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Conserved domains on  [gi|315571921|gb|ADU33894|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Azadinium spinosum]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Heme_Cu_Oxidase_I super family cl00275
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-307 3.16e-121

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: 356.41  E-value: 3.16e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921   1 TLISVLIRIELYSSGNRIISPEnqnFYNISITLHGFLMIFFLIMPGLFGGFGNYFVPIFQGSPEVVYPRVNNFSILILSL 80
Cdd:cd01663   22 TSLSLLIRLELSQPGSQLGNDQ---LYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPP 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921  81 SYLFLILSLISEFGGGTGWTLYPPLSTSfMSLSPSSTGNLIFGLLISGISSCLTSLNFWTTILNLRSYYLTLKTMPLFPW 160
Cdd:cd01663   99 SLLLLLLSALVEGGAGTGWTVYPPLSSI-LAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVW 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921 161 ALLITGGMLLLTLPILSGALLMVLADLHSNTLFFDPIFGGDPIFYQHLFWFFGHPEVYILIIPAF-GIISIIISGILQKI 239
Cdd:cd01663  178 SVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFgIISHIISTFSGKKP 257

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 315571921 240 IFGNQSMIYAMSCISLLGSVVWGHHMYTVGLETDTRAYFTGVTILISLPTGTKIFNWLSTYLG-----NPPLL 307
Cdd:cd01663  258 VFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGgsikfETPML 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 ...
 1-307 3.16e-121

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: 356.41  E-value: 3.16e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921   1 TLISVLIRIELYSSGNRIISPEnqnFYNISITLHGFLMIFFLIMPGLFGGFGNYFVPIFQGSPEVVYPRVNNFSILILSL 80
Cdd:cd01663   22 TSLSLLIRLELSQPGSQLGNDQ---LYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPP 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921  81 SYLFLILSLISEFGGGTGWTLYPPLSTSfMSLSPSSTGNLIFGLLISGISSCLTSLNFWTTILNLRSYYLTLKTMPLFPW 160
Cdd:cd01663   99 SLLLLLLSALVEGGAGTGWTVYPPLSSI-LAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVW 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921 161 ALLITGGMLLLTLPILSGALLMVLADLHSNTLFFDPIFGGDPIFYQHLFWFFGHPEVYILIIPAF-GIISIIISGILQKI 239
Cdd:cd01663  178 SVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFgIISHIISTFSGKKP 257

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 315571921 240 IFGNQSMIYAMSCISLLGSVVWGHHMYTVGLETDTRAYFTGVTILISLPTGTKIFNWLSTYLG-----NPPLL 307
Cdd:cd01663  258 VFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGgsikfETPML 330
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-307 5.29e-109

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 326.05  E-value: 5.29e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921   1 TLISVLIRIELYSSGNRIispENQNFYNISITLHGFLMIFFLIMPGLFGGFGNYFVPIFQGSPEVVYPRVNNFSILILSL 80
Cdd:MTH00153  29 TSLSLLIRAELGQPGSLI---GDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPP 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921  81 SYLFLILSLISEFGGGTGWTLYPPLStSFMSLSPSSTGNLIFGLLISGISSCLTSLNFWTTILNLRSYYLTLKTMPLFPW 160
Cdd:MTH00153 106 SLTLLLSSSMVESGAGTGWTVYPPLS-SNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVW 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921 161 ALLITGGMLLLTLPILSGALLMVLADLHSNTLFFDPIFGGDPIFYQHLFWFFGHPEVYILIIPAFGIISIIISGILQKI- 239
Cdd:MTH00153 185 SVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKe 264

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 315571921 240 IFGNQSMIYAMSCISLLGSVVWGHHMYTVGLETDTRAYFTGVTILISLPTGTKIFNWLSTYLG-----NPPLL 307
Cdd:MTH00153 265 TFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGsqinySPSLL 337
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 2-299 6.28e-89

