|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
1-236 |
2.03e-152 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 423.82 E-value: 2.03e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 1 MGAMALTSGLAKWFHTFNINLFMIGMTITLLTMYQWWRDVVREGTMQGLHTSVVSVGLRWGMILFIASEVLFFVSFFWAY 80
Cdd:MTH00155 20 IGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGMILFIVSEVFFFISFFWAF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 81 FNSSLAPAVEMGLAWPPMGIKPFNPMQVPLLNTVVLLSSGVTVTWAHHSLMEANHSQTTQGLLATVILGLYFTMLQAYEY 160
Cdd:MTH00155 100 FHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSLFFTIILGIYFTMLQAYEY 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 938339317 161 WEAPFTIADAVYGSSFFMATGFHGIHVIIGTSFLLMCLIRHYSNHFSPTHHFGFEAAAWYWHFVDVVWLFLYVSIY 236
Cdd:MTH00155 180 YEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYWHFVDVVWLFLYISIY 255
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-238 |
1.90e-124 |
|
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: 352.59 E-value: 1.90e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 1 MGAMALTSGLAKWFHTF-NINLFMIGMTITLLTMYQWWRDVVREGTMQGLHTSVVSVGLRWGMILFIASEVLFFVSFFWA 79
Cdd:cd01665 5 FGLLLLALGLVLWMHGYgGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFSFFWA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 80 YFNSSLAPAVEMGLAWPPMGIKPFNPMQVPLLNTVVLLSSGVTVTWAHHSLMEANHSQTTQGLLATVILGLYFTMLQAYE 159
Cdd:cd01665 85 FFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGLQAYE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 938339317 160 YWEAPFTIADAVYGSSFFMATGFHGIHVIIGTSFLLMCLIRHYSNHFSPTHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 238
Cdd:cd01665 165 YYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFVYWW 243
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
2-240 |
6.32e-119 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 339.39 E-value: 6.32e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 2 GAMALTSGLAKWFHTF--NINLFMIGMTITLLTMYQWWRDVVREGTMQGLHTSVVSVGLRWGMILFIASEVLFFVSFFWA 79
Cdd:pfam00510 18 ALLLLTSGLVLWFHGYsgNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGMILFIISEVFFFLGIFWA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 80 YFNSSLAPAVEMGLAWPPMGIKPFNPMQVPLLNTVVLLSSGVTVTWAHHSLMEANHSQTTQGLLATVILGLYFTMLQAYE 159
Cdd:pfam00510 98 FFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGLILTILLAVYFTGLQAME 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 160 YWEAPFTIADAVYGSSFFMATGFHGIHVIIGTSFLLMCLIRHYSNHFSPTHHFGFEAAAWYWHFVDVVWLFLYVSIYWWG 239
Cdd:pfam00510 178 YTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWHFVDVVWLFLYVSVYWWG 257
|
.
gi 938339317 240 S 240
Cdd:pfam00510 258 S 258
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
49-238 |
6.07e-55 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 174.65 E-value: 6.07e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 49 LHTSVVSVGLRWGMILFIASEVLFFVSFFWAYFNSSlapaveMGLAWPPMGIKPFNPmQVPLLNTVVLLSSGVTVTWAHH 128
Cdd:COG1845 7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLR------ASAPDWPAGAELLDL-PLPLINTLLLLLSSFTVALAVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 129 SLMEANHSQTTQGLLATVILGLYFTMLQAYEY---WEAPFTIADAVYGSSFFMATGFHGIHVIIGTSFLLMCLIRHYSNH 205
Cdd:COG1845 80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159
|
170 180 190
....*....|....*....|....*....|...
