|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
3-256 |
6.13e-86 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 256.26 E-value: 6.13e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 3 FNNHFFHLVSSSPWPIVVSSNIFNVGVGLI-WMIGGEFFFFFFFTFLMLIMSFQWWRDVVYEGVYEGSHTCSITAGLDMG 81
Cdd:MTH00155 1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIkWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 82 VVGFIISEICFFFSFFWMFFYFSLSPDFILGFTWPPLGVFSVSFLGVPFLNTLILLSSGFFITLSHLNLVSRFSAKFFYS 161
Cdd:MTH00155 81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 162 YFFGLALGGYFLLVQFYEYYNLSYDFSDGSFGCAFYILTGFHGFHVLLGFVFLFINFIRFYIGHLSTFFVSGFDYSVWYW 241
Cdd:MTH00155 161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240
|
250
....*....|....*
gi 52220973 242 HFVDVVWLFLYLFVY 256
Cdd:MTH00155 241 HFVDVVWLFLYISIY 255
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
18-258 |
1.01e-75 |
|
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: 230.10 E-value: 1.01e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 18 IVVSSNIFNVGVGLIWMIGGEFFFFFFFTFL--MLIMSFQWWRDVVYEGVYEGSHTCSITAGLDMGVVGFIISEICFFFS 95
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHGYGGPLLLFLGLilLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 96 FFWMFFYFSLSPDFILGFTWPPLGVFSVSFLGVPFLNTLILLSSGFFITLSHLNLVSRFSAKFFYSYFFGLALGGYFLLV 175
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 176 QFYEYYNLSYDFSDGSFGCAFYILTGFHGFHVLLGFVFLFINFIRFYIGHLSTFFVSGFDYSVWYWHFVDVVWLFLYLFV 255
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 52220973 256 YWW 258
Cdd:cd01665 241 YWW 243
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
6-259 |
1.81e-62 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 196.86 E-value: 1.81e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 6 HFFHLVSSSPWPIVVSSNIFNVGVGLI-WMIGGEFFFFFFFTFL--MLIMSFQWWRDVVYEGVYEGSHTCSITAGLDMGV 82
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVlWFHGYSGNMTLFIIALfsLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 83 VGFIISEICFFFSFFWMFFYFSLSPDFILGFTWPPLGVFSVSFLGVPFLNTLILLSSGFFITLSHLNLVSRFSAKFFYSY 162
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 163 FFGLALGGYFLLVQFYEYYNLSYDFSDGSFGCAFYILTGFHGFHVLLGFVFLFINFIRFYIGHLSTFFVSGFDYSVWYWH 242
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*..
gi 52220973 243 FVDVVWLFLYLFVYWWG 259
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWG 257
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
126-258 |
5.93e-30 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 111.09 E-value: 5.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 126 LGVPFLNTLILLSSGFFITLSHLNLVSRFSAKFFYSYFFGLALGGYFLLVQFYEYYNLS---YDFSDGSFGCAFYILTGF 202
Cdd:COG1845 57 LPLPLINTLLLLLSSFTVALAVRAARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHLIaegLTPTSNAFGSFFFLLTGF 136
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 52220973 203 HGFHVLLGFVFLFINFIRFYIGHLSTFFVSGFDYSVWYWHFVDVVWLFLYLFVYWW 258
Cdd:COG1845 137 HGLHVIIGLIWLLVVLVRALRGGFTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
133-259 |
4.49e-06 |
|
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: 46.00 E-value: 4.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 133 TLILLSSGFFITLSHLNLVSRFSAKFFYSYFFGLALGGYFLLVQFYE---YYNLSYDFSDGSFGCAFYILTGFHGFHVLL 209
Cdd:TIGR02897 59 TFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCHVTL 138
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 52220973 210 GFVFLFINFIRFYIGHLSTFFVSGFDYSVWYWHFVDVVWLFLYLFVYWWG 259
