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Conserved domains on  [gi|836643578|ref|YP_009144713|]
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cytchrome c oxidase sububnit 3 (mitochondrion) [Saccharomyces cerevisiae]

Protein Classification

cytochrome c oxidase subunit 3( domain architecture ID 11096856)

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 pfam00510
Cytochrome c oxidase subunit III;
12-269 1.10e-135

Cytochrome c oxidase subunit III;


:

Pssm-ID: 395410  Cd Length: 258  Bit Score: 382.91  E-value: 1.10e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578   12 HPFHMVMPSPWPIVVSFALLSLALSTALTMHGYIGNMNMVYLALFVLLTSSILWFRDIVAEATYLGDHTMAVRKGINLGF 91
Cdd:pfam00510   1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYSGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578   92 LMFVLSEVLIFAGLFWAYFHSAMSPDVTLGACWPPVGIEAVQPTELPLLNTIILLSSGATVTYSHHALIAGNRNKALSGL 171
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578  172 LITFWLIVIFVTCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMVMLAAMLGVNYWRMRNYHLTAGHHVGYETTIIYTH 251
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240

                         250
                  ....*....|....*...
gi 836643578  252 VLDVIWLFLYVTFYWWGV 269
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWGS 258
 
Name Accession Description Interval E-value