gi 938339317 206 FSPTHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 238
Cdd:COG1845 160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
61-239 |
3.19e-10 |
|
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: 57.56 E-value: 3.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 61 GMILFIASEVLFFVSFFWAYFNSSLApavemGLAWPPMGIKPFNpMQVPLLNTVVLLSSGVTVTWAHHSLMEANHSQTTQ 140
Cdd:TIGR02897 13 GFWIFLGAEIALFATLFATYLVLQHG-----GDYAGKMPAELFE-LPLVLIMTFLLLFSSFTCGIAIYEMRKENQKLMMF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 141 GLLATVILGLYFTMLQAYE---YWEAPFTIADAVYGSSFFMATGFHGIHVIIGTSFLLMCLIRHYSNHFSPTHHFGFEAA 217
Cdd:TIGR02897 87 WMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCHVTLGIVWAICLLIQIQRRGLTPYTAPKVFIV 166
|
170 180
....*....|....*....|..
gi 938339317 218 AWYWHFVDVVWLFLYVSIYWWG 239
Cdd:TIGR02897 167 SLYWHFLDVVWVFIFTAVYLIG 188
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
1-236 |
2.03e-152 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 423.82 E-value: 2.03e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 1 MGAMALTSGLAKWFHTFNINLFMIGMTITLLTMYQWWRDVVREGTMQGLHTSVVSVGLRWGMILFIASEVLFFVSFFWAY 80
Cdd:MTH00155 20 IGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGMILFIVSEVFFFISFFWAF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 81 FNSSLAPAVEMGLAWPPMGIKPFNPMQVPLLNTVVLLSSGVTVTWAHHSLMEANHSQTTQGLLATVILGLYFTMLQAYEY 160
Cdd:MTH00155 100 FHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSLFFTIILGIYFTMLQAYEY 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 938339317 161 WEAPFTIADAVYGSSFFMATGFHGIHVIIGTSFLLMCLIRHYSNHFSPTHHFGFEAAAWYWHFVDVVWLFLYVSIY 236
Cdd:MTH00155 180 YEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYWHFVDVVWLFLYISIY 255
|
|
| COX3 |
MTH00118 |
cytochrome c oxidase subunit III; Provisional |
1-240 |
2.65e-138 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177179 Cd Length: 261 Bit Score: 388.54 E-value: 2.65e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 1 MGAMALTSGLAKWFHTFNINLFMIGMTITLLTMYQWWRDVVREGTMQGLHTSVVSVGLRWGMILFIASEVLFFVSFFWAY 80
Cdd:MTH00118 22 MAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRYGMILFITSEVFFFLGFFWAF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 81 FNSSLAPAVEMGLAWPPMGIKPFNPMQVPLLNTVVLLSSGVTVTWAHHSLMEANHSQTTQGLLATVILGLYFTMLQAYEY 160
Cdd:MTH00118 102 YHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQALTLTILLGLYFTALQAMEY 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 161 WEAPFTIADAVYGSSFFMATGFHGIHVIIGTSFLLMCLIRHYSNHFSPTHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS 240
Cdd:MTH00118 182 YEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWYWHFVDVVWLFLYISIYWWGS 261
|
|
| COX3 |
MTH00189 |
cytochrome c oxidase subunit III; Provisional |
1-240 |
3.08e-129 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177238 Cd Length: 260 Bit Score: 365.45 E-value: 3.08e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 1 MGAMALTSGLAKWFHTFNINLFMIGMTITLLTMYQWWRDVVREGTMQGLHTSVVSVGLRWGMILFIASEVLFFVSFFWAY 80
Cdd:MTH00189 21 IAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRYGMILFITSEVFFFLGFFWAF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 81 FNSSLAPAVEMGLAWPPMGIKPFNPMQVPLLNTVVLLSSGVTVTWAHHSLMEANHSQTTQGLLATVILGLYFTMLQAYEY 160
Cdd:MTH00189 101 FHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQALTLTVILGVYFTLLQAMEY 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 161 WEAPFTIADAVYGSSFFMATGFHGIHVIIGTSFLLMCLIRHYSNHFSPTHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS 240
Cdd:MTH00189 181 YEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS 260
|
|
| COX3 |
MTH00141 |
cytochrome c oxidase subunit III; Provisional |
1-240 |
2.12e-128 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177199 Cd Length: 259 Bit Score: 363.44 E-value: 2.12e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 1 MGAMALTSGLAKWFHTFNINLFMIGMTITLLTMYQWWRDVVREGTMQGLHTSVVSVGLRWGMILFIASEVLFFVSFFWAY 80
Cdd:MTH00141 20 IGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFILFIVSEVCFFFAFFWAY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 81 FNSSLAPAVEMGLAWPPMGIKPFNPMQVPLLNTVVLLSSGVTVTWAHHSLMEANHSQTTQGLLATVILGLYFTMLQAYEY 160
Cdd:MTH00141 100 FHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGLTIILGVYFTFLQAGEY 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 161 WEAPFTIADAVYGSSFFMATGFHGIHVIIGTSFLLMCLIRHYSNHFSPTHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS 240
Cdd:MTH00141 180 YEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFVDVVWLFLYLSIYWWGS 259
|
|
| COX3 |
MTH00039 |
cytochrome c oxidase subunit III; Validated |
1-240 |
3.50e-126 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177114 Cd Length: 260 Bit Score: 357.89 E-value: 3.50e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 1 MGAMALTSGLAKWFHTFNINLFMIGMTITLLTMYQWWRDVVREGTMQGLHTSVVSVGLRWGMILFIASEVLFFVSFFWAY 80
Cdd:MTH00039 21 IGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRYGMILFITSEVCFFFAFFWAF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 81 FNSSLAPAVEMGLAWPPMGIKPFNPMQVPLLNTVVLLSSGVTVTWAHHSLMEANHSQTTQGLLATVILGLYFTMLQAYEY 160
Cdd:MTH00039 101 FHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQALFLTVLLGLYFTALQAWEY 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 161 WEAPFTIADAVYGSSFFMATGFHGIHVIIGTSFLLMCLIRHYSNHFSPTHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS 240
Cdd:MTH00039 181 YDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWYWHFVDVVWLFLYVCIYWWGS 260
|
|
| COX3 |
MTH00099 |
cytochrome c oxidase subunit III; Validated |
1-240 |
2.28e-125 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177161 Cd Length: 261 Bit Score: 355.96 E-value: 2.28e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 1 MGAMALTSGLAKWFHTFNINLFMIGMTITLLTMYQWWRDVVREGTMQGLHTSVVSVGLRWGMILFIASEVLFFVSFFWAY 80
Cdd:MTH00099 22 LSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRYGMILFIISEVFFFAGFFWAF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 81 FNSSLAPAVEMGLAWPPMGIKPFNPMQVPLLNTVVLLSSGVTVTWAHHSLMEANHSQTTQGLLATVILGLYFTMLQAYEY 160
Cdd:MTH00099 102 YHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQALFITILLGLYFTLLQASEY 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 161 WEAPFTIADAVYGSSFFMATGFHGIHVIIGTSFLLMCLIRHYSNHFSPTHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS 240
Cdd:MTH00099 182 YEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS 261
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-238 |
1.90e-124 |
|
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: 352.59 E-value: 1.90e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 1 MGAMALTSGLAKWFHTF-NINLFMIGMTITLLTMYQWWRDVVREGTMQGLHTSVVSVGLRWGMILFIASEVLFFVSFFWA 79
Cdd:cd01665 5 FGLLLLALGLVLWMHGYgGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFSFFWA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 80 YFNSSLAPAVEMGLAWPPMGIKPFNPMQVPLLNTVVLLSSGVTVTWAHHSLMEANHSQTTQGLLATVILGLYFTMLQAYE 159
Cdd:cd01665 85 FFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGLQAYE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 938339317 160 YWEAPFTIADAVYGSSFFMATGFHGIHVIIGTSFLLMCLIRHYSNHFSPTHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 238
Cdd:cd01665 165 YYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFVYWW 243
|
|
| COX3 |
MTH00219 |