Cdd:TIGR02897 139 GIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
3-256 |
6.13e-86 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 256.26 E-value: 6.13e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 3 FNNHFFHLVSSSPWPIVVSSNIFNVGVGLI-WMIGGEFFFFFFFTFLMLIMSFQWWRDVVYEGVYEGSHTCSITAGLDMG 81
Cdd:MTH00155 1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIkWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 82 VVGFIISEICFFFSFFWMFFYFSLSPDFILGFTWPPLGVFSVSFLGVPFLNTLILLSSGFFITLSHLNLVSRFSAKFFYS 161
Cdd:MTH00155 81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 162 YFFGLALGGYFLLVQFYEYYNLSYDFSDGSFGCAFYILTGFHGFHVLLGFVFLFINFIRFYIGHLSTFFVSGFDYSVWYW 241
Cdd:MTH00155 161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240
|
250
....*....|....*
gi 52220973 242 HFVDVVWLFLYLFVY 256
Cdd:MTH00155 241 HFVDVVWLFLYISIY 255
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
18-258 |
1.01e-75 |
|
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: 230.10 E-value: 1.01e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 18 IVVSSNIFNVGVGLIWMIGGEFFFFFFFTFL--MLIMSFQWWRDVVYEGVYEGSHTCSITAGLDMGVVGFIISEICFFFS 95
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHGYGGPLLLFLGLilLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 96 FFWMFFYFSLSPDFILGFTWPPLGVFSVSFLGVPFLNTLILLSSGFFITLSHLNLVSRFSAKFFYSYFFGLALGGYFLLV 175
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 176 QFYEYYNLSYDFSDGSFGCAFYILTGFHGFHVLLGFVFLFINFIRFYIGHLSTFFVSGFDYSVWYWHFVDVVWLFLYLFV 255
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 52220973 256 YWW 258
Cdd:cd01665 241 YWW 243
|
|
| COX3 |
MTH00141 |
cytochrome c oxidase subunit III; Provisional |
8-260 |
1.61e-68 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177199 Cd Length: 259 Bit Score: 212.44 E-value: 1.61e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 8 FHLVSSSPWPIVVSSNIFNVGVGLI-WMIGGEFFFFFFFTFLMLIMSFQWWRDVVYEGVYEGSHTCSITAGLDMGVVGFI 86
Cdd:MTH00141 6 FHLVEFSPWPLTGSIGALFLTVGLVsWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFILFI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 87 ISEICFFFSFFWMFFYFSLSPDFILGFTWPPLGVFSVSFLGVPFLNTLILLSSGFFITLSHLNLVSRFSAKFFYSYFFGL 166
Cdd:MTH00141 86 VSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGLTI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 167 ALGGYFLLVQFYEYYNLSYDFSDGSFGCAFYILTGFHGFHVLLGFVFLFINFIRFYIGHLSTFFVSGFDYSVWYWHFVDV 246
Cdd:MTH00141 166 ILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFVDV 245
|
250
....*....|....
gi 52220973 247 VWLFLYLFVYWWGG 260
Cdd:MTH00141 246 VWLFLYLSIYWWGS 259
|
|
| COX3 |
MTH00189 |
cytochrome c oxidase subunit III; Provisional |
2-259 |
1.26e-65 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177238 Cd Length: 260 Bit Score: 204.82 E-value: 1.26e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 2 MFNNHFFHLVSSSPWPIVVSSNIFNVGVGL-IWMIGGEFFFFFFFTFLMLIMSFQWWRDVVYEGVYEGSHTCSITAGLDM 80
Cdd:MTH00189 1 MHQAHPFHLVDPSPWPLTGAIAALLLTSGLaMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 81 GVVGFIISEICFFFSFFWMFFYFSLSPDFILGFTWPPLGVFSVSFLGVPFLNTLILLSSGFFITLSHLNLVSRFSAKFFY 160
Cdd:MTH00189 81 GMILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 161 SYFFGLALGGYFLLVQFYEYYNLSYDFSDGSFGCAFYILTGFHGFHVLLGFVFLFINFIRFYIGHLSTFFVSGFDYSVWY 240
Cdd:MTH00189 161 ALTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWY 240
|
250
....*....|....*....
