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Conserved domains on  [gi|2057278934|gb|QWY15129|]
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cytochrome c oxidase subunit 3, partial [Chorthippus parallelus erythropus]

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
 1-221 4.16e-128

cytochrome c oxidase subunit III; Provisional


:

Pssm-ID: 214439  Cd Length: 255  Bit Score: 361.42  E-value: 4.16e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278934   1 TGAIGAMVLVSGLVKWFHMFNINLFIIGFSITLLTMIQWWRDVIREGTYQGLHTGYVSIGLRWGMILFIASEVLFFFSFF 80
Cdd:MTH00155   17 TGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGMILFIVSEVFFFISFF 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278934  81 WAFFSSSLTPTIELGMLWPPMGIQPFNPMQIPLLNTVILLASGVTVTWAHHSIMESNHNQTLQGLFFTVMLGLYFTMLQT 160
Cdd:MTH00155   97 WAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSLFFTIILGIYFTMLQA 176

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2057278934 161 YEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTIFLTTCMTRHLMNQFSPNHHFGFEAAA 221
Cdd:MTH00155  177 YEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAA 237
 
Name Accession Description Interval E-value
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 1-221 4.16e-128

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 361.42  E-value: 4.16e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278934   1 TGAIGAMVLVSGLVKWFHMFNINLFIIGFSITLLTMIQWWRDVIREGTYQGLHTGYVSIGLRWGMILFIASEVLFFFSFF 80
Cdd:MTH00155   17 TGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGMILFIVSEVFFFISFF 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278934  81 WAFFSSSLTPTIELGMLWPPMGIQPFNPMQIPLLNTVILLASGVTVTWAHHSIMESNHNQTLQGLFFTVMLGLYFTMLQT 160
Cdd:MTH00155   97 WAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSLFFTIILGIYFTMLQA 176

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2057278934 161 YEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTIFLTTCMTRHLMNQFSPNHHFGFEAAA 221
Cdd:MTH00155  177 YEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAA 237
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-221 7.96e-99

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: 287.10  E-value: 7.96e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278934   1 TGAIGAMVLVSGLVKWFHMF-NINLFIIGFSITLLTMIQWWRDVIREGTYQGLHTGYVSIGLRWGMILFIASEVLFFFSF 79
Cdd:cd01665     2 LGSFGLLLLALGLVLWMHGYgGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFSF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278934  80 FWAFFSSSLTPTIELGMLWPPMGIQPFNPMQIPLLNTVILLASGVTVTWAHHSIMESNHNQTLQGLFFTVMLGLYFTMLQ 159
Cdd:cd01665    82 FWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGLQ 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2057278934 160 TYEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTIFLTTCMTRHLMNQFSPNHHFGFEAAA 221
Cdd:cd01665   162 AYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAI 223
COX3 pfam00510
Cytochrome c oxidase subunit III;
1-221 1.77e-94

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 276.60  E-value: 1.77e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278934   1 TGAIGAMVLVSGLVKWFHMF--NINLFIIGFSITLLTMIQWWRDVIREGTYQGLHTGYVSIGLRWGMILFIASEVLFFFS 78
Cdd:pfam00510  14 FGSFALLLLTSGLVLWFHGYsgNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGMILFIISEVFFFLG 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278934  79 FFWAFFSSSLTPTIELGMLWPPMGIQPFNPMQIPLLNTVILLASGVTVTWAHHSIMESNHNQTLQGLFFTVMLGLYFTML 158
Cdd:pfam00510  94 IFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGLILTILLAVYFTGL 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2057278934 159 QTYEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTIFLTTCMTRHLMNQFSPNHHFGFEAAA 221
Cdd:pfam00510 174 QAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAI 236
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
52-221 5.90e-33

