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Conserved domains on  [gi|2288442730|gb|UVF28246|]
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cytochrome c oxidase subunit III (mitochondrion) [Opsarius pulchellus]

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 4.55e-172

cytochrome c oxidase subunit III; Provisional


:

Pssm-ID: 177179  Cd Length: 261  Bit Score: 474.82  E-value: 4.55e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730   1 MTHQAHAFHMVDPSPWPLTGAVGALLMTSGLAMWFHFHSVTLMILGTILLLLTMVQWWRDIVREGTFQGHHTPPVQKGLR 80
Cdd:MTH00118    1 MTHQAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730  81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPAGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAI 160
Cdd:MTH00118   81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730 161 QSLGLTILLGLYFTLLQAVEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLGVCLLRQILHHFTSDHHFGFEAAAW 240
Cdd:MTH00118  161 QALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAW 240

                         250       260
                  ....*....|....*....|.
gi 2288442730 241 YWHFVDVVWLFLYVSIYWWGS 261
Cdd:MTH00118  241 YWHFVDVVWLFLYISIYWWGS 261
 
Name Accession Description Interval E-value
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 1-261 4.55e-172

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 474.82  E-value: 4.55e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730   1 MTHQAHAFHMVDPSPWPLTGAVGALLMTSGLAMWFHFHSVTLMILGTILLLLTMVQWWRDIVREGTFQGHHTPPVQKGLR 80
Cdd:MTH00118    1 MTHQAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730  81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPAGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAI 160
Cdd:MTH00118   81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730 161 QSLGLTILLGLYFTLLQAVEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLGVCLLRQILHHFTSDHHFGFEAAAW 240
Cdd:MTH00118  161 QALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAW 240

                         250       260
                  ....*....|....*....|.
gi 2288442730 241 YWHFVDVVWLFLYVSIYWWGS 261
Cdd:MTH00118  241 YWHFVDVVWLFLYISIYWWGS 261
COX3 pfam00510
Cytochrome c oxidase subunit III;
6-261 1.17e-132

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 375.21  E-value: 1.17e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730   6 HAFHMVDPSPWPLTGAVGALLMTSGLAMWFHF--HSVTLMILGTILLLLTMVQWWRDIVREGTFQGHHTPPVQKGLRYGM 83
Cdd:pfam00510   1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGysGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730  84 ILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPAGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQSL 163
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730 164 GLTILLGLYFTLLQAVEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLGVCLLRQILHHFTSDHHFGFEAAAWYWH 243
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240

                         250
                  ....*....|....*...
gi 2288442730 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 1.10e-125

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: 356.83  E-value: 1.10e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730  18 LTGAVGALLMTSGLAMWFH-FHSVTLMILGTILLLLTMVQWWRDIVREGTFQGHHTPPVQKGLRYGMILFITSEVFFFLG 96
Cdd:cd01665     1 ILGSFGLLLLALGLVLWMHgYGGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730  97 FFWAFYHSSLAPTPELGGCWPPAGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQSLGLTILLGLYFTLL 176
Cdd:cd01665    81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730 177 QAVEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLGVCLLRQILHHFTSDHHFGFEAAAWYWHFVDVVWLFLYVSI 256
Cdd:cd01665   161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240


                  ...
gi 2288442730 257 YWW 259
Cdd:cd01665   241 YWW 243
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
70-259 3.87e-51

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 165.41  E-value: 3.87e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730  70 HHTPPVQKGLRYGMILFITSEVFF-FLGFFWAFYHSSLAPtpelggcWPPAGITTLDPFeVPLLNTAVLLASGVTVTWAH 148
Cdd:COG1845     7 PHAPERRSPGKLGMWLFLASEVMLfAALFAAYFVLRASAP-------DWPAGAELLDLP-LPLINTLLLLLSSFTVALAV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730 149 HSIMEGNRKQAIQSLGLTILLGLYFTLLQAVEYYE---APFTIADGVYGSTFFVATGFHGLHVIIGSTFLGVCLLRQILH 225
Cdd:COG1845    79 RAARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHliaEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRG 158

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2288442730 226 HFTSDHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 259
Cdd:COG1845   159 GFTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 119-260 3.06e-13

