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Conserved domains on  [gi|410736585|gb|AFV80466|]
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cytochrome oxidase subunit 3, partial (mitochondrion) [Zonaria flabellata]

Protein Classification

cytochrome c oxidase subunit 3( domain architecture ID 10009592)

cytochrome c oxidase subunit 3 is one of main transmembrane subunits of cytochrome c oxidase, the last enzyme in the respiratory electron transport chain of mitochondria or bacteria located in the mitochondrial or bacterial membrane

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 1-230 5.56e-89

cytochrome c oxidase subunit III; Provisional


:

Pssm-ID: 214439  Cd Length: 255  Bit Score: 262.81  E-value: 5.56e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585   1 VDPSPWPFVASIGALSLTFGGVMFMHNYSGgaQLLCLGVSTILYVMATWWRDIIREASFEGQHTSAVQEGLRIGMILFIV 80
Cdd:MTH00155   9 VDYSPWPLTGSIGAMTLTSGLIKWFHQFNM--NLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGMILFIV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585  81 SEIMFFFAFFWAFFTSSLAPVFNIGGVWPPVGIEVISPWGLPLLNTLLLLSSGATVTWAHHAIVGGLKYEAQTGLYLTLT 160
Cdd:MTH00155  87 SEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSLFFTII 166

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585 161 FAIYFTTFQFLEYLEAPFSMSDGVYGSTFFMATGFHGFHVLIGTIFLAICTIRLYYDHFSRQHHFGFEAA 230
Cdd:MTH00155 167 LGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAA 236
 
Name Accession Description Interval E-value
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 1-230 5.56e-89

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 262.81  E-value: 5.56e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585   1 VDPSPWPFVASIGALSLTFGGVMFMHNYSGgaQLLCLGVSTILYVMATWWRDIIREASFEGQHTSAVQEGLRIGMILFIV 80
Cdd:MTH00155   9 VDYSPWPLTGSIGAMTLTSGLIKWFHQFNM--NLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGMILFIV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585  81 SEIMFFFAFFWAFFTSSLAPVFNIGGVWPPVGIEVISPWGLPLLNTLLLLSSGATVTWAHHAIVGGLKYEAQTGLYLTLT 160
Cdd:MTH00155  87 SEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSLFFTII 166

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585 161 FAIYFTTFQFLEYLEAPFSMSDGVYGSTFFMATGFHGFHVLIGTIFLAICTIRLYYDHFSRQHHFGFEAA 230
Cdd:MTH00155 167 LGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAA 236
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 8-230 1.57e-88

Cytochrome c oxidase subunit III. 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. CcO 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, is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. 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 III contains bound phospholipids in several crystal structures and is proposed to contain a "lipid pool." These phospholipids are believed to intrinsic constituents similar to cofactors of the enzyme.


Pssm-ID: 238834  Cd Length: 243  Bit Score: 261.30  E-value: 1.57e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585   8 FVASIGALSLTFGGVMFMHNYSGGAqLLCLGVSTILYVMATWWRDIIREASFEGQHTSAVQEGLRIGMILFIVSEIMFFF 87
Cdd:cd01665    1 ILGSFGLLLLALGLVLWMHGYGGPL-LLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585  88 AFFWAFFTSSLAPVFNIGGVWPPVGIEVISPWGLPLLNTLLLLSSGATVTWAHHAIVGGLKYEAQTGLYLTLTFAIYFTT 167
Cdd:cd01665   80 SFFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTG 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 410736585 168 FQFLEYLEAPFSMSDGVYGSTFFMATGFHGFHVLIGTIFLAICTIRLYYDHFSRQHHFGFEAA 230
Cdd:cd01665  160 LQAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAA 222
COX3 pfam00510
Cytochrome c oxidase subunit III;
1-230 1.29e-84