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 117.26  E-value: 5.90e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278934  52 LHTGYVSIGLRWGMILFIASEVLFFFSFFWAFFSSSLTptielgMLWPPMGIQPFNPmQIPLLNTVILLASGVTVTWAHH 131
Cdd:COG1845     7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS------APDWPAGAELLDL-PLPLINTLLLLLSSFTVALAVR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278934 132 SIMESNHNQTLQGLFFTVMLGLYFTMLQTYEY---WEAPFTIADAVYGSTFFVATGFHGLHVIIGTIFLTTCMTRHLMNQ 208
Cdd:COG1845    80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159

                         170
                  ....*....|...
gi 2057278934 209 FSPNHHFGFEAAA 221
Cdd:COG1845   160 FTPENHTGVEAAA 172
 
Name Accession Description Interval E-value
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 1-221 4.16e-128

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 361.42  E-value: 4.16e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278934   1 TGAIGAMVLVSGLVKWFHMFNINLFIIGFSITLLTMIQWWRDVIREGTYQGLHTGYVSIGLRWGMILFIASEVLFFFSFF 80
Cdd:MTH00155   17 TGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGMILFIVSEVFFFISFF 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278934  81 WAFFSSSLTPTIELGMLWPPMGIQPFNPMQIPLLNTVILLASGVTVTWAHHSIMESNHNQTLQGLFFTVMLGLYFTMLQT 160
Cdd:MTH00155   97 WAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSLFFTIILGIYFTMLQA 176

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2057278934 161 YEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTIFLTTCMTRHLMNQFSPNHHFGFEAAA 221
Cdd:MTH00155  177 YEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAA 237
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 1-221 9.07e-108

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 310.34  E-value: 9.07e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278934   1 TGAIGAMVLVSGLVKWFHMFNINLFIIGFSITLLTMIQWWRDVIREGTYQGLHTGYVSIGLRWGMILFIASEVLFFFSFF 80
Cdd:MTH00118   19 TGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRYGMILFITSEVFFFLGFF 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278934  81 WAFFSSSLTPTIELGMLWPPMGIQPFNPMQIPLLNTVILLASGVTVTWAHHSIMESNHNQTLQGLFFTVMLGLYFTMLQT 160
Cdd:MTH00118   99 WAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQALTLTILLGLYFTALQA 178

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2057278934 161 YEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTIFLTTCMTRHLMNQFSPNHHFGFEAAA 221
Cdd:MTH00118  179 MEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAA 239
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 1-221 4.32e-105

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 303.43  E-value: 4.32e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278934   1 TGAIGAMVLVSGLVKWFHMFNINLFIIGFSITLLTMIQWWRDVIREGTYQGLHTGYVSIGLRWGMILFIASEVLFFFSFF 80
Cdd:MTH00189   18 TGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRYGMILFITSEVFFFLGFF 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278934  81 WAFFSSSLTPTIELGMLWPPMGIQPFNPMQIPLLNTVILLASGVTVTWAHHSIMESNHNQTLQGLFFTVMLGLYFTMLQT 160
Cdd:MTH00189   98 WAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQALTLTVILGVYFTLLQA 177

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2057278934 161 YEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTIFLTTCMTRHLMNQFSPNHHFGFEAAA 221
Cdd:MTH00189  178 MEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAA 238
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 1-221 7.19e-102

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 295.48  E-value: 7.19e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278934   1 TGAIGAMVLVSGLVKWFHMFNINLFIIGFSITLLTMIQWWRDVIREGTYQGLHTGYVSIGLRWGMILFIASEVLFFFSFF 80
Cdd:MTH00039   18 TAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRYGMILFITSEVCFFFAFF 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278934  81 WAFFSSSLTPTIELGMLWPPMGIQPFNPMQIPLLNTVILLASGVTVTWAHHSIMESNHNQTLQGLFFTVMLGLYFTMLQT 160
Cdd:MTH00039   98 WAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQALFLTVLLGLYFTALQA 177

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2057278934 161 YEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTIFLTTCMTRHLMNQFSPNHHFGFEAAA 221
Cdd:MTH00039  178 WEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAA 238
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 1-221 3.38e-101