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: 66.42  E-value: 3.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730 119 AGITTLDPFEVPLL--NTAVLLASGVTVTWAHHSIMEGNRKQAIQSLGLTILLG---LYFTLLQAVEYYEAPFTIADGVY 193
Cdd:TIGR02897  42 AGKMPAELFELPLVliMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGagfVGFEIYEFAHYASEGVTPQIGSY 121

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2288442730 194 GSTFFVATGFHGLHVIIGsTFLGVCLLRQILHH-FTSDHHFGFEAAAWYWHFVDVVWLFLYVSIYWWG 260
Cdd:TIGR02897 122 WSSFFVLLGTHGCHVTLG-IVWAICLLIQIQRRgLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
 
Name Accession Description Interval E-value
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 1-261 4.55e-172

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 474.82  E-value: 4.55e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730   1 MTHQAHAFHMVDPSPWPLTGAVGALLMTSGLAMWFHFHSVTLMILGTILLLLTMVQWWRDIVREGTFQGHHTPPVQKGLR 80
Cdd:MTH00118    1 MTHQAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730  81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPAGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAI 160
Cdd:MTH00118   81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730 161 QSLGLTILLGLYFTLLQAVEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLGVCLLRQILHHFTSDHHFGFEAAAW 240
Cdd:MTH00118  161 QALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAW 240

                         250       260
                  ....*....|....*....|.
gi 2288442730 241 YWHFVDVVWLFLYVSIYWWGS 261
Cdd:MTH00118  241 YWHFVDVVWLFLYISIYWWGS 261
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 1-261 3.76e-170

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 470.01  E-value: 3.76e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730   1 MTHQAHAFHMVDPSPWPLTGAVGALLMTSGLAMWFHFHSVTLMILGTILLLLTMVQWWRDIVREGTFQGHHTPPVQKGLR 80
Cdd:MTH00130    1 MAHQAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730  81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPAGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAI 160
Cdd:MTH00130   81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730 161 QSLGLTILLGLYFTLLQAVEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLGVCLLRQILHHFTSDHHFGFEAAAW 240
Cdd:MTH00130  161 QSLTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAW 240

                         250       260
                  ....*....|....*....|.
gi 2288442730 241 YWHFVDVVWLFLYVSIYWWGS 261
Cdd:MTH00130  241 YWHFVDVVWLFLYISIYWWGS 261
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 1-261 7.03e-162

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 449.20  E-value: 7.03e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730   1 MTHQAHAFHMVDPSPWPLTGAVGALLMTSGLAMWFHFHSVTLMILGTILLLLTMVQWWRDIVREGTFQGHHTPPVQKGLR 80
Cdd:MTH00075    1 MAHQAHAFHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730  81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPAGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAI 160
Cdd:MTH00075   81 YGMILFITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730 161 QSLGLTILLGLYFTLLQAVEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLGVCLLRQILHHFTSDHHFGFEAAAW 240
Cdd:MTH00075  161 QSLALTIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAW 240

                         250       260
                  ....*....|....*....|.
gi 2288442730 241 YWHFVDVVWLFLYVSIYWWGS 261
Cdd:MTH00075  241 YWHFVDVVWLFLYVSIYWWGS 261
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 1-261 4.69e-160

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 444.55  E-value: 4.69e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730   1 MTHQAHAFHMVDPSPWPLTGAVGALLMTSGLAMWFHFHSVTLMILGTILLLLTMVQWWRDIVREGTFQGHHTPPVQKGLR 80
Cdd:MTH00099    1 MTHQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730  81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPAGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAI 160
Cdd:MTH00099   81 YGMILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHML 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730 161 QSLGLTILLGLYFTLLQAVEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLGVCLLRQILHHFTSDHHFGFEAAAW 240
Cdd:MTH00099  161 QALFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAW 240

                         250       260
                  ....*....|....*....|.
gi 2288442730 241 YWHFVDVVWLFLYVSIYWWGS 261
Cdd:MTH00099  241 YWHFVDVVWLFLYVSIYWWGS 261
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 2-261 3.65e-154