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 251.95  E-value: 1.29e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585    1 VDPSPWPFVASIGALSLTFGGVMFMHNYSGGAQLLCLGVSTILYVMATWWRDIIREASFEGQHTSAVQEGLRIGMILFIV 80
Cdd:pfam00510   6 VSPSPWPLFGSFALLLLTSGLVLWFHGYSGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGMILFII 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585   81 SEIMFFFAFFWAFFTSSLAPVFNIGGVWPPVGIEVISPWGLPLLNTLLLLSSGATVTWAHHAIVGGLKYEAQTGLYLTLT 160
Cdd:pfam00510  86 SEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGLILTIL 165

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585  161 FAIYFTTFQFLEYLEAPFSMSDGVYGSTFFMATGFHGFHVLIGTIFLAICTIRLYYDHFSRQHHFGFEAA 230
Cdd:pfam00510 166 LAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAA 235
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
60-230 5.94e-25

Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];


Pssm-ID: 441450  Cd Length: 192  Bit Score: 96.84  E-value: 5.94e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585  60 EGQHTSAVQEGLRIGMILFIVSEIMFFFAFfwaffTSSLAPVFNIGGVWPPvGIEVISPWgLPLLNTLLLLSSGATVTWA 139
Cdd:COG1845    5 EAPHAPERRSPGKLGMWLFLASEVMLFAAL-----FAAYFVLRASAPDWPA-GAELLDLP-LPLINTLLLLLSSFTVALA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585 140 HHAIVGGLKYEAQTGLYLTLTFAIYFTTFQFLEY---LEAPFSMSDGVYGSTFFMATGFHGFHVLIGTIFLAICTIRLYY 216
Cdd:COG1845   78 VRAARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALR 157

                        170
                 ....*....|....
gi 410736585 217 DHFSRQHHFGFEAA 230
Cdd:COG1845  158 GGFTPENHTGVEAA 171
 
Name Accession Description Interval E-value
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 1-230 5.56e-89

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 262.81  E-value: 5.56e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585   1 VDPSPWPFVASIGALSLTFGGVMFMHNYSGgaQLLCLGVSTILYVMATWWRDIIREASFEGQHTSAVQEGLRIGMILFIV 80
Cdd:MTH00155   9 VDYSPWPLTGSIGAMTLTSGLIKWFHQFNM--NLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGMILFIV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585  81 SEIMFFFAFFWAFFTSSLAPVFNIGGVWPPVGIEVISPWGLPLLNTLLLLSSGATVTWAHHAIVGGLKYEAQTGLYLTLT 160
Cdd:MTH00155  87 SEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSLFFTII 166

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585 161 FAIYFTTFQFLEYLEAPFSMSDGVYGSTFFMATGFHGFHVLIGTIFLAICTIRLYYDHFSRQHHFGFEAA 230
Cdd:MTH00155 167 LGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAA 236
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 8-230 1.57e-88

Cytochrome c oxidase subunit III. 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. CcO 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, is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. 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 III contains bound phospholipids in several crystal structures and is proposed to contain a "lipid pool." These phospholipids are believed to intrinsic constituents similar to cofactors of the enzyme.


Pssm-ID: 238834  Cd Length: 243  Bit Score: 261.30  E-value: 1.57e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585   8 FVASIGALSLTFGGVMFMHNYSGGAqLLCLGVSTILYVMATWWRDIIREASFEGQHTSAVQEGLRIGMILFIVSEIMFFF 87
Cdd:cd01665    1 ILGSFGLLLLALGLVLWMHGYGGPL-LLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585  88 AFFWAFFTSSLAPVFNIGGVWPPVGIEVISPWGLPLLNTLLLLSSGATVTWAHHAIVGGLKYEAQTGLYLTLTFAIYFTT 167
Cdd:cd01665   80 SFFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTG 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 410736585 168 FQFLEYLEAPFSMSDGVYGSTFFMATGFHGFHVLIGTIFLAICTIRLYYDHFSRQHHFGFEAA 230
Cdd:cd01665  160 LQAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAA 222
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 1-230 1.69e-87

