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Conserved domains on  [gi|2473932309|ref|YP_010735838|]
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cytochrome c oxidase subunit III (mitochondrion) [Phytomastax pentaspinula]

Protein Classification

cytochrome c oxidase subunit 3( domain architecture ID 10009592)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 6-259 5.57e-164

cytochrome c oxidase subunit III; Provisional


:

Pssm-ID: 214439  Cd Length: 255  Bit Score: 454.25  E-value: 5.57e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309   6 NNQPYHLVDKSPWPLTAAIGAMVTASGLAKWFHMFNSSLMYNGMMITLLTLYQWWRDVTREGTLQGLHTLLVSKGLRLGM 85
Cdd:MTH00155    2 KNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309  86 ILFISSEVLFFMAFFWAYFHSSLAPTIELGMMWPPEGIKPFNPMQVPLLNTVILLSSGITVTWAHHSLMESNYSMGSQGL 165
Cdd:MTH00155   82 ILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309 166 MLTVILGLYFTLLQGYEYWESPFTISDSIYGSTFFLATGFHGIHVIIGTTFLLICLIRHYYNHFSNNHHFGFEAAAWYWH 245
Cdd:MTH00155  162 FFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYWH 241

                         250
                  ....*....|....
gi 2473932309 246 FVDVVWLFLYISIY 259
Cdd:MTH00155  242 FVDVVWLFLYISIY 255
 
Name Accession Description Interval E-value
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 6-259 5.57e-164

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 454.25  E-value: 5.57e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309   6 NNQPYHLVDKSPWPLTAAIGAMVTASGLAKWFHMFNSSLMYNGMMITLLTLYQWWRDVTREGTLQGLHTLLVSKGLRLGM 85
Cdd:MTH00155    2 KNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309  86 ILFISSEVLFFMAFFWAYFHSSLAPTIELGMMWPPEGIKPFNPMQVPLLNTVILLSSGITVTWAHHSLMESNYSMGSQGL 165
Cdd:MTH00155   82 ILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309 166 MLTVILGLYFTLLQGYEYWESPFTISDSIYGSTFFLATGFHGIHVIIGTTFLLICLIRHYYNHFSNNHHFGFEAAAWYWH 245
Cdd:MTH00155  162 FFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYWH 241

                         250
                  ....*....|....
gi 2473932309 246 FVDVVWLFLYISIY 259
Cdd:MTH00155  242 FVDVVWLFLYISIY 255
COX3 pfam00510
Cytochrome c oxidase subunit III;
9-262 4.99e-127

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 360.96  E-value: 4.99e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309   9 PYHLVDKSPWPLTAAIGAMVTASGLAKWFHMF--NSSLMYNGMMITLLTLYQWWRDVTREGTLQGLHTLLVSKGLRLGMI 86
Cdd:pfam00510   2 PFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYsgNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGMI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309  87 LFISSEVLFFMAFFWAYFHSSLAPTIELGMMWPPEGIKPFNPMQVPLLNTVILLSSGITVTWAHHSLMESNYSMGSQGLM 166
Cdd:pfam00510  82 LFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGLI 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309 167 LTVILGLYFTLLQGYEYWESPFTISDSIYGSTFFLATGFHGIHVIIGTTFLLICLIRHYYNHFSNNHHFGFEAAAWYWHF 246
Cdd:pfam00510 162 LTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWHF 241

                         250
                  ....*....|....*.
gi 2473932309 247 VDVVWLFLYISIYWWS 262
Cdd:pfam00510 242 VDVVWLFLYVSVYWWG 257
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 20-261 1.07e-126

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: 359.52  E-value: 1.07e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309  20 LTAAIGAMVTASGLAKWFHMFNSS-LMYNGMMITLLTLYQWWRDVTREGTLQGLHTLLVSKGLRLGMILFISSEVLFFMA 98
Cdd:cd01665     1 ILGSFGLLLLALGLVLWMHGYGGPlLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309  99 FFWAYFHSSLAPTIELGMMWPPEGIKPFNPMQVPLLNTVILLSSGITVTWAHHSLMESNYSMGSQGLMLTVILGLYFTLL 178
Cdd:cd01665    81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309 179 QGYEYWESPFTISDSIYGSTFFLATGFHGIHVIIGTTFLLICLIRHYYNHFSNNHHFGFEAAAWYWHFVDVVWLFLYISI 258
Cdd:cd01665   161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240


