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Conserved domains on  [gi|84488627|ref|YP_448822|]
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cytochrome c oxidase subunit III (mitochondrion) [Stigmochelys pardalis]

Protein Classification

cytochrome c oxidase subunit 3( domain architecture ID 10791089)

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 MTH00118
cytochrome c oxidase subunit III; Provisional
 1-261 0e+00

cytochrome c oxidase subunit III; Provisional


:

Pssm-ID: 177179  Cd Length: 261  Bit Score: 502.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627    1 MAHQTHAYHMVDPSPWPLTGAAAALLMTSGLAMWFHYDSMLLMTLGLSIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLR 80
Cdd:MTH00118   1 MTHQAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627   81 YGMILFITSEVFFFIGFFWAFYHSSLAPTPELGGCWPPTGITPLNPFEVPLLNTAVLLASGVTITWAHHSLMETNRNQTI 160
Cdd:MTH00118  81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627  161 QALSLTILLGLYFTMLQTMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLTVCLLRQIKFHFTSTHHFGFEAAAW 240
Cdd:MTH00118 161 QALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAW 240

                        250       260
                 ....*....|....*....|.
gi 84488627  241 YWHFVDVVWLFLYVSIYWWGS 261
Cdd:MTH00118 241 YWHFVDVVWLFLYISIYWWGS 261
 
Name Accession Description Interval E-value
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 1-261 0e+00

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 502.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627    1 MAHQTHAYHMVDPSPWPLTGAAAALLMTSGLAMWFHYDSMLLMTLGLSIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLR 80
Cdd:MTH00118   1 MTHQAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627   81 YGMILFITSEVFFFIGFFWAFYHSSLAPTPELGGCWPPTGITPLNPFEVPLLNTAVLLASGVTITWAHHSLMETNRNQTI 160
Cdd:MTH00118  81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627  161 QALSLTILLGLYFTMLQTMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLTVCLLRQIKFHFTSTHHFGFEAAAW 240
Cdd:MTH00118 161 QALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAW 240

                        250       260
                 ....*....|....*....|.
gi 84488627  241 YWHFVDVVWLFLYVSIYWWGS 261
Cdd:MTH00118 241 YWHFVDVVWLFLYISIYWWGS 261
COX3 pfam00510
Cytochrome c oxidase subunit III;
6-261 7.99e-139

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 390.62  E-value: 7.99e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627     6 HAYHMVDPSPWPLTGAAAALLMTSGLAMWFHY--DSMLLMTLGLSIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRYGM 83
Cdd:pfam00510   1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGysGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627    84 ILFITSEVFFFIGFFWAFYHSSLAPTPELGGCWPPTGITPLNPFEVPLLNTAVLLASGVTITWAHHSLMETNRNQTIQAL 163
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627   164 SLTILLGLYFTMLQTMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLTVCLLRQIKFHFTSTHHFGFEAAAWYWH 243
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240

                         250
                  ....*....|....*...
gi 84488627   244 FVDVVWLFLYVSIYWWGS 261
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWGS 258
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 18-259 8.81e-133

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: 374.54  E-value: 8.81e-133
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627  18 LTGAAAALLMTSGLAMWFH-YDSMLLMTLGLSIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRYGMILFITSEVFFFIG 96
Cdd:cd01665   1 ILGSFGLLLLALGLVLWMHgYGGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627  97 FFWAFYHSSLAPTPELGGCWPPTGITPLNPFEVPLLNTAVLLASGVTITWAHHSLMETNRNQTIQALSLTILLGLYFTML 176
Cdd:cd01665  81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627 177 QTMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLTVCLLRQIKFHFTSTHHFGFEAAAWYWHFVDVVWLFLYVSI 256
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240


                ...
gi 84488627 257 YWW 259
Cdd:cd01665 241 YWW 243
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
70-259 1.21e-48