cytochrome c oxidase subunit III; Provisional |
1-240 |
7.13e-124 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214464 Cd Length: 262 Bit Score: 352.17 E-value: 7.13e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 1 MGAMALTSGLAKWFHTFNINLFMIGMTITLLTMYQWWRDVVREGTMQGLHTSVVSVGLRWGMILFIASEVLFFVSFFWAY 80
Cdd:MTH00219 23 LGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLRIGMILFIVSEILFFFAFFWAF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 81 FNSSLAPAVEMGLAWPPMGIKPFNPMQVPLLNTVVLLSSGVTVTWAHHSLMEANHSQTTQGLLATVILGLYFTMLQAYEY 160
Cdd:MTH00219 103 FHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQQGLLFTILLGLYFTMLQGMEY 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 161 WEAPFTIADAVYGSSFFMATGFHGIHVIIGTSFLLMCLIRHYSNHFSPTHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS 240
Cdd:MTH00219 183 LEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS 262
|
|
| COX3 |
MTH00075 |
cytochrome c oxidase subunit III; Provisional |
3-240 |
3.11e-123 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177146 Cd Length: 261 Bit Score: 350.58 E-value: 3.11e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 3 AMALTSGLAKWFHTFNINLFMIGMTITLLTMYQWWRDVVREGTMQGLHTSVVSVGLRWGMILFIASEVLFFVSFFWAYFN 82
Cdd:MTH00075 24 ALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRYGMILFITSEVFFFLGFFWAFYN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 83 SSLAPAVEMGLAWPPMGIKPFNPMQVPLLNTVVLLSSGVTVTWAHHSLMEANHSQTTQGLLATVILGLYFTMLQAYEYWE 162
Cdd:MTH00075 104 SSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQSLALTIILGLYFTLLQAMEYYE 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 938339317 163 APFTIADAVYGSSFFMATGFHGIHVIIGTSFLLMCLIRHYSNHFSPTHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS 240
Cdd:MTH00075 184 APFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS 261
|
|
| COX3 |
MTH00130 |
cytochrome c oxidase subunit III; Provisional |
1-240 |
3.95e-123 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177188 Cd Length: 261 Bit Score: 350.22 E-value: 3.95e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 1 MGAMALTSGLAKWFHTFNINLFMIGMTITLLTMYQWWRDVVREGTMQGLHTSVVSVGLRWGMILFIASEVLFFVSFFWAY 80
Cdd:MTH00130 22 VAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRYGMILFITSEVFFFLGFFWAF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 81 FNSSLAPAVEMGLAWPPMGIKPFNPMQVPLLNTVVLLSSGVTVTWAHHSLMEANHSQTTQGLLATVILGLYFTMLQAYEY 160
Cdd:MTH00130 102 YHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQSLTLTILLGFYFTFLQAMEY 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 161 WEAPFTIADAVYGSSFFMATGFHGIHVIIGTSFLLMCLIRHYSNHFSPTHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS 240
Cdd:MTH00130 182 YEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWYWHFVDVVWLFLYISIYWWGS 261
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
2-240 |
6.32e-119 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 339.39 E-value: 6.32e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 2 GAMALTSGLAKWFHTF--NINLFMIGMTITLLTMYQWWRDVVREGTMQGLHTSVVSVGLRWGMILFIASEVLFFVSFFWA 79
Cdd:pfam00510 18 ALLLLTSGLVLWFHGYsgNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGMILFIISEVFFFLGIFWA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 80 YFNSSLAPAVEMGLAWPPMGIKPFNPMQVPLLNTVVLLSSGVTVTWAHHSLMEANHSQTTQGLLATVILGLYFTMLQAYE 159
Cdd:pfam00510 98 FFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGLILTILLAVYFTGLQAME 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 160 YWEAPFTIADAVYGSSFFMATGFHGIHVIIGTSFLLMCLIRHYSNHFSPTHHFGFEAAAWYWHFVDVVWLFLYVSIYWWG 239
Cdd:pfam00510 178 YTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWHFVDVVWLFLYVSVYWWG 257
|
.