                  ...
gi 2473932309 259 YWW 261
Cdd:cd01665   241 YWW 243
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
72-261 3.77e-55

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 175.81  E-value: 3.77e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309  72 LHTLLVSKGLRLGMILFISSEVLFFMAFFWAYFHSSLAPTielgmmWPPEGIKPFNPmQVPLLNTVILLSSGITVTWAHH 151
Cdd:COG1845     7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRASAP------DWPAGAELLDL-PLPLINTLLLLLSSFTVALAVR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309 152 SLMESNYSMGSQGLMLTVILGLYFTLLQGYEY---WESPFTISDSIYGSTFFLATGFHGIHVIIGTTFLLICLIRHYYNH 228
Cdd:COG1845    80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2473932309 229 FSNNHHFGFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:COG1845   160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 83-259 1.09e-09

cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]


Pssm-ID: 131943  Cd Length: 190  Bit Score: 56.40  E-value: 1.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309  83 LGMILFISSEVLFFMAFFWAYFHSSLAPTielgmmwpPEGIKPFNPMQVPLL--NTVILLSSGITVTWAHHSLMESNYSM 160
Cdd:TIGR02897  12 LGFWIFLGAEIALFATLFATYLVLQHGGD--------YAGKMPAELFELPLVliMTFLLLFSSFTCGIAIYEMRKENQKL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309 161 GSQGLMLTVILGLYFTLLQGYE---YWESPFTISDSIYGSTFFLATGFHGIHV---IIGTTFLLICLIRHYYNHFSNNHH 234
Cdd:TIGR02897  84 MMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCHVtlgIVWAICLLIQIQRRGLTPYTAPKV 163

                         170       180
                  ....*....|....*....|....*
gi 2473932309 235 FgfeAAAWYWHFVDVVWLFLYISIY 259
Cdd:TIGR02897 164 F---IVSLYWHFLDVVWVFIFTAVY 185
 
Name Accession Description Interval E-value
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 6-259 5.57e-164

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 454.25  E-value: 5.57e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309   6 NNQPYHLVDKSPWPLTAAIGAMVTASGLAKWFHMFNSSLMYNGMMITLLTLYQWWRDVTREGTLQGLHTLLVSKGLRLGM 85
Cdd:MTH00155    2 KNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309  86 ILFISSEVLFFMAFFWAYFHSSLAPTIELGMMWPPEGIKPFNPMQVPLLNTVILLSSGITVTWAHHSLMESNYSMGSQGL 165
Cdd:MTH00155   82 ILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309 166 MLTVILGLYFTLLQGYEYWESPFTISDSIYGSTFFLATGFHGIHVIIGTTFLLICLIRHYYNHFSNNHHFGFEAAAWYWH 245
Cdd:MTH00155  162 FFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYWH 241

                         250
                  ....*....|....
gi 2473932309 246 FVDVVWLFLYISIY 259
Cdd:MTH00155  242 FVDVVWLFLYISIY 255
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 4-261 3.15e-150

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 419.74  E-value: 3.15e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309   4 TDNNQPYHLVDKSPWPLTAAIGAMVTASGLAKWFHMFNSSLMYNGMMITLLTLYQWWRDVTREGTLQGLHTLLVSKGLRL 83
Cdd:MTH00118    2 THQAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309  84 GMILFISSEVLFFMAFFWAYFHSSLAPTIELGMMWPPEGIKPFNPMQVPLLNTVILLSSGITVTWAHHSLMESNYSMGSQ 163
Cdd:MTH00118   82 GMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309 164 GLMLTVILGLYFTLLQGYEYWESPFTISDSIYGSTFFLATGFHGIHVIIGTTFLLICLIRHYYNHFSNNHHFGFEAAAWY 243
Cdd:MTH00118  162 ALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWY 241

                         250
                  ....*....|....*...
gi 2473932309 244 WHFVDVVWLFLYISIYWW 261
Cdd:MTH00118  242 WHFVDVVWLFLYISIYWW 259
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 9-261 4.93e-146

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 408.98  E-value: 4.93e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309   9 PYHLVDKSPWPLTAAIGAMVTASGLAKWFHMFNSSLMYNGMMITLLTLYQWWRDVTREGTLQGLHTLLVSKGLRLGMILF 88
Cdd:MTH00189    6 PFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRYGMILF 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309  89 ISSEVLFFMAFFWAYFHSSLAPTIELGMMWPPEGIKPFNPMQVPLLNTVILLSSGITVTWAHHSLMESNYSMGSQGLMLT 168
Cdd:MTH00189   86 ITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQALTLT 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309 169 VILGLYFTLLQGYEYWESPFTISDSIYGSTFFLATGFHGIHVIIGTTFLLICLIRHYYNHFSNNHHFGFEAAAWYWHFVD 248
Cdd:MTH00189  166 VILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWYWHFVD 245

                         250
                  ....*....|...
gi 2473932309 249 VVWLFLYISIYWW 261
Cdd:MTH00189  246 VVWLFLYVSIYWW 258
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 9-261 2.88e-139

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 391.78  E-value: 2.88e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309   9 PYHLVDKSPWPLTAAIGAMVTASGLAKWFHMFNSSLMYNGMMITLLTLYQWWRDVTREGTLQGLHTLLVSKGLRLGMILF 88
Cdd:MTH00039    6 PYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRYGMILF 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309  89 ISSEVLFFMAFFWAYFHSSLAPTIELGMMWPPEGIKPFNPMQVPLLNTVILLSSGITVTWAHHSLMESNYSMGSQGLMLT 168
Cdd:MTH00039   86 ITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQALFLT 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309 169 VILGLYFTLLQGYEYWESPFTISDSIYGSTFFLATGFHGIHVIIGTTFLLICLIRHYYNHFSNNHHFGFEAAAWYWHFVD 248
Cdd:MTH00039  166 VLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWYWHFVD 245

                         250
                  ....*....|...
gi 2473932309 249 VVWLFLYISIYWW 261
Cdd:MTH00039  246 VVWLFLYVCIYWW 258
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 8-262 1.01e-138

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 390.41  E-value: 1.01e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309   8 QPYHLVDKSPWPLTAAIGAMVTASGLAKWFHMFNSSLMYNGMMITLLTLYQWWRDVTREGTLQGLHTLLVSKGLRLGMIL 87
Cdd:MTH00141    4 NPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFIL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309  88 FISSEVLFFMAFFWAYFHSSLAPTIELGMMWPPEGIKPFNPMQVPLLNTVILLSSGITVTWAHHSLMESNYSMGSQGLML 167
Cdd:MTH00141   84 FIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309 168 TVILGLYFTLLQGYEYWESPFTISDSIYGSTFFLATGFHGIHVIIGTTFLLICLIRHYYNHFSNNHHFGFEAAAWYWHFV 247
Cdd:MTH00141  164 TIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFV 243

                         250
                  ....*....|....*
gi 2473932309 248 DVVWLFLYISIYWWS 262
Cdd:MTH00141  244 DVVWLFLYLSIYWWG 258
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 2-261 1.59e-135

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 382.60  E-value: 1.59e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309   2 MTTDNNQPYHLVDKSPWPLTAAIGAMVTASGLAKWFHMFNSSLMYNGMMITLLTLYQWWRDVTREGTLQGLHTLLVSKGL 81
Cdd:MTH00219    1 MMFFQTNPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309  82 RLGMILFISSEVLFFMAFFWAYFHSSLAPTIELGMMWPPEGIKPFNPMQVPLLNTVILLSSGITVTWAHHSLMESNYSMG 161
Cdd:MTH00219   81 RIGMILFIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309 162 SQGLMLTVILGLYFTLLQGYEYWESPFTISDSIYGSTFFLATGFHGIHVIIGTTFLLICLIRHYYNHFSNNHHFGFEAAA 241
Cdd:MTH00219  161 QQGLLFTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAA 240

                         250       260
                  ....*....|....*....|
gi 2473932309 242 WYWHFVDVVWLFLYISIYWW 261
Cdd:MTH00219  241 WYWHFVDVVWLFLYVSIYWW 260
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 9-261 1.28e-133

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 377.57  E-value: 1.28e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309   9 PYHLVDKSPWPLTAAIGAMVTASGLAKWFHMFNSSLMYNGMMITLLTLYQWWRDVTREGTLQGLHTLLVSKGLRLGMILF 88
Cdd:MTH00130    7 AYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRYGMILF 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309  89 ISSEVLFFMAFFWAYFHSSLAPTIELGMMWPPEGIKPFNPMQVPLLNTVILLSSGITVTWAHHSLMESNYSMGSQGLMLT 168
Cdd:MTH00130   87 ITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQSLTLT 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309 169 VILGLYFTLLQGYEYWESPFTISDSIYGSTFFLATGFHGIHVIIGTTFLLICLIRHYYNHFSNNHHFGFEAAAWYWHFVD 248
Cdd:MTH00130  167 ILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWYWHFVD 246

                         250
                  ....*....|...
gi 2473932309 249 VVWLFLYISIYWW 261
Cdd:MTH00130  247 VVWLFLYISIYWW 259
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 4-261 8.59e-132

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 372.91  E-value: 8.59e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309   4 TDNNQPYHLVDKSPWPLTAAIGAMVTASGLAKWFHMFNSSLMYNGMMITLLTLYQWWRDVTREGTLQGLHTLLVSKGLRL 83
Cdd:MTH00099    2 THQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309  84 GMILFISSEVLFFMAFFWAYFHSSLAPTIELGMMWPPEGIKPFNPMQVPLLNTVILLSSGITVTWAHHSLMESNYSMGSQ 163
Cdd:MTH00099   82 GMILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309 164 GLMLTVILGLYFTLLQGYEYWESPFTISDSIYGSTFFLATGFHGIHVIIGTTFLLICLIRHYYNHFSNNHHFGFEAAAWY 243
Cdd:MTH00099  162 ALFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWY 241

                         250
                  ....*....|....*...
gi 2473932309 244 WHFVDVVWLFLYISIYWW 261
Cdd:MTH00099  242 WHFVDVVWLFLYVSIYWW 259
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 10-261 1.72e-130

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 369.84  E-value: 1.72e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309  10 YHLVDKSPWPLTAAIGAMVTASGLAKWFHMFNSSLMYNGMMITLLTLYQWWRDVTREGTLQGLHTLLVSKGLRLGMILFI 89
Cdd:MTH00075    8 FHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRYGMILFI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309  90 SSEVLFFMAFFWAYFHSSLAPTIELGMMWPPEGIKPFNPMQVPLLNTVILLSSGITVTWAHHSLMESNYSMGSQGLMLTV 169
Cdd:MTH00075   88 TSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQSLALTI 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309 170 ILGLYFTLLQGYEYWESPFTISDSIYGSTFFLATGFHGIHVIIGTTFLLICLIRHYYNHFSNNHHFGFEAAAWYWHFVDV 249
Cdd:MTH00075  168 ILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWYWHFVDV 247

                         250
                  ....*....|..
gi 2473932309 250 VWLFLYISIYWW 261
Cdd:MTH00075  248 VWLFLYVSIYWW 259
COX3 pfam00510
Cytochrome c oxidase subunit III;
9-262 4.99e-127

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 360.96  E-value: 4.99e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309   9 PYHLVDKSPWPLTAAIGAMVTASGLAKWFHMF--NSSLMYNGMMITLLTLYQWWRDVTREGTLQGLHTLLVSKGLRLGMI 86
Cdd:pfam00510   2 PFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYsgNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGMI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309  87 LFISSEVLFFMAFFWAYFHSSLAPTIELGMMWPPEGIKPFNPMQVPLLNTVILLSSGITVTWAHHSLMESNYSMGSQGLM 166
Cdd:pfam00510  82 LFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGLI 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309 167 LTVILGLYFTLLQGYEYWESPFTISDSIYGSTFFLATGFHGIHVIIGTTFLLICLIRHYYNHFSNNHHFGFEAAAWYWHF 246
Cdd:pfam00510 162 LTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWHF 241

                         250
                  ....*....|....*.
gi 2473932309 247 VDVVWLFLYISIYWWS 262
Cdd:pfam00510 242 VDVVWLFLYVSVYWWG 257
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 20-261 1.07e-126

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: 359.52  E-value: 1.07e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309  20 LTAAIGAMVTASGLAKWFHMFNSS-LMYNGMMITLLTLYQWWRDVTREGTLQGLHTLLVSKGLRLGMILFISSEVLFFMA 98
Cdd:cd01665     1 ILGSFGLLLLALGLVLWMHGYGGPlLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309  99 FFWAYFHSSLAPTIELGMMWPPEGIKPFNPMQVPLLNTVILLSSGITVTWAHHSLMESNYSMGSQGLMLTVILGLYFTLL 178
Cdd:cd01665    81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309 179 QGYEYWESPFTISDSIYGSTFFLATGFHGIHVIIGTTFLLICLIRHYYNHFSNNHHFGFEAAAWYWHFVDVVWLFLYISI 258
Cdd:cd01665   161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240


                  ...
gi 2473932309 259 YWW 261
Cdd:cd01665   241 YWW 243
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 8-261 1.09e-121

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 347.59  E-value: 1.09e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309   8 QPYHLVDKSPWPLTAAIGAMVTASGLAKWFHMFNSSLMYNGMMITLLTLYQWWRDVTREGTLQGLHTLLVSKGLRLGMIL 87
Cdd:MTH00009    4 QPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMIL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309  88 FISSEVLFFMAFFWAYFHSSLAPTIELGMMWPPEGIKPFNPMQVPLLNTVILLSSGITVTWAHHSLMESNYSMGSQGLML 167
Cdd:MTH00009   84 FIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALIL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309 168 TVILGLYFTLLQGYEYWESPFTISDSIYGSTFFLATGFHGIHVIIGTTFLLICLIRHYYNHFSNNHHFGFEAAAWYWHFV 247
Cdd:MTH00009  164 TVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFV 243

                         250
                  ....*....|....
gi 2473932309 248 DVVWLFLYISIYWW 261
Cdd:MTH00009  244 DVVWIFLYLCIYWW 257
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 9-261 2.33e-121

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 346.74  E-value: 2.33e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309   9 PYHLVDKSPWPLTAAIGAMVTASGLAKWFHMFNSSLMYNGMMITLLTLYQWWRDVTREGTLQGLHTLLVSKGLRLGMILF 88
Cdd:MTH00024    7 PYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGMLLF 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309  89 ISSEVLFFMAFFWAYFHSSLAPTIELGMMWPPEGIKPFNPMQVPLLNTVILLSSGITVTWAHHSLMESNYSMGSQGLMLT 168
Cdd:MTH00024   87 ILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFLT 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309 169 VILGLYFTLLQGYEYWESPFTISDSIYGSTFFLATGFHGIHVIIGTTFLLICLIRHYYNHFSNNHHFGFEAAAWYWHFVD 248
Cdd:MTH00024  167 VFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASWYWHFVD 246

                         250
                  ....*....|...
gi 2473932309 249 VVWLFLYISIYWW 261
Cdd:MTH00024  247 VVWLFLYLCIYWW 259
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 8-261 7.70e-114

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 327.52  E-value: 7.70e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309   8 QPYHLVDKSPWPLTAAIGAMVTASGLAKWFHMFNSSLMYNGMMITLLTLYQWWRDVTREGTLQGLHTLLVSKGLRLGMIL 87
Cdd:MTH00052    7 HPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGLKYGMIL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309  88 FISSEVLFFMAFFWAYFHSSLAPTIELGMMWPPEGIKPFNPMQVPLLNTVILLSSGITVTWAHHSLMESNYSMGSQGLML 167
Cdd:MTH00052   87 FIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEAIIGLAL 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309 168 TVILGLYFTLLQGYEYWESPFTISDSIYGSTFFLATGFHGIHVIIGTTFLLICLIRHYYNHFSNNHHFGFEAAAWYWHFV 247
Cdd:MTH00052  167 TVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAAWYWHFV 246

                         250
                  ....*....|....
gi 2473932309 248 DVVWLFLYISIYWW 261
Cdd:MTH00052  247 DVVWLFLFIFMYWW 260
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 8-261 1.60e-101

