NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|52220973|ref|YP_086819|]
View 

cytochrome c oxidase subunit III (mitochondrion) [Trialeurodes vaporariorum]

Protein Classification

cytochrome c oxidase subunit 3( domain architecture ID 10009592)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

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
 
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
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH