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Conserved domains on  [gi|401065085|gb|AFP90479|]
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cytochrome c oxidase subunit 1, partial (mitochondrion) [Dinophysis tripos]

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 ...
 2-309 4.79e-115

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: 341.38  E-value: 4.79e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085   2 GTLISILIRIELYSSGNRIISPEnqnFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFQGSPEVVYPKINNFSILILS 81
Cdd:cd01663   21 GTSLSLLIRLELSQPGSQLGNDQ---LYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLP 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085  82 LSYLFVILSLISEFGGGTGWTLYPPLSTSfLSLSPSSTGNLIFGLLISGISSCLTSLNFWTTIINLRSYYLTLKTMPLFL 161
Cdd:cd01663   98 PSLLLLLLSALVEGGAGTGWTVYPPLSSI-LAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFV 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085 162 WSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILIVPAF-GIISIIISGILQK 240
Cdd:cd01663  177 WSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFgIISHIISTFSGKK 256

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 401065085 241 IIFGNQSMIFALSCISLLGSVVWGHHMYTVGLETDTRAYFTGVTILISLPTGTKIFNWLSTYLG-----NPPLL 309
Cdd:cd01663  257 PVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGgsikfETPML 330
 
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 ...
 2-309 4.79e-115

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: 341.38  E-value: 4.79e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085   2 GTLISILIRIELYSSGNRIISPEnqnFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFQGSPEVVYPKINNFSILILS 81
Cdd:cd01663   21 GTSLSLLIRLELSQPGSQLGNDQ---LYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLP 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085  82 LSYLFVILSLISEFGGGTGWTLYPPLSTSfLSLSPSSTGNLIFGLLISGISSCLTSLNFWTTIINLRSYYLTLKTMPLFL 161
Cdd:cd01663   98 PSLLLLLLSALVEGGAGTGWTVYPPLSSI-LAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFV 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085 162 WSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILIVPAF-GIISIIISGILQK 240
Cdd:cd01663  177 WSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFgIISHIISTFSGKK 256

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 401065085 241 IIFGNQSMIFALSCISLLGSVVWGHHMYTVGLETDTRAYFTGVTILISLPTGTKIFNWLSTYLG-----NPPLL 309
Cdd:cd01663  257 PVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGgsikfETPML 330
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 2-309 1.56e-105

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 317.58  E-value: 1.56e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085   2 GTLISILIRIELYSSGNRIispENQNFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFQGSPEVVYPKINNFSILILS 81
Cdd:MTH00153  28 GTSLSLLIRAELGQPGSLI---GDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLP 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085  82 LSYLFVILSLISEFGGGTGWTLYPPLStSFLSLSPSSTGNLIFGLLISGISSCLTSLNFWTTIINLRSYYLTLKTMPLFL 161
Cdd:MTH00153 105 PSLTLLLSSSMVESGAGTGWTVYPPLS-SNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFV 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085 162 WSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILIVPAFGIISIIISGILQKI 241
Cdd:MTH00153 184 WSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKK 263

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 401065085 242 -IFGNQSMIFALSCISLLGSVVWGHHMYTVGLETDTRAYFTGVTILISLPTGTKIFNWLSTYLG-----NPPLL 309
Cdd:MTH00153 264 eTFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGsqinySPSLL 337
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 2-306 5.12e-85

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: 264.47  E-value: 5.12e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085    2 GTLISILIRIELYSSGNRIISPEnqnFYNISITLHGFLMIFFLVMPgLFGGFGNYFVPIFQGSPEVVYPKINNFSILILS 81
Cdd:TIGR02891  24 GGVLALLMRAQLATPGNTFMDAE---TYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLPLMIGARDMAFPRLNAFSYWLYL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085   82 LSYLFVILSLISEFGGGTGWTLYPPLSTsfLSLSPSSTGNL-IFGLLISGISSCLTSLNFWTTIINLRSYYLTLKTMPLF 160
Cdd:TIGR02891 100 FGGLLLLASFFTGGAPDTGWTMYPPLSS--TSGSPGVGVDLwLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLF 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085  161 LWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILIVPAFGIISIIISGILQK 240
Cdd:TIGR02891 178 VWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARK 257

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 401065085  241 IIFGNQSMIFALSCISLLGSVVWGHHMYTVGLETDTRAYFTGVTILISLPTGTKIFNWLST-YLGNP 306
Cdd:TIGR02891 258 PIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATlWGGSI 324
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-324 3.29e-83