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 429.39  E-value: 3.65e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730   2 THQAHAFHMVDPSPWPLTGAVGALLMTSGLAMWFHFHSVTLMILGTILLLLTMVQWWRDIVREGTFQGHHTPPVQKGLRY 81
Cdd:MTH00189    1 MHQAHPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730  82 GMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPAGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQ 161
Cdd:MTH00189   81 GMILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730 162 SLGLTILLGLYFTLLQAVEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLGVCLLRQILHHFTSDHHFGFEAAAWY 241
Cdd:MTH00189  161 ALTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWY 240

                         250       260
                  ....*....|....*....|
gi 2288442730 242 WHFVDVVWLFLYVSIYWWGS 261
Cdd:MTH00189  241 WHFVDVVWLFLYVSIYWWGS 260
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 3-257 2.35e-142

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 399.55  E-value: 2.35e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730   3 HQAHAFHMVDPSPWPLTGAVGALLMTSGLAMWFHFHSVTLMILGTILLLLTMVQWWRDIVREGTFQGHHTPPVQKGLRYG 82
Cdd:MTH00155    1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730  83 MILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPAGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQS 162
Cdd:MTH00155   81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730 163 LGLTILLGLYFTLLQAVEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLGVCLLRQILHHFTSDHHFGFEAAAWYW 242
Cdd:MTH00155  161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240

                         250
                  ....*....|....*
gi 2288442730 243 HFVDVVWLFLYVSIY 257
Cdd:MTH00155  241 HFVDVVWLFLYISIY 255
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 1-261 1.28e-138

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 390.24  E-value: 1.28e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730   1 MTHQaHAFHMVDPSPWPLTGAVGALLMTSGLAMWFHFHSVTLMILGTILLLLTMVQWWRDIVREGTFQGHHTPPVQKGLR 80
Cdd:MTH00039    1 MTHQ-HPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730  81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPAGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAI 160
Cdd:MTH00039   80 YGMILFITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730 161 QSLGLTILLGLYFTLLQAVEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLGVCLLRQILHHFTSDHHFGFEAAAW 240
Cdd:MTH00039  160 QALFLTVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAW 239

                         250       260
                  ....*....|....*....|.
gi 2288442730 241 YWHFVDVVWLFLYVSIYWWGS 261
Cdd:MTH00039  240 YWHFVDVVWLFLYVCIYWWGS 260
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 6-261 1.49e-138

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 390.02  E-value: 1.49e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730   6 HAFHMVDPSPWPLTGAVGALLMTSGLAMWFHFHSVTLMILGTILLLLTMVQWWRDIVREGTFQGHHTPPVQKGLRYGMIL 85
Cdd:MTH00141    4 NPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFIL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730  86 FITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPAGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQSLGL 165
Cdd:MTH00141   84 FIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730 166 TILLGLYFTLLQAVEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLGVCLLRQILHHFTSDHHFGFEAAAWYWHFV 245
Cdd:MTH00141  164 TIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFV 243

                         250
                  ....*....|....*.
gi 2288442730 246 DVVWLFLYVSIYWWGS 261
Cdd:MTH00141  244 DVVWLFLYLSIYWWGS 259
COX3 pfam00510
Cytochrome c oxidase subunit III;
6-261 1.17e-132

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 375.21  E-value: 1.17e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730   6 HAFHMVDPSPWPLTGAVGALLMTSGLAMWFHF--HSVTLMILGTILLLLTMVQWWRDIVREGTFQGHHTPPVQKGLRYGM 83
Cdd:pfam00510   1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGysGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730  84 ILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPAGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQSL 163
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730 164 GLTILLGLYFTLLQAVEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLGVCLLRQILHHFTSDHHFGFEAAAWYWH 243
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240

                         250
                  ....*....|....*...
gi 2288442730 244 FVDVVWLFLYVSIYWWGS 261
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWGS 258
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 1-261 6.08e-129

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 365.65  E-value: 6.08e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730   1 MTHQAHAFHMVDPSPWPLTGAVGALLMTSGLAMWFHFHSVTLMILGTILLLLTMVQWWRDIVREGTFQGHHTPPVQKGLR 80
Cdd:MTH00219    2 MFFQTNPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730  81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPAGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAI 160
Cdd:MTH00219   82 IGMILFIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730 161 QSLGLTILLGLYFTLLQAVEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLGVCLLRQILHHFTSDHHFGFEAAAW 240
Cdd:MTH00219  162 QGLLFTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAAW 241