gi 938339317 240 S 240
Cdd:pfam00510 258 S 258
|
|
| COX3 |
MTH00009 |
cytochrome c oxidase subunit III; Validated |
1-240 |
1.34e-115 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177101 Cd Length: 259 Bit Score: 331.03 E-value: 1.34e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 1 MGAMALTSGLAKWFHTFNINLFMIGMTITLLTMYQWWRDVVREGTMQGLHTSVVSVGLRWGMILFIASEVLFFVSFFWAY 80
Cdd:MTH00009 20 IGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMILFIASEVMFFFAFFWAF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 81 FNSSLAPAVEMGLAWPPMGIKPFNPMQVPLLNTVVLLSSGVTVTWAHHSLMEANHSQTTQGLLATVILGLYFTMLQAYEY 160
Cdd:MTH00009 100 FHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALILTVLLGAYFTFLQAGEY 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 161 WEAPFTIADAVYGSSFFMATGFHGIHVIIGTSFLLMCLIRHYSNHFSPTHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS 240
Cdd:MTH00009 180 IEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFVDVVWIFLYLCIYWWGS 259
|
|
| COX3 |
MTH00024 |
cytochrome c oxidase subunit III; Validated |
1-240 |
3.98e-110 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 214403 Cd Length: 261 Bit Score: 317.08 E-value: 3.98e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 1 MGAMALTSGLAKWFHTFNINLFMIGMTITLLTMYQWWRDVVREGTMQGLHTSVVSVGLRWGMILFIASEVLFFVSFFWAY 80
Cdd:MTH00024 22 GGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGMLLFILSEVLFFFSFFWAF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 81 FNSSLAPAVEMGLAWPPMGIKPFNPMQVPLLNTVVLLSSGVTVTWAHHSLMEANHSQTTQGLLATVILGLYFTMLQAYEY 160
Cdd:MTH00024 102 FHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFLTVFLGVLFTGLQAIEY 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 161 WEAPFTIADAVYGSSFFMATGFHGIHVIIGTSFLLMCLIRHYSNHFSPTHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS 240
Cdd:MTH00024 182 YEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASWYWHFVDVVWLFLYLCIYWWGS 261
|
|
| COX3 |
MTH00052 |
cytochrome c oxidase subunit III; Provisional |
2-240 |
3.62e-101 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 164623 Cd Length: 262 Bit Score: 294.39 E-value: 3.62e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 2 GAMALTSGLAKWFHTFNINLFMIGMTITLLTMYQWWRDVVREGTMQGLHTSVVSVGLRWGMILFIASEVLFFVSFFWAYF 81
Cdd:MTH00052 24 GALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGLKYGMILFIVSEVCLFFSFFWAFF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 82 NSSLAPAVEMGLAWPPMGIKPFNPMQVPLLNTVVLLSSGVTVTWAHHSLMEANHSQTTQGLLATVILGLYFTMLQAYEYW 161
Cdd:MTH00052 104 HSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEAIIGLALTVALGLLFTGLQAMEYY 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 938339317 162 EAPFTIADAVYGSSFFMATGFHGIHVIIGTSFLLMCLIRHYSNHFSPTHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS 240
Cdd:MTH00052 184 EAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAAWYWHFVDVVWLFLFIFMYWWGS 262
|
|
| COX3 |
MTH00028 |
cytochrome c oxidase subunit III; Provisional |
2-240 |
1.79e-89 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214406 Cd Length: 297 Bit Score: 266.16 E-value: 1.79e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 2 GAMALTSGLAKWFHTFNINLFMIGMTITLLTMYQWWRDVVREGTMQGLHTSVVSVGLRWGMILFIASEVLFFVSFFWAYF 81
Cdd:MTH00028 23 GAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLLFILSEVCLFFAFFWAFF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 82 NSSLAPAVEMGLAWPPMGIKPFNPMQVPLLNTVVLLSSGVTVTWAHHSLMEANHSQTTQ--------------------- 140
Cdd:MTH00028 103 HSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTGNPASLEkgtqgiegpnpsngappdpqk 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 141 ---------------GLLATVILGLYFTMLQAYEYWEAPFTIADAVYGSSFFMATGFHGIHVIIGTSFLLMCLIRHYSNH 205