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 260.83  E-value: 3.29e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085   2 GTLISILIRIELYSSGNRIISPEnqnFYNISITLHGFLMIFFLVMPgLFGGFGNYFVPIFQGSPEVVYPKINNFSILILS 81
Cdd:COG0843   33 GGLLALLMRLQLAGPGLGLLSPE---TYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYL 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085  82 LSYLFVILSLISEFGGGTGWTLYPPLSTsfLSLSPSSTGNL-IFGLLISGISSCLTSLNFWTTIINLRSYYLTLKTMPLF 160
Cdd:COG0843  109 FGGLLLLISLFVGGAADVGWTFYPPLSG--LEASPGVGVDLwLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLF 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085 161 LWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILIVPAFGIISIIISGILQK 240
Cdd:COG0843  187 TWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRK 266

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085 241 IIFGNQSMIFALSCISLLGSVVWGHHMYTVGLETDTRAYFTGVTILISLPTGTKIFNWLST-YLGNPPLlqlkTSSAFFG 319
Cdd:COG0843  267 PLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATmWRGRIRF----TTPMLFA 342


                 ....*
gi 401065085 320 LLFLL 324
Cdd:COG0843  343 LGFII 347
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 2-301 6.68e-59

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: 195.10  E-value: 6.68e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085    2 GTLISILIRIELYSSGNRIISPEnqnFYNISITLHGFLMIFFLVMPGLFGgFGNYFVPIFQGSPEVVYPKINNFSILILS 81
Cdd:pfam00115  17 GGLLGLLIRLQLAFPGLNFLSPL---TYNQLRTLHGNLMIFWFATPFLFG-FGNYLVPLMIGARDMAFPRLNALSFWLVV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085   82 LSylfVILSLISEFGGGTGWTLYPPLSTSFLslspsstgnLIFGLLISGISSCLTSLNFWTTIINLRSYYLTLKtMPLFL 161
Cdd:pfam00115  93 LG---AVLLLASFGGATTGWTEYPPLVGVDL---------WYIGLLLAGVSSLLGAINFIVTILKRRAPGMTLR-MPLFV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085  162 WSLLITGGMLLLTLPILSGALLMVTADLHSNTLFfdpifeGDPIFYQHLFWFFGHPEVYILIVPAFGIISIIISGILQKI 241
Cdd:pfam00115 160 WAILATAILILLAFPVLAAALLLLLLDRSLGAGG------GDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP 233

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085  242 IFGNQSMIFALSCISLLGSVVWGHHMYTVGLETDTRAYFTGVTILISLPTGTKIFNWLST 301
Cdd:pfam00115 234 LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLAT 293
 
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 ...
 2-309 4.79e-115

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: 341.38  E-value: 4.79e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085   2 GTLISILIRIELYSSGNRIISPEnqnFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFQGSPEVVYPKINNFSILILS 81
Cdd:cd01663   21 GTSLSLLIRLELSQPGSQLGNDQ---LYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLP 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085  82 LSYLFVILSLISEFGGGTGWTLYPPLSTSfLSLSPSSTGNLIFGLLISGISSCLTSLNFWTTIINLRSYYLTLKTMPLFL 161
Cdd:cd01663   98 PSLLLLLLSALVEGGAGTGWTVYPPLSSI-LAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFV 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085 162 WSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILIVPAF-GIISIIISGILQK 240
Cdd:cd01663  177 WSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFgIISHIISTFSGKK 256

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 401065085 241 IIFGNQSMIFALSCISLLGSVVWGHHMYTVGLETDTRAYFTGVTILISLPTGTKIFNWLSTYLG-----NPPLL 309
Cdd:cd01663  257 PVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGgsikfETPML 330
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 2-309 1.56e-105

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 317.58  E-value: 1.56e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085   2 GTLISILIRIELYSSGNRIispENQNFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFQGSPEVVYPKINNFSILILS 81
Cdd:MTH00153  28 GTSLSLLIRAELGQPGSLI---GDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLP 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085  82 LSYLFVILSLISEFGGGTGWTLYPPLStSFLSLSPSSTGNLIFGLLISGISSCLTSLNFWTTIINLRSYYLTLKTMPLFL 161
Cdd:MTH00153 105 PSLTLLLSSSMVESGAGTGWTVYPPLS-SNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFV 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085 162 WSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILIVPAFGIISIIISGILQKI 241
Cdd:MTH00153 184 WSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKK 263

