|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00141 |
cytochrome c oxidase subunit III; Provisional |
1-258 |
7.71e-138 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177199 Cd Length: 259 Bit Score: 388.09 E-value: 7.71e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 1 MRQPFHLVEFSPWPLLISFSIFSMPIGLINYIRSSNISLLILGLFTTALISFLWWRDVVRESTYQGFHNKLVMKGLKIGI 80
Cdd:MTH00141 2 TRNPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 81 MLFILSEVCFFFAFFWAYFHSSLAPSVEIGAIWPPTGIFTLQAFQVPLLNTSVLLLSGVSITWVHHSIEEGNYKSAMQGL 160
Cdd:MTH00141 82 ILFIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 161 FITILLGLYFLMLQYGEYSETMFSISDGIYGSCLFMATGFHGTHVAVGATFLIVCFFRLKNFHFNKNHHIGFLAAAWYWH 240
Cdd:MTH00141 162 GLTIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWH 241
|
250
....*....|....*...
gi 168487804 241 FVDVVWLFLYVSIYWWGS 258
Cdd:MTH00141 242 FVDVVWLFLYLSIYWWGS 259
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
4-258 |
3.19e-108 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 313.19 E-value: 3.19e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 4 PFHLVEFSPWPLLISFSIFSMPIGLINYIR--SSNISLLILGLFTTALISFLWWRDVVRESTYQGFHNKLVMKGLKIGIM 81
Cdd:pfam00510 2 PFHMVSPSPWPLFGSFALLLLTSGLVLWFHgySGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGMI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 82 LFILSEVCFFFAFFWAYFHSSLAPSVEIGAIWPPTGIFTLQAFQVPLLNTSVLLLSGVSITWVHHSIEEGNYKSAMQGLF 161
Cdd:pfam00510 82 LFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGLI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 162 ITILLGLYFLMLQYGEYSETMFSISDGIYGSCLFMATGFHGTHVAVGATFLIVCFFRLKNFHFNKNHHIGFLAAAWYWHF 241
Cdd:pfam00510 162 LTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWHF 241
|
250
....*....|....*..
gi 168487804 242 VDVVWLFLYVSIYWWGS 258
Cdd:pfam00510 242 VDVVWLFLYVSVYWWGS 258
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
15-256 |
6.33e-106 |
|
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: 306.75 E-value: 6.33e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 15 LLISFSIFSMPIGLINYIR-SSNISLLILGLFTTALISFLWWRDVVRESTYQGFHNKLVMKGLKIGIMLFILSEVCFFFA 93
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHgYGGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 94 FFWAYFHSSLAPSVEIGAIWPPTGIFTLQAFQVPLLNTSVLLLSGVSITWVHHSIEEGNYKSAMQGLFITILLGLYFLML 173
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 174 QYGEYSETMFSISDGIYGSCLFMATGFHGTHVAVGATFLIVCFFRLKNFHFNKNHHIGFLAAAWYWHFVDVVWLFLYVSI 253
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 168487804 254 YWW 256
Cdd:cd01665 241 YWW 243
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
127-256 |
4.91e-41 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 139.60 E-value: 4.91e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 127 PLLNTSVLLLSGVSITWVHHSIEEGNYKSAMQGLFITILLGLYFLMLQYGEYSETM---FSISDGIYGSCLFMATGFHGT 203
Cdd:COG1845 60 PLINTLLLLLSSFTVALAVRAARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHLIaegLTPTSNAFGSFFFLLTGFHGL 139
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 168487804 204 HVAVGATFLIVCFFRLKNFHFNKNHHIGFLAAAWYWHFVDVVWLFLYVSIYWW 256
Cdd:COG1845 140 HVIIGLIWLLVVLVRALRGGFTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
114-257 |
1.16e-09 |
|
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]
Pssm-ID: 131943 Cd Length: 190 Bit Score: 56.40 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 114 PPTGIFTLQAFqvpLLNTSVLLLSGVSITWVHHSIEEGNYKSAMQGLFITILLGLYFL---MLQYGEYSETMFSISDGIY 190