gi 52220973 241 WHFVDVVWLFLYLFVYWWG 259
Cdd:MTH00189 241 WHFVDVVWLFLYVSIYWWG 259
|
|
| COX3 |
MTH00039 |
cytochrome c oxidase subunit III; Validated |
2-260 |
1.52e-62 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177114 Cd Length: 260 Bit Score: 197.26 E-value: 1.52e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 2 MFNNHFFHLVSSSPWPIVVSSNIFNVGVGLI-WMIGGEFFFFFFFTFLMLIMSFQWWRDVVYEGVYEGSHTCSITAGLDM 80
Cdd:MTH00039 1 MTHQHPYHLVDQSPWPLTAAIGALIMTSGLVlWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 81 GVVGFIISEICFFFSFFWMFFYFSLSPDFILGFTWPPLGVFSVSFLGVPFLNTLILLSSGFFITLSHLNLVSRFSAKFFY 160
Cdd:MTH00039 81 GMILFITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 161 SYFFGLALGGYFLLVQFYEYYNLSYDFSDGSFGCAFYILTGFHGFHVLLGFVFLFINFIRFYIGHLSTFFVSGFDYSVWY 240
Cdd:MTH00039 161 ALFLTVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWY 240
|
250 260
....*....|....*....|
gi 52220973 241 WHFVDVVWLFLYLFVYWWGG 260
Cdd:MTH00039 241 WHFVDVVWLFLYVCIYWWGS 260
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
6-259 |
1.81e-62 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 196.86 E-value: 1.81e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 6 HFFHLVSSSPWPIVVSSNIFNVGVGLI-WMIGGEFFFFFFFTFL--MLIMSFQWWRDVVYEGVYEGSHTCSITAGLDMGV 82
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVlWFHGYSGNMTLFIIALfsLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 83 VGFIISEICFFFSFFWMFFYFSLSPDFILGFTWPPLGVFSVSFLGVPFLNTLILLSSGFFITLSHLNLVSRFSAKFFYSY 162
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 163 FFGLALGGYFLLVQFYEYYNLSYDFSDGSFGCAFYILTGFHGFHVLLGFVFLFINFIRFYIGHLSTFFVSGFDYSVWYWH 242
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*..
gi 52220973 243 FVDVVWLFLYLFVYWWG 259
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWG 257
|
|
| COX3 |
MTH00118 |
cytochrome c oxidase subunit III; Provisional |
1-259 |
4.70e-60 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177179 Cd Length: 261 Bit Score: 190.55 E-value: 4.70e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 1 MMFNNHFFHLVSSSPWPIVVSSNIFNVGVGL-IWMIGGEFFFFFFFTFLMLIMSFQWWRDVVYEGVYEGSHTCSITAGLD 79
Cdd:MTH00118 1 MTHQAHPYHMVDPSPWPLTGAMAALLLTSGLaMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 80 MGVVGFIISEICFFFSFFWMFFYFSLSPDFILGFTWPPLGVFSVSFLGVPFLNTLILLSSGFFITLSHLNLVSRFSAKFF 159
Cdd:MTH00118 81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 160 YSYFFGLALGGYFLLVQFYEYYNLSYDFSDGSFGCAFYILTGFHGFHVLLGFVFLFINFIRFYIGHLSTFFVSGFDYSVW 239
Cdd:MTH00118 161 QALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAW 240
|
250 260
....*....|....*....|
gi 52220973 240 YWHFVDVVWLFLYLFVYWWG 259
Cdd:MTH00118 241 YWHFVDVVWLFLYISIYWWG 260
|
|
| COX3 |
MTH00219 |
cytochrome c oxidase subunit III; Provisional |
1-259 |