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 159.24  E-value: 1.21e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627  70 HHTPPVQKGLRYGMILFITSEVFF-FIGFFWAFYHSSLAPtpelggcWPPTGITPLNPFeVPLLNTAVLLASGVTITWAH 148
Cdd:COG1845   7 PHAPERRSPGKLGMWLFLASEVMLfAALFAAYFVLRASAP-------DWPAGAELLDLP-LPLINTLLLLLSSFTVALAV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627 149 HSLMETNRNQTIQALSLTILLGLYFTMLQTMEYYE---APFTIADGVYGSTFFVATGFHGLHVIIGSTFLTVCLLRQIKF 225
Cdd:COG1845  79 RAARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHliaEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRG 158

                       170       180       190
                ....*....|....*....|....*....|....
gi 84488627 226 HFTSTHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 259
Cdd:COG1845 159 GFTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 120-260 6.33e-12

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: 62.57  E-value: 6.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627   120 GITPLNPFEVPLL--NTAVLLASGVTITWAHHSLMETNRNQTIQALSLTILLGLYFTMLQTME---YYEAPFTIADGVYG 194
Cdd:TIGR02897  43 GKMPAELFELPLVliMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYW 122

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 84488627   195 STFFVATGFHGLHVIIGsTFLTVCLLRQIKFH-FTSTHHFGFEAAAWYWHFVDVVWLFLYVSIYWWG 260
Cdd:TIGR02897 123 SSFFVLLGTHGCHVTLG-IVWAICLLIQIQRRgLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
 
Name Accession Description Interval E-value
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 1-261 0e+00

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 502.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627    1 MAHQTHAYHMVDPSPWPLTGAAAALLMTSGLAMWFHYDSMLLMTLGLSIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLR 80
Cdd:MTH00118   1 MTHQAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627   81 YGMILFITSEVFFFIGFFWAFYHSSLAPTPELGGCWPPTGITPLNPFEVPLLNTAVLLASGVTITWAHHSLMETNRNQTI 160
Cdd:MTH00118  81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627  161 QALSLTILLGLYFTMLQTMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLTVCLLRQIKFHFTSTHHFGFEAAAW 240
Cdd:MTH00118 161 QALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAW 240

                        250       260
                 ....*....|....*....|.
gi 84488627  241 YWHFVDVVWLFLYVSIYWWGS 261
Cdd:MTH00118 241 YWHFVDVVWLFLYISIYWWGS 261
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 1-261 1.05e-174

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 481.57  E-value: 1.05e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627    1 MAHQTHAYHMVDPSPWPLTGAAAALLMTSGLAMWFHYDSMLLMTLGLSIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLR 80
Cdd:MTH00130   1 MAHQAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627   81 YGMILFITSEVFFFIGFFWAFYHSSLAPTPELGGCWPPTGITPLNPFEVPLLNTAVLLASGVTITWAHHSLMETNRNQTI 160
Cdd:MTH00130  81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627  161 QALSLTILLGLYFTMLQTMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLTVCLLRQIKFHFTSTHHFGFEAAAW 240
Cdd:MTH00130 161 QSLTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAW 240

                        250       260
                 ....*....|....*....|.
gi 84488627  241 YWHFVDVVWLFLYVSIYWWGS 261
Cdd:MTH00130 241 YWHFVDVVWLFLYISIYWWGS 261
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 1-261 7.94e-171

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 471.52  E-value: 7.94e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627    1 MAHQTHAYHMVDPSPWPLTGAAAALLMTSGLAMWFHYDSMLLMTLGLSIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLR 80
Cdd:MTH00099   1 MTHQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627   81 YGMILFITSEVFFFIGFFWAFYHSSLAPTPELGGCWPPTGITPLNPFEVPLLNTAVLLASGVTITWAHHSLMETNRNQTI 160
Cdd:MTH00099  81 YGMILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHML 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627  161 QALSLTILLGLYFTMLQTMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLTVCLLRQIKFHFTSTHHFGFEAAAW 240
Cdd:MTH00099 161 QALFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAW 240

                        250       260
                 ....*....|....*....|.
gi 84488627  241 YWHFVDVVWLFLYVSIYWWGS 261
Cdd:MTH00099 241 YWHFVDVVWLFLYVSIYWWGS 261
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 1-261 3.56e-170