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 297.75  E-value: 1.60e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309   8 QPYHLVDKSPWPLTAAIGAMVTASGLAKWFHMFNSSLMYNGMMITLLTLYQWWRDVTREGTLQGLHTLLVSKGLRLGMIL 87
Cdd:MTH00028    6 HPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309  88 FISSEVLFFMAFFWAYFHSSLAPTIELGMMWPPEGIKPFNPMQVPLLNTVILLSSGITVTWAHHSLM----ESNYSMGSQ 163
Cdd:MTH00028   86 FILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIgtgnPASLEKGTQ 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309 164 --------------------------------GLMLTVILGLYFTLLQGYEYWESPFTISDSIYGSTFFLATGFHGIHVI 211
Cdd:MTH00028  166 giegpnpsngappdpqkgptfllsdfrtnaviGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVL 245

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2473932309 212 IGTTFLLICLIRHYYNHFSNNHHFGFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:MTH00028  246 VGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWW 295
PLN02194 PLN02194
cytochrome-c oxidase
 2-261 5.06e-92

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 272.31  E-value: 5.06e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309   2 MTTDNNQPYHLVDKSPWPLTAAIGAMVTASGLAKWFHMFN--SSLMYNGMMITLLTLYQWWRDVTREGTLQGLHTLLVSK 79
Cdd:PLN02194    1 MIESQRHSYHLVDPSPWPISGSLGALATTVGGVMYMHPFQggARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309  80 GLRLGMILFISSEVLFFMAFFWAYFHSSLAPTIELGMMWPPEGIKPFNPMQVPLLNTVILLSSGITVTWAHHSLMESNYS 159
Cdd:PLN02194   81 GPRYGSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309 160 MGSQGLMLTVILGLYFTLLQGYEYWESPFTISDSIYGSTFFLATGFHGIHVIIGTTFLLICLIRHYYNHFSNNHHFGFEA 239
Cdd:PLN02194  161 RAVYALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEA 240

                         250       260
                  ....*....|....*....|..
gi 2473932309 240 AAWYWHFVDVVWLFLYISIYWW 261
Cdd:PLN02194  241 AAWYWHFVDVVWLFLFVSIYWW 262
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
 10-262 1.66e-72

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 222.52  E-value: 1.66e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309  10 YHLVDKSPWPLTAAIGAMVTASGLAKWFHMFNSSLMYNGMMITLLTLYQWWRDVTREGtLQGLHTLLVSKGLRLGMILFI 89
Cdd:MTH00083    5 FHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMILFI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309  90 SSEVLFFMAFFWAYFHSSLAPTIELGMMWPPEGIKPFNPMQVPLLNTVILLSSGITVTWAHHSLMESNYSMGSqGLMLTV 169
Cdd:MTH00083   84 FSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSNKSCTN-SLLLTC 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309 170 ILGLYFTLLQGYEYWESPFTISDSIYGSTFFLATGFHGIHVIIGTTFLLICLIRHYYNHFSNNHHFGFEAAAWYWHFVDV 249
Cdd:MTH00083  163 FLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFVDV 242

                         250
                  ....*....|...
gi 2473932309 250 VWLFLYISIYWWS 262
Cdd:MTH00083  243 VWLFLFVFVYWWS 255
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 73-261 6.96e-71

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: 215.53  E-value: 6.96e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309  73 HTLLVSKGLRLGMILFISSEVLFFMAFFWAYFHSSLAPTIELGMmwppegikPFNPMQVPLLNTVILLSSGITVTWAHHS 152
Cdd:cd00386     1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFGA--------GLDPLDLPLLNTNTLLLSGSSVTWAHAS 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309 153 LM--ESNYSMGSQGLMLTVILGLYFTLLQGYEYWESPFTISDSIYGSTFFLATGFHGIHVIIGTTFLLICLIRHYYNHFS 230
Cdd:cd00386    73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2473932309 231 NNHHFGFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:cd00386   153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
72-261 3.77e-55

