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Conserved domains on  [gi|165932500|ref|YP_001650859|]
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cytochrome c oxidase subunit III (mitochondrion) [Fistularia commersonii]

Protein Classification

cytochrome c oxidase subunit 3( domain architecture ID 10791090)

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 MTH00130
cytochrome c oxidase subunit III; Provisional
1-261 0e+00

cytochrome c oxidase subunit III; Provisional


:

Pssm-ID: 177188  Cd Length: 261  Bit Score: 530.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500   1 MAHQAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFHYNSTVLMTLGTALLLLTMYQWWRDIIREGTFQGHHTPPVQKGLR 80
Cdd:MTH00130   1 MAHQAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500  81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGISTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAI 160
Cdd:MTH00130  81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500 161 QSLTLTILLGFYFTFLQGMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIHYHFTSEHHFGFEAAAW 240
Cdd:MTH00130 161 QSLTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAW 240
                        250       260
                 ....*....|....*....|.
gi 165932500 241 YWHFVDVVWLFLYVSIYWWGS 261
Cdd:MTH00130 241 YWHFVDVVWLFLYISIYWWGS 261
 
Name Accession Description Interval E-value
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
1-261 0e+00

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 530.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500   1 MAHQAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFHYNSTVLMTLGTALLLLTMYQWWRDIIREGTFQGHHTPPVQKGLR 80
Cdd:MTH00130   1 MAHQAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500  81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGISTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAI 160
Cdd:MTH00130  81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500 161 QSLTLTILLGFYFTFLQGMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIHYHFTSEHHFGFEAAAW 240
Cdd:MTH00130 161 QSLTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAW 240
                        250       260
                 ....*....|....*....|.
gi 165932500 241 YWHFVDVVWLFLYVSIYWWGS 261
Cdd:MTH00130 241 YWHFVDVVWLFLYISIYWWGS 261
COX3 pfam00510
Cytochrome c oxidase subunit III;
6-261 3.12e-135

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 381.37  E-value: 3.12e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500    6 HAYHMVDPSPWPLTGAVAALLMTSGLAIWFHY--NSTVLMTLGTALLLLTMYQWWRDIIREGTFQGHHTPPVQKGLRYGM 83
Cdd:pfam00510   1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGysGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500   84 ILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGISTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQSL 163
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500  164 TLTILLGFYFTFLQGMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIHYHFTSEHHFGFEAAAWYWH 243
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
                         250
                  ....*....|....*...
gi 165932500  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 2.38e-126

Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. CcO catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function, but subunit III, which is also conserved, is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit III contains bound phospholipids in several crystal structures and is proposed to contain a "lipid pool." These phospholipids are believed to intrinsic constituents similar to cofactors of the enzyme.


Pssm-ID: 238834  Cd Length: 243  Bit Score: 358.37  E-value: 2.38e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500  18 LTGAVAALLMTSGLAIWFH-YNSTVLMTLGTALLLLTMYQWWRDIIREGTFQGHHTPPVQKGLRYGMILFITSEVFFFLG 96
Cdd:cd01665    1 ILGSFGLLLLALGLVLWMHgYGGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500  97 FFWAFYHSSLAPTPELGGCWPPTGISTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQSLTLTILLGFYFTFL 176
Cdd:cd01665   81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500 177 QGMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIHYHFTSEHHFGFEAAAWYWHFVDVVWLFLYVSI 256
Cdd:cd01665  161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240