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 294.00  E-value: 3.38e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278934   1 TGAIGAMVLVSGLVKWFHMFNINLFIIGFSITLLTMIQWWRDVIREGTYQGLHTGYVSIGLRWGMILFIASEVLFFFSFF 80
Cdd:MTH00219   20 TGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLRIGMILFIVSEILFFFAFF 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278934  81 WAFFSSSLTPTIELGMLWPPMGIQPFNPMQIPLLNTVILLASGVTVTWAHHSIMESNHNQTLQGLFFTVMLGLYFTMLQT 160
Cdd:MTH00219  100 WAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQQGLLFTILLGLYFTMLQG 179

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2057278934 161 YEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTIFLTTCMTRHLMNQFSPNHHFGFEAAA 221
Cdd:MTH00219  180 MEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAA 240
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 1-221 7.92e-100

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 290.25  E-value: 7.92e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278934   1 TGAIGAMVLVSGLVKWFHMFNINLFIIGFSITLLTMIQWWRDVIREGTYQGLHTGYVSIGLRWGMILFIASEVLFFFSFF 80
Cdd:MTH00141   17 TGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFILFIVSEVCFFFAFF 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278934  81 WAFFSSSLTPTIELGMLWPPMGIQPFNPMQIPLLNTVILLASGVTVTWAHHSIMESNHNQTLQGLFFTVMLGLYFTMLQT 160
Cdd:MTH00141   97 WAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGLTIILGVYFTFLQA 176

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2057278934 161 YEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTIFLTTCMTRHLMNQFSPNHHFGFEAAA 221
Cdd:MTH00141  177 GEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAA 237
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-221 7.96e-99

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: 287.10  E-value: 7.96e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278934   1 TGAIGAMVLVSGLVKWFHMF-NINLFIIGFSITLLTMIQWWRDVIREGTYQGLHTGYVSIGLRWGMILFIASEVLFFFSF 79
Cdd:cd01665     2 LGSFGLLLLALGLVLWMHGYgGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFSF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278934  80 FWAFFSSSLTPTIELGMLWPPMGIQPFNPMQIPLLNTVILLASGVTVTWAHHSIMESNHNQTLQGLFFTVMLGLYFTMLQ 159
Cdd:cd01665    82 FWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGLQ 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2057278934 160 TYEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTIFLTTCMTRHLMNQFSPNHHFGFEAAA 221
Cdd:cd01665   162 AYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAI 223
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 1-221 1.55e-98

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 287.03  E-value: 1.55e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278934   1 TGAIGAMVLVSGLVKWFHMFNINLFIIGFSITLLTMIQWWRDVIREGTYQGLHTGYVSIGLRWGMILFIASEVLFFFSFF 80
Cdd:MTH00075   19 TGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRYGMILFITSEVFFFLGFF 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278934  81 WAFFSSSLTPTIELGMLWPPMGIQPFNPMQIPLLNTVILLASGVTVTWAHHSIMESNHNQTLQGLFFTVMLGLYFTMLQT 160
Cdd:MTH00075   99 WAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQSLALTIILGLYFTLLQA 178

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2057278934 161 YEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTIFLTTCMTRHLMNQFSPNHHFGFEAAA 221
Cdd:MTH00075  179 MEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAA 239
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 1-221 6.50e-98

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 285.47  E-value: 6.50e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278934   1 TGAIGAMVLVSGLVKWFHMFNINLFIIGFSITLLTMIQWWRDVIREGTYQGLHTGYVSIGLRWGMILFIASEVLFFFSFF 80
Cdd:MTH00099   19 TGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRYGMILFIISEVFFFAGFF 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278934  81 WAFFSSSLTPTIELGMLWPPMGIQPFNPMQIPLLNTVILLASGVTVTWAHHSIMESNHNQTLQGLFFTVMLGLYFTMLQT 160
Cdd:MTH00099   99 WAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQALFITILLGLYFTLLQA 178

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2057278934 161 YEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTIFLTTCMTRHLMNQFSPNHHFGFEAAA 221
Cdd:MTH00099  179 SEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAA 239
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 1-221 1.56e-96

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 282.04  E-value: 1.56e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278934   1 TGAIGAMVLVSGLVKWFHMFNINLFIIGFSITLLTMIQWWRDVIREGTYQGLHTGYVSIGLRWGMILFIASEVLFFFSFF 80
Cdd:MTH00130   19 TGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRYGMILFITSEVFFFLGFF 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278934  81 WAFFSSSLTPTIELGMLWPPMGIQPFNPMQIPLLNTVILLASGVTVTWAHHSIMESNHNQTLQGLFFTVMLGLYFTMLQT 160
Cdd:MTH00130   99 WAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQSLTLTILLGFYFTFLQA 178

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2057278934 161 YEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTIFLTTCMTRHLMNQFSPNHHFGFEAAA 221
Cdd:MTH00130  179 MEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAA 239
COX3 pfam00510
Cytochrome c oxidase subunit III;
1-221 1.77e-94

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 276.60  E-value: 1.77e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278934   1 TGAIGAMVLVSGLVKWFHMF--NINLFIIGFSITLLTMIQWWRDVIREGTYQGLHTGYVSIGLRWGMILFIASEVLFFFS 78
Cdd:pfam00510  14 FGSFALLLLTSGLVLWFHGYsgNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGMILFIISEVFFFLG 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278934  79 FFWAFFSSSLTPTIELGMLWPPMGIQPFNPMQIPLLNTVILLASGVTVTWAHHSIMESNHNQTLQGLFFTVMLGLYFTML 158
Cdd:pfam00510  94 IFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGLILTILLAVYFTGL 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2057278934 159 QTYEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTIFLTTCMTRHLMNQFSPNHHFGFEAAA 221
Cdd:pfam00510 174 QAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAI 236
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 1-221 3.02e-92

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 270.94  E-value: 3.02e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278934   1 TGAIGAMVLVSGLVKWFHMFNINLFIIGFSITLLTMIQWWRDVIREGTYQGLHTGYVSIGLRWGMILFIASEVLFFFSFF 80
Cdd:MTH00009   17 TGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMILFIASEVMFFFAFF 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278934  81 WAFFSSSLTPTIELGMLWPPMGIQPFNPMQIPLLNTVILLASGVTVTWAHHSIMESNHNQTLQGLFFTVMLGLYFTMLQT 160
Cdd:MTH00009   97 WAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALILTVLLGAYFTFLQA 176

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2057278934 161 YEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTIFLTTCMTRHLMNQFSPNHHFGFEAAA 221
Cdd:MTH00009  177 GEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAA 237
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 1-221 2.91e-85

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 253.52  E-value: 2.91e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278934   1 TGAIGAMVLVSGLVKWFHMFNINLFIIGFSITLLTMIQWWRDVIREGTYQGLHTGYVSIGLRWGMILFIASEVLFFFSFF 80
Cdd:MTH00024   19 LGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGMLLFILSEVLFFFSFF 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278934  81 WAFFSSSLTPTIELGMLWPPMGIQPFNPMQIPLLNTVILLASGVTVTWAHHSIMESNHNQTLQGLFFTVMLGLYFTMLQT 160
Cdd:MTH00024   99 WAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFLTVFLGVLFTGLQA 178

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2057278934 161 YEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTIFLTTCMTRHLMNQFSPNHHFGFEAAA 221
Cdd:MTH00024  179 IEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAAS 239
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 2-221 1.01e-79

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 239.31  E-value: 1.01e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278934   2 GAIGAMVLVSGLVKWFHMFNINLFIIGFSITLLTMIQWWRDVIREGTYQGLHTGYVSIGLRWGMILFIASEVLFFFSFFW 81
Cdd:MTH00052   21 GGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGLKYGMILFIVSEVCLFFSFFW 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278934  82 AFFSSSLTPTIELGMLWPPMGIQPFNPMQIPLLNTVILLASGVTVTWAHHSIMESNHNQTLQGLFFTVMLGLYFTMLQTY 161
Cdd:MTH00052  101 AFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEAIIGLALTVALGLLFTGLQAM 180