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 175.81  E-value: 3.77e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309  72 LHTLLVSKGLRLGMILFISSEVLFFMAFFWAYFHSSLAPTielgmmWPPEGIKPFNPmQVPLLNTVILLSSGITVTWAHH 151
Cdd:COG1845     7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRASAP------DWPAGAELLDL-PLPLINTLLLLLSSFTVALAVR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309 152 SLMESNYSMGSQGLMLTVILGLYFTLLQGYEY---WESPFTISDSIYGSTFFLATGFHGIHVIIGTTFLLICLIRHYYNH 228
Cdd:COG1845    80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2473932309 229 FSNNHHFGFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:COG1845   160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
NorE_like cd02862
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ...
 82-259 1.54e-24

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: 96.54  E-value: 1.54e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309  82 RLGMILFISSEVLFFMAFFWAYF-HSSLAP--------TIELGMmwppegikpfnpmqvPLLNTVILLSSGITVTWAHHS 152
Cdd:cd02862    10 KLGMWVFILSELLAFGALFIAYAvYRALYPelfaagsaHLDLLL---------------GALNTLVLLTSSFTVALAVRA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309 153 LMESNYSMGSQGLMLTVILGLYFTLLQGYEYWES---PFTISDSIYGSTFFLATGFHGIHVIIGTTFLLICLIRHYYNHF 229
Cdd:cd02862    75 ARAGRRRRARRWLAAAVLLGLVFLVIKYFEYAHKiaaGIDPDAGLFFTLYFLLTGFHLLHVLIGLGILLWVAWRARRGRY 154

                         170       180       190
                  ....*....|....*....|....*....|
gi 2473932309 230 SNNHHFGFEAAAWYWHFVDVVWLFLYISIY 259
Cdd:cd02862   155 SARDYEGVEAAALYWHMVDLVWIVLFPLLY 184
Heme_Cu_Oxidase_III_2 cd02865
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 80-261 7.43e-18

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: 78.95  E-value: 7.43e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309  80 GLRLGMILFISSEVLFFMAFFWAYFHSSLAPTielgmMWPPEgikPFNPMQVPLLNTVILLSSGITVTWAHHSLMESNYS 159
Cdd:cd02865     8 PGWWGLWVFMAVEGTLFALLISAYFMRMTSGD-----WQPGA---PLPLPNLLSLNTAVLAASSVAMQWARRAARRNRRV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309 160 MGSQGLMLTVILGLYFTLLQGYEYWESPF---TISDSIYGSTFFLATGFHGIHVIIGTTFLLICLIRHYYNHFSNNHHFG 236
Cdd:cd02865    80 LARLGLALAGALALAFLAGQLLAWHALNDagyGPTSNPAGSFFYLLTGLHGLHVIGGLVALAIVLAGLIRGHYGPRRRLP 159

                         170       180
                  ....*....|....*....|....*
gi 2473932309 237 FEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:cd02865   160 VELCALYWHFLLLVWLVLLALLYGT 184
Ubiquinol_oxidase_III cd02863
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ...
 83-259 1.24e-16

Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the respiratory chains of aerobic bacteria, is a multi-chain transmembrane protein located in the cell membrane. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. Ubiquinol oxidases feature four subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of bovine CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in bovine CcO. Although not required for catalytic activity, subunit III appears to be involved in assembly of the multimer complex.


Pssm-ID: 239214  Cd Length: 186  Bit Score: 75.35  E-value: 1.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309  83 LGMILFISSEVLFFMAFFWAYF--HSSLAPTielgmmwpPEGIKPFNPMQVpLLNTVILLSSGITVTWAHHSLMESNYSM 160
Cdd:cd02863    11 LGFWIYLMSDCILFATLFATYAvlSGNTAGG--------PPGHELFELPLV-FIETFLLLLSSFTCGLAMIAMNKNNKKK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309 161 GSQGLMLTVILGLYFTLLQGYE---YWESPFTISDSIYGSTFFLATGFHGIHVIIGTTFLLICLIRHYYNHFSNNHHFGF 237
Cdd:cd02863    82 VILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLVGTHGLHVTFGLIWILVMIIQLKKRGLTPDTARRL 161

                         170       180
                  ....*....|....*....|..
gi 2473932309 238 EAAAWYWHFVDVVWLFLYISIY 259
Cdd:cd02863   162 FCLSLFWHFLDIVWIFVFTVVY 183
COX3 MTH00049
cytochrome c oxidase subunit III; Validated
 87-259 1.49e-16