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: 274.10  E-value: 6.28e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921    2 LISVLIRIELYSSGNRIISPEnqnFYNISITLHGFLMIFFLIMPgLFGGFGNYFVPIFQGSPEVVYPRVNNFSILILSLS 81
Cdd:TIGR02891  26 VLALLMRAQLATPGNTFMDAE---TYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLPLMIGARDMAFPRLNAFSYWLYLFG 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921   82 YLFLILSLISEFGGGTGWTLYPPLSTsfMSLSPSSTGNL-IFGLLISGISSCLTSLNFWTTILNLRSYYLTLKTMPLFPW 160
Cdd:TIGR02891 102 GLLLLASFFTGGAPDTGWTMYPPLSS--TSGSPGVGVDLwLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVW 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921  161 ALLITGGMLLLTLPILSGALLMVLADLHSNTLFFDPIFGGDPIFYQHLFWFFGHPEVYILIIPAFGIISIIISGILQKII 240
Cdd:TIGR02891 180 GILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKPI 259

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 315571921  241 FGNQSMIYAMSCISLLGSVVWGHHMYTVGLETDTRAYFTGVTILISLPTGTKIFNWLST 299
Cdd:TIGR02891 260 FGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIAT 318
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
4-306 5.92e-85

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 265.07  E-value: 5.92e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921   4 SVLIRIELYSSGNRIISPEnqnFYNISITLHGFLMIFFLIMPgLFGGFGNYFVPIFQGSPEVVYPRVNNFSILILSLSYL 83
Cdd:COG0843   37 ALLMRLQLAGPGLGLLSPE---TYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921  84 FLILSLISEFGGGTGWTLYPPLSTsfMSLSPSSTGNL-IFGLLISGISSCLTSLNFWTTILNLRSYYLTLKTMPLFPWAL 162
Cdd:COG0843  113 LLLISLFVGGAADVGWTFYPPLSG--LEASPGVGVDLwLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAA 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921 163 LITGGMLLLTLPILSGALLMVLADLHSNTLFFDPIFGGDPIFYQHLFWFFGHPEVYILIIPAFGIISIIISGILQKIIFG 242
Cdd:COG0843  191 LVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKPLFG 270

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 315571921 243 NQSMIYAMSCISLLGSVVWGHHMYTVGLETDTRAYFTGVTILISLPTGTKIFNWLST-YLGNPPL 306
Cdd:COG0843  271 YKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATmWRGRIRF 335
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-299 2.74e-60

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: 198.18  E-value: 2.74e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921    1 TLISVLIRIELYSSGNRIISPEnqnFYNISITLHGFLMIFFLIMPGLFGgFGNYFVPIFQGSPEVVYPRVNNFSILILSL 80
Cdd:pfam00115  18 GLLGLLIRLQLAFPGLNFLSPL---TYNQLRTLHGNLMIFWFATPFLFG-FGNYLVPLMIGARDMAFPRLNALSFWLVVL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921   81 SYLFLILSLIsefGGGTGWTLYPPLSTSFMslspsstgnLIFGLLISGISSCLTSLNFWTTILNLRSYYLTLKtMPLFPW 160
Cdd:pfam00115  94 GAVLLLASFG---GATTGWTEYPPLVGVDL---------WYIGLLLAGVSSLLGAINFIVTILKRRAPGMTLR-MPLFVW 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921  161 ALLITGGMLLLTLPILSGALLMVLADLHSNTLffdpifGGDPIFYQHLFWFFGHPEVYILIIPAFGIISIIISGILQKII 240
Cdd:pfam00115 161 AILATAILILLAFPVLAAALLLLLLDRSLGAG------GGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRPL 234

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 315571921  241 FGNQSMIYAMSCISLLGSVVWGHHMYTVGLETDTRAYFTGVTILISLPTGTKIFNWLST 299
Cdd:pfam00115 235 FGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLAT 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 ...
 1-307 3.16e-121

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: 356.41  E-value: 3.16e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921   1 TLISVLIRIELYSSGNRIISPEnqnFYNISITLHGFLMIFFLIMPGLFGGFGNYFVPIFQGSPEVVYPRVNNFSILILSL 80
Cdd:cd01663   22 TSLSLLIRLELSQPGSQLGNDQ---LYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPP 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921  81 SYLFLILSLISEFGGGTGWTLYPPLSTSfMSLSPSSTGNLIFGLLISGISSCLTSLNFWTTILNLRSYYLTLKTMPLFPW 160
Cdd:cd01663   99 SLLLLLLSALVEGGAGTGWTVYPPLSSI-LAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVW 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921 161 ALLITGGMLLLTLPILSGALLMVLADLHSNTLFFDPIFGGDPIFYQHLFWFFGHPEVYILIIPAF-GIISIIISGILQKI 239
Cdd:cd01663  178 SVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFgIISHIISTFSGKKP 257

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 315571921 240 IFGNQSMIYAMSCISLLGSVVWGHHMYTVGLETDTRAYFTGVTILISLPTGTKIFNWLSTYLG-----NPPLL 307
Cdd:cd01663  258 VFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGgsikfETPML 330
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-307 5.29e-109

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 326.05  E-value: 5.29e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921   1 TLISVLIRIELYSSGNRIispENQNFYNISITLHGFLMIFFLIMPGLFGGFGNYFVPIFQGSPEVVYPRVNNFSILILSL 80
Cdd:MTH00153  29 TSLSLLIRAELGQPGSLI---GDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPP 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921  81 SYLFLILSLISEFGGGTGWTLYPPLStSFMSLSPSSTGNLIFGLLISGISSCLTSLNFWTTILNLRSYYLTLKTMPLFPW 160
Cdd:MTH00153 106 SLTLLLSSSMVESGAGTGWTVYPPLS-SNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVW 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921 161 ALLITGGMLLLTLPILSGALLMVLADLHSNTLFFDPIFGGDPIFYQHLFWFFGHPEVYILIIPAFGIISIIISGILQKI- 239
Cdd:MTH00153 185 SVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKe 264

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 315571921 240 IFGNQSMIYAMSCISLLGSVVWGHHMYTVGLETDTRAYFTGVTILISLPTGTKIFNWLSTYLG-----NPPLL 307
Cdd:MTH00153 265 TFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGsqinySPSLL 337
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-302 7.85e-107

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 320.39  E-value: 7.85e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921   1 TLISVLIRIELYSSGNRIISPEnqnFYNISITLHGFLMIFFLIMPGLFGGFGNYFVPIFQGSPEVVYPRVNNFSILILSL 80
Cdd:MTH00223  28 TSLSLLIRAELGQPGALLGDDQ---LYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPP 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921  81 SYLFLILSLISEFGGGTGWTLYPPLStSFMSLSPSSTGNLIFGLLISGISSCLTSLNFWTTILNLRSYYLTLKTMPLFPW 160
Cdd:MTH00223 105 SLYLLLSSSAVESGVGTGWTVYPPLS-SNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVW 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921 161 ALLITGGMLLLTLPILSGALLMVLADLHSNTLFFDPIFGGDPIFYQHLFWFFGHPEVYILIIPAFGIISIIISGILQKI- 239
Cdd:MTH00223 184 SVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKe 263

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 315571921 240 IFGNQSMIYAMSCISLLGSVVWGHHMYTVGLETDTRAYFTGVTILISLPTGTKIFNWLSTYLG 302
Cdd:MTH00223 264 VFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYG 326
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-304 1.07e-99

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 302.37  E-value: 1.07e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921   1 TLISVLIRIELYSSGNRIispENQNFYNISITLHGFLMIFFLIMPGLFGGFGNYFVPIFQGSPEVVYPRVNNFSILILSL 80
Cdd:MTH00167  31 TALSLLIRAELSQPGSLL---GDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPP 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921  81 SYLFLILSLISEFGGGTGWTLYPPLStSFMSLSPSSTGNLIFGLLISGISSCLTSLNFWTTILNLRSYYLTLKTMPLFPW 160
Cdd:MTH00167 108 SLLLLLASSGVEAGAGTGWTVYPPLA-GNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVW 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921 161 ALLITGGMLLLTLPILSGALLMVLADLHSNTLFFDPIFGGDPIFYQHLFWFFGHPEVYILIIPAF-GIISIIISGILQKI 239
Cdd:MTH00167 187 SILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFgMISHIVVYYSGKKE 266

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 315571921 240 IFGNQSMIYAMSCISLLGSVVWGHHMYTVGLETDTRAYFTGVTILISLPTGTKIFNWLSTYLGNP 304
Cdd:MTH00167 267 PFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGK 331
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-302 2.07e-97