Cdd:TIGR02897 45 MPAELFELPLV---LIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVgfeIYEFAHYASEGVTPQIGSY 121
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 168487804 191 GSCLFMATGFHGTHVAVGATFLIVCFFRLKNFHFNKNHHIGFLAAAWYWHFVDVVWLFLYVSIYWWG 257
Cdd:TIGR02897 122 WSSFFVLLGTHGCHVTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00141 |
cytochrome c oxidase subunit III; Provisional |
1-258 |
7.71e-138 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177199 Cd Length: 259 Bit Score: 388.09 E-value: 7.71e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 1 MRQPFHLVEFSPWPLLISFSIFSMPIGLINYIRSSNISLLILGLFTTALISFLWWRDVVRESTYQGFHNKLVMKGLKIGI 80
Cdd:MTH00141 2 TRNPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 81 MLFILSEVCFFFAFFWAYFHSSLAPSVEIGAIWPPTGIFTLQAFQVPLLNTSVLLLSGVSITWVHHSIEEGNYKSAMQGL 160
Cdd:MTH00141 82 ILFIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 161 FITILLGLYFLMLQYGEYSETMFSISDGIYGSCLFMATGFHGTHVAVGATFLIVCFFRLKNFHFNKNHHIGFLAAAWYWH 240
Cdd:MTH00141 162 GLTIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWH 241
|
250
....*....|....*...
gi 168487804 241 FVDVVWLFLYVSIYWWGS 258
Cdd:MTH00141 242 FVDVVWLFLYLSIYWWGS 259
|
|
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
1-254 |
3.82e-122 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 347.94 E-value: 3.82e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 1 MRQPFHLVEFSPWPLLISFSIFSMPIGLINYIRSSNISLLILGLFTTALISFLWWRDVVRESTYQGFHNKLVMKGLKIGI 80
Cdd:MTH00155 2 KNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 81 MLFILSEVCFFFAFFWAYFHSSLAPSVEIGAIWPPTGIFTLQAFQVPLLNTSVLLLSGVSITWVHHSIEEGNYKSAMQGL 160
Cdd:MTH00155 82 ILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 161 FITILLGLYFLMLQYGEYSETMFSISDGIYGSCLFMATGFHGTHVAVGATFLIVCFFRLKNFHFNKNHHIGFLAAAWYWH 240
Cdd:MTH00155 162 FFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYWH 241
|
250
....*....|....
gi 168487804 241 FVDVVWLFLYVSIY 254
Cdd:MTH00155 242 FVDVVWLFLYISIY 255
|
|
| COX3 |
MTH00189 |
cytochrome c oxidase subunit III; Provisional |
4-258 |
3.64e-117 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177238 Cd Length: 260 Bit Score: 335.79 E-value: 3.64e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 4 PFHLVEFSPWPLLISFSIFSMPIGLINYIRSSNISLLILGLFTTALISFLWWRDVVRESTYQGFHNKLVMKGLKIGIMLF 83
Cdd:MTH00189 6 PFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRYGMILF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 84 ILSEVCFFFAFFWAYFHSSLAPSVEIGAIWPPTGIFTLQAFQVPLLNTSVLLLSGVSITWVHHSIEEGNYKSAMQGLFIT 163
Cdd:MTH00189 86 ITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQALTLT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 164 ILLGLYFLMLQYGEYSETMFSISDGIYGSCLFMATGFHGTHVAVGATFLIVCFFRLKNFHFNKNHHIGFLAAAWYWHFVD 243
Cdd:MTH00189 166 VILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWYWHFVD 245
|
250
....*....|....*
gi 168487804 244 VVWLFLYVSIYWWGS 258
Cdd:MTH00189 246 VVWLFLYVSIYWWGS 260
|
|
| COX3 |
MTH00118 |
cytochrome c oxidase subunit III; Provisional |
4-258 |
1.12e-116 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177179 Cd Length: 261 Bit Score: 334.61 E-value: 1.12e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 4 PFHLVEFSPWPLLISFSIFSMPIGLINYIRSSNISLLILGLFTTALISFLWWRDVVRESTYQGFHNKLVMKGLKIGIMLF 83