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 401065085 242 -IFGNQSMIFALSCISLLGSVVWGHHMYTVGLETDTRAYFTGVTILISLPTGTKIFNWLSTYLG-----NPPLL 309
Cdd:MTH00153 264 eTFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGsqinySPSLL 337
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 2-304 3.57e-102

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 309.22  E-value: 3.57e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085   2 GTLISILIRIELYSSGNRIISPEnqnFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFQGSPEVVYPKINNFSILILS 81
Cdd:MTH00223  27 GTSLSLLIRAELGQPGALLGDDQ---LYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLP 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085  82 LSYLFVILSLISEFGGGTGWTLYPPLStSFLSLSPSSTGNLIFGLLISGISSCLTSLNFWTTIINLRSYYLTLKTMPLFL 161
Cdd:MTH00223 104 PSLYLLLSSSAVESGVGTGWTVYPPLS-SNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFV 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085 162 WSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILIVPAFGIISIIISGILQKI 241
Cdd:MTH00223 183 WSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKK 262

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 401065085 242 -IFGNQSMIFALSCISLLGSVVWGHHMYTVGLETDTRAYFTGVTILISLPTGTKIFNWLSTYLG 304
Cdd:MTH00223 263 eVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYG 326
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 2-323 2.90e-97

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 296.59  E-value: 2.90e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085   2 GTLISILIRIELYSSGNRIispENQNFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFQGSPEVVYPKINNFSILILS 81
Cdd:MTH00167  30 GTALSLLIRAELSQPGSLL---GDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLP 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085  82 LSYLFVILSLISEFGGGTGWTLYPPLStSFLSLSPSSTGNLIFGLLISGISSCLTSLNFWTTIINLRSYYLTLKTMPLFL 161
Cdd:MTH00167 107 PSLLLLLASSGVEAGAGTGWTVYPPLA-GNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFV 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085 162 WSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILIVPAF-GIISIIISGILQK 240
Cdd:MTH00167 186 WSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFgMISHIVVYYSGKK 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085 241 IIFGNQSMIFALSCISLLGSVVWGHHMYTVGLETDTRAYFTGVTILISLPTGTKIFNWLSTYLGNPPLLQLKTSSAfFGL 320
Cdd:MTH00167 266 EPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWETPMLWA-LGF 344


                 ...
gi 401065085 321 LFL 323
Cdd:MTH00167 345 IFL 347
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 2-304 7.38e-95

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 290.43  E-value: 7.38e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085   2 GTLISILIRIELYSSGnriISPENQNFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFQGSPEVVYPKINNFSILILS 81
Cdd:MTH00079  31 GTSLSLIIRLELSKPG---LLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLP 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085  82 LSYLFVILSLISEFGGGTGWTLYPPLSTsfLSLSPSSTGNLIFGLLISGISSCLTSLNFWTTIINLRSYYLTLKTMPLFL 161
Cdd:MTH00079 108 TSLFLILDSCFVDMGPGTSWTVYPPLST--LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFV 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085 162 WSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILIVPAFGIISIIISGIL-QK 240
Cdd:MTH00079 186 WTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTgKK 265

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 401065085 241 IIFGNQSMIFALSCISLLGSVVWGHHMYTVGLETDTRAYFTGVTILISLPTGTKIFNWLSTYLG 304
Cdd:MTH00079 266 EVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFG 329
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 2-304 5.68e-94

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 288.14  E-value: 5.68e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085   2 GTLISILIRIELYSSGNRIispENQNFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFQGSPEVVYPKINNFSILILS 81
Cdd:MTH00116  30 GTALSLLIRAELGQPGTLL---GDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLP 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085  82 LSYLFVILSLISEFGGGTGWTLYPPLSTSfLSLSPSSTGNLIFGLLISGISSCLTSLNFWTTIINLRSYYLTLKTMPLFL 161
Cdd:MTH00116 107 PSFLLLLASSTVEAGAGTGWTVYPPLAGN-LAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFV 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085 162 WSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILIVPAF-GIISIIISGILQK 240
Cdd:MTH00116 186 WSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFgIISHIVTYYAGKK 265

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 401065085 241 IIFGNQSMIFALSCISLLGSVVWGHHMYTVGLETDTRAYFTGVTILISLPTGTKIFNWLSTYLG 304
Cdd:MTH00116 266 EPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHG 329
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 2-309 1.33e-93

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 287.00  E-value: 1.33e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085   2 GTLISILIRIELYSSGNRIispENQNFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFQGSPEVVYPKINNFSILILS 81
Cdd:MTH00142  28 GTGLSLLIRAELGQPGSLL---GDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLP 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085  82 LSYLFVILSLISEFGGGTGWTLYPPLStSFLSLSPSSTGNLIFGLLISGISSCLTSLNFWTTIINLRSYYLTLKTMPLFL 161
Cdd:MTH00142 105 PALLLLLSSAAVESGAGTGWTVYPPLS-SNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFV 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085 162 WSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILIVPAF-GIISIIISGILQK 240
Cdd:MTH00142 184 WSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFgMISHIINHYSGKK 263

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 401065085 241 IIFGNQSMIFALSCISLLGSVVWGHHMYTVGLETDTRAYFTGVTILISLPTGTKIFNWLSTYLGN-----PPLL 309
Cdd:MTH00142 264 EVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSkvkyePPML 337
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 2-324 4.60e-90

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: 276.33  E-value: 4.60e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085   2 GTLISILIRIELYSSGNRIISPEnqnFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFqGSPEVVYPKINNFSILILS 81
Cdd:cd00919   19 GGLLALLIRLELATPGSLFLDPQ---LYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPPLI-GARDLAFPRLNNLSFWLFP 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085  82 LSYLFVILSLISEFGGGTGWTLYPPLSTSFLSLSPSStGNLIFGLLISGISSCLTSLNFWTTIINLRSYYLTLKTMPLFL 161
Cdd:cd00919   95 PGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGV-DLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFV 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085 162 WSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILIVPAFGIISIIISGILQKI 241
Cdd:cd00919  174 WSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFSGKP 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085 242 IFGNQSMIFALSCISLLGSVVWGHHMYTVGLETDTRAYFTGVTILISLPTGTKIFNWLSTYLG-----NPPLLqlktSSA 316
Cdd:cd00919  254 LFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGgrirfDPPML----FAL 329


                 ....*...
gi 401065085 317 FFGLLFLL 324
Cdd:cd00919  330 GFLFLFTI 337
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 2-306 3.75e-89

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 275.63  E-value: 3.75e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085   2 GTLISILIRIELYSSGNRIISPEnqnFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFQGSPEVVYPKINNFSILILS 81
Cdd:MTH00007  27 GTSMSLLIRIELGQPGAFLGSDQ---LYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLP 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085  82 LSYLFVILSLISEFGGGTGWTLYPPLSTSFLSLSPSsTGNLIFGLLISGISSCLTSLNFWTTIINLRSYYLTLKTMPLFL 161
Cdd:MTH00007 104 PALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPS-VDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFV 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085 162 WSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILIVPAFGIISIIISGILQKI 241
Cdd:MTH00007 183 WAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGKL 262

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 401065085 242 -IFGNQSMIFALSCISLLGSVVWGHHMYTVGLETDTRAYFTGVTILISLPTGTKIFNWLSTYLGNP 306
Cdd:MTH00007 263 ePFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSP 328
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 2-304 1.90e-88

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 274.01  E-value: 1.90e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085   2 GTLISILIRIELYSSGNRIispENQNFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFQGSPEVVYPKINNFSILILS 81
Cdd:MTH00184  32 GTAFSMLIRLELSAPGSML---GDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLP 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085  82 LSYLFVILSLISEFGGGTGWTLYPPLStSFLSLSPSSTGNLIFGLLISGISSCLTSLNFWTTIINLRSYYLTLKTMPLFL 161
Cdd:MTH00184 109 PALTLLLGSAFVEQGAGTGWTVYPPLS-SIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFV 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085 162 WSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILIVPAF-GIISIIISGILQK 240
Cdd:MTH00184 188 WSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFgIISQIIPTFAAKK 267

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 401065085 241 IIFGNQSMIFALSCISLLGSVVWGHHMYTVGLETDTRAYFTGVTILISLPTGTKIFNWLSTYLG 304
Cdd:MTH00184 268 QIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFG 331
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 2-304 3.71e-87