                         250       260
                  ....*....|....*....|.
gi 2288442730 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 1.10e-125

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: 356.83  E-value: 1.10e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730  18 LTGAVGALLMTSGLAMWFH-FHSVTLMILGTILLLLTMVQWWRDIVREGTFQGHHTPPVQKGLRYGMILFITSEVFFFLG 96
Cdd:cd01665     1 ILGSFGLLLLALGLVLWMHgYGGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730  97 FFWAFYHSSLAPTPELGGCWPPAGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQSLGLTILLGLYFTLL 176
Cdd:cd01665    81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730 177 QAVEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLGVCLLRQILHHFTSDHHFGFEAAAWYWHFVDVVWLFLYVSI 256
Cdd:cd01665   161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240


                  ...
gi 2288442730 257 YWW 259
Cdd:cd01665   241 YWW 243
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 6-261 6.07e-122

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 347.98  E-value: 6.07e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730   6 HAFHMVDPSPWPLTGAVGALLMTSGLAMWFHFHSVTLMILGTILLLLTMVQWWRDIVREGTFQGHHTPPVQKGLRYGMIL 85
Cdd:MTH00009    4 QPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMIL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730  86 FITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPAGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQSLGL 165
Cdd:MTH00009   84 FIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALIL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730 166 TILLGLYFTLLQAVEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLGVCLLRQILHHFTSDHHFGFEAAAWYWHFV 245
Cdd:MTH00009  164 TVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFV 243

                         250
                  ....*....|....*.
gi 2288442730 246 DVVWLFLYVSIYWWGS 261
Cdd:MTH00009  244 DVVWIFLYLCIYWWGS 259
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 1-261 1.96e-120

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 344.04  E-value: 1.96e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730   1 MTHQAHAFHMVDPSPWPLTGAVGALLMTSGLAMWFHFHSVTLMILGTILLLLTMVQWWRDIVREGTFQGHHTPPVQKGLR 80
Cdd:MTH00024    1 MSKLYHPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730  81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPAGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAI 160
Cdd:MTH00024   81 YGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730 161 QSLGLTILLGLYFTLLQAVEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLGVCLLRQILHHFTSDHHFGFEAAAW 240
Cdd:MTH00024  161 LGLFLTVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASW 240

                         250       260
                  ....*....|....*....|.
gi 2288442730 241 YWHFVDVVWLFLYVSIYWWGS 261
Cdd:MTH00024  241 YWHFVDVVWLFLYLCIYWWGS 261
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 1-261 7.35e-120

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 342.93  E-value: 7.35e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730   1 MTHQAHAFHMVDPSPWPLTGAVGALLMTSGLAMWFHFHSVTLMILGTILLLLTMVQWWRDIVREGTFQGHHTPPVQKGLR 80
Cdd:MTH00052    2 MQQYYHPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGLK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730  81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPAGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAI 160
Cdd:MTH00052   82 YGMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEAI 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730 161 QSLGLTILLGLYFTLLQAVEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLGVCLLRQILHHFTSDHHFGFEAAAW 240
Cdd:MTH00052  162 IGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAAW 241

                         250       260
                  ....*....|....*....|.
gi 2288442730 241 YWHFVDVVWLFLYVSIYWWGS 261
Cdd:MTH00052  242 YWHFVDVVWLFLFIFMYWWGS 262
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 1-261 6.49e-97

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 285.81  E-value: 6.49e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730   1 MTHQAHAFHMVDPSPWPLTGAVGALLMTSGLAMWFHFHSVTLMILGTILLLLTMVQWWRDIVREGTFQGHHTPPVQKGLR 80
Cdd:MTH00028    1 MSLVYHPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730  81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPAGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGN----- 155
Cdd:MTH00028   81 LGMLLFILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTGnpasl 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730 156 -------------------------------RKQAIQSLGLTILLGLYFTLLQAVEYYEAPFTIADGVYGSTFFVATGFH 204
Cdd:MTH00028  161 ekgtqgiegpnpsngappdpqkgptfllsdfRTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTH 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2288442730 205 GLHVIIGSTFLGVCLLRQILHHFTSDHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS 261
Cdd:MTH00028  241 GLHVLVGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWGS 297
PLN02194 PLN02194
cytochrome-c oxidase
 4-260 1.49e-89