4.09e-58 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214464 Cd Length: 262 Bit Score: 185.76 E-value: 4.09e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 1 MMFNNHFFHLVSSSPWPIVVSSNIFNVGVGLI-WMIGGEFFFFFFFTFLMLIMSFQWWRDVVYEGVYEGSHTCSITAGLD 79
Cdd:MTH00219 2 MFFQTNPYHLVDYSPWPLTGSLGALMLTSGLVaWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 80 MGVVGFIISEICFFFSFFWMFFYFSLSPDFILGFTWPPLGVFSVSFLGVPFLNTLILLSSGFFITLSHLNLVSRFSAKFF 159
Cdd:MTH00219 82 IGMILFIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 160 YSYFFGLALGGYFLLVQFYEYYNLSYDFSDGSFGCAFYILTGFHGFHVLLGFVFLFINFIRFYIGHLSTFFVSGFDYSVW 239
Cdd:MTH00219 162 QGLLFTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAAW 241
|
250 260
....*....|....*....|
gi 52220973 240 YWHFVDVVWLFLYLFVYWWG 259
Cdd:MTH00219 242 YWHFVDVVWLFLYVSIYWWG 261
|
|
| COX3 |
MTH00099 |
cytochrome c oxidase subunit III; Validated |
1-259 |
6.12e-56 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177161 Cd Length: 261 Bit Score: 180.31 E-value: 6.12e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 1 MMFNNHFFHLVSSSPWPIVVSSNIFNVGVGLI-WMIGGEFFFFFFFTFLMLIMSFQWWRDVVYEGVYEGSHTCSITAGLD 79
Cdd:MTH00099 1 MTHQTHAYHMVNPSPWPLTGALSALLMTSGLImWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 80 MGVVGFIISEICFFFSFFWMFFYFSLSPDFILGFTWPPLGVFSVSFLGVPFLNTLILLSSGFFITLSHLNLVSRFSAKFF 159
Cdd:MTH00099 81 YGMILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 160 YSYFFGLALGGYFLLVQFYEYYNLSYDFSDGSFGCAFYILTGFHGFHVLLGFVFLFINFIRFYIGHLSTFFVSGFDYSVW 239
Cdd:MTH00099 161 QALFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAW 240
|
250 260
....*....|....*....|
gi 52220973 240 YWHFVDVVWLFLYLFVYWWG 259
Cdd:MTH00099 241 YWHFVDVVWLFLYVSIYWWG 260
|
|
| COX3 |
MTH00075 |
cytochrome c oxidase subunit III; Provisional |
1-259 |
9.72e-55 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177146 Cd Length: 261 Bit Score: 177.24 E-value: 9.72e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 1 MMFNNHFFHLVSSSPWPIVVSSNIFNVGVGL-IWMIGGEFFFFFFFTFLMLIMSFQWWRDVVYEGVYEGSHTCSITAGLD 79
Cdd:MTH00075 1 MAHQAHAFHMVDPSPWPLTGAIAALLLTSGLaMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 80 MGVVGFIISEICFFFSFFWMFFYFSLSPDFILGFTWPPLGVFSVSFLGVPFLNTLILLSSGFFITLSHLNLVSRFSAKFF 159
Cdd:MTH00075 81 YGMILFITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 160 YSYFFGLALGGYFLLVQFYEYYNLSYDFSDGSFGCAFYILTGFHGFHVLLGFVFLFINFIRFYIGHLSTFFVSGFDYSVW 239
Cdd:MTH00075 161 QSLALTIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAW 240
|
250 260
....*....|....*....|
gi 52220973 240 YWHFVDVVWLFLYLFVYWWG 259
Cdd:MTH00075 241 YWHFVDVVWLFLYVSIYWWG 260
|
|
| COX3 |
MTH00130 |
cytochrome c oxidase subunit III; Provisional |
1-259 |
3.62e-54 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177188 Cd Length: 261 Bit Score: 175.72 E-value: 3.62e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 1 MMFNNHFFHLVSSSPWPIVVSSNIFNVGVGL-IWMIGGEFFFFFFFTFLMLIMSFQWWRDVVYEGVYEGSHTCSITAGLD 79
Cdd:MTH00130 1 MAHQAHAYHMVDPSPWPLTGAVAALLMTSGLaIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 80 MGVVGFIISEICFFFSFFWMFFYFSLSPDFILGFTWPPLGVFSVSFLGVPFLNTLILLSSGFFITLSHLNLVSRFSAKFF 159
Cdd:MTH00130 81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 160 YSYFFGLALGGYFLLVQFYEYYNLSYDFSDGSFGCAFYILTGFHGFHVLLGFVFLFINFIRFYIGHLSTFFVSGFDYSVW 239
Cdd:MTH00130 161 QSLTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAW 240
|
250 260
....*....|....*....|
gi 52220973 240 YWHFVDVVWLFLYLFVYWWG 259
Cdd:MTH00130 241 YWHFVDVVWLFLYISIYWWG 260
|
|
| COX3 |
MTH00009 |
cytochrome c oxidase subunit III; Validated |
8-259 |
2.10e-52 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177101 Cd Length: 259 Bit Score: 171.17 E-value: 2.10e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 8 FHLVSSSPWPIVVSSNIFNVGVGLI-WMIGGEFFFFFFFTFLMLIMSFQWWRDVVYEGVYEGSHTCSITAGLDMGVVGFI 86
Cdd:MTH00009 6 FHLVEYSPWPLTGSIGAFTLTVGLAsWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMILFI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 87 ISEICFFFSFFWMFFYFSLSPDFILGFTWPPLGVFSVSFLGVPFLNTLILLSSGFFITLSHLNLVSRFSAKFFYSYFFGL 166
Cdd:MTH00009 86 ASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALILTV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 167 ALGGYFLLVQFYEYYNLSYDFSDGSFGCAFYILTGFHGFHVLLGFVFLFINFIRFYIGHLSTFFVSGFDYSVWYWHFVDV 246
Cdd:MTH00009 166 LLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFVDV 245
|
250
....*....|...
gi 52220973 247 VWLFLYLFVYWWG 259
Cdd:MTH00009 246 VWIFLYLCIYWWG 258
|
|
| COX3 |
MTH00024 |
cytochrome c oxidase subunit III; Validated |
6-259 |
8.23e-52 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 214403 Cd Length: 261 Bit Score: 169.55 E-value: 8.23e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 6 HFFHLVSSSPWPIVVSSNIFNVGVG-LIWMIGGEFFFFFFFTFLMLIMSFQWWRDVVYEGVYEGSHTCSITAGLDMGVVG 84
Cdd:MTH00024 6 HPYHLVEPSPWPFLGAGGAFFITVGsVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGMLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 85 FIISEICFFFSFFWMFFYFSLSPDFILGFTWPPLGVFSVSFLGVPFLNTLILLSSGFFITLSHLNLVSRFSAKFFYSYFF 164
Cdd:MTH00024 86 FILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 165 GLALGGYFLLVQFYEYYNLSYDFSDGSFGCAFYILTGFHGFHVLLGFVFLFINFIRFYIGHLSTFFVSGFDYSVWYWHFV 244
Cdd:MTH00024 166 TVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASWYWHFV 245
|
250
....*....|....*
gi 52220973 245 DVVWLFLYLFVYWWG 259
Cdd:MTH00024 246 DVVWLFLYLCIYWWG 260
|
|
| COX3 |
MTH00052 |
cytochrome c oxidase subunit III; Provisional |
1-259 |