                 ...
gi 165932500 257 YWW 259
Cdd:cd01665  241 YWW 243
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
70-259 5.02e-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: 5.02e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500  70 HHTPPVQKGLRYGMILFITSEVFF-FLGFFWAFYHSSLAPtpelggcWPPTGISTLDPFeVPLLNTAVLLASGVTVTWAH 148
Cdd:COG1845    7 PHAPERRSPGKLGMWLFLASEVMLfAALFAAYFVLRASAP-------DWPAGAELLDLP-LPLINTLLLLLSSFTVALAV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500 149 HSIMEGERKQAIQSLTLTILLGFYFTFLQGMEYYE---APFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIHY 225
Cdd:COG1845   79 RAARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHliaEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRG 158
                        170       180       190
                 ....*....|....*....|....*....|....
gi 165932500 226 HFTSEHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 259
Cdd:COG1845  159 GFTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
120-260 2.39e-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: 63.72  E-value: 2.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500  120 GISTLDPFEVPLL--NTAVLLASGVTVTWAHHSIMEGERKQAIQSLTLTILLGFYFTFLQGME---YYEAPFTIADGVYG 194
Cdd:TIGR02897  43 GKMPAELFELPLVliMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYW 122
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 165932500  195 STFFVATGFHGLHVIIGsTFLAVCLLRQIHYH-FTSEHHFGFEAAAWYWHFVDVVWLFLYVSIYWWG 260
Cdd:TIGR02897 123 SSFFVLLGTHGCHVTLG-IVWAICLLIQIQRRgLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
 
Name Accession Description Interval E-value
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
1-261 0e+00

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 530.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500   1 MAHQAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFHYNSTVLMTLGTALLLLTMYQWWRDIIREGTFQGHHTPPVQKGLR 80
Cdd:MTH00130   1 MAHQAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500  81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGISTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAI 160
Cdd:MTH00130  81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500 161 QSLTLTILLGFYFTFLQGMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIHYHFTSEHHFGFEAAAW 240
Cdd:MTH00130 161 QSLTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAW 240
                        250       260
                 ....*....|....*....|.
gi 165932500 241 YWHFVDVVWLFLYVSIYWWGS 261
Cdd:MTH00130 241 YWHFVDVVWLFLYISIYWWGS 261
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
1-261 1.62e-173

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 478.29  E-value: 1.62e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500   1 MAHQAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFHYNSTVLMTLGTALLLLTMYQWWRDIIREGTFQGHHTPPVQKGLR 80
Cdd:MTH00118   1 MTHQAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500  81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGISTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAI 160
Cdd:MTH00118  81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500 161 QSLTLTILLGFYFTFLQGMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIHYHFTSEHHFGFEAAAW 240
Cdd:MTH00118 161 QALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAW 240
                        250       260
                 ....*....|....*....|.
gi 165932500 241 YWHFVDVVWLFLYVSIYWWGS 261
Cdd:MTH00118 241 YWHFVDVVWLFLYISIYWWGS 261
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
1-261 8.47e-163

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 451.51  E-value: 8.47e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500   1 MAHQAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFHYNSTVLMTLGTALLLLTMYQWWRDIIREGTFQGHHTPPVQKGLR 80
Cdd:MTH00075   1 MAHQAHAFHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500  81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGISTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAI 160
Cdd:MTH00075  81 YGMILFITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500 161 QSLTLTILLGFYFTFLQGMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIHYHFTSEHHFGFEAAAW 240
Cdd:MTH00075 161 QSLALTIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAW 240
                        250       260
                 ....*....|....*....|.
gi 165932500 241 YWHFVDVVWLFLYVSIYWWGS 261
Cdd:MTH00075 241 YWHFVDVVWLFLYVSIYWWGS 261
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
1-261 4.39e-159

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 441.86  E-value: 4.39e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500   1 MAHQAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFHYNSTVLMTLGTALLLLTMYQWWRDIIREGTFQGHHTPPVQKGLR 80
Cdd:MTH00099   1 MTHQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500  81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGISTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAI 160
Cdd:MTH00099  81 YGMILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHML 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500 161 QSLTLTILLGFYFTFLQGMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIHYHFTSEHHFGFEAAAW 240
Cdd:MTH00099 161 QALFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAW 240
                        250       260
                 ....*....|....*....|.
gi 165932500 241 YWHFVDVVWLFLYVSIYWWGS 261
Cdd:MTH00099 241 YWHFVDVVWLFLYVSIYWWGS 261
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
2-261 6.12e-155

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 431.32  E-value: 6.12e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500   2 AHQAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFHYNSTVLMTLGTALLLLTMYQWWRDIIREGTFQGHHTPPVQKGLRY 81
Cdd:MTH00189   1 MHQAHPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500  82 GMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGISTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQ 161
Cdd:MTH00189  81 GMILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQ 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500 162 SLTLTILLGFYFTFLQGMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIHYHFTSEHHFGFEAAAWY 241
Cdd:MTH00189 161 ALTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWY 240
                        250       260
                 ....*....|....*....|
gi 165932500 242 WHFVDVVWLFLYVSIYWWGS 261
Cdd:MTH00189 241 WHFVDVVWLFLYVSIYWWGS 260
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
3-257 1.24e-140

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 394.93  E-value: 1.24e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500   3 HQAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFHYNSTVLMTLGTALLLLTMYQWWRDIIREGTFQGHHTPPVQKGLRYG 82
Cdd:MTH00155   1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500  83 MILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGISTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQS 162
Cdd:MTH00155  81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500 163 LTLTILLGFYFTFLQGMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIHYHFTSEHHFGFEAAAWYW 242
Cdd:MTH00155 161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240
                        250
                 ....*....|....*
gi 165932500 243 HFVDVVWLFLYVSIY 257
Cdd:MTH00155 241 HFVDVVWLFLYISIY 255
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
1-261 5.01e-137

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 386.01  E-value: 5.01e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500   1 MAHQaHAYHMVDPSPWPLTGAVAALLMTSGLAIWFHYNSTVLMTLGTALLLLTMYQWWRDIIREGTFQGHHTPPVQKGLR 80
Cdd:MTH00039   1 MTHQ-HPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500  81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGISTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAI 160
Cdd:MTH00039  80 YGMILFITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500 161 QSLTLTILLGFYFTFLQGMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIHYHFTSEHHFGFEAAAW 240
Cdd:MTH00039 160 QALFLTVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAW 239
                        250       260
                 ....*....|....*....|.
gi 165932500 241 YWHFVDVVWLFLYVSIYWWGS 261
Cdd:MTH00039 240 YWHFVDVVWLFLYVCIYWWGS 260
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
6-261 6.44e-137

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 385.78  E-value: 6.44e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500   6 HAYHMVDPSPWPLTGAVAALLMTSGLAIWFHYNSTVLMTLGTALLLLTMYQWWRDIIREGTFQGHHTPPVQKGLRYGMIL 85
Cdd:MTH00141   4 NPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFIL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500  86 FITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGISTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQSLTL 165
Cdd:MTH00141  84 FIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500 166 TILLGFYFTFLQGMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIHYHFTSEHHFGFEAAAWYWHFV 245
Cdd:MTH00141 164 TIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFV 243
                        250
                 ....*....|....*.
gi 165932500 246 DVVWLFLYVSIYWWGS 261
Cdd:MTH00141 244 DVVWLFLYLSIYWWGS 259
COX3 pfam00510
Cytochrome c oxidase subunit III;
6-261 3.12e-135

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 381.37  E-value: 3.12e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500    6 HAYHMVDPSPWPLTGAVAALLMTSGLAIWFHY--NSTVLMTLGTALLLLTMYQWWRDIIREGTFQGHHTPPVQKGLRYGM 83
Cdd:pfam00510   1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGysGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500   84 ILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGISTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQSL 163
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500  164 TLTILLGFYFTFLQGMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIHYHFTSEHHFGFEAAAWYWH 243
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
                         250
                  ....*....|....*...
gi 165932500  244 FVDVVWLFLYVSIYWWGS 261
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWGS 258
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
1-261 5.16e-129

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 366.03  E-value: 5.16e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500   1 MAHQAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFHYNSTVLMTLGTALLLLTMYQWWRDIIREGTFQGHHTPPVQKGLR 80
Cdd:MTH00219   2 MFFQTNPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500  81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGISTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAI 160
Cdd:MTH00219  82 IGMILFIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQ 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500 161 QSLTLTILLGFYFTFLQGMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIHYHFTSEHHFGFEAAAW 240
Cdd:MTH00219 162 QGLLFTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAAW 241
                        250       260
                 ....*....|....*....|.
gi 165932500 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 2.38e-126

Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. CcO catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function, but subunit III, which is also conserved, is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit III contains bound phospholipids in several crystal structures and is proposed to contain a "lipid pool." These phospholipids are believed to intrinsic constituents similar to cofactors of the enzyme.


Pssm-ID: 238834  Cd Length: 243  Bit Score: 358.37  E-value: 2.38e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500  18 LTGAVAALLMTSGLAIWFH-YNSTVLMTLGTALLLLTMYQWWRDIIREGTFQGHHTPPVQKGLRYGMILFITSEVFFFLG 96
Cdd:cd01665    1 ILGSFGLLLLALGLVLWMHgYGGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500  97 FFWAFYHSSLAPTPELGGCWPPTGISTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQSLTLTILLGFYFTFL 176
Cdd:cd01665   81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500 177 QGMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIHYHFTSEHHFGFEAAAWYWHFVDVVWLFLYVSI 256
Cdd:cd01665  161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240

                 ...
gi 165932500 257 YWW 259
Cdd:cd01665  241 YWW 243
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
1-261 1.21e-121

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 347.13  E-value: 1.21e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500   1 MAHQAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFHYNSTVLMTLGTALLLLTMYQWWRDIIREGTFQGHHTPPVQKGLR 80
Cdd:MTH00024   1 MSKLYHPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500  81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGISTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAI 160
Cdd:MTH00024  81 YGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500 161 QSLTLTILLGFYFTFLQGMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIHYHFTSEHHFGFEAAAW 240
Cdd:MTH00024 161 LGLFLTVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASW 240
                        250       260
                 ....*....|....*....|.
gi 165932500 241 YWHFVDVVWLFLYVSIYWWGS 261
Cdd:MTH00024 241 YWHFVDVVWLFLYLCIYWWGS 261
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
1-261 2.10e-121

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 346.78  E-value: 2.10e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500   1 MAHQAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFHYNSTVLMTLGTALLLLTMYQWWRDIIREGTFQGHHTPPVQKGLR 80
Cdd:MTH00052   2 MQQYYHPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGLK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500  81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGISTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAI 160
Cdd:MTH00052  82 YGMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEAI 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500 161 QSLTLTILLGFYFTFLQGMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIHYHFTSEHHFGFEAAAW 240
Cdd:MTH00052 162 IGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAAW 241
                        250       260
                 ....*....|....*....|.
gi 165932500 241 YWHFVDVVWLFLYVSIYWWGS 261
Cdd:MTH00052 242 YWHFVDVVWLFLFIFMYWWGS 262
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
6-261 8.73e-120

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 342.59  E-value: 8.73e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500   6 HAYHMVDPSPWPLTGAVAALLMTSGLAIWFHYNSTVLMTLGTALLLLTMYQWWRDIIREGTFQGHHTPPVQKGLRYGMIL 85
Cdd:MTH00009   4 QPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMIL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500  86 FITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGISTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQSLTL 165
Cdd:MTH00009  84 FIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALIL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500 166 TILLGFYFTFLQGMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIHYHFTSEHHFGFEAAAWYWHFV 245
Cdd:MTH00009 164 TVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFV 243
                        250
                 ....*....|....*.
gi 165932500 246 DVVWLFLYVSIYWWGS 261
Cdd:MTH00009 244 DVVWIFLYLCIYWWGS 259
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
6-261 1.26e-98

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 290.43  E-value: 1.26e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500   6 HAYHMVDPSPWPLTGAVAALLMTSGLAIWFHYNSTVLMTLGTALLLLTMYQWWRDIIREGTFQGHHTPPVQKGLRYGMIL 85
Cdd:MTH00028   6 HPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500  86 FITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGISTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGE---------- 155
Cdd:MTH00028  86 FILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTGnpaslekgtq 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500 156 --------------------------RKQAIQSLTLTILLGFYFTFLQGMEYYEAPFTIADGVYGSTFFVATGFHGLHVI 209
Cdd:MTH00028 166 giegpnpsngappdpqkgptfllsdfRTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVL 245
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 165932500 210 IGSTFLAVCLLRQIHYHFTSEHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS 261
Cdd:MTH00028 246 VGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWGS 297
PLN02194 PLN02194
cytochrome-c oxidase
4-260 9.24e-91