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 470.00  E-value: 3.56e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627    1 MAHQTHAYHMVDPSPWPLTGAAAALLMTSGLAMWFHYDSMLLMTLGLSIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLR 80
Cdd:MTH00075   1 MAHQAHAFHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627   81 YGMILFITSEVFFFIGFFWAFYHSSLAPTPELGGCWPPTGITPLNPFEVPLLNTAVLLASGVTITWAHHSLMETNRNQTI 160
Cdd:MTH00075  81 YGMILFITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627  161 QALSLTILLGLYFTMLQTMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLTVCLLRQIKFHFTSTHHFGFEAAAW 240
Cdd:MTH00075 161 QSLALTIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAW 240

                        250       260
                 ....*....|....*....|.
gi 84488627  241 YWHFVDVVWLFLYVSIYWWGS 261
Cdd:MTH00075 241 YWHFVDVVWLFLYVSIYWWGS 261
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 2-261 8.62e-162

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 448.65  E-value: 8.62e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627    2 AHQTHAYHMVDPSPWPLTGAAAALLMTSGLAMWFHYDSMLLMTLGLSIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRY 81
Cdd:MTH00189   1 MHQAHPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627   82 GMILFITSEVFFFIGFFWAFYHSSLAPTPELGGCWPPTGITPLNPFEVPLLNTAVLLASGVTITWAHHSLMETNRNQTIQ 161
Cdd:MTH00189  81 GMILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627  162 ALSLTILLGLYFTMLQTMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLTVCLLRQIKFHFTSTHHFGFEAAAWY 241
Cdd:MTH00189 161 ALTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWY 240

                        250       260
                 ....*....|....*....|
gi 84488627  242 WHFVDVVWLFLYVSIYWWGS 261
Cdd:MTH00189 241 WHFVDVVWLFLYVSIYWWGS 260
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 3-257 4.38e-149

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 416.50  E-value: 4.38e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627    3 HQTHAYHMVDPSPWPLTGAAAALLMTSGLAMWFHYDSMLLMTLGLSIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRYG 82
Cdd:MTH00155   1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627   83 MILFITSEVFFFIGFFWAFYHSSLAPTPELGGCWPPTGITPLNPFEVPLLNTAVLLASGVTITWAHHSLMETNRNQTIQA 162
Cdd:MTH00155  81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627  163 LSLTILLGLYFTMLQTMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLTVCLLRQIKFHFTSTHHFGFEAAAWYW 242
Cdd:MTH00155 161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240

                        250
                 ....*....|....*
gi 84488627  243 HFVDVVWLFLYVSIY 257
Cdd:MTH00155 241 HFVDVVWLFLYISIY 255
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 1-261 1.66e-143

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 402.57  E-value: 1.66e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627    1 MAHQtHAYHMVDPSPWPLTGAAAALLMTSGLAMWFHYDSMLLMTLGLSIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLR 80
Cdd:MTH00039   1 MTHQ-HPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627   81 YGMILFITSEVFFFIGFFWAFYHSSLAPTPELGGCWPPTGITPLNPFEVPLLNTAVLLASGVTITWAHHSLMETNRNQTI 160
Cdd:MTH00039  80 YGMILFITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627  161 QALSLTILLGLYFTMLQTMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLTVCLLRQIKFHFTSTHHFGFEAAAW 240
Cdd:MTH00039 160 QALFLTVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAW 239

                        250       260
                 ....*....|....*....|.
gi 84488627  241 YWHFVDVVWLFLYVSIYWWGS 261
Cdd:MTH00039 240 YWHFVDVVWLFLYVCIYWWGS 260
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 6-261 1.67e-143