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 296.21  E-value: 2.07e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921   1 TLISVLIRIELYSSGnriISPENQNFYNISITLHGFLMIFFLIMPGLFGGFGNYFVPIFQGSPEVVYPRVNNFSILILSL 80
Cdd:MTH00079  32 TSLSLIIRLELSKPG---LLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPT 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921  81 SYLFLILSLISEFGGGTGWTLYPPLSTsfMSLSPSSTGNLIFGLLISGISSCLTSLNFWTTILNLRSYYLTLKTMPLFPW 160
Cdd:MTH00079 109 SLFLILDSCFVDMGPGTSWTVYPPLST--LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVW 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921 161 ALLITGGMLLLTLPILSGALLMVLADLHSNTLFFDPIFGGDPIFYQHLFWFFGHPEVYILIIPAFGIISIIISGIL-QKI 239
Cdd:MTH00079 187 TVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTgKKE 266

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 315571921 240 IFGNQSMIYAMSCISLLGSVVWGHHMYTVGLETDTRAYFTGVTILISLPTGTKIFNWLSTYLG 302
Cdd:MTH00079 267 VFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFG 329
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-307 2.37e-96

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 293.55  E-value: 2.37e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921   1 TLISVLIRIELYSSGNRIispENQNFYNISITLHGFLMIFFLIMPGLFGGFGNYFVPIFQGSPEVVYPRVNNFSILILSL 80
Cdd:MTH00142  29 TGLSLLIRAELGQPGSLL---GDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPP 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921  81 SYLFLILSLISEFGGGTGWTLYPPLStSFMSLSPSSTGNLIFGLLISGISSCLTSLNFWTTILNLRSYYLTLKTMPLFPW 160
Cdd:MTH00142 106 ALLLLLSSAAVESGAGTGWTVYPPLS-SNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVW 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921 161 ALLITGGMLLLTLPILSGALLMVLADLHSNTLFFDPIFGGDPIFYQHLFWFFGHPEVYILIIPAF-GIISIIISGILQKI 239
Cdd:MTH00142 185 SVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFgMISHIINHYSGKKE 264

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 315571921 240 IFGNQSMIYAMSCISLLGSVVWGHHMYTVGLETDTRAYFTGVTILISLPTGTKIFNWLSTYLGN-----PPLL 307
Cdd:MTH00142 265 VFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSkvkyePPML 337
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-302 2.01e-95

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 291.23  E-value: 2.01e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921   1 TLISVLIRIELYSSGNRIispENQNFYNISITLHGFLMIFFLIMPGLFGGFGNYFVPIFQGSPEVVYPRVNNFSILILSL 80
Cdd:MTH00116  31 TALSLLIRAELGQPGTLL---GDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPP 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921  81 SYLFLILSLISEFGGGTGWTLYPPLSTSfMSLSPSSTGNLIFGLLISGISSCLTSLNFWTTILNLRSYYLTLKTMPLFPW 160
Cdd:MTH00116 108 SFLLLLASSTVEAGAGTGWTVYPPLAGN-LAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVW 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921 161 ALLITGGMLLLTLPILSGALLMVLADLHSNTLFFDPIFGGDPIFYQHLFWFFGHPEVYILIIPAFGIISIIISGIL-QKI 239
Cdd:MTH00116 187 SVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAgKKE 266

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 315571921 240 IFGNQSMIYAMSCISLLGSVVWGHHMYTVGLETDTRAYFTGVTILISLPTGTKIFNWLSTYLG 302
Cdd:MTH00116 267 PFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHG 329
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-307 2.19e-93

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: 284.42  E-value: 2.19e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921   1 TLISVLIRIELYSSGNRIISPEnqnFYNISITLHGFLMIFFLIMPGLFGGFGNYFVPIFqGSPEVVYPRVNNFSILILSL 80
Cdd:cd00919   20 GLLALLIRLELATPGSLFLDPQ---LYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPPLI-GARDLAFPRLNNLSFWLFPP 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921  81 SYLFLILSLISEFGGGTGWTLYPPLSTSFMSLSPSStGNLIFGLLISGISSCLTSLNFWTTILNLRSYYLTLKTMPLFPW 160
Cdd:cd00919   96 GLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGV-DLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVW 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921 161 ALLITGGMLLLTLPILSGALLMVLADLHSNTLFFDPIFGGDPIFYQHLFWFFGHPEVYILIIPAFGIISIIISGILQKII 240
Cdd:cd00919  175 SVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFSGKPL 254