Cdd:MTH00118 7 PYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRYGMILF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 84 ILSEVCFFFAFFWAYFHSSLAPSVEIGAIWPPTGIFTLQAFQVPLLNTSVLLLSGVSITWVHHSIEEGNYKSAMQGLFIT 163
Cdd:MTH00118 87 ITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQALTLT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 164 ILLGLYFLMLQYGEYSETMFSISDGIYGSCLFMATGFHGTHVAVGATFLIVCFFRLKNFHFNKNHHIGFLAAAWYWHFVD 243
Cdd:MTH00118 167 ILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWYWHFVD 246
|
250
....*....|....*
gi 168487804 244 VVWLFLYVSIYWWGS 258
Cdd:MTH00118 247 VVWLFLYISIYWWGS 261
|
|
| COX3 |
MTH00039 |
cytochrome c oxidase subunit III; Validated |
4-258 |
8.25e-112 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177114 Cd Length: 260 Bit Score: 322.06 E-value: 8.25e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 4 PFHLVEFSPWPLLISFSIFSMPIGLINYIRSSNISLLILGLFTTALISFLWWRDVVRESTYQGFHNKLVMKGLKIGIMLF 83
Cdd:MTH00039 6 PYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRYGMILF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 84 ILSEVCFFFAFFWAYFHSSLAPSVEIGAIWPPTGIFTLQAFQVPLLNTSVLLLSGVSITWVHHSIEEGNYKSAMQGLFIT 163
Cdd:MTH00039 86 ITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQALFLT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 164 ILLGLYFLMLQYGEYSETMFSISDGIYGSCLFMATGFHGTHVAVGATFLIVCFFRLKNFHFNKNHHIGFLAAAWYWHFVD 243
Cdd:MTH00039 166 VLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWYWHFVD 245
|
250
....*....|....*
gi 168487804 244 VVWLFLYVSIYWWGS 258
Cdd:MTH00039 246 VVWLFLYVCIYWWGS 260
|
|
| COX3 |
MTH00099 |
cytochrome c oxidase subunit III; Validated |
4-258 |
9.53e-112 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177161 Cd Length: 261 Bit Score: 322.06 E-value: 9.53e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 4 PFHLVEFSPWPLLISFSIFSMPIGLINYIRSSNISLLILGLFTTALISFLWWRDVVRESTYQGFHNKLVMKGLKIGIMLF 83
Cdd:MTH00099 7 AYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRYGMILF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 84 ILSEVCFFFAFFWAYFHSSLAPSVEIGAIWPPTGIFTLQAFQVPLLNTSVLLLSGVSITWVHHSIEEGNYKSAMQGLFIT 163
Cdd:MTH00099 87 IISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQALFIT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 164 ILLGLYFLMLQYGEYSETMFSISDGIYGSCLFMATGFHGTHVAVGATFLIVCFFRLKNFHFNKNHHIGFLAAAWYWHFVD 243
Cdd:MTH00099 167 ILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWYWHFVD 246
|
250
....*....|....*
gi 168487804 244 VVWLFLYVSIYWWGS 258
Cdd:MTH00099 247 VVWLFLYVSIYWWGS 261
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
4-258 |
3.19e-108 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 313.19 E-value: 3.19e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 4 PFHLVEFSPWPLLISFSIFSMPIGLINYIR--SSNISLLILGLFTTALISFLWWRDVVRESTYQGFHNKLVMKGLKIGIM 81
Cdd:pfam00510 2 PFHMVSPSPWPLFGSFALLLLTSGLVLWFHgySGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGMI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 82 LFILSEVCFFFAFFWAYFHSSLAPSVEIGAIWPPTGIFTLQAFQVPLLNTSVLLLSGVSITWVHHSIEEGNYKSAMQGLF 161
Cdd:pfam00510 82 LFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGLI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 162 ITILLGLYFLMLQYGEYSETMFSISDGIYGSCLFMATGFHGTHVAVGATFLIVCFFRLKNFHFNKNHHIGFLAAAWYWHF 241
Cdd:pfam00510 162 LTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWHF 241
|
250
....*....|....*..