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 266.14  E-value: 1.49e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730   4 QAHAFHMVDPSPWPLTGAVGALLMTSGLAMWFHFHS--VTLMILGTILLLLTMVQWWRDIVREGTFQGHHTPPVQKGLRY 81
Cdd:PLN02194    5 QRHSYHLVDPSPWPISGSLGALATTVGGVMYMHPFQggARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGPRY 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730  82 GMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPAGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQ 161
Cdd:PLN02194   85 GSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEKRAVY 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730 162 SLGLTILLGLYFTLLQAVEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLGVCLLRQILHHFTSDHHFGFEAAAWY 241
Cdd:PLN02194  165 ALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWY 244

                         250
                  ....*....|....*....
gi 2288442730 242 WHFVDVVWLFLYVSIYWWG 260
Cdd:PLN02194  245 WHFVDVVWLFLFVSIYWWG 263
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
 6-261 2.18e-76

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 232.15  E-value: 2.18e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730   6 HAFHMVDPSPWPLTGAVGALLMTSGLAMWFHFHSVTLMILGTILLLLTMVQWWRDIVREGtFQGHHTPPVQKGLRYGMIL 85
Cdd:MTH00083    3 HNFHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMIL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730  86 FITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPAGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGNrKQAIQSLGL 165
Cdd:MTH00083   82 FIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSN-KSCTNSLLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730 166 TILLGLYFTLLQAVEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLGVCLLRQILHHFTSDHHFGFEAAAWYWHFV 245
Cdd:MTH00083  161 TCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFV 240

                         250
                  ....*....|....*.
gi 2288442730 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 5.79e-69

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: 210.52  E-value: 5.79e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730  71 HTPPVQKGLRYGMILFITSEVFFFLGFFWAFYHSSLAPTPELGgcwppagiTTLDPFEVPLLNTAVLLASGVTVTWAHHS 150
Cdd:cd00386     1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFG--------AGLDPLDLPLLNTNTLLLSGSSVTWAHAS 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730 151 IM--EGNRKQAIQSLGLTILLGLYFTLLQAVEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLGVCLLRQILHHFT 228
Cdd:cd00386    73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2288442730 229 SDHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 259
Cdd:cd00386   153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
70-259 3.87e-51

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 165.41  E-value: 3.87e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730  70 HHTPPVQKGLRYGMILFITSEVFF-FLGFFWAFYHSSLAPtpelggcWPPAGITTLDPFeVPLLNTAVLLASGVTVTWAH 148
Cdd:COG1845     7 PHAPERRSPGKLGMWLFLASEVMLfAALFAAYFVLRASAP-------DWPAGAELLDLP-LPLINTLLLLLSSFTVALAV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730 149 HSIMEGNRKQAIQSLGLTILLGLYFTLLQAVEYYE---APFTIADGVYGSTFFVATGFHGLHVIIGSTFLGVCLLRQILH 225
Cdd:COG1845    79 RAARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHliaEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRG 158

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2288442730 226 HFTSDHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 259
Cdd:COG1845   159 GFTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
NorE_like cd02862
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ...
 131-257 1.07e-27

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: 105.01  E-value: 1.07e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730 131 LLNTAVLLASGVTVTWAHHSIMEGNRKQAIQSLGLTILLGLYFTLLQAVEYYE---APFTIADGVYGSTFFVATGFHGLH 207
Cdd:cd02862    55 ALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYAHkiaAGIDPDAGLFFTLYFLLTGFHLLH 134

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2288442730 208 VIIGSTFLGVCLLRQILHHFTSDHHFGFEAAAWYWHFVDVVWLFLYVSIY 257
Cdd:cd02862   135 VLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVLFPLLY 184
Heme_Cu_Oxidase_III_2 cd02865
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 129-259 6.69e-21

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: 87.04  E-value: 6.69e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730 129 VPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQSLGLTILLGLYFTLLQAVEYYEAPF---TIADGVYGSTFFVATGFHG 205
Cdd:cd02865    51 LLSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWHALNDagyGPTSNPAGSFFYLLTGLHG 130