1.31e-51 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 164623 Cd Length: 262 Bit Score: 169.20 E-value: 1.31e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 1 MMFNNHFFHLVSSSPWPIVVSSNIFNVGVG-LIWMIGGEFFFFFFFTFLMLIMSFQWWRDVVYEGVYEGSHTCSITAGLD 79
Cdd:MTH00052 2 MQQYYHPYHLVDPSPWPYIGGCGALFTTVGgVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 80 MGVVGFIISEICFFFSFFWMFFYFSLSPDFILGFTWPPLGVFSVSFLGVPFLNTLILLSSGFFITLSHLNLVSRFSAKFF 159
Cdd:MTH00052 82 YGMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEAI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 160 YSYFFGLALGGYFLLVQFYEYYNLSYDFSDGSFGCAFYILTGFHGFHVLLGFVFLFINFIRFYIGHLSTFFVSGFDYSVW 239
Cdd:MTH00052 162 IGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAAW 241
|
250 260
....*....|....*....|
gi 52220973 240 YWHFVDVVWLFLYLFVYWWG 259
Cdd:MTH00052 242 YWHFVDVVWLFLFIFMYWWG 261
|
|
| COX3 |
MTH00028 |
cytochrome c oxidase subunit III; Provisional |
6-259 |
9.32e-50 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214406 Cd Length: 297 Bit Score: 165.63 E-value: 9.32e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 6 HFFHLVSSSPWPIVVSSNIFNVGVGLIWMIG-GEFFFFFFFTFLMLIMSFQWWRDVVYEGVYEGSHTCSITAGLDMGVVG 84
Cdd:MTH00028 6 HPYHLVDPSPWPFVGASGAFLFTSGAVILFHySDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 85 FIISEICFFFSFFWMFFYFSLSPDFILGFTWPPLGVFSVSFLGVPFLNTLILLSSGFFITLSH----------------- 147
Cdd:MTH00028 86 FILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHhaiigtgnpaslekgtq 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 148 -------------------LNLVSRFSAKFFYSYFFGLALGGYFLLVQFYEYYNLSYDFSDGSFGCAFYILTGFHGFHVL 208
Cdd:MTH00028 166 giegpnpsngappdpqkgpTFLLSDFRTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVL 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 52220973 209 LGFVFLFINFIRFYIGHLSTFFVSGFDYSVWYWHFVDVVWLFLYLFVYWWG 259
Cdd:MTH00028 246 VGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWG 296
|
|
| PLN02194 |
PLN02194 |
cytochrome-c oxidase |
6-260 |
6.22e-45 |
|
cytochrome-c oxidase
Pssm-ID: 177845 Cd Length: 265 Bit Score: 152.12 E-value: 6.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 6 HFFHLVSSSPWPIVVSSNIFNVGVGLIWMI----GGEFFFFFFFTFLMLIMsFQWWRDVVYEGVYEGSHTCSITAGLDMG 81
Cdd:PLN02194 7 HSYHLVDPSPWPISGSLGALATTVGGVMYMhpfqGGARLLSLGLIFILYTM-FVWWRDVLRESTLEGHHTKVVQLGPRYG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 82 VVGFIISEICFFFSFFWMFFYFSLSPDFILGFTWPPLGVFSVSFLGVPFLNTLILLSSGFFITLSHLNLVSRFSAKFFYS 161
Cdd:PLN02194 86 SILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEKRAVYA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 162 YFFGLALGGYFLLVQFYEYYNLSYDFSDGSFGCAFYILTGFHGFHVLLGFVFLFINFIRFYIGHLSTFFVSGFDYSVWYW 241
Cdd:PLN02194 166 LVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWYW 245
|
250
....*....|....*....
gi 52220973 242 HFVDVVWLFLYLFVYWWGG 260
Cdd:PLN02194 246 HFVDVVWLFLFVSIYWWGG 264
|
|
| COX3 |
MTH00083 |
cytochrome c oxidase subunit III; Provisional |
6-259 |
6.36e-41 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177150 Cd Length: 256 Bit Score: 141.25 E-value: 6.36e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 6 HFFHLVSSSPWPIVVSSNIFNVGVGLIWMIG-GEFFFFFFFTFLMLIMSFQWWRDVVYEGvYEGSHTCSITAGLDMGVVG 84
Cdd:MTH00083 3 HNFHILSLSSYPYMMFFSSLGLTSSLVVFFKyGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 85 FIISEICFFFSFFWMFFYFSLSPDFILGFTWPPLGVFSVSFLGVPFLNTLILLSSGFFITLSHlNLVSRFSAKFFYSYFF 164
Cdd:MTH00083 82 FIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSH-HSLCLSNKSCTNSLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 165 GLALGGYFLLVQFYEYYNLSYDFSDGSFGCAFYILTGFHGFHVLLGFVFLFINFIRFYIGHLSTFFVSGFDYSVWYWHFV 244
Cdd:MTH00083 161 TCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFV 240
|
250
....*....|....*
gi 52220973 245 DVVWLFLYLFVYWWG 259
Cdd:MTH00083 241 DVVWLFLFVFVYWWS 255
|
|
| Heme_Cu_Oxidase_III_like |
cd00386 |
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ... |
70-258 |
4.94e-38 |
|
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. This group additionally contains proteins which are fusions between subunits I and III, such as Sulfolobus acidocaldarius SoxM, a subunit of the SoxM terminal oxidase complex. It also includes NorE which has been speculated to be a subunit of nitric oxide reductase. Some archaebacterial cytochrome oxidases lack subunit III. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria.
Pssm-ID: 238227 Cd Length: 183 Bit Score: 131.56 E-value: 4.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 70 HTCSITAGLDMGVVGFIISEICFFFSFFWMFFYFSLSPDFILGFtwpplgvfSVSFLGVPFLNTLILLSSGFFITLSH-- 147
Cdd:cd00386 1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFGA--------GLDPLDLPLLNTNTLLLSGSSVTWAHas 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 148 LNLVSRFSAKFFYSYFFGLALGGYFLLVQFYEYYNLSYDFSDGSFGCAFYILTGFHGFHVLLGFVFLFINFIRFYIGHLS 227
Cdd:cd00386 73 LAARRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152
|
170 180 190
....*....|....*....|....*....|.
gi 52220973 228 TFFVSGFDYSVWYWHFVDVVWLFLYLFVYWW 258
Cdd:cd00386 153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
126-258 |
5.93e-30 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 111.09 E-value: 5.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 126 LGVPFLNTLILLSSGFFITLSHLNLVSRFSAKFFYSYFFGLALGGYFLLVQFYEYYNLS---YDFSDGSFGCAFYILTGF 202
Cdd:COG1845 57 LPLPLINTLLLLLSSFTVALAVRAARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHLIaegLTPTSNAFGSFFFLLTGF 136
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 52220973 203 HGFHVLLGFVFLFINFIRFYIGHLSTFFVSGFDYSVWYWHFVDVVWLFLYLFVYWW 258
Cdd:COG1845 137 HGLHVIIGLIWLLVVLVRALRGGFTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| NorE_like |
cd02862 |
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ... |
131-256 |
6.38e-15 |
|
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: 70.73 E-value: 6.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 131 LNTLILLSSGFFITLSHLNLVSRFSAKFFYSYFFGLALGGYFLLVQFYEYY---NLSYDFSDGSFGCAFYILTGFHGFHV 207
Cdd:cd02862 56 LNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYAhkiAAGIDPDAGLFFTLYFLLTGFHLLHV 135
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 52220973 208 LLGFVFLFINFIRFYIGHLSTFFVSGFDYSVWYWHFVDVVWLFLYLFVY 256
Cdd:cd02862 136 LIGLGILLWVAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVLFPLLY 184
|
|
| Ubiquinol_oxidase_III |