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 269.23  E-value: 9.24e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500   4 QAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFH--YNSTVLMTLGTALLLLTMYQWWRDIIREGTFQGHHTPPVQKGLRY 81
Cdd:PLN02194   5 QRHSYHLVDPSPWPISGSLGALATTVGGVMYMHpfQGGARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGPRY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500  82 GMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGISTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQ 161
Cdd:PLN02194  85 GSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEKRAVY 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500 162 SLTLTILLGFYFTFLQGMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIHYHFTSEHHFGFEAAAWY 241
Cdd:PLN02194 165 ALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWY 244
                        250
                 ....*....|....*....
gi 165932500 242 WHFVDVVWLFLYVSIYWWG 260
Cdd:PLN02194 245 WHFVDVVWLFLFVSIYWWG 263
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
6-261 3.09e-74

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 226.76  E-value: 3.09e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500   6 HAYHMVDPSPWPLTGAVAALLMTSGLAIWFHYNSTVLMTLGTALLLLTMYQWWRDIIREGtFQGHHTPPVQKGLRYGMIL 85
Cdd:MTH00083   3 HNFHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMIL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500  86 FITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGISTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEgERKQAIQSLTL 165
Cdd:MTH00083  82 FIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCL-SNKSCTNSLLL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500 166 TILLGFYFTFLQGMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIHYHFTSEHHFGFEAAAWYWHFV 245
Cdd:MTH00083 161 TCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFV 240
                        250
                 ....*....|....*.
gi 165932500 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 7.77e-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: 7.77e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500  71 HTPPVQKGLRYGMILFITSEVFFFLGFFWAFYHSSLAPTPELGgcwpptgiSTLDPFEVPLLNTAVLLASGVTVTWAHHS 150
Cdd:cd00386    1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFG--------AGLDPLDLPLLNTNTLLLSGSSVTWAHAS 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500 151 IM--EGERKQAIQSLTLTILLGFYFTFLQGMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIHYHFT 228
Cdd:cd00386   73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152
                        170       180       190
                 ....*....|....*....|....*....|.
gi 165932500 229 SEHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 259
Cdd:cd00386  153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
70-259 5.02e-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: 5.02e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500  70 HHTPPVQKGLRYGMILFITSEVFF-FLGFFWAFYHSSLAPtpelggcWPPTGISTLDPFeVPLLNTAVLLASGVTVTWAH 148
Cdd:COG1845    7 PHAPERRSPGKLGMWLFLASEVMLfAALFAAYFVLRASAP-------DWPAGAELLDLP-LPLINTLLLLLSSFTVALAV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500 149 HSIMEGERKQAIQSLTLTILLGFYFTFLQGMEYYE---APFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIHY 225
Cdd:COG1845   79 RAARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHliaEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRG 158
                        170       180       190
                 ....*....|....*....|....*....|....
gi 165932500 226 HFTSEHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 259
Cdd:COG1845  159 GFTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
NorE_like cd02862
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ...
131-257 8.20e-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: 102.70  E-value: 8.20e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500 131 LLNTAVLLASGVTVTWAHHSIMEGERKQAIQSLTLTILLGFYFTFLQGMEYYE---APFTIADGVYGSTFFVATGFHGLH 207
Cdd:cd02862   55 ALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYAHkiaAGIDPDAGLFFTLYFLLTGFHLLH 134
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 165932500 208 VIIGSTFLAVCLLRQIHYHFTSEHHFGFEAAAWYWHFVDVVWLFLYVSIY 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 1.65e-20

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: 85.88  E-value: 1.65e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500 129 VPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQSLTLTILLGFYFTFLQGMEYYEAPF---TIADGVYGSTFFVATGFHG 205
Cdd:cd02865   51 LLSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWHALNDagyGPTSNPAGSFFYLLTGLHG 130
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 165932500 206 LHVIIGSTFLAVCLLRQIHYHFTSEHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 259
Cdd:cd02865  131 LHVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVLLALLYGT 184
Ubiquinol_oxidase_III cd02863
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ...
120-257 1.65e-18