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 259.14  E-value: 1.69e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585   1 VDPSPWPFVASIGALSLTFGGVMFMHNYSGGaqLLCLGVSTILYVMATWWRDIIREASFEGQHTSAVQEGLRIGMILFIV 80
Cdd:MTH00189  10 VDPSPWPLTGAIAALLLTSGLAMWFHYNSFI--LLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRYGMILFIT 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585  81 SEIMFFFAFFWAFFTSSLAPVFNIGGVWPPVGIEVISPWGLPLLNTLLLLSSGATVTWAHHAIVGGLKYEAQTGLYLTLT 160
Cdd:MTH00189  88 SEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQALTLTVI 167

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585 161 FAIYFTTFQFLEYLEAPFSMSDGVYGSTFFMATGFHGFHVLIGTIFLAICTIRLYYDHFSRQHHFGFEAA 230
Cdd:MTH00189 168 LGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAA 237
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 1-230 5.59e-86

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 255.65  E-value: 5.59e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585   1 VDPSPWPFVASIGALSLTFGGVMFMHNYSggAQLLCLGVSTILYVMATWWRDIIREASFEGQHTSAVQEGLRIGMILFIV 80
Cdd:MTH00118  11 VDPSPWPLTGAMAALLLTSGLAMWFHYNS--TTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRYGMILFIT 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585  81 SEIMFFFAFFWAFFTSSLAPVFNIGGVWPPVGIEVISPWGLPLLNTLLLLSSGATVTWAHHAIVGGLKYEAQTGLYLTLT 160
Cdd:MTH00118  89 SEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQALTLTIL 168

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585 161 FAIYFTTFQFLEYLEAPFSMSDGVYGSTFFMATGFHGFHVLIGTIFLAICTIRLYYDHFSRQHHFGFEAA 230
Cdd:MTH00118 169 LGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAA 238
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 1-230 8.93e-86

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 254.82  E-value: 8.93e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585   1 VDPSPWPFVASIGALSLTFGGVMFMHNYSggAQLLCLGVSTILYVMATWWRDIIREASFEGQHTSAVQEGLRIGMILFIV 80
Cdd:MTH00141   9 VEFSPWPLTGSIGALFLTVGLVSWFHGGS--FLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFILFIV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585  81 SEIMFFFAFFWAFFTSSLAPVFNIGGVWPPVGIEVISPWGLPLLNTLLLLSSGATVTWAHHAIVGGLKYEAQTGLYLTLT 160
Cdd:MTH00141  87 SEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGLTII 166

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585 161 FAIYFTTFQFLEYLEAPFSMSDGVYGSTFFMATGFHGFHVLIGTIFLAICTIRLYYDHFSRQHHFGFEAA 230
Cdd:MTH00141 167 LGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAA 236
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 1-230 1.69e-85

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 254.29  E-value: 1.69e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585   1 VDPSPWPFVASIGALSLTFGGVMFMHnySGGAQLLCLGVSTILYVMATWWRDIIREASFEGQHTSAVQEGLRIGMILFIV 80
Cdd:MTH00024  11 VEPSPWPFLGAGGAFFITVGSVVYFH--YGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGMLLFIL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585  81 SEIMFFFAFFWAFFTSSLAPVFNIGGVWPPVGIEVISPWGLPLLNTLLLLSSGATVTWAHHAIVGGLKYEAQTGLYLTLT 160
Cdd:MTH00024  89 SEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFLTVF 168

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585 161 FAIYFTTFQFLEYLEAPFSMSDGVYGSTFFMATGFHGFHVLIGTIFLAICTIRLYYDHFSRQHHFGFEAA 230
Cdd:MTH00024 169 LGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAA 238
COX3 pfam00510
Cytochrome c oxidase subunit III;
1-230 1.29e-84