Cdd:MTH00028 183 gptfllsdfrtnaviGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVLVGTTFLIVCFIRLLSNQ 262
|
250 260 270
....*....|....*....|....*....|....*
gi 938339317 206 FSPTHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS 240
Cdd:MTH00028 263 FTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWGS 297
|
|
| PLN02194 |
PLN02194 |
cytochrome-c oxidase |
1-239 |
8.39e-83 |
|
cytochrome-c oxidase
Pssm-ID: 177845 Cd Length: 265 Bit Score: 248.04 E-value: 8.39e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 1 MGAMALTSGLAKWFHTFN--INLFMIGMTITLLTMYQWWRDVVREGTMQGLHTSVVSVGLRWGMILFIASEVLFFVSFFW 78
Cdd:PLN02194 23 LGALATTVGGVMYMHPFQggARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGPRYGSILFIVSEVMFFFAFFW 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 79 AYFNSSLAPAVEMGLAWPPMGIKPFNPMQVPLLNTVVLLSSGVTVTWAHHSLMEANHSQTTQGLLATVILGLYFTMLQAY 158
Cdd:PLN02194 103 ASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEKRAVYALVATVLLALVFTGFQGM 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 159 EYWEAPFTIADAVYGSSFFMATGFHGIHVIIGTSFLLMCLIRHYSNHFSPTHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 238
Cdd:PLN02194 183 EYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWYWHFVDVVWLFLFVSIYWW 262
|
.
gi 938339317 239 G 239
Cdd:PLN02194 263 G 263
|
|
| COX3 |
MTH00083 |
cytochrome c oxidase subunit III; Provisional |
1-240 |
1.22e-68 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177150 Cd Length: 256 Bit Score: 211.74 E-value: 1.22e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 1 MGAMALTSGLAKWFHTFNINLFMIGMTITLLTMYQWWRDVVREGtMQGLHTSVVSVGLRWGMILFIASEVLFFVSFFWAY 80
Cdd:MTH00083 19 FSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMILFIFSEFMFFFSIFWTF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 81 FNSSLAPAVEMGLAWPPMGIKPFNPMQVPLLNTVVLLSSGVTVTWAHHSLMeANHSQTTQGLLATVILGLYFTMLQAYEY 160
Cdd:MTH00083 98 FDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLC-LSNKSCTNSLLLTCFLGLYFTSFQLMEY 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 161 WEAPFTIADAVYGSSFFMATGFHGIHVIIGTSFLLMCLIRHYSNHFSPTHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS 240
Cdd:MTH00083 177 KEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFVDVVWLFLFVFVYWWSY 256
|
|
| Heme_Cu_Oxidase_III_like |
cd00386 |
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ... |
50-238 |
6.48e-68 |
|
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: 207.06 E-value: 6.48e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 50 HTSVVSVGLRWGMILFIASEVLFFVSFFWAYFNSSLAPAVEMGLawppmgikPFNPMQVPLLNTVVLLSSGVTVTWAHHS 129
Cdd:cd00386 1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFGA--------GLDPLDLPLLNTNTLLLSGSSVTWAHAS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 130 LMEANHS--QTTQGLLATVILGLYFTMLQAYEYWEAPFTIADAVYGSSFFMATGFHGIHVIIGTSFLLMCLIRHYSNHFS 207
Cdd:cd00386 73 LAARRGNrkKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152
|
170 180 190
....*....|....*....|....*....|.
gi 938339317 208 PTHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 238
Cdd:cd00386 153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
49-238 |
6.07e-55 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 174.65 E-value: 6.07e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 49 LHTSVVSVGLRWGMILFIASEVLFFVSFFWAYFNSSlapaveMGLAWPPMGIKPFNPmQVPLLNTVVLLSSGVTVTWAHH 128
Cdd:COG1845 7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLR------ASAPDWPAGAELLDL-PLPLINTLLLLLSSFTVALAVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 129 SLMEANHSQTTQGLLATVILGLYFTMLQAYEY---WEAPFTIADAVYGSSFFMATGFHGIHVIIGTSFLLMCLIRHYSNH 205
Cdd:COG1845 80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159
|
170 180 190
....*....|....*....|....*....|...