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 402.35  E-value: 1.67e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627    6 HAYHMVDPSPWPLTGAAAALLMTSGLAMWFHYDSMLLMTLGLSIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRYGMIL 85
Cdd:MTH00141   4 NPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFIL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627   86 FITSEVFFFIGFFWAFYHSSLAPTPELGGCWPPTGITPLNPFEVPLLNTAVLLASGVTITWAHHSLMETNRNQTIQALSL 165
Cdd:MTH00141  84 FIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGL 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627  166 TILLGLYFTMLQTMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLTVCLLRQIKFHFTSTHHFGFEAAAWYWHFV 245
Cdd:MTH00141 164 TIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFV 243

                        250
                 ....*....|....*.
gi 84488627  246 DVVWLFLYVSIYWWGS 261
Cdd:MTH00141 244 DVVWLFLYLSIYWWGS 259
COX3 pfam00510
Cytochrome c oxidase subunit III;
6-261 7.99e-139

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 390.62  E-value: 7.99e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627     6 HAYHMVDPSPWPLTGAAAALLMTSGLAMWFHY--DSMLLMTLGLSIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRYGM 83
Cdd:pfam00510   1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGysGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627    84 ILFITSEVFFFIGFFWAFYHSSLAPTPELGGCWPPTGITPLNPFEVPLLNTAVLLASGVTITWAHHSLMETNRNQTIQAL 163
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627   164 SLTILLGLYFTMLQTMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLTVCLLRQIKFHFTSTHHFGFEAAAWYWH 243
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240

                         250
                  ....*....|....*...
gi 84488627   244 FVDVVWLFLYVSIYWWGS 261
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWGS 258
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 1-261 1.94e-135

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 382.21  E-value: 1.94e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627    1 MAHQTHAYHMVDPSPWPLTGAAAALLMTSGLAMWFHYDSMLLMTLGLSIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLR 80
Cdd:MTH00219   2 MFFQTNPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627   81 YGMILFITSEVFFFIGFFWAFYHSSLAPTPELGGCWPPTGITPLNPFEVPLLNTAVLLASGVTITWAHHSLMETNRNQTI 160
Cdd:MTH00219  82 IGMILFIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQ 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627  161 QALSLTILLGLYFTMLQTMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLTVCLLRQIKFHFTSTHHFGFEAAAW 240
Cdd:MTH00219 162 QGLLFTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAAW 241

                        250       260
                 ....*....|....*....|.
gi 84488627  241 YWHFVDVVWLFLYVSIYWWGS 261
Cdd:MTH00219 242 YWHFVDVVWLFLYVSIYWWGS 262
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 18-259 8.81e-133

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: 374.54  E-value: 8.81e-133
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627  18 LTGAAAALLMTSGLAMWFH-YDSMLLMTLGLSIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRYGMILFITSEVFFFIG 96
Cdd:cd01665   1 ILGSFGLLLLALGLVLWMHgYGGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627  97 FFWAFYHSSLAPTPELGGCWPPTGITPLNPFEVPLLNTAVLLASGVTITWAHHSLMETNRNQTIQALSLTILLGLYFTML 176
Cdd:cd01665  81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627 177 QTMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLTVCLLRQIKFHFTSTHHFGFEAAAWYWHFVDVVWLFLYVSI 256
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240


                ...
gi 84488627 257 YWW 259
Cdd:cd01665 241 YWW 243
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 1-261 3.02e-126

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 359.07  E-value: 3.02e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627    1 MAHQTHAYHMVDPSPWPLTGAAAALLMTSGLAMWFHYDSMLLMTLGLSIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLR 80
Cdd:MTH00024   1 MSKLYHPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627   81 YGMILFITSEVFFFIGFFWAFYHSSLAPTPELGGCWPPTGITPLNPFEVPLLNTAVLLASGVTITWAHHSLMETNRNQTI 160
Cdd:MTH00024  81 YGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627  161 QALSLTILLGLYFTMLQTMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLTVCLLRQIKFHFTSTHHFGFEAAAW 240
Cdd:MTH00024 161 LGLFLTVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASW 240

                        250       260
                 ....*....|....*....|.
gi 84488627  241 YWHFVDVVWLFLYVSIYWWGS 261
Cdd:MTH00024 241 YWHFVDVVWLFLYLCIYWWGS 261
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 6-261 4.49e-126