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 315571921 241 FGNQSMIYAMSCISLLGSVVWGHHMYTVGLETDTRAYFTGVTILISLPTGTKIFNWLSTYLG-----NPPLL 307
Cdd:cd00919  255 FGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGgrirfDPPML 326
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-304 5.36e-92

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 282.56  E-value: 5.36e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921   1 TLISVLIRIELYSSGNRIISPEnqnFYNISITLHGFLMIFFLIMPGLFGGFGNYFVPIFQGSPEVVYPRVNNFSILILSL 80
Cdd:MTH00007  28 TSMSLLIRIELGQPGAFLGSDQ---LYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPP 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921  81 SYLFLILSLISEFGGGTGWTLYPPLSTSFMSLSPSsTGNLIFGLLISGISSCLTSLNFWTTILNLRSYYLTLKTMPLFPW 160
Cdd:MTH00007 105 ALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPS-VDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVW 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921 161 ALLITGGMLLLTLPILSGALLMVLADLHSNTLFFDPIFGGDPIFYQHLFWFFGHPEVYILIIPAFGIISIIISGILQKI- 239
Cdd:MTH00007 184 AVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGKLe 263

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 315571921 240 IFGNQSMIYAMSCISLLGSVVWGHHMYTVGLETDTRAYFTGVTILISLPTGTKIFNWLSTYLGNP 304
Cdd:MTH00007 264 PFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSP 328
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-302 1.56e-91

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 281.33  E-value: 1.56e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921   1 TLISVLIRIELYSSGNRIispENQNFYNISITLHGFLMIFFLIMPGLFGGFGNYFVPIFQGSPEVVYPRVNNFSILILSL 80
Cdd:MTH00184  33 TAFSMLIRLELSAPGSML---GDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPP 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921  81 SYLFLILSLISEFGGGTGWTLYPPLStSFMSLSPSSTGNLIFGLLISGISSCLTSLNFWTTILNLRSYYLTLKTMPLFPW 160
Cdd:MTH00184 110 ALTLLLGSAFVEQGAGTGWTVYPPLS-SIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVW 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921 161 ALLITGGMLLLTLPILSGALLMVLADLHSNTLFFDPIFGGDPIFYQHLFWFFGHPEVYILIIPAF-GIISIIISGILQKI 239
Cdd:MTH00184 189 SILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFgIISQIIPTFAAKKQ 268

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 315571921 240 IFGNQSMIYAMSCISLLGSVVWGHHMYTVGLETDTRAYFTGVTILISLPTGTKIFNWLSTYLG 302
Cdd:MTH00184 269 IFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFG 331
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 2-299 6.28e-89

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: 274.10  E-value: 6.28e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921    2 LISVLIRIELYSSGNRIISPEnqnFYNISITLHGFLMIFFLIMPgLFGGFGNYFVPIFQGSPEVVYPRVNNFSILILSLS 81
Cdd:TIGR02891  26 VLALLMRAQLATPGNTFMDAE---TYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLPLMIGARDMAFPRLNAFSYWLYLFG 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921   82 YLFLILSLISEFGGGTGWTLYPPLSTsfMSLSPSSTGNL-IFGLLISGISSCLTSLNFWTTILNLRSYYLTLKTMPLFPW 160
Cdd:TIGR02891 102 GLLLLASFFTGGAPDTGWTMYPPLSS--TSGSPGVGVDLwLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVW 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921  161 ALLITGGMLLLTLPILSGALLMVLADLHSNTLFFDPIFGGDPIFYQHLFWFFGHPEVYILIIPAFGIISIIISGILQKII 240
Cdd:TIGR02891 180 GILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKPI 259

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 315571921  241 FGNQSMIYAMSCISLLGSVVWGHHMYTVGLETDTRAYFTGVTILISLPTGTKIFNWLST 299
Cdd:TIGR02891 260 FGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIAT 318
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-302 1.26e-88

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 274.01  E-value: 1.26e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921   1 TLISVLIRIELYSSGNRIispENQNFYNISITLHGFLMIFFLIMPGLFGGFGNYFVPIFQGSPEVVYPRVNNFSILILSL 80
Cdd:MTH00182  33 TAFSMLIRLELSAPGAML---GDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPP 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921  81 SYLFLILSLISEFGGGTGWTLYPPLStSFMSLSPSSTGNLIFGLLISGISSCLTSLNFWTTILNLRSYYLTLKTMPLFPW 160
Cdd:MTH00182 110 ALILLLGSAFVEQGAGTGWTVYPPLS-SIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVW 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921 161 ALLITGGMLLLTLPILSGALLMVLADLHSNTLFFDPIFGGDPIFYQHLFWFFGHPEVYILIIPAFGIISIII-SGILQKI 239
Cdd:MTH00182 189 SILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIpTFVAKKQ 268