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 270.60  E-value: 3.71e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085   2 GTLISILIRIELYSSGNRIispENQNFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFQGSPEVVYPKINNFSILILS 81
Cdd:MTH00103  30 GTALSLLIRAELGQPGTLL---GDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLP 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085  82 LSYLFVILSLISEFGGGTGWTLYPPLSTSfLSLSPSSTGNLIFGLLISGISSCLTSLNFWTTIINLRSYYLTLKTMPLFL 161
Cdd:MTH00103 107 PSFLLLLASSMVEAGAGTGWTVYPPLAGN-LAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFV 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085 162 WSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILIVPAFGIISIIISGIL-QK 240
Cdd:MTH00103 186 WSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSgKK 265

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 401065085 241 IIFGNQSMIFALSCISLLGSVVWGHHMYTVGLETDTRAYFTGVTILISLPTGTKIFNWLSTYLG 304
Cdd:MTH00103 266 EPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHG 329
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 2-304 6.88e-86

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 267.58  E-value: 6.88e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085   2 GTLISILIRIELYSSGNRIispENQNFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFQGSPEVVYPKINNFSILILS 81
Cdd:MTH00077  30 GTALSLLIRAELSQPGTLL---GDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLP 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085  82 LSYLFVILSLISEFGGGTGWTLYPPLSTSFLSLSPSsTGNLIFGLLISGISSCLTSLNFWTTIINLRSYYLTLKTMPLFL 161
Cdd:MTH00077 107 PSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGAS-VDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFV 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085 162 WSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILIVPAF-GIISIIISGILQK 240
Cdd:MTH00077 186 WSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFgMISHIVTYYSAKK 265

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 401065085 241 IIFGNQSMIFALSCISLLGSVVWGHHMYTVGLETDTRAYFTGVTILISLPTGTKIFNWLSTYLG 304
Cdd:MTH00077 266 EPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHG 329
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 2-304 7.26e-86

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 267.56  E-value: 7.26e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085   2 GTLISILIRIELYSSGNRIispENQNFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFQGSPEVVYPKINNFSILILS 81
Cdd:MTH00183  30 GTALSLLIRAELSQPGALL---GDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLP 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085  82 LSYLFVILSLISEFGGGTGWTLYPPLSTSfLSLSPSSTGNLIFGLLISGISSCLTSLNFWTTIINLRSYYLTLKTMPLFL 161
Cdd:MTH00183 107 PSFLLLLASSGVEAGAGTGWTVYPPLAGN-LAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFV 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085 162 WSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILIVPAFGIISIIISGIL-QK 240
Cdd:MTH00183 186 WAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSgKK 265

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 401065085 241 IIFGNQSMIFALSCISLLGSVVWGHHMYTVGLETDTRAYFTGVTILISLPTGTKIFNWLSTYLG 304
Cdd:MTH00183 266 EPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHG 329
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 2-304 1.08e-85

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 267.07  E-value: 1.08e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085   2 GTLISILIRIELYSSGNRIispENQNFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFQGSPEVVYPKINNFSILILS 81
Cdd:MTH00182  32 GTAFSMLIRLELSAPGAML---GDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLP 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085  82 LSYLFVILSLISEFGGGTGWTLYPPLStSFLSLSPSSTGNLIFGLLISGISSCLTSLNFWTTIINLRSYYLTLKTMPLFL 161
Cdd:MTH00182 109 PALILLLGSAFVEQGAGTGWTVYPPLS-SIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFV 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085 162 WSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILIVPAFGIISIII-SGILQK 240
Cdd:MTH00182 188 WSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIpTFVAKK 267

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 401065085 241 IIFGNQSMIFALSCISLLGSVVWGHHMYTVGLETDTRAYFTGVTILISLPTGTKIFNWLSTYLG 304
Cdd:MTH00182 268 QIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYG 331
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 2-306 5.12e-85

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: 264.47  E-value: 5.12e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085    2 GTLISILIRIELYSSGNRIISPEnqnFYNISITLHGFLMIFFLVMPgLFGGFGNYFVPIFQGSPEVVYPKINNFSILILS 81
Cdd:TIGR02891  24 GGVLALLMRAQLATPGNTFMDAE---TYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLPLMIGARDMAFPRLNAFSYWLYL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085   82 LSYLFVILSLISEFGGGTGWTLYPPLSTsfLSLSPSSTGNL-IFGLLISGISSCLTSLNFWTTIINLRSYYLTLKTMPLF 160
Cdd:TIGR02891 100 FGGLLLLASFFTGGAPDTGWTMYPPLSS--TSGSPGVGVDLwLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLF 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085  161 LWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILIVPAFGIISIIISGILQK 240
Cdd:TIGR02891 178 VWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARK 257

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 401065085  241 IIFGNQSMIFALSCISLLGSVVWGHHMYTVGLETDTRAYFTGVTILISLPTGTKIFNWLST-YLGNP 306
Cdd:TIGR02891 258 PIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATlWGGSI 324
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 2-309 7.63e-84

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 262.07  E-value: 7.63e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085   2 GTLISILIRIELYSSGNRIispENQNFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFQGSPEVVYPKINNFSILILS 81
Cdd:MTH00037  30 GTAMSVIIRTELAQPGSLL---QDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIP 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085  82 LSYLFVILSLISEFGGGTGWTLYPPLStSFLSLSPSSTGNLIFGLLISGISSCLTSLNFWTTIINLRSYYLTLKTMPLFL 161
Cdd:MTH00037 107 PSFLLLLASAGVESGAGTGWTIYPPLS-SNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFV 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085 162 WSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILIVPAFGIISIIISGILQKI 241
Cdd:MTH00037 186 WSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKQ 265

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 401065085 242 -IFGNQSMIFALSCISLLGSVVWGHHMYTVGLETDTRAYFTGVTILISLPTGTKIFNWLSTYLG-----NPPLL 309
Cdd:MTH00037 266 ePFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGsnlrwETPLL 339
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-324 3.29e-83

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 260.83  E-value: 3.29e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085   2 GTLISILIRIELYSSGNRIISPEnqnFYNISITLHGFLMIFFLVMPgLFGGFGNYFVPIFQGSPEVVYPKINNFSILILS 81
Cdd:COG0843   33 GGLLALLMRLQLAGPGLGLLSPE---TYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYL 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085  82 LSYLFVILSLISEFGGGTGWTLYPPLSTsfLSLSPSSTGNL-IFGLLISGISSCLTSLNFWTTIINLRSYYLTLKTMPLF 160
Cdd:COG0843  109 FGGLLLLISLFVGGAADVGWTFYPPLSG--LEASPGVGVDLwLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLF 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085 161 LWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILIVPAFGIISIIISGILQK 240
Cdd:COG0843  187 TWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRK 266

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085 241 IIFGNQSMIFALSCISLLGSVVWGHHMYTVGLETDTRAYFTGVTILISLPTGTKIFNWLST-YLGNPPLlqlkTSSAFFG 319
Cdd:COG0843  267 PLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATmWRGRIRF----TTPMLFA 342


                 ....*
gi 401065085 320 LLFLL 324
Cdd:COG0843  343 LGFII 347
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 2-324 8.84e-82

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 257.25  E-value: 8.84e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085   2 GTLISILIRIELYSSGNRIispENQNFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFQGSPEVVYPKINNFSILILS 81
Cdd:MTH00026  31 GTAFSMLIRLELSSPGSML---GDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLP 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085  82 LSYLFVILSLISEFGGGTGWTLYPPLStSFLSLSPSSTGNLIFGLLISGISSCLTSLNFWTTIINLRSYYLTLKTMPLFL 161
Cdd:MTH00026 108 PALFLLLGSSLVEQGAGTGWTVYPPLA-SIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFV 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085 162 WSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILIVPAF-GIISIIISGILQK 240
Cdd:MTH00026 187 WSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFgIISQILSLFSYKK 266

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085 241 IIFGNQSMIFALSCISLLGSVVWGHHMYTVGLETDTRAYFTGVTILISLPTGTKIFNWLSTYLGNPPLLQLKTSSAF-FG 319
Cdd:MTH00026 267 QIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSGRNLIFTTPMAWaLG 346


                 ....*
gi 401065085 320 LLFLL 324
Cdd:MTH00026 347 FIFLF 351
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 2-301 6.89e-76