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: 80.36  E-value: 1.65e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500 120 GISTLDPFEVPL--LNTAVLLASGVTVTWAHHSIMEGERKQAIQSLTLTILLGFYFTFLQGME---YYEAPFTIADGVYG 194
Cdd:cd02863   41 GPPGHELFELPLvfIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFL 120
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 165932500 195 STFFVATGFHGLHVIIGSTFLAVCLLRQIHYHFTSEHHFGFEAAAWYWHFVDVVWLFLYVSIY 257
Cdd:cd02863  121 SAFFTLVGTHGLHVTFGLIWILVMIIQLKKRGLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
COX3 MTH00049
cytochrome c oxidase subunit III; Validated
125-257 2.76e-16

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177124  Cd Length: 215  Bit Score: 75.34  E-value: 2.76e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500 125 DPFEVPLLNTAVLLASGVTVTWAHHSI-MEGERKQaiqsLTLTILLGFYFTFLQGMEYYEAPFTIADGVYGSTFFVATGF 203
Cdd:MTH00049  88 SSLEIPFVGCFLLLGSSITVTAYHHLLgWKYCDLF----LYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGL 163
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 165932500 204 HGLHVIIGStflaVCLLRQIHYHFTSEHHFGFEAAAWYWHFVDVVWLFLYVSIY 257
Cdd:MTH00049 164 HFSHVVLGV----VGLSTLLLVGSSSFGVYRSTVLTWYWHFVDYIWLLVYLIVY 213
Heme_Cu_Oxidase_III_1 cd02864
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
127-259 1.11e-13

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: 67.91  E-value: 1.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500 127 FEVPL----LNTAVLLASGVTVTWAHHSIMEGERKQAIQSLTLTILLGFYFTFLQGMEYYEAPFTIADG---------VY 193
Cdd:cd02864   56 FNIPLvliaIMTFILITSSGTMAMAVNFGYRGNRKAAARLMLATALLGATFVGMQAFEWTKLIVEEGVRpwgnpwgaaQF 135
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 165932500 194 GSTFFVATGFHGLHVIIGSTFLAVCLLRQIHYHFTSEHHFG-FEAAAWYWHFVDVVWLFLYVSIYWW 259
Cdd:cd02864  136 GASFFMITGFHGTHVTIGVIYLIIIARKVWRGKYQRIGRYEiVEIAGLYWHFVDLVWVFIFAFFYLW 202
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
120-260 2.39e-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: 63.72  E-value: 2.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500  120 GISTLDPFEVPLL--NTAVLLASGVTVTWAHHSIMEGERKQAIQSLTLTILLGFYFTFLQGME---YYEAPFTIADGVYG 194
Cdd:TIGR02897  43 GKMPAELFELPLVliMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYW 122
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 165932500  195 STFFVATGFHGLHVIIGsTFLAVCLLRQIHYH-FTSEHHFGFEAAAWYWHFVDVVWLFLYVSIYWWG 260
Cdd:TIGR02897 123 SSFFVLLGTHGCHVTLG-IVWAICLLIQIQRRgLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
PRK10663 PRK10663
cytochrome o ubiquinol oxidase subunit III; Provisional
120-261 1.02e-10

cytochrome o ubiquinol oxidase subunit III; Provisional


Pssm-ID: 182628  Cd Length: 204  Bit Score: 59.41  E-value: 1.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932500 120 GISTLDPFEVP--LLNTAVLLASGVTVTWAHHSIMEGERKQAIQSLTLTILLGFYFTflqGMEYYEAPFTIADGvYG--- 194
Cdd:PRK10663  57 GPTGKDIFELPfvLVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFI---GMEIYEFHHLIVEG-MGpdr 132
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 165932500 195 ----STFFVATGFHGLHVIIGSTFLAVCLLRQIHYHFTSEHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS 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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