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 315571921 240 IFGNQSMIYAMSCISLLGSVVWGHHMYTVGLETDTRAYFTGVTILISLPTGTKIFNWLSTYLG 302
Cdd:MTH00182 269 IFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYG 331
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-302 2.64e-88

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 272.91  E-value: 2.64e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921   1 TLISVLIRIELYSSGNRIispENQNFYNISITLHGFLMIFFLIMPGLFGGFGNYFVPIFQGSPEVVYPRVNNFSILILSL 80
Cdd:MTH00103  31 TALSLLIRAELGQPGTLL---GDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPP 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921  81 SYLFLILSLISEFGGGTGWTLYPPLSTSfMSLSPSSTGNLIFGLLISGISSCLTSLNFWTTILNLRSYYLTLKTMPLFPW 160
Cdd:MTH00103 108 SFLLLLASSMVEAGAGTGWTVYPPLAGN-LAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVW 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921 161 ALLITGGMLLLTLPILSGALLMVLADLHSNTLFFDPIFGGDPIFYQHLFWFFGHPEVYILIIPAFGIISIIISGIL-QKI 239
Cdd:MTH00103 187 SVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSgKKE 266

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 315571921 240 IFGNQSMIYAMSCISLLGSVVWGHHMYTVGLETDTRAYFTGVTILISLPTGTKIFNWLSTYLG 302
Cdd:MTH00103 267 PFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHG 329
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-302 9.25e-88

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 271.81  E-value: 9.25e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921   1 TLISVLIRIELYSSGNRIispENQNFYNISITLHGFLMIFFLIMPGLFGGFGNYFVPIFQGSPEVVYPRVNNFSILILSL 80
Cdd:MTH00077  31 TALSLLIRAELSQPGTLL---GDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPP 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921  81 SYLFLILSLISEFGGGTGWTLYPPLSTSFMSLSPSsTGNLIFGLLISGISSCLTSLNFWTTILNLRSYYLTLKTMPLFPW 160
Cdd:MTH00077 108 SFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGAS-VDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVW 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921 161 ALLITGGMLLLTLPILSGALLMVLADLHSNTLFFDPIFGGDPIFYQHLFWFFGHPEVYILIIPAF-GIISIIISGILQKI 239
Cdd:MTH00077 187 SVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFgMISHIVTYYSAKKE 266

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 315571921 240 IFGNQSMIYAMSCISLLGSVVWGHHMYTVGLETDTRAYFTGVTILISLPTGTKIFNWLSTYLG 302
Cdd:MTH00077 267 PFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHG 329
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-302 1.47e-87

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 271.03  E-value: 1.47e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921   1 TLISVLIRIELYSSGNRIispENQNFYNISITLHGFLMIFFLIMPGLFGGFGNYFVPIFQGSPEVVYPRVNNFSILILSL 80
Cdd:MTH00183  31 TALSLLIRAELSQPGALL---GDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPP 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921  81 SYLFLILSLISEFGGGTGWTLYPPLSTSFMSLSPSsTGNLIFGLLISGISSCLTSLNFWTTILNLRSYYLTLKTMPLFPW 160
Cdd:MTH00183 108 SFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGAS-VDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVW 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921 161 ALLITGGMLLLTLPILSGALLMVLADLHSNTLFFDPIFGGDPIFYQHLFWFFGHPEVYILIIPAFGIISIIISGIL-QKI 239
Cdd:MTH00183 187 AVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSgKKE 266

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 315571921 240 IFGNQSMIYAMSCISLLGSVVWGHHMYTVGLETDTRAYFTGVTILISLPTGTKIFNWLSTYLG 302
Cdd:MTH00183 267 PFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHG 329
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-307 4.37e-86