gi 168487804 242 VDVVWLFLYVSIYWWGS 258
Cdd:pfam00510 242 VDVVWLFLYVSVYWWGS 258
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
15-256 |
6.33e-106 |
|
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: 306.75 E-value: 6.33e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 15 LLISFSIFSMPIGLINYIR-SSNISLLILGLFTTALISFLWWRDVVRESTYQGFHNKLVMKGLKIGIMLFILSEVCFFFA 93
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHgYGGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 94 FFWAYFHSSLAPSVEIGAIWPPTGIFTLQAFQVPLLNTSVLLLSGVSITWVHHSIEEGNYKSAMQGLFITILLGLYFLML 173
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 174 QYGEYSETMFSISDGIYGSCLFMATGFHGTHVAVGATFLIVCFFRLKNFHFNKNHHIGFLAAAWYWHFVDVVWLFLYVSI 253
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 168487804 254 YWW 256
Cdd:cd01665 241 YWW 243
|
|
| COX3 |
MTH00219 |
cytochrome c oxidase subunit III; Provisional |
2-258 |
1.51e-105 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214464 Cd Length: 262 Bit Score: 306.33 E-value: 1.51e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 2 RQPFHLVEFSPWPLLISFSIFSMPIGLINYIRSSNISLLILGLFTTALISFLWWRDVVRESTYQGFHNKLVMKGLKIGIM 81
Cdd:MTH00219 6 TNPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLRIGMI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 82 LFILSEVCFFFAFFWAYFHSSLAPSVEIGAIWPPTGIFTLQAFQVPLLNTSVLLLSGVSITWVHHSIEEGNYKSAMQGLF 161
Cdd:MTH00219 86 LFIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQQGLL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 162 ITILLGLYFLMLQYGEYSETMFSISDGIYGSCLFMATGFHGTHVAVGATFLIVCFFRLKNFHFNKNHHIGFLAAAWYWHF 241
Cdd:MTH00219 166 FTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAAWYWHF 245
|
250
....*....|....*..
gi 168487804 242 VDVVWLFLYVSIYWWGS 258
Cdd:MTH00219 246 VDVVWLFLYVSIYWWGS 262
|
|
| COX3 |
MTH00130 |
cytochrome c oxidase subunit III; Provisional |
4-258 |
7.34e-103 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177188 Cd Length: 261 Bit Score: 299.37 E-value: 7.34e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 4 PFHLVEFSPWPLLISFSIFSMPIGLINYIRSSNISLLILGLFTTALISFLWWRDVVRESTYQGFHNKLVMKGLKIGIMLF 83
Cdd:MTH00130 7 AYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRYGMILF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 84 ILSEVCFFFAFFWAYFHSSLAPSVEIGAIWPPTGIFTLQAFQVPLLNTSVLLLSGVSITWVHHSIEEGNYKSAMQGLFIT 163
Cdd:MTH00130 87 ITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQSLTLT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 164 ILLGLYFLMLQYGEYSETMFSISDGIYGSCLFMATGFHGTHVAVGATFLIVCFFRLKNFHFNKNHHIGFLAAAWYWHFVD 243
Cdd:MTH00130 167 ILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWYWHFVD 246
|
250
....*....|....*
gi 168487804 244 VVWLFLYVSIYWWGS 258
Cdd:MTH00130 247 VVWLFLYISIYWWGS 261
|
|
| COX3 |
MTH00075 |
cytochrome c oxidase subunit III; Provisional |
5-258 |
7.80e-102 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177146 Cd Length: 261 Bit Score: 297.04 E-value: 7.80e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 5 FHLVEFSPWPLLISFSIFSMPIGLINYIRSSNISLLILGLFTTALISFLWWRDVVRESTYQGFHNKLVMKGLKIGIMLFI 84
Cdd:MTH00075 8 FHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRYGMILFI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 85 LSEVCFFFAFFWAYFHSSLAPSVEIGAIWPPTGIFTLQAFQVPLLNTSVLLLSGVSITWVHHSIEEGNYKSAMQGLFITI 164
Cdd:MTH00075 88 TSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQSLALTI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 165 LLGLYFLMLQYGEYSETMFSISDGIYGSCLFMATGFHGTHVAVGATFLIVCFFRLKNFHFNKNHHIGFLAAAWYWHFVDV 244
Cdd:MTH00075 168 ILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWYWHFVDV 247
|
250
....*....|....