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: 240.95  E-value: 6.89e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085   2 GTLISILIRIELYSSGNRIISPENqnfYNISITLHGFLMIFFLVMPgLFGGFGNYFVPIFQGSPEVVYPKINNFSILILS 81
Cdd:cd01662   25 GGVDALLMRTQLALPGNDFLSPEH---YNQIFTMHGTIMIFLFAMP-LVFGLMNYLVPLQIGARDVAFPRLNALSFWLFL 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085  82 LSYLFVILSLISEFGGGTGWTLYPPLSTsfLSLSPSSTGNL-IFGLLISGISSCLTSLNFWTTIINLRSYYLTLKTMPLF 160
Cdd:cd01662  101 FGGLLLNASLLIGGFPDAGWFAYPPLSG--LEYSPGVGVDYwILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIF 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085 161 LWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILIVPAFGIISIIISGILQK 240
Cdd:cd01662  179 TWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFSRK 258

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 401065085 241 IIFGNQSMIFALSCISLLGSVVWGHHMYTVGLETDTRAYFTGVTILISLPTGTKIFNWLST 301
Cdd:cd01662  259 PLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFT 319
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 2-304 3.53e-72

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 231.88  E-value: 3.53e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085   2 GTLISILIRIELYSSGNRIISPEnqnFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFQGSPEVVYPKINNFSILILS 81
Cdd:MTH00048  31 GLSLSLLIRLNFLDPYYNVISLD---VYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLV 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085  82 LSYLFVILSLIseFGGGTGWTLYPPLSTSFLSLSpSSTGNLIFGLLISGISSCLTSLNFWTTIINLRSYYLTLKTmPLFL 161
Cdd:MTH00048 108 PSIVFLLLSMC--LGAGVGWTFYPPLSSSLFSSS-WGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFSRT-SIIL 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085 162 WSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILIVPAFGIISII-ISGILQK 240
Cdd:MTH00048 184 WSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHIcLSLSNND 263

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 401065085 241 IIFGNQSMIFALSCISLLGSVVWGHHMYTVGLETDTRAYFTGVTILISLPTGTKIFNWLSTYLG 304
Cdd:MTH00048 264 DPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLN 327
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 2-301 6.68e-59

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: 195.10  E-value: 6.68e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085    2 GTLISILIRIELYSSGNRIISPEnqnFYNISITLHGFLMIFFLVMPGLFGgFGNYFVPIFQGSPEVVYPKINNFSILILS 81
Cdd:pfam00115  17 GGLLGLLIRLQLAFPGLNFLSPL---TYNQLRTLHGNLMIFWFATPFLFG-FGNYLVPLMIGARDMAFPRLNALSFWLVV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085   82 LSylfVILSLISEFGGGTGWTLYPPLSTSFLslspsstgnLIFGLLISGISSCLTSLNFWTTIINLRSYYLTLKtMPLFL 161
Cdd:pfam00115  93 LG---AVLLLASFGGATTGWTEYPPLVGVDL---------WYIGLLLAGVSSLLGAINFIVTILKRRAPGMTLR-MPLFV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085  162 WSLLITGGMLLLTLPILSGALLMVTADLHSNTLFfdpifeGDPIFYQHLFWFFGHPEVYILIVPAFGIISIIISGILQKI 241
Cdd:pfam00115 160 WAILATAILILLAFPVLAAALLLLLLDRSLGAGG------GDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP 233

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085  242 IFGNQSMIFALSCISLLGSVVWGHHMYTVGLETDTRAYFTGVTILISLPTGTKIFNWLST 301
Cdd:pfam00115 234 LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLAT 293
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 6-301 9.95e-51

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 178.21  E-value: 9.95e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085   6 SILIRIE--LYSSGNRIISPENQnfYNISITLHGFLMIFFLVMPGLFGgFGNYFVPIFQGSPEVVYPKINNFSILILSLS 83
Cdd:PRK15017  76 AIMMRSQqaLASAGEAGFLPPHH--YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVG 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085  84 YLFVILSL-ISEFGGgTGWTLYPPLSTsfLSLSPS-STGNLIFGLLISGISSCLTSLNFWTTIINLRSYYLTLKTMPLFL 161
Cdd:PRK15017 153 VILVNVSLgVGEFAQ-TGWLAYPPLSG--IEYSPGvGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFT 229

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085 162 WSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILIVPAFGIISIIISGILQKI 241
Cdd:PRK15017 230 WASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFSRKR 309

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 401065085 242 IFGNQSMIFALSCISLLGSVVWGHHMYTVGLETDTRAYFTGVTILISLPTGTKIFNWLST 301
Cdd:PRK15017 310 LFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFT 369
 
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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