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 267.47  E-value: 4.37e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921   1 TLISVLIRIELYSSGNRIispENQNFYNISITLHGFLMIFFLIMPGLFGGFGNYFVPIFQGSPEVVYPRVNNFSILILSL 80
Cdd:MTH00037  31 TAMSVIIRTELAQPGSLL---QDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPP 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921  81 SYLFLILSLISEFGGGTGWTLYPPLStSFMSLSPSSTGNLIFGLLISGISSCLTSLNFWTTILNLRSYYLTLKTMPLFPW 160
Cdd:MTH00037 108 SFLLLLASAGVESGAGTGWTIYPPLS-SNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVW 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921 161 ALLITGGMLLLTLPILSGALLMVLADLHSNTLFFDPIFGGDPIFYQHLFWFFGHPEVYILIIPAFGIISIIISGILQKI- 239
Cdd:MTH00037 187 SVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKQe 266

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 315571921 240 IFGNQSMIYAMSCISLLGSVVWGHHMYTVGLETDTRAYFTGVTILISLPTGTKIFNWLSTYLG-----NPPLL 307
Cdd:MTH00037 267 PFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGsnlrwETPLL 339
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
4-306 5.92e-85

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 265.07  E-value: 5.92e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921   4 SVLIRIELYSSGNRIISPEnqnFYNISITLHGFLMIFFLIMPgLFGGFGNYFVPIFQGSPEVVYPRVNNFSILILSLSYL 83
Cdd:COG0843   37 ALLMRLQLAGPGLGLLSPE---TYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921  84 FLILSLISEFGGGTGWTLYPPLSTsfMSLSPSSTGNL-IFGLLISGISSCLTSLNFWTTILNLRSYYLTLKTMPLFPWAL 162
Cdd:COG0843  113 LLLISLFVGGAADVGWTFYPPLSG--LEASPGVGVDLwLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAA 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921 163 LITGGMLLLTLPILSGALLMVLADLHSNTLFFDPIFGGDPIFYQHLFWFFGHPEVYILIIPAFGIISIIISGILQKIIFG 242
Cdd:COG0843  191 LVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKPLFG 270

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 315571921 243 NQSMIYAMSCISLLGSVVWGHHMYTVGLETDTRAYFTGVTILISLPTGTKIFNWLST-YLGNPPL 306
Cdd:COG0843  271 YKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATmWRGRIRF 335
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-303 1.50e-83

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 261.49  E-value: 1.50e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921   1 TLISVLIRIELYSSGNRIispENQNFYNISITLHGFLMIFFLIMPGLFGGFGNYFVPIFQGSPEVVYPRVNNFSILILSL 80
Cdd:MTH00026  32 TAFSMLIRLELSSPGSML---GDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPP 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921  81 SYLFLILSLISEFGGGTGWTLYPPLStSFMSLSPSSTGNLIFGLLISGISSCLTSLNFWTTILNLRSYYLTLKTMPLFPW 160
Cdd:MTH00026 109 ALFLLLGSSLVEQGAGTGWTVYPPLA-SIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVW 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921 161 ALLITGGMLLLTLPILSGALLMVLADLHSNTLFFDPIFGGDPIFYQHLFWFFGHPEVYILIIPAF-GIISIIISGILQKI 239
Cdd:MTH00026 188 SVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFgIISQILSLFSYKKQ 267

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 315571921 240 IFGNQSMIYAMSCISLLGSVVWGHHMYTVGLETDTRAYFTGVTILISLPTGTKIFNWLSTYLGN 303
Cdd:MTH00026 268 IFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGS 331
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 5-299 3.01e-77

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: 244.03  E-value: 3.01e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921   5 VLIRIELYSSGNRIISPENqnfYNISITLHGFLMIFFLIMPgLFGGFGNYFVPIFQGSPEVVYPRVNNFSILILSLSYLF 84
Cdd:cd01662   30 LLMRTQLALPGNDFLSPEH---YNQIFTMHGTIMIFLFAMP-LVFGLMNYLVPLQIGARDVAFPRLNALSFWLFLFGGLL 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921  85 LILSLISEFGGGTGWTLYPPLSTsfMSLSPSSTGNL-IFGLLISGISSCLTSLNFWTTILNLRSYYLTLKTMPLFPWALL 163
Cdd:cd01662  106 LNASLLIGGFPDAGWFAYPPLSG--LEYSPGVGVDYwILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTL 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921 164 ITGGMLLLTLPILSGALLMVLADLHSNTLFFDPIFGGDPIFYQHLFWFFGHPEVYILIIPAFGIISIIISGILQKIIFGN 243
Cdd:cd01662  184 VTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFSRKPLFGY 263