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 251.95  E-value: 1.29e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585    1 VDPSPWPFVASIGALSLTFGGVMFMHNYSGGAQLLCLGVSTILYVMATWWRDIIREASFEGQHTSAVQEGLRIGMILFIV 80
Cdd:pfam00510   6 VSPSPWPLFGSFALLLLTSGLVLWFHGYSGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGMILFII 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585   81 SEIMFFFAFFWAFFTSSLAPVFNIGGVWPPVGIEVISPWGLPLLNTLLLLSSGATVTWAHHAIVGGLKYEAQTGLYLTLT 160
Cdd:pfam00510  86 SEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGLILTIL 165

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585  161 FAIYFTTFQFLEYLEAPFSMSDGVYGSTFFMATGFHGFHVLIGTIFLAICTIRLYYDHFSRQHHFGFEAA 230
Cdd:pfam00510 166 LAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAA 235
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 1-230 2.22e-81

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 243.87  E-value: 2.22e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585   1 VDPSPWPFVASIGALSLTFGGVMFMHNYSggAQLLCLGVSTILYVMATWWRDIIREASFEGQHTSAVQEGLRIGMILFIV 80
Cdd:MTH00039  10 VDQSPWPLTAAIGALIMTSGLVLWFHGDS--ILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRYGMILFIT 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585  81 SEIMFFFAFFWAFFTSSLAPVFNIGGVWPPVGIEVISPWGLPLLNTLLLLSSGATVTWAHHAIVGGLKYEAQTGLYLTLT 160
Cdd:MTH00039  88 SEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQALFLTVL 167

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585 161 FAIYFTTFQFLEYLEAPFSMSDGVYGSTFFMATGFHGFHVLIGTIFLAICTIRLYYDHFSRQHHFGFEAA 230
Cdd:MTH00039 168 LGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAA 237
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 1-230 4.61e-81

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 243.16  E-value: 4.61e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585   1 VDPSPWPFVASIGALSLTFGGVMFMHnySGGAQLLCLGVSTILYVMATWWRDIIREASFEGQHTSAVQEGLRIGMILFIV 80
Cdd:MTH00052  12 VDPSPWPYIGGCGALFTTVGGVMYFH--YSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGLKYGMILFIV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585  81 SEIMFFFAFFWAFFTSSLAPVFNIGGVWPPVGIEVISPWGLPLLNTLLLLSSGATVTWAHHAIVGGLKYEAQTGLYLTLT 160
Cdd:MTH00052  90 SEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEAIIGLALTVA 169

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585 161 FAIYFTTFQFLEYLEAPFSMSDGVYGSTFFMATGFHGFHVLIGTIFLAICTIRLYYDHFSRQHHFGFEAA 230
Cdd:MTH00052 170 LGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAA 239
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 1-230 2.42e-78

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 236.22  E-value: 2.42e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585   1 VDPSPWPFVASIGALSLTFGGVMFMHNYSggAQLLCLGVSTILYVMATWWRDIIREASFEGQHTSAVQEGLRIGMILFIV 80
Cdd:MTH00219  12 VDYSPWPLTGSLGALMLTSGLVAWFHHYN--LDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLRIGMILFIV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585  81 SEIMFFFAFFWAFFTSSLAPVFNIGGVWPPVGIEVISPWGLPLLNTLLLLSSGATVTWAHHAIVGGLKYEAQTGLYLTLT 160
Cdd:MTH00219  90 SEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQQGLLFTIL 169

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585 161 FAIYFTTFQFLEYLEAPFSMSDGVYGSTFFMATGFHGFHVLIGTIFLAICTIRLYYDHFSRQHHFGFEAA 230
Cdd:MTH00219 170 LGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAA 239
PLN02194 PLN02194
cytochrome-c oxidase
 1-230 1.55e-76