gi 938339317 206 FSPTHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 238
Cdd:COG1845 160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| NorE_like |
cd02862 |
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ... |
61-236 |
1.01e-23 |
|
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: 93.84 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 61 GMILFIASEVLFFVSFFWAYF-NSSLAPAVEMGLAW---PPMGikpfnpmqvpLLNTVVLLSSGVTVTWAHHSLMEANHS 136
Cdd:cd02862 12 GMWVFILSELLAFGALFIAYAvYRALYPELFAAGSAhldLLLG----------ALNTLVLLTSSFTVALAVRAARAGRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 137 QTTQGLLATVILGLYFTMLQAYEYwEAPFTIADAVYGSSFFMA----TGFHGIHVIIGTSFLLMCLIRHYSNHFSPTHHF 212
Cdd:cd02862 82 RARRWLAAAVLLGLVFLVIKYFEY-AHKIAAGIDPDAGLFFTLyfllTGFHLLHVLIGLGILLWVAWRARRGRYSARDYE 160
|
170 180
....*....|....*....|....
gi 938339317 213 GFEAAAWYWHFVDVVWLFLYVSIY 236
Cdd:cd02862 161 GVEAAALYWHMVDLVWIVLFPLLY 184
|
|
| Heme_Cu_Oxidase_III_2 |
cd02865 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
57-238 |
6.55e-20 |
|
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: 83.96 E-value: 6.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 57 GLRWGMILFIASEVLFFVSFFWAYFNSSLapaveMGLAWPPmgiKPFNPMQVPLLNTVVLLSSGVTVTWAHHSLMEANHS 136
Cdd:cd02865 8 PGWWGLWVFMAVEGTLFALLISAYFMRMT-----SGDWQPG---APLPLPNLLSLNTAVLAASSVAMQWARRAARRNRRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 137 QTTQGLLATVILGLYFTMLQAYEYWEAPF---TIADAVYGSSFFMATGFHGIHVIIGTSFLLMCLIRHYSNHFSPTHHFG 213
Cdd:cd02865 80 LARLGLALAGALALAFLAGQLLAWHALNDagyGPTSNPAGSFFYLLTGLHGLHVIGGLVALAIVLAGLIRGHYGPRRRLP 159
|
170 180
....*....|....*....|....*
gi 938339317 214 FEAAAWYWHFVDVVWLFLYVSIYWW 238
Cdd:cd02865 160 VELCALYWHFLLLVWLVLLALLYGT 184
|
|
| Heme_Cu_Oxidase_III_1 |
cd02864 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
61-238 |
1.01e-17 |
|
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: 78.31 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 61 GMILFIASEVLFFVSFFWAYFNSSLAPAVEMGLAWPPMGIkPFNPMQVPL----LNTVVLLSSGVTVTWAHHSLMEANHS 136
Cdd:cd02864 12 MMWFFLLSDAFIFSSFLIAYMTARISTTEPWPLPSDVFAL-RIGHFNIPLvliaIMTFILITSSGTMAMAVNFGYRGNRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 137 QTTQGLLATVILGLYFTMLQAYEY-----------WEAPFTIAdaVYGSSFFMATGFHGIHVIIGTSFLLMCLIRHYSNH 205
Cdd:cd02864 91 AAARLMLATALLGATFVGMQAFEWtkliveegvrpWGNPWGAA--QFGASFFMITGFHGTHVTIGVIYLIIIARKVWRGK 168
|
170 180 190
....*....|....*....|....*....|....