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 358.38  E-value: 4.49e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627    6 HAYHMVDPSPWPLTGAAAALLMTSGLAMWFHYDSMLLMTLGLSIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRYGMIL 85
Cdd:MTH00009   4 QPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMIL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627   86 FITSEVFFFIGFFWAFYHSSLAPTPELGGCWPPTGITPLNPFEVPLLNTAVLLASGVTITWAHHSLMETNRNQTIQALSL 165
Cdd:MTH00009  84 FIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALIL 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627  166 TILLGLYFTMLQTMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLTVCLLRQIKFHFTSTHHFGFEAAAWYWHFV 245
Cdd:MTH00009 164 TVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFV 243

                        250
                 ....*....|....*.
gi 84488627  246 DVVWLFLYVSIYWWGS 261
Cdd:MTH00009 244 DVVWIFLYLCIYWWGS 259
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 1-261 7.11e-125

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 355.64  E-value: 7.11e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627    1 MAHQTHAYHMVDPSPWPLTGAAAALLMTSGLAMWFHYDSMLLMTLGLSIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLR 80
Cdd:MTH00052   2 MQQYYHPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGLK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627   81 YGMILFITSEVFFFIGFFWAFYHSSLAPTPELGGCWPPTGITPLNPFEVPLLNTAVLLASGVTITWAHHSLMETNRNQTI 160
Cdd:MTH00052  82 YGMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEAI 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627  161 QALSLTILLGLYFTMLQTMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLTVCLLRQIKFHFTSTHHFGFEAAAW 240
Cdd:MTH00052 162 IGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAAW 241

                        250       260
                 ....*....|....*....|.
gi 84488627  241 YWHFVDVVWLFLYVSIYWWGS 261
Cdd:MTH00052 242 YWHFVDVVWLFLFIFMYWWGS 262
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 1-261 1.44e-99

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 292.74  E-value: 1.44e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627    1 MAHQTHAYHMVDPSPWPLTGAAAALLMTSGLAMWFHYDSMLLMTLGLSIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLR 80
Cdd:MTH00028   1 MSLVYHPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627   81 YGMILFITSEVFFFIGFFWAFYHSSLAPTPELGGCWPPTGITPLNPFEVPLLNTAVLLASGVTITWAHHSLMETN----- 155
Cdd:MTH00028  81 LGMLLFILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTGnpasl 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627  156 -------------------------------RNQTIQALSLTILLGLYFTMLQTMEYYEAPFTIADGVYGSTFFVATGFH 204
Cdd:MTH00028 161 ekgtqgiegpnpsngappdpqkgptfllsdfRTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTH 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 84488627  205 GLHVIIGSTFLTVCLLRQIKFHFTSTHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS 261
Cdd:MTH00028 241 GLHVLVGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWGS 297
PLN02194 PLN02194
cytochrome-c oxidase
 4-260 3.31e-93

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 275.39  E-value: 3.31e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627    4 QTHAYHMVDPSPWPLTGAAAALLMTSGLAMWFH--YDSMLLMTLGLSIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRY 81
Cdd:PLN02194   5 QRHSYHLVDPSPWPISGSLGALATTVGGVMYMHpfQGGARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGPRY 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627   82 GMILFITSEVFFFIGFFWAFYHSSLAPTPELGGCWPPTGITPLNPFEVPLLNTAVLLASGVTITWAHHSLMETNRNQTIQ 161
Cdd:PLN02194  85 GSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEKRAVY 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627  162 ALSLTILLGLYFTMLQTMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLTVCLLRQIKFHFTSTHHFGFEAAAWY 241
Cdd:PLN02194 165 ALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWY 244

                        250
                 ....*....|....*....
gi 84488627  242 WHFVDVVWLFLYVSIYWWG 260
Cdd:PLN02194 245 WHFVDVVWLFLFVSIYWWG 263
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
 6-261 6.67e-77