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177124  Cd Length: 215  Bit Score: 76.11  E-value: 1.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309  87 LFISSEVLFFMAFFWAYFHSSLAPTIELGmmwppegikpfNPMQVPLLNTVILLSSGITVTWAHHSLmesNYSMGSQGLM 166
Cdd:MTH00049   59 LFILSEVIIFGSLLVCCLWFDDWSYISLS-----------SSLEIPFVGCFLLLGSSITVTAYHHLL---GWKYCDLFLY 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309 167 LTVILGLYFTLLQGYEYWESPFTISDSIYGSTFFLATGFHGIHVIIGTTFLLICLirhYYNHFSNNHHFGfEAAAWYWHF 246
Cdd:MTH00049  125 LTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHFSHVVLGVVGLSTLL---LVGSSSFGVYRS-TVLTWYWHF 200

                         170
                  ....*....|...
gi 2473932309 247 VDVVWLFLYISIY 259
Cdd:MTH00049  201 VDYIWLLVYLIVY 213
Heme_Cu_Oxidase_III_1 cd02864
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 82-261 3.36e-16

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: 74.85  E-value: 3.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309  82 RLGMILFISSEVLFFMAFFWAYFHSSLAPTIELGMMWPPEGIkPFNPMQVPL----LNTVILLSSGITVTWAHHSLMESN 157
Cdd:cd02864    10 KAMMWFFLLSDAFIFSSFLIAYMTARISTTEPWPLPSDVFAL-RIGHFNIPLvliaIMTFILITSSGTMAMAVNFGYRGN 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309 158 YSMGSQGLMLTVILGLYFTLLQGYEY-----------WESPFTISdsIYGSTFFLATGFHGIHVIIGTTFLLICLIRHYY 226
Cdd:cd02864    89 RKAAARLMLATALLGATFVGMQAFEWtkliveegvrpWGNPWGAA--QFGASFFMITGFHGTHVTIGVIYLIIIARKVWR 166

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2473932309 227 NHFSNNHHF-GFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:cd02864   167 GKYQRIGRYeIVEIAGLYWHFVDLVWVFIFAFFYLW 202
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 83-259 1.09e-09

cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]


Pssm-ID: 131943  Cd Length: 190  Bit Score: 56.40  E-value: 1.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309  83 LGMILFISSEVLFFMAFFWAYFHSSLAPTielgmmwpPEGIKPFNPMQVPLL--NTVILLSSGITVTWAHHSLMESNYSM 160
Cdd:TIGR02897  12 LGFWIFLGAEIALFATLFATYLVLQHGGD--------YAGKMPAELFELPLVliMTFLLLFSSFTCGIAIYEMRKENQKL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309 161 GSQGLMLTVILGLYFTLLQGYE---YWESPFTISDSIYGSTFFLATGFHGIHV---IIGTTFLLICLIRHYYNHFSNNHH 234
Cdd:TIGR02897  84 MMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCHVtlgIVWAICLLIQIQRRGLTPYTAPKV 163

                         170       180
                  ....*....|....*....|....*
gi 2473932309 235 FgfeAAAWYWHFVDVVWLFLYISIY 259
Cdd:TIGR02897 164 F---IVSLYWHFLDVVWVFIFTAVY 185
PRK10663 PRK10663
cytochrome o ubiquinol oxidase subunit III; Provisional
 133-259 1.98e-07

cytochrome o ubiquinol oxidase subunit III; Provisional


Pssm-ID: 182628  Cd Length: 204  Bit Score: 50.16  E-value: 1.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932309 133 LLNTVILLSSGITVTWAHHSLMESNYSMGSQGLMLTVILGLYFTLLQGYEYW---ESPFTISDSIYGSTFFLATGFHGIH 209
Cdd:PRK10663   70 LVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFHhliVEGMGPDRSGFLSAFFALVGTHGLH 149

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2473932309 210 VIIGTTFLLICLIRHYYNHFSNNHHFGFEAAAWYWHFVDVVWLFLYISIY 259
Cdd:PRK10663  150 VTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVY 199
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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