cd02863 |
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ... |
130-256 |
2.65e-11 |
|
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: 60.72 E-value: 2.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 130 FLNTLILLSSGFFITLSHLNLVSRFSAKFFYSYFFGLALGGYFLLVQFYEYYNL---SYDFSDGSFGCAFYILTGFHGFH 206
Cdd:cd02863 54 FIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEFHHLiaeGAGPDRSAFLSAFFTLVGTHGLH 133
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 52220973 207 VLLGFVFLFINFIRFYIGHLSTFFVSGFDYSVWYWHFVDVVWLFLYLFVY 256
Cdd:cd02863 134 VTFGLIWILVMIIQLKKRGLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
|
|
| COX3 |
MTH00049 |
cytochrome c oxidase subunit III; Validated |
124-256 |
1.08e-10 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177124 Cd Length: 215 Bit Score: 59.54 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 124 SFLGVPFLNTLILLSSGFFITLSHLNLVSRFSAKFFYsyfFGLALGGYFLLVQFYEYYNLSYDFSDGSFGCAFYILTGFH 203
Cdd:MTH00049 88 SSLEIPFVGCFLLLGSSITVTAYHHLLGWKYCDLFLY---LTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLH 164
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 52220973 204 GFHVLLGFVFLfinfIRFYIGHLSTFFVSGFDYSVWYWHFVDVVWLFLYLFVY 256
Cdd:MTH00049 165 FSHVVLGVVGL----STLLLVGSSSFGVYRSTVLTWYWHFVDYIWLLVYLIVY 213
|
|
| Heme_Cu_Oxidase_III_2 |
cd02865 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
165-258 |
1.81e-09 |
|
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: 55.84 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 165 GLALGGYFLLVQFYEYYNLSYDFSDG---SFGCAFYILTGFHGFHVLLGFVFLFINFIRFYIGHLSTFFVSGFDYSVWYW 241
Cdd:cd02865 88 AGALALAFLAGQLLAWHALNDAGYGPtsnPAGSFFYLLTGLHGLHVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYW 167
|
90
....*....|....*..
gi 52220973 242 HFVDVVWLFLYLFVYWW 258
Cdd:cd02865 168 HFLLLVWLVLLALLYGT 184
|
|
| Heme_Cu_Oxidase_III_1 |
cd02864 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
192-258 |
5.12e-08 |
|
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: 51.73 E-value: 5.12e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52220973 192 FGCAFYILTGFHGFHVLLGFVFLFINFIRFYIG-HLSTFFVSGFDYSVWYWHFVDVVWLFLYLFVYWW 258
Cdd:cd02864 135 FGASFFMITGFHGTHVTIGVIYLIIIARKVWRGkYQRIGRYEIVEIAGLYWHFVDLVWVFIFAFFYLW 202
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
133-259 |
4.49e-06 |
|
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: 46.00 E-value: 4.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 133 TLILLSSGFFITLSHLNLVSRFSAKFFYSYFFGLALGGYFLLVQFYE---YYNLSYDFSDGSFGCAFYILTGFHGFHVLL 209
Cdd:TIGR02897 59 TFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCHVTL 138
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 52220973 210 GFVFLFINFIRFYIGHLSTFFVSGFDYSVWYWHFVDVVWLFLYLFVYWWG 259
Cdd:TIGR02897 139 GIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
| PRK10663 |
PRK10663 |
cytochrome o ubiquinol oxidase subunit III; Provisional |
134-259 |
6.78e-05 |
|
cytochrome o ubiquinol oxidase subunit III; Provisional
Pssm-ID: 182628 Cd Length: 204 Bit Score: 42.85 E-value: 6.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52220973 134 LILLSS---GFFITLSHLNLVSRFSAKFFYSYFFGLAlggyFLLVQFYEYYNL---SYDFSDGSFGCAFYILTGFHGFHV 207
Cdd:PRK10663 75 LLLFSSityGMAAIAMYKNNKSQVISWLALTFLFGAG----FIGMEIYEFHHLiveGMGPDRSGFLSAFFALVGTHGLHV 150
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 52220973 208 LLGFVFLFINFIRFYIGHLSTFFVSGFDYSVWYWHFVDVVWLFLYLFVYWWG 259
Cdd:PRK10663 151 TSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMG 202
|
|
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