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 233.31  E-value: 6.67e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627    6 HAYHMVDPSPWPLTGAAAALLMTSGLAMWFHYDSMLLMTLGLSIMLLTMFQWWRDIVREGtFQGHHTPPVQKGLRYGMIL 85
Cdd:MTH00083   3 HNFHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMIL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627   86 FITSEVFFFIGFFWAFYHSSLAPTPELGGCWPPTGITPLNPFEVPLLNTAVLLASGVTITWAHHSLMETNRNQTIqALSL 165
Cdd:MTH00083  82 FIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSNKSCTN-SLLL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627  166 TILLGLYFTMLQTMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLTVCLLRQIKFHFTSTHHFGFEAAAWYWHFV 245
Cdd:MTH00083 161 TCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFV 240

                        250
                 ....*....|....*.
gi 84488627  246 DVVWLFLYVSIYWWGS 261
Cdd:MTH00083 241 DVVWLFLFVFVYWWSY 256
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 71-259 1.16e-67

Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. This group additionally contains proteins which are fusions between subunits I and III, such as Sulfolobus acidocaldarius SoxM, a subunit of the SoxM terminal oxidase complex. It also includes NorE which has been speculated to be a subunit of nitric oxide reductase. Some archaebacterial cytochrome oxidases lack subunit III. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria.


Pssm-ID: 238227  Cd Length: 183  Bit Score: 207.44  E-value: 1.16e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627  71 HTPPVQKGLRYGMILFITSEVFFFIGFFWAFYHSSLAPTPELGgcwpptgiTPLNPFEVPLLNTAVLLASGVTITWAHHS 150
Cdd:cd00386   1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFG--------AGLDPLDLPLLNTNTLLLSGSSVTWAHAS 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627 151 LM--ETNRNQTIQALSLTILLGLYFTMLQTMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLTVCLLRQIKFHFT 228
Cdd:cd00386  73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152

                       170       180       190
                ....*....|....*....|....*....|.
gi 84488627 229 STHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 259
Cdd:cd00386 153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
70-259 1.21e-48

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 159.24  E-value: 1.21e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627  70 HHTPPVQKGLRYGMILFITSEVFF-FIGFFWAFYHSSLAPtpelggcWPPTGITPLNPFeVPLLNTAVLLASGVTITWAH 148
Cdd:COG1845   7 PHAPERRSPGKLGMWLFLASEVMLfAALFAAYFVLRASAP-------DWPAGAELLDLP-LPLINTLLLLLSSFTVALAV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627 149 HSLMETNRNQTIQALSLTILLGLYFTMLQTMEYYE---APFTIADGVYGSTFFVATGFHGLHVIIGSTFLTVCLLRQIKF 225
Cdd:COG1845  79 RAARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHliaEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRG 158

                       170       180       190
                ....*....|....*....|....*....|....
gi 84488627 226 HFTSTHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 259
Cdd:COG1845 159 GFTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
NorE_like cd02862
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ...
 131-257 7.45e-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: 94.61  E-value: 7.45e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627 131 LLNTAVLLASGVTITWAHHSLMETNRNQTIQALSLTILLGLYFTMLQTMEYYE---APFTIADGVYGSTFFVATGFHGLH 207
Cdd:cd02862  55 ALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYAHkiaAGIDPDAGLFFTLYFLLTGFHLLH 134

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 84488627 208 VIIGSTFLTVCLLRQIKFHFTSTHHFGFEAAAWYWHFVDVVWLFLYVSIY 257
Cdd:cd02862 135 VLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVLFPLLY 184
Ubiquinol_oxidase_III cd02863
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ...
 120-257 5.64e-19

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: 81.90  E-value: 5.64e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627 120 GITPLNPFEVPL--LNTAVLLASGVTITWAHHSLMETNRNQTIQALSLTILLGLYFTMLQTME---YYEAPFTIADGVYG 194
Cdd:cd02863  41 GPPGHELFELPLvfIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFL 120

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 84488627 195 STFFVATGFHGLHVIIGSTFLTVCLLRQIKFHFTSTHHFGFEAAAWYWHFVDVVWLFLYVSIY 257
Cdd:cd02863 121 SAFFTLVGTHGLHVTFGLIWILVMIIQLKKRGLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
Heme_Cu_Oxidase_III_2 cd02865
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 129-259 3.11e-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: 79.72  E-value: 3.11e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627 129 VPLLNTAVLLASGVTITWAHHSLMETNRNQTIQALSLTILLGLYFTMLQTMEYYEAPF---TIADGVYGSTFFVATGFHG 205
Cdd:cd02865  51 LLSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWHALNDagyGPTSNPAGSFFYLLTGLHG 130

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 84488627 206 LHVIIGSTFLTVCLLRQIKFHFTSTHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 259
Cdd:cd02865 131 LHVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVLLALLYGT 184
COX3 MTH00049
cytochrome c oxidase subunit III; Validated
 126-257 5.97e-16

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177124  Cd Length: 215  Bit Score: 74.18  E-value: 5.97e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627  126 PFEVPLLNTAVLLASGVTITwAHHSLMETNRNQTIqaLSLTILLGLYFTMLQTMEYYEAPFTIADGVYGSTFFVATGFHG 205
Cdd:MTH00049  89 SLEIPFVGCFLLLGSSITVT-AYHHLLGWKYCDLF--LYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHF 165

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 84488627  206 LHVIIGSTFLTVCLLrqikFHFTSTHHFGFEAAAWYWHFVDVVWLFLYVSIY 257
Cdd:MTH00049 166 SHVVLGVVGLSTLLL----VGSSSFGVYRSTVLTWYWHFVDYIWLLVYLIVY 213
Heme_Cu_Oxidase_III_1 cd02864
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 116-259 7.42e-14

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: 68.30  E-value: 7.42e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627 116 WPPTG---ITPLNPFEVPL----LNTAVLLASGVTITWAHHSLMETNRNQTIQALSLTILLGLYFTMLQTMEYYEAPFTI 188
Cdd:cd02864  42 WPLPSdvfALRIGHFNIPLvliaIMTFILITSSGTMAMAVNFGYRGNRKAAARLMLATALLGATFVGMQAFEWTKLIVEE 121

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627 189 ADG---------VYGSTFFVATGFHGLHVIIGSTFLTVCLLRQIKFHFTSTHHFG-FEAAAWYWHFVDVVWLFLYVSIYW 258
Cdd:cd02864 122 GVRpwgnpwgaaQFGASFFMITGFHGTHVTIGVIYLIIIARKVWRGKYQRIGRYEiVEIAGLYWHFVDLVWVFIFAFFYL 201


                .
gi 84488627 259 W 259
Cdd:cd02864 202 W 202
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 120-260 6.33e-12

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: 62.57  E-value: 6.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627   120 GITPLNPFEVPLL--NTAVLLASGVTITWAHHSLMETNRNQTIQALSLTILLGLYFTMLQTME---YYEAPFTIADGVYG 194
Cdd:TIGR02897  43 GKMPAELFELPLVliMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYW 122

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 84488627   195 STFFVATGFHGLHVIIGsTFLTVCLLRQIKFH-FTSTHHFGFEAAAWYWHFVDVVWLFLYVSIYWWG 260
Cdd:TIGR02897 123 SSFFVLLGTHGCHVTLG-IVWAICLLIQIQRRgLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
PRK10663 PRK10663
cytochrome o ubiquinol oxidase subunit III; Provisional
 127-261 1.01e-10

cytochrome o ubiquinol oxidase subunit III; Provisional


Pssm-ID: 182628  Cd Length: 204  Bit Score: 59.41  E-value: 1.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488627  127 FEVP--LLNTAVLLASGVTITWAHHSLMETNRNQTIQALSLTILLGLYFTmlqTMEYYEAPFTIADGvYG-------STF 197
Cdd:PRK10663  64 FELPfvLVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFI---GMEIYEFHHLIVEG-MGpdrsgflSAF 139

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 84488627  198 FVATGFHGLHVIIGSTFLTVCLLRQIKFHFTSTHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS 261
Cdd:PRK10663 140 FALVGTHGLHVTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGA 203
 
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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