gi 168487804 245 VWLFLYVSIYWWGS 258
Cdd:MTH00075 248 VWLFLYVSIYWWGS 261
|
|
| COX3 |
MTH00024 |
cytochrome c oxidase subunit III; Validated |
4-258 |
6.69e-100 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 214403 Cd Length: 261 Bit Score: 292.04 E-value: 6.69e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 4 PFHLVEFSPWPLLISFSIFSMPIGLINYIRSSNISLLILGLFTTALISFLWWRDVVRESTYQGFHNKLVMKGLKIGIMLF 83
Cdd:MTH00024 7 PYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGMLLF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 84 ILSEVCFFFAFFWAYFHSSLAPSVEIGAIWPPTGIFTLQAFQVPLLNTSVLLLSGVSITWVHHSIEEGNYKSAMQGLFIT 163
Cdd:MTH00024 87 ILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFLT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 164 ILLGLYFLMLQYGEYSETMFSISDGIYGSCLFMATGFHGTHVAVGATFLIVCFFRLKNFHFNKNHHIGFLAAAWYWHFVD 243
Cdd:MTH00024 167 VFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASWYWHFVD 246
|
250
....*....|....*
gi 168487804 244 VVWLFLYVSIYWWGS 258
Cdd:MTH00024 247 VVWLFLYLCIYWWGS 261
|
|
| COX3 |
MTH00052 |
cytochrome c oxidase subunit III; Provisional |
3-258 |
2.74e-97 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 164623 Cd Length: 262 Bit Score: 285.53 E-value: 2.74e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 3 QPFHLVEFSPWPLLISFSIFSMPIGLINYIRSSNISLLILGLFTTALISFLWWRDVVRESTYQGFHNKLVMKGLKIGIML 82
Cdd:MTH00052 7 HPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGLKYGMIL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 83 FILSEVCFFFAFFWAYFHSSLAPSVEIGAIWPPTGIFTLQAFQVPLLNTSVLLLSGVSITWVHHSIEEGNYKSAMQGLFI 162
Cdd:MTH00052 87 FIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEAIIGLAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 163 TILLGLYFLMLQYGEYSETMFSISDGIYGSCLFMATGFHGTHVAVGATFLIVCFFRLKNFHFNKNHHIGFLAAAWYWHFV 242
Cdd:MTH00052 167 TVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAAWYWHFV 246
|
250
....*....|....*.