gi 938339317 206 FSPTHHF-GFEAAAWYWHFVDVVWLFLYVSIYWW 238
Cdd:cd02864 169 YQRIGRYeIVEIAGLYWHFVDLVWVFIFAFFYLW 202
|
|
| Ubiquinol_oxidase_III |
cd02863 |
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ... |
61-236 |
4.37e-16 |
|
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: 73.43 E-value: 4.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 61 GMILFIASEVLFFVSFFWAYFnsslapAVEMGLAWPPMGIKPFNPMQVpLLNTVVLLSSGVTVTWAHHSLMEANHSQTTQ 140
Cdd:cd02863 12 GFWIYLMSDCILFATLFATYA------VLSGNTAGGPPGHELFELPLV-FIETFLLLLSSFTCGLAMIAMNKNNKKKVIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 141 GLLATVILGLYFTMLQAYE---YWEAPFTIADAVYGSSFFMATGFHGIHVIIGTSFLLMCLIRHYSNHFSPTHHFGFEAA 217
Cdd:cd02863 85 WLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLVGTHGLHVTFGLIWILVMIIQLKKRGLTPDTARRLFCL 164
|
170
....*....|....*....
gi 938339317 218 AWYWHFVDVVWLFLYVSIY 236
Cdd:cd02863 165 SLFWHFLDIVWIFVFTVVY 183
|
|
| COX3 |
MTH00049 |
cytochrome c oxidase subunit III; Validated |
64-236 |
1.13e-15 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177124 Cd Length: 215 Bit Score: 73.03 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 64 LFIASEVLFFVSFFWA------YFNSSLAPAVEmglawppmgikpfnpmqVPLLNTVVLLSSGVTVTWAHHSL-MEANHS 136
Cdd:MTH00049 59 LFILSEVIIFGSLLVCclwfddWSYISLSSSLE-----------------IPFVGCFLLLGSSITVTAYHHLLgWKYCDL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 137 QttqgLLATVILGLYFTMLQAYEYWEAPFTIADAVYGSSFFMATGFHGIHVIIGtSFLLMCLIRHYSNHFSPTHHfgfEA 216
Cdd:MTH00049 122 F----LYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHFSHVVLG-VVGLSTLLLVGSSSFGVYRS---TV 193
|
170 180
....*....|....*....|
gi 938339317 217 AAWYWHFVDVVWLFLYVSIY 236
Cdd:MTH00049 194 LTWYWHFVDYIWLLVYLIVY 213
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
61-239 |
3.19e-10 |
|
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: 57.56 E-value: 3.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 61 GMILFIASEVLFFVSFFWAYFNSSLApavemGLAWPPMGIKPFNpMQVPLLNTVVLLSSGVTVTWAHHSLMEANHSQTTQ 140
Cdd:TIGR02897 13 GFWIFLGAEIALFATLFATYLVLQHG-----GDYAGKMPAELFE-LPLVLIMTFLLLFSSFTCGIAIYEMRKENQKLMMF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 141 GLLATVILGLYFTMLQAYE---YWEAPFTIADAVYGSSFFMATGFHGIHVIIGTSFLLMCLIRHYSNHFSPTHHFGFEAA 217
Cdd:TIGR02897 87 WMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCHVTLGIVWAICLLIQIQRRGLTPYTAPKVFIV 166
|
170 180
....*....|....*....|..
gi 938339317 218 AWYWHFVDVVWLFLYVSIYWWG 239
Cdd:TIGR02897 167 SLYWHFLDVVWVFIFTAVYLIG 188
|
|
| PRK10663 |
PRK10663 |
cytochrome o ubiquinol oxidase subunit III; Provisional |
110-240 |
7.57e-08 |
|
cytochrome o ubiquinol oxidase subunit III; Provisional
Pssm-ID: 182628 Cd Length: 204 Bit Score: 50.94 E-value: 7.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339317 110 LLNTVVLLSSGVTVTWAHHSLMEANHSQTTQGLLATVILGLYFTMLQAYEYW---EAPFTIADAVYGSSFFMATGFHGIH 186
Cdd:PRK10663 70 LVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFHhliVEGMGPDRSGFLSAFFALVGTHGLH 149
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 938339317 187 VIIGTSFLLMCLIRHYSNHFSPTHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS 240
Cdd:PRK10663 150 VTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGA 203
|
|
|