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278934 162 EYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTIFLTTCMTRHLMNQFSPNHHFGFEAAA 221
Cdd:MTH00052  181 EYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAA 240
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 2-220 3.39e-64

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 201.06  E-value: 3.39e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278934   2 GAIGAMVLVSGLVKWFHMFNINLFIIGFSITLLTMIQWWRDVIREGTYQGLHTGYVSIGLRWGMILFIASEVLFFFSFFW 81
Cdd:MTH00028   20 GASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLLFILSEVCLFFAFFW 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278934  82 AFFSSSLTPTIELGMLWPPMGIQPFNPMQIPLLNTVILLASGVTVTWAHHSIMESNHNQTLQ------------------ 143
Cdd:MTH00028  100 AFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTGNPASLEkgtqgiegpnpsngappd 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278934 144 ------------------GLFFTVMLGLYFTMLQTYEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTIFLTTCMTRHL 205
Cdd:MTH00028  180 pqkgptfllsdfrtnaviGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVLVGTTFLIVCFIRLL 259

                         250
                  ....*....|....*
gi 2057278934 206 MNQFSPNHHFGFEAA 220
Cdd:MTH00028  260 SNQFTNSHHLGLEAA 274
PLN02194 PLN02194
cytochrome-c oxidase
 1-221 2.92e-58

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 184.87  E-value: 2.92e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278934   1 TGAIGAMVLVSGLVKWFHMFN--INLFIIGFSITLLTMIQWWRDVIREGTYQGLHTGYVSIGLRWGMILFIASEVLFFFS 78
Cdd:PLN02194   20 SGSLGALATTVGGVMYMHPFQggARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGPRYGSILFIVSEVMFFFA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278934  79 FFWAFFSSSLTPTIELGMLWPPMGIQPFNPMQIPLLNTVILLASGVTVTWAHHSIMESNHNQTLQGLFFTVMLGLYFTML 158
Cdd:PLN02194  100 FFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEKRAVYALVATVLLALVFTGF 179

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2057278934 159 QTYEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTIFLTTCMTRHLMNQFSPNHHFGFEAAA 221
Cdd:PLN02194  180 QGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAA 242
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
 5-221 3.57e-49

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 161.28  E-value: 3.57e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278934   5 GAMVLVSGLVKWFHMFNINLFIIGFSITLLTMIQWWRDVIREGtYQGLHTGYVSIGLRWGMILFIASEVLFFFSFFWAFF 84
Cdd:MTH00083   20 SSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMILFIFSEFMFFFSIFWTFF 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278934  85 SSSLTPTIELGMLWPPMGIQPFNPMQIPLLNTVILLASGVTVTWAHHSIMESNhNQTLQGLFFTVMLGLYFTMLQTYEYW 164
Cdd:MTH00083   99 DAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSN-KSCTNSLLLTCFLGLYFTSFQLMEYK 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2057278934 165 EAPFTIADAVYGSTFFVATGFHGLHVIIGTIFLTTCMTRHLMNQFSPNHHFGFEAAA 221
Cdd:MTH00083  178 EASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAI 234
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 53-221 1.16e-44

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: 147.35  E-value: 1.16e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278934  53 HTGYVSIGLRWGMILFIASEVLFFFSFFWAFFSSSLTPTIELGMlwppmgiqPFNPMQIPLLNTVILLASGVTVTWAHHS 132
Cdd:cd00386     1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFGA--------GLDPLDLPLLNTNTLLLSGSSVTWAHAS 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278934 133 IMESNHN--QTLQGLFFTVMLGLYFTMLQTYEYWEAPFTIADAVYGSTFFVATGFHGLHVIIGTIFLTTCMTRHLMNQFS 210
Cdd:cd00386    73 LAARRGNrkKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152

                         170
                  ....*....|.
gi 2057278934 211 PNHHFGFEAAA 221
Cdd:cd00386   153 PRHHLGLEAAA 163
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
52-221 5.90e-33