gi 168487804 243 DVVWLFLYVSIYWWGS 258
Cdd:MTH00052 247 DVVWLFLFIFMYWWGS 262
|
|
| COX3 |
MTH00009 |
cytochrome c oxidase subunit III; Validated |
1-258 |
1.85e-95 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177101 Cd Length: 259 Bit Score: 280.57 E-value: 1.85e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 1 MRQPFHLVEFSPWPLLISFSIFSMPIGLINYIRSSNISLLILGLFTTALISFLWWRDVVRESTYQGFHNKLVMKGLKIGI 80
Cdd:MTH00009 2 IRQPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 81 MLFILSEVCFFFAFFWAYFHSSLAPSVEIGAIWPPTGIFTLQAFQVPLLNTSVLLLSGVSITWVHHSIEEGNYKSAMQGL 160
Cdd:MTH00009 82 ILFIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 161 FITILLGLYFLMLQYGEYSETMFSISDGIYGSCLFMATGFHGTHVAVGATFLIVCFFRLKNFHFNKNHHIGFLAAAWYWH 240
Cdd:MTH00009 162 ILTVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWH 241
|
250
....*....|....*...
gi 168487804 241 FVDVVWLFLYVSIYWWGS 258
Cdd:MTH00009 242 FVDVVWIFLYLCIYWWGS 259
|
|
| COX3 |
MTH00028 |
cytochrome c oxidase subunit III; Provisional |
3-258 |
3.11e-87 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214406 Cd Length: 297 Bit Score: 261.15 E-value: 3.11e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 3 QPFHLVEFSPWPLLISFSIFSMPIGLINYIRSSNISLLILGLFTTALISFLWWRDVVRESTYQGFHNKLVMKGLKIGIML 82
Cdd:MTH00028 6 HPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 83 FILSEVCFFFAFFWAYFHSSLAPSVEIGAIWPPTGIFTLQAFQVPLLNTSVLLLSGVSITWVHHSI-------------- 148
Cdd:MTH00028 86 FILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIigtgnpaslekgtq 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 149 -EEGNYKS---------------------AMQGLFITILLGLYFLMLQYGEYSETMFSISDGIYGSCLFMATGFHGTHVA 206
Cdd:MTH00028 166 gIEGPNPSngappdpqkgptfllsdfrtnAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVL 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 168487804 207 VGATFLIVCFFRLKNFHFNKNHHIGFLAAAWYWHFVDVVWLFLYVSIYWWGS 258
Cdd:MTH00028 246 VGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWGS 297
|
|
| PLN02194 |
PLN02194 |
cytochrome-c oxidase |
2-257 |
1.88e-73 |
|
cytochrome-c oxidase
Pssm-ID: 177845 Cd Length: 265 Bit Score: 224.93 E-value: 1.88e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 2 RQPFHLVEFSPWPLLISFSIFSMPIGLINYIR--SSNISLLILGLFTTALISFLWWRDVVRESTYQGFHNKLVMKGLKIG 79
Cdd:PLN02194 6 RHSYHLVDPSPWPISGSLGALATTVGGVMYMHpfQGGARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGPRYG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 80 IMLFILSEVCFFFAFFWAYFHSSLAPSVEIGAIWPPTGIFTLQAFQVPLLNTSVLLLSGVSITWVHHSIEEGNYKSAMQG 159
Cdd:PLN02194 86 SILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEKRAVYA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 160 LFITILLGLYFLMLQYGEYSETMFSISDGIYGSCLFMATGFHGTHVAVGATFLIVCFFRLKNFHFNKNHHIGFLAAAWYW 239
Cdd:PLN02194 166 LVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWYW 245
|
250
....*....|....*...
gi 168487804 240 HFVDVVWLFLYVSIYWWG 257
Cdd:PLN02194 246 HFVDVVWLFLFVSIYWWG 263
|
|
| COX3 |
MTH00083 |
cytochrome c oxidase subunit III; Provisional |
5-258 |
1.36e-66 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177150 Cd Length: 256 Bit Score: 207.12 E-value: 1.36e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 5 FHLVEFSPWPLLISFSIFSMPIGLINYIRSSNISLLILGLFTTALISFLWWRDVVREStYQGFHNKLVMKGLKIGIMLFI 84
Cdd:MTH00083 5 FHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMILFI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 85 LSEVCFFFAFFWAYFHSSLAPSVEIGAIWPPTGIFTLQAFQVPLLNTSVLLLSGVSITWVHHSIEEGNyKSAMQGLFITI 164
Cdd:MTH00083 84 FSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSN-KSCTNSLLLTC 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 165 LLGLYFLMLQYGEYSETMFSISDGIYGSCLFMATGFHGTHVAVGATFLIVCFFRLKNFHFNKNHHIGFLAAAWYWHFVDV 244
Cdd:MTH00083 163 FLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFVDV 242
|
250
....*....|....
gi 168487804 245 VWLFLYVSIYWWGS 258
Cdd:MTH00083 243 VWLFLFVFVYWWSY 256
|
|
| Heme_Cu_Oxidase_III_like |
cd00386 |
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ... |
68-256 |
3.54e-56 |
|
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: 178.17 E-value: 3.54e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 68 HNKLVMKGLKIGIMLFILSEVCFFFAFFWAYFHSSLAPSVEIGAiwpptgifTLQAFQVPLLNTSVLLLSGVSITWVHHS 147
Cdd:cd00386 1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFGA--------GLDPLDLPLLNTNTLLLSGSSVTWAHAS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 148 I--EEGNYKSAMQGLFITILLGLYFLMLQYGEYSETMFSISDGIYGSCLFMATGFHGTHVAVGATFLIVCFFRLKNFHFN 225
Cdd:cd00386 73 LaaRRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152
|
170 180 190
....*....|....*....|....*....|.
gi 168487804 226 KNHHIGFLAAAWYWHFVDVVWLFLYVSIYWW 256
Cdd:cd00386 153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
127-256 |
4.91e-41 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 139.60 E-value: 4.91e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 127 PLLNTSVLLLSGVSITWVHHSIEEGNYKSAMQGLFITILLGLYFLMLQYGEYSETM---FSISDGIYGSCLFMATGFHGT 203
Cdd:COG1845 60 PLINTLLLLLSSFTVALAVRAARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHLIaegLTPTSNAFGSFFFLLTGFHGL 139
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 168487804 204 HVAVGATFLIVCFFRLKNFHFNKNHHIGFLAAAWYWHFVDVVWLFLYVSIYWW 256
Cdd:COG1845 140 HVIIGLIWLLVVLVRALRGGFTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| NorE_like |
cd02862 |
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ... |
128-254 |
2.20e-21 |
|
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: 88.06 E-value: 2.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 128 LLNTSVLLLSGVSITWVHHSIEEGNYKSAMQGLFITILLGLYFLMLQYGEYSE---TMFSISDGIYGSCLFMATGFHGTH 204
Cdd:cd02862 55 ALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYAHkiaAGIDPDAGLFFTLYFLLTGFHLLH 134
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 168487804 205 VAVGATFLIVCFFRLKNFHFNKNHHIGFLAAAWYWHFVDVVWLFLYVSIY 254
Cdd:cd02862 135 VLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVLFPLLY 184
|
|
| Ubiquinol_oxidase_III |
cd02863 |
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ... |
124-254 |
6.89e-15 |
|
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: 70.73 E-value: 6.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 124 FQVPL--LNTSVLLLSGVSITWVHHSIEEGNYKSAMQGLFITILLGLYFLMLQYGEYSETM---FSISDGIYGSCLFMAT 198
Cdd:cd02863 48 FELPLvfIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEFHHLIaegAGPDRSAFLSAFFTLV 127
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 168487804 199 GFHGTHVAVGATFLIVCFFRLKNFHFNKNHHIGFLAAAWYWHFVDVVWLFLYVSIY 254
Cdd:cd02863 128 GTHGLHVTFGLIWILVMIIQLKKRGLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
|
|
| Heme_Cu_Oxidase_III_2 |
cd02865 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
126-256 |
1.22e-13 |
|
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: 67.39 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 126 VPLLNTSVLLLSGVSITWVHHSIEEGNYKSAMQGLFITILLGLYFLMLQYGEY---SETMFSISDGIYGSCLFMATGFHG 202
Cdd:cd02865 51 LLSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWhalNDAGYGPTSNPAGSFFYLLTGLHG 130
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 168487804 203 THVAVGATFLIVCFFRLKNFHFNKNHHIGFLAAAWYWHFVDVVWLFLYVSIYWW 256