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2288442730 206 LHVIIGSTFLGVCLLRQILHHFTSDHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 259
Cdd:cd02865   131 LHVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVLLALLYGT 184
Ubiquinol_oxidase_III cd02863
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ...
 120-257 3.77e-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: 82.29  E-value: 3.77e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730 120 GITTLDPFEVPL--LNTAVLLASGVTVTWAHHSIMEGNRKQAIQSLGLTILLGLYFTLLQAVE---YYEAPFTIADGVYG 194
Cdd:cd02863    41 GPPGHELFELPLvfIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFL 120

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2288442730 195 STFFVATGFHGLHVIIGSTFLGVCLLRQILHHFTSDHHFGFEAAAWYWHFVDVVWLFLYVSIY 257
Cdd:cd02863   121 SAFFTLVGTHGLHVTFGLIWILVMIIQLKKRGLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
COX3 MTH00049
cytochrome c oxidase subunit III; Validated
 125-257 7.30e-17

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177124  Cd Length: 215  Bit Score: 76.88  E-value: 7.30e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730 125 DPFEVPLLNTAVLLASGVTVTWAHHSImegNRKQAIQSLGLTILLGLYFTLLQAVEYYEAPFTIADGVYGSTFFVATGFH 204
Cdd:MTH00049   88 SSLEIPFVGCFLLLGSSITVTAYHHLL---GWKYCDLFLYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLH 164

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2288442730 205 GLHVIIGSTFLGvcllrqILHHFTSDHhFGF---EAAAWYWHFVDVVWLFLYVSIY 257
Cdd:MTH00049  165 FSHVVLGVVGLS------TLLLVGSSS-FGVyrsTVLTWYWHFVDYIWLLVYLIVY 213
Heme_Cu_Oxidase_III_1 cd02864
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 127-259 4.11e-15

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: 71.76  E-value: 4.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730 127 FEVPL----LNTAVLLASGVTVTWAHHSIMEGNRKQAIQSLGLTILLGLYFTLLQAVEYYEAPFTIADG---------VY 193
Cdd:cd02864    56 FNIPLvliaIMTFILITSSGTMAMAVNFGYRGNRKAAARLMLATALLGATFVGMQAFEWTKLIVEEGVRpwgnpwgaaQF 135

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2288442730 194 GSTFFVATGFHGLHVIIGSTFLGVCLLRQILHHFTSDHHF-GFEAAAWYWHFVDVVWLFLYVSIYWW 259
Cdd:cd02864   136 GASFFMITGFHGTHVTIGVIYLIIIARKVWRGKYQRIGRYeIVEIAGLYWHFVDLVWVFIFAFFYLW 202
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 119-260 3.06e-13

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: 66.42  E-value: 3.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730 119 AGITTLDPFEVPLL--NTAVLLASGVTVTWAHHSIMEGNRKQAIQSLGLTILLG---LYFTLLQAVEYYEAPFTIADGVY 193
Cdd:TIGR02897  42 AGKMPAELFELPLVliMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGagfVGFEIYEFAHYASEGVTPQIGSY 121

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2288442730 194 GSTFFVATGFHGLHVIIGsTFLGVCLLRQILHH-FTSDHHFGFEAAAWYWHFVDVVWLFLYVSIYWWG 260
Cdd:TIGR02897 122 WSSFFVLLGTHGCHVTLG-IVWAICLLIQIQRRgLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
PRK10663 PRK10663
cytochrome o ubiquinol oxidase subunit III; Provisional
 120-261 8.92e-11

cytochrome o ubiquinol oxidase subunit III; Provisional


Pssm-ID: 182628  Cd Length: 204  Bit Score: 59.79  E-value: 8.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288442730 120 GITTLDPFEVP--LLNTAVLLASGVTVTWAHHSIMEGNRKQAIQSLGLTILLGLYFTllqAVEYYEAPFTIADGvYG--- 194
Cdd:PRK10663   57 GPTGKDIFELPfvLVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFI---GMEIYEFHHLIVEG-MGpdr 132

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2288442730 195 ----STFFVATGFHGLHVIIGSTFLGVCLLRQILHHFTSDHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS 261
Cdd:PRK10663  133 sgflSAFFALVGTHGLHVTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGA 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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