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 117.26  E-value: 5.90e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278934  52 LHTGYVSIGLRWGMILFIASEVLFFFSFFWAFFSSSLTptielgMLWPPMGIQPFNPmQIPLLNTVILLASGVTVTWAHH 131
Cdd:COG1845     7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS------APDWPAGAELLDL-PLPLINTLLLLLSSFTVALAVR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278934 132 SIMESNHNQTLQGLFFTVMLGLYFTMLQTYEY---WEAPFTIADAVYGSTFFVATGFHGLHVIIGTIFLTTCMTRHLMNQ 208
Cdd:COG1845    80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159

                         170
                  ....*....|...
gi 2057278934 209 FSPNHHFGFEAAA 221
Cdd:COG1845   160 FTPENHTGVEAAA 172
NorE_like cd02862
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ...
 113-221 2.94e-12

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: 62.64  E-value: 2.94e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278934 113 LLNTVILLASGVTVTWAHHSIMESNHNQTLQGLFFTVMLGLYFTMLQTYEYWE---APFTIADAVYGSTFFVATGFHGLH 189
Cdd:cd02862    55 ALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYAHkiaAGIDPDAGLFFTLYFLLTGFHLLH 134

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2057278934 190 VIIGTIFLTTCMTRHLMNQFSPNHHFGFEAAA 221
Cdd:cd02862   135 VLIGLGILLWVAWRARRGRYSARDYEGVEAAA 166
Ubiquinol_oxidase_III cd02863
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ...
 113-201 1.42e-09

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: 55.32  E-value: 1.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278934 113 LLNTVILLASGVTVTWAHHSIMESNHNQTLQGLFFTVMLGLYFTMLQTYE---YWEAPFTIADAVYGSTFFVATGFHGLH 189
Cdd:cd02863    54 FIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLVGTHGLH 133

                          90
                  ....*....|..
gi 2057278934 190 VIIGTIFLTTCM 201
Cdd:cd02863   134 VTFGLIWILVMI 145
COX3 MTH00049
cytochrome c oxidase subunit III; Validated
 108-199 8.22e-09

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177124  Cd Length: 215  Bit Score: 53.77  E-value: 8.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278934 108 PMQIPLLNTVILLASGVTVTwAHHSIMESNHNQTLqgLFFTVMLGLYFTMLQTYEYWEAPFTIADAVYGSTFFVATGFHG 187
Cdd:MTH00049   89 SLEIPFVGCFLLLGSSITVT-AYHHLLGWKYCDLF--LYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHF 165

                          90
                  ....*....|..
gi 2057278934 188 LHVIIGTIFLTT 199
Cdd:MTH00049  166 SHVVLGVVGLST 177
Heme_Cu_Oxidase_III_1 cd02864
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 116-197 1.96e-06

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: 46.73  E-value: 1.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278934 116 TVILLASGVTVTWAHHSIMESNHNQTLQGLFFTVMLGLYFTMLQTYEY-----------WEAPFTIAdaVYGSTFFVATG 184
Cdd:cd02864    67 TFILITSSGTMAMAVNFGYRGNRKAAARLMLATALLGATFVGMQAFEWtkliveegvrpWGNPWGAA--QFGASFFMITG 144

                          90
                  ....*....|...
gi 2057278934 185 FHGLHVIIGTIFL 197
Cdd:cd02864   145 FHGTHVTIGVIYL 157
Heme_Cu_Oxidase_III_2 cd02865
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 112-197 2.04e-06

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: 239216  Cd Length: 184  Bit Score: 46.59  E-value: 2.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057278934 112 PLLNTVILLASGVTVTWAHHSIMESNHNQTLQGLFFTVMLGLYFTMLQTYEYWEAPF---TIADAVYGSTFFVATGFHGL 188
Cdd:cd02865    52 LSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWHALNDagyGPTSNPAGSFFYLLTGLHGL 131


                  ....*....
gi 2057278934 189 HVIIGTIFL 197
Cdd:cd02865   132 HVIGGLVAL 140
 
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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