETDTRA 165
Cdd:MTH00048 222 GGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHIcLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAV 301

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 963775408 166 YFSAITMMIAIPTGTKIFNWLSTFMGNPFSTISLDIWYALSFIFLFTLGGTTGVVLGNSAIDVALHDTYYVIA 238
Cdd:MTH00048 302 FFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKSDPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVA 374
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 7-238 6.71e-67

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: 214.37  E-value: 6.71e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408   7 VDLIVFGLAISGISSFLSSVNFLSTIAVL---GVTNGAKPwcLFTWAIVFTAIMLIATLPILTGGLLMLVLDLHLNTQFY 83
Cdd:cd01662  137 VDYWILGLQFSGIGTLLGAINFIVTILKMrapGMTLMRMP--IFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFF 214

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408  84 DASFNGDPVLYQHLFWFFGHPEVYIIILPAFGVISQTLSTSAGKLVFGGPSMILAMGCITVLGSLVWAHHMMTVGLETDT 163
Cdd:cd01662  215 TNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFSRKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALV 294

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 963775408 164 RAYFSAITMMIAIPTGTKIFNWLSTFMGNPFSTISLDIWyALSFIFLFTLGGTTGVVLGNSAIDVALHDTYYVIA 238
Cdd:cd01662  295 NAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLW-AIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVA 368
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 3-238 2.11e-63

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 206.40  E-value: 2.11e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408   3 SPTSVDLIVFGLAISGISSFLSSVNFLSTIAVL---GVTNGAKPwcLFTWAIVFTAIMLIATLPILTGGLLMLVLDLHLN 79
Cdd:MTH00026 140 SGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMrtpGMTMSRIP--LFVWSVFITAILLLLSLPVLAGAITMLLTDRNFN 217

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408  80 TQFYDASFNGDPVLYQHLFWFFGHPEVYIIILPAFGVISQTLST-SAGKLVFGGPSMILAMGCITVLGSLVWAHHMMTVG 158
Cdd:MTH00026 218 TTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLfSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVG 297

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408 159 LETDTRAYFSAITMMIAIPTGTKIFNWLSTFMGNPFSTI-SLDIWYALSFIFLFTLGGTTGVVLGNSAIDVALHDTYYVI 237
Cdd:MTH00026 298 MDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSGRNLIfTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVV 377


                 .
gi 963775408 238 A 238
Cdd:MTH00026 378 A 378
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 7-238 9.99e-53

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: 175.84  E-value: 9.99e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408    7 VDLIVFGLAISGISSFLSSVNFLSTIAVLGVTNGAKPWCLFTWAIVFTAIMLIATLPILTGGLLMLVLDLHLNTqfydas 86
Cdd:pfam00115 118 VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTLRMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA------ 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408   87 FNGDPVLYQHLFWFFGHPEVYIIILPAFGVISQTLSTSAGKLVFGGPSMILAMGCITVLGSLVWAHHMMTVGLETDTRAY 166
Cdd:pfam00115 192 GGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQAL 271

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 963775408  167 FSAITMMIAIPTGTKIFNWLSTFMGNPFSTISLDIWYALSFIFLFTLGGTTGVVLGNSAIDVALHDTYYVIA 238
Cdd:pfam00115 272 FSVFSMLIAVPSGVKVFNWLATLWGGWIRFRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVA 343
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 7-238 1.95e-44

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 157.79  E-value: 1.95e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408   7 VDLIVFGLAISGISSFLSSVNFLSTIAVL---GVTNGAKPwcLFTWAIVFTAIMLIATLPILTGGLLMLVLDLHLNTQFY 83
Cdd:PRK15017 187 VDYWIWSLQLSGIGTTLTGINFFVTILKMrapGMTMFKMP--VFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFF 264

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408  84 DASFNGDPVLYQHLFWFFGHPEVYIIILPAFGVISQTLSTSAGKLVFGGPSMILAMGCITVLGSLVWAHHMMTVGLETDT 163
Cdd:PRK15017 265 TNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFSRKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANV 344

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 963775408 164 RAYFSAITMMIAIPTGTKIFNWLSTFMGNPFSTISLDIWyALSFIFLFTLGGTTGVVLGNSAIDVALHDTYYVIA 238
Cdd:PRK15017 345 NAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLW-TIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIA 418
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 13-236 7.83e-04

ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and some archaea which catalyze the reduction of O2 and simultaneously pump protons across the membrane. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. The ba3 family contains oxidases that lack the conserved residues that form the D- and K-pathways in CcO and ubiquinol oxidase. Instead they contain a potential alternative K-pathway. Additional proton channels have been proposed for this family of oxidases but none have been identified definitively. For general information on the heme-copper oxidase superfamily, please see cd00919.


Pssm-ID: 238830  Cd Length: 473  Bit Score: 39.96  E-value: 7.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408  13 GLAISGISSFLSSVNFLSTIAVLGVTNGAKPWCLFTWAIVFTAIM-LIATLPILTGGLLMLVLDLHLNTQfydasfNGDP 91
Cdd:cd01660  128 GAALVVVGSWISGFAMFVTLWRWKKANPGKKVPLATFMVVTTMILwLVASLGVALEVLFQLLPWSLGLVD------TVDV 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408  92 VLYQHLFWFFGHPEVYIIILPAFGVISQTLSTSAGKLVFGGPSMILAMGCITVLGSLVWAHHMMT-VGLETDTRAYFSAI 170
Cdd:cd01660  202 LLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKLFSDPLARLAFILFLLFSTPVGFHHQFAdPGIGPGWKFIHMVL 281

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775408 171 TMMIAIPT-------------------GTKIFNWLSTFMGNPFSTISLdiwyALSFIFlFTLGGTTGVVLGNSAIDVALH 231
Cdd:cd01660  282 TFMVALPSlltaftvfasleiagrlrgGKGLFGWIRALPWGDPMFLAL----FLAMLM-FIPGGAGGIINASYQLNYVVH 356


                 ....*
gi 963775408 232 DTYYV 236
Cdd:cd01660  357 NTAWV 361
 
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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