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 231.86  E-value: 1.55e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585   1 VDPSPWPFVASIGALSLTFGGVMFMHNYSGGAQLLCLGVSTILYVMATWWRDIIREASFEGQHTSAVQEGLRIGMILFIV 80
Cdd:PLN02194  12 VDPSPWPISGSLGALATTVGGVMYMHPFQGGARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGPRYGSILFIV 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585  81 SEIMFFFAFFWAFFTSSLAPVFNIGGVWPPVGIEVISPWGLPLLNTLLLLSSGATVTWAHHAIVGGLKYEAQTGLYLTLT 160
Cdd:PLN02194  92 SEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEKRAVYALVATVL 171

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585 161 FAIYFTTFQFLEYLEAPFSMSDGVYGSTFFMATGFHGFHVLIGTIFLAICTIRLYYDHFSRQHHFGFEAA 230
Cdd:PLN02194 172 LALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAA 241
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 1-230 2.52e-76

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 231.19  E-value: 2.52e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585   1 VDPSPWPFVASIGALSLTFGGVMFMHNYSggAQLLCLGVSTILYVMATWWRDIIREASFEGQHTSAVQEGLRIGMILFIV 80
Cdd:MTH00130  11 VDPSPWPLTGAVAALLMTSGLAIWFHFHS--TTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRYGMILFIT 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585  81 SEIMFFFAFFWAFFTSSLAPVFNIGGVWPPVGIEVISPWGLPLLNTLLLLSSGATVTWAHHAIVGGLKYEAQTGLYLTLT 160
Cdd:MTH00130  89 SEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQSLTLTIL 168

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585 161 FAIYFTTFQFLEYLEAPFSMSDGVYGSTFFMATGFHGFHVLIGTIFLAICTIRLYYDHFSRQHHFGFEAA 230
Cdd:MTH00130 169 LGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAA 238
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 1-230 4.77e-76

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 230.38  E-value: 4.77e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585   1 VDPSPWPFVASIGALSLTFGGVMFMHNYSggAQLLCLGVSTILYVMATWWRDIIREASFEGQHTSAVQEGLRIGMILFIV 80
Cdd:MTH00099  11 VNPSPWPLTGALSALLMTSGLIMWFHFNS--TTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRYGMILFII 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585  81 SEIMFFFAFFWAFFTSSLAPVFNIGGVWPPVGIEVISPWGLPLLNTLLLLSSGATVTWAHHAIVGGLKYEAQTGLYLTLT 160
Cdd:MTH00099  89 SEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQALFITIL 168

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585 161 FAIYFTTFQFLEYLEAPFSMSDGVYGSTFFMATGFHGFHVLIGTIFLAICTIRLYYDHFSRQHHFGFEAA 230
Cdd:MTH00099 169 LGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAA 238
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 1-230 1.03e-74

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 226.94  E-value: 1.03e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585   1 VDPSPWPFVASIGALSLTFGGVMFMHnySGGAQLLCLGVSTILYVMATWWRDIIREASFEGQHTSAVQEGLRIGMILFIV 80
Cdd:MTH00075  11 VDPSPWPLTGAIAALLLTSGLAMWFH--FGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRYGMILFIT 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585  81 SEIMFFFAFFWAFFTSSLAPVFNIGGVWPPVGIEVISPWGLPLLNTLLLLSSGATVTWAHHAIVGGLKYEAQTGLYLTLT 160
Cdd:MTH00075  89 SEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQSLALTII 168

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585 161 FAIYFTTFQFLEYLEAPFSMSDGVYGSTFFMATGFHGFHVLIGTIFLAICTIRLYYDHFSRQHHFGFEAA 230
Cdd:MTH00075 169 LGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAA 238
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 1-230 5.65e-70

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 214.70  E-value: 5.65e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585   1 VDPSPWPFVASIGALSLTFGGVMFMHNYsgGAQLLCLGVSTILYVMATWWRDIIREASFEGQHTSAVQEGLRIGMILFIV 80
Cdd:MTH00009   9 VEYSPWPLTGSIGAFTLTVGLASWFHGY--GTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMILFIA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585  81 SEIMFFFAFFWAFFTSSLAPVFNIGGVWPPVGIEVISPWGLPLLNTLLLLSSGATVTWAHHAIVGGLKYEAQTGLYLTLT 160
Cdd:MTH00009  87 SEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALILTVL 166