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 315571921 244 QSMIYAMSCISLLGSVVWGHHMYTVGLETDTRAYFTGVTILISLPTGTKIFNWLST 299
Cdd:cd01662  264 RSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFT 319
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 3-302 9.95e-76

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 240.35  E-value: 9.95e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921   3 ISVLIRIELYSSGNRIISPEnqnFYNISITLHGFLMIFFLIMPGLFGGFGNYFVPIFQGSPEVVYPRVNNFSILILSLSY 82
Cdd:MTH00048  34 LSLLIRLNFLDPYYNVISLD---VYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSI 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921  83 LFLILSLIseFGGGTGWTLYPPLSTSFMSLSpSSTGNLIFGLLISGISSCLTSLNFWTTILNLRSYYLTLKTmPLFPWAL 162
Cdd:MTH00048 111 VFLLLSMC--LGAGVGWTFYPPLSSSLFSSS-WGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFSRT-SIILWSY 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921 163 LITGGMLLLTLPILSGALLMVLADLHSNTLFFDPIFGGDPIFYQHLFWFFGHPEVYILIIPAFGIISII-ISGILQKIIF 241
Cdd:MTH00048 187 LFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHIcLSLSNNDDPF 266

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 315571921 242 GNQSMIYAMSCISLLGSVVWGHHMYTVGLETDTRAYFTGVTILISLPTGTKIFNWLSTYLG 302
Cdd:MTH00048 267 GYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLN 327
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-299 2.74e-60

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: 198.18  E-value: 2.74e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921    1 TLISVLIRIELYSSGNRIISPEnqnFYNISITLHGFLMIFFLIMPGLFGgFGNYFVPIFQGSPEVVYPRVNNFSILILSL 80
Cdd:pfam00115  18 GLLGLLIRLQLAFPGLNFLSPL---TYNQLRTLHGNLMIFWFATPFLFG-FGNYLVPLMIGARDMAFPRLNALSFWLVVL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921   81 SYLFLILSLIsefGGGTGWTLYPPLSTSFMslspsstgnLIFGLLISGISSCLTSLNFWTTILNLRSYYLTLKtMPLFPW 160
Cdd:pfam00115  94 GAVLLLASFG---GATTGWTEYPPLVGVDL---------WYIGLLLAGVSSLLGAINFIVTILKRRAPGMTLR-MPLFVW 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921  161 ALLITGGMLLLTLPILSGALLMVLADLHSNTLffdpifGGDPIFYQHLFWFFGHPEVYILIIPAFGIISIIISGILQKII 240
Cdd:pfam00115 161 AILATAILILLAFPVLAAALLLLLLDRSLGAG------GGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRPL 234

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 315571921  241 FGNQSMIYAMSCISLLGSVVWGHHMYTVGLETDTRAYFTGVTILISLPTGTKIFNWLST 299
Cdd:pfam00115 235 FGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLAT 293
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 11-299 2.39e-51

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 179.36  E-value: 2.39e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921  11 LYSSGNRIISPENQnfYNISITLHGFLMIFFLIMPGLFGgFGNYFVPIFQGSPEVVYPRVNNFSILILSLSYLFLILSL- 89
Cdd:PRK15017  85 LASAGEAGFLPPHH--YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLg 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921  90 ISEFGGgTGWTLYPPLSTsfMSLSPS-STGNLIFGLLISGISSCLTSLNFWTTILNLRSYYLTLKTMPLFPWALLITGGM 168
Cdd:PRK15017 162 VGEFAQ-TGWLAYPPLSG--IEYSPGvGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVL 238

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315571921 169 LLLTLPILSGALLMVLADLHSNTLFFDPIFGGDPIFYQHLFWFFGHPEVYILIIPAFGIISIIISGILQKIIFGNQSMIY 248
Cdd:PRK15017 239 IIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFSRKRLFGYTSLVW 318

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 315571921 249 AMSCISLLGSVVWGHHMYTVGLETDTRAYFTGVTILISLPTGTKIFNWLST 299
Cdd:PRK15017 319 ATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFT 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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