Cdd:cd02865 131 LHVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVLLALLYGT 184
|
|
| Heme_Cu_Oxidase_III_1 |
cd02864 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
113-256 |
2.46e-13 |
|
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: 66.76 E-value: 2.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 113 WPPTGIF---TLQAFQVPL----LNTSVLLLSGVSITWVHHSIEEGNYKSAMQGLFITILLGLYFLMLQYGEYSETMFSI 185
Cdd:cd02864 42 WPLPSDVfalRIGHFNIPLvliaIMTFILITSSGTMAMAVNFGYRGNRKAAARLMLATALLGATFVGMQAFEWTKLIVEE 121
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 186 SDG---------IYGSCLFMATGFHGTHVAVGATFLIVCFFRLKNFHFN-KNHHIGFLAAAWYWHFVDVVWLFLYVSIYW 255
Cdd:cd02864 122 GVRpwgnpwgaaQFGASFFMITGFHGTHVTIGVIYLIIIARKVWRGKYQrIGRYEIVEIAGLYWHFVDLVWVFIFAFFYL 201
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gi 168487804 256 W 256
Cdd:cd02864 202 W 202
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| COX3 |
MTH00049 |
cytochrome c oxidase subunit III; Validated |
123-254 |
4.48e-12 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177124 Cd Length: 215 Bit Score: 63.40 E-value: 4.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 123 AFQVPLLNTSVLLLSGVSITWVHHSIeegNYKSAMQGLFITILLGLYFLMLQYGEYSETMFSISDGIYGSCLFMATGFHG 202
Cdd:MTH00049 89 SLEIPFVGCFLLLGSSITVTAYHHLL---GWKYCDLFLYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHF 165
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90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 168487804 203 THVAVGATFLI-VCFFRLKNFHFNKNHHIgflaaAWYWHFVDVVWLFLYVSIY 254
Cdd:MTH00049 166 SHVVLGVVGLStLLLVGSSSFGVYRSTVL-----TWYWHFVDYIWLLVYLIVY 213
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| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
114-257 |
1.16e-09 |
|
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]
Pssm-ID: 131943 Cd Length: 190 Bit Score: 56.40 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 114 PPTGIFTLQAFqvpLLNTSVLLLSGVSITWVHHSIEEGNYKSAMQGLFITILLGLYFL---MLQYGEYSETMFSISDGIY 190
Cdd:TIGR02897 45 MPAELFELPLV---LIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVgfeIYEFAHYASEGVTPQIGSY 121
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90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 168487804 191 GSCLFMATGFHGTHVAVGATFLIVCFFRLKNFHFNKNHHIGFLAAAWYWHFVDVVWLFLYVSIYWWG 257
Cdd:TIGR02897 122 WSSFFVLLGTHGCHVTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
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| PRK10663 |
PRK10663 |
cytochrome o ubiquinol oxidase subunit III; Provisional |
124-258 |
2.29e-06 |
|
cytochrome o ubiquinol oxidase subunit III; Provisional
Pssm-ID: 182628 Cd Length: 204 Bit Score: 47.08 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 124 FQVP--LLNTSVLLLSGVSITWVHHSIEEGNYKSAMQGLFITILLGLYFLMLQYGEYSETM---FSISDGIYGSCLFMAT 198
Cdd:PRK10663 64 FELPfvLVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFHHLIvegMGPDRSGFLSAFFALV 143
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90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 168487804 199 GFHGTHVAVGATFLIVCFFRLKNFHFNKNHHIGFLAAAWYWHFVDVVWLFLYVSIYWWGS 258
Cdd:PRK10663 144 GTHGLHVTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGA 203
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