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585 161 FAIYFTTFQFLEYLEAPFSMSDGVYGSTFFMATGFHGFHVLIGTIFLAICTIRLYYDHFSRQHHFGFEAA 230
Cdd:MTH00009 167 LGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAA 236
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 1-230 5.69e-64

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 200.68  E-value: 5.69e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585   1 VDPSPWPFVASIGALSLTFGGVMFMHnYSGgAQLLCLGVSTILYVMATWWRDIIREASFEGQHTSAVQEGLRIGMILFIV 80
Cdd:MTH00028  11 VDPSPWPFVGASGAFLFTSGAVILFH-YSD-YRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLLFIL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585  81 SEIMFFFAFFWAFFTSSLAPVFNIGGVWPPVGIEVISPWGLPLLNTLLLLSSGATVTWAHHAIVGG-------------- 146
Cdd:MTH00028  89 SEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTgnpaslekgtqgie 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585 147 ----------------------LKYEAQTGLYLTLTFAIYFTTFQFLEYLEAPFSMSDGVYGSTFFMATGFHGFHVLIGT 204
Cdd:MTH00028 169 gpnpsngappdpqkgptfllsdFRTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVLVGT 248

                        250       260
                 ....*....|....*....|....*.
gi 410736585 205 IFLAICTIRLYYDHFSRQHHFGFEAA 230
Cdd:MTH00028 249 TFLIVCFIRLLSNQFTNSHHLGLEAA 274
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
 4-228 1.18e-46

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 155.11  E-value: 1.18e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585   4 SPWPFVASIGALSLTFGGVMFMHNYSGGAQLLCLgvSTILYVMATWWRDIIREaSFEGQHTSAVQEGLRIGMILFIVSEI 83
Cdd:MTH00083  11 SSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSL--LYLLFISFLWGKDISME-GLSGYHNFFVMDGFKFGMILFIFSEF 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585  84 MFFFAFFWAFFTSSLAPVFNIGGVWPPVGIEVISPWGLPLLNTLLLLSSGATVTWAHHAIVGGLKyEAQTGLYLTLTFAI 163
Cdd:MTH00083  88 MFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSNK-SCTNSLLLTCFLGL 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 410736585 164 YFTTFQFLEYLEAPFSMSDGVYGSTFFMATGFHGFHVLIGTIFLAICTIRLYYDHFSRQHHFGFE 228
Cdd:MTH00083 167 YFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLE 231
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 63-230 8.40e-38

Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). 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. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. This group additionally contains proteins which are fusions between subunits I and III, such as Sulfolobus acidocaldarius SoxM, a subunit of the SoxM terminal oxidase complex. It also includes NorE which has been speculated to be a subunit of nitric oxide reductase. Some archaebacterial cytochrome oxidases lack subunit III. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria.


Pssm-ID: 238227  Cd Length: 183  Bit Score: 130.02  E-value: 8.40e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585  63 HTSAVQEGLRIGMILFIVSEIMFFFAFFWAFFTSSLAPVfniggVWPPVGIeviSPWGLPLLNTLLLLSSGATVTWAHHA 142
Cdd:cd00386    1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPP-----VEFGAGL---DPLDLPLLNTNTLLLSGSSVTWAHAS 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585 143 IVGGL--KYEAQTGLYLTLTFAIYFTTFQFLEYLEAPFSMSDGVYGSTFFMATGFHGFHVLIGTIFLAICTIRLYYDHFS 220
Cdd:cd00386   73 LAARRgnRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152

                        170
                 ....*....|
gi 410736585 221 RQHHFGFEAA 230
Cdd:cd00386  153 PRHHLGLEAA 162
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
60-230 5.94e-25

Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];


Pssm-ID: 441450  Cd Length: 192  Bit Score: 96.84  E-value: 5.94e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585  60 EGQHTSAVQEGLRIGMILFIVSEIMFFFAFfwaffTSSLAPVFNIGGVWPPvGIEVISPWgLPLLNTLLLLSSGATVTWA 139
Cdd:COG1845    5 EAPHAPERRSPGKLGMWLFLASEVMLFAAL-----FAAYFVLRASAPDWPA-GAELLDLP-LPLINTLLLLLSSFTVALA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585 140 HHAIVGGLKYEAQTGLYLTLTFAIYFTTFQFLEY---LEAPFSMSDGVYGSTFFMATGFHGFHVLIGTIFLAICTIRLYY 216
Cdd:COG1845   78 VRAARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALR 157

                        170
                 ....*....|....
gi 410736585 217 DHFSRQHHFGFEAA 230
Cdd:COG1845  158 GGFTPENHTGVEAA 171
NorE_like cd02862
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ...
 131-230 7.90e-07

NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include cytochrome c and ubiquinol oxidases. Alcaligenes faecalis norE is found in a gene cluster containing norCB. norCB encodes the cytochrome c and cytochrome b subunits of nitric oxide reductase (NOR). Based on this and on its similarity to subunit III of cytochrome c oxidase (CcO) and ubiquinol oxidase, NorE has been speculated to be a subunit of NOR.


Pssm-ID: 239213  Cd Length: 186  Bit Score: 47.62  E-value: 7.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585 131 SSGATVTWAHHAIVGGLKYEAQTGLYLTLTFAIYFTTFQFLEY---LEAPFSMSDGVYGSTFFMATGFHGFHVLIGTIFL 207
Cdd:cd02862   63 TSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYahkIAAGIDPDAGLFFTLYFLLTGFHLLHVLIGLGIL 142

                         90       100
                 ....*....|....*....|...
gi 410736585 208 AICTIRLYYDHFSRQHHFGFEAA 230
Cdd:cd02862  143 LWVAWRARRGRYSARDYEGVEAA 165
Heme_Cu_Oxidase_III_1 cd02864
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 131-221 1.86e-05

Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). 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. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria.


Pssm-ID: 239215  Cd Length: 202  Bit Score: 44.03  E-value: 1.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585 131 SSGATVTWAHHAIVGGLKYEAQTGLYLTLTFAIYFTTFQFLEYLEAPFSMSDG---------VYGSTFFMATGFHGFHVL 201
Cdd:cd02864   72 TSSGTMAMAVNFGYRGNRKAAARLMLATALLGATFVGMQAFEWTKLIVEEGVRpwgnpwgaaQFGASFFMITGFHGTHVT 151

                         90       100
                 ....*....|....*....|
gi 410736585 202 IGTIFLAICTIRLYYDHFSR 221
Cdd:cd02864  152 IGVIYLIIIARKVWRGKYQR 171
Ubiquinol_oxidase_III cd02863
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ...
 139-216 3.38e-04

Ubiquinol oxidase subunit III subfamily. 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. Ubiquinol oxidases feature four subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of bovine CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in bovine CcO. Although not required for catalytic activity, subunit III appears to be involved in assembly of the multimer complex.


Pssm-ID: 239214  Cd Length: 186  Bit Score: 40.30  E-value: 3.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410736585 139 AHHAIVGGLKYEAQTGLYLTLTFAIYFTTFQ---FLEYLEAPFSMSDGVYGSTFFMATGFHGFHVLIGTIFLAICTIRLY 215
Cdd:cd02863   70 AMIAMNKNNKKKVILWLIITFLLGLGFVGMEiyeFHHLIAEGAGPDRSAFLSAFFTLVGTHGLHVTFGLIWILVMIIQLK 149


                 .
gi 410736585 216 Y 216
Cdd:cd02863  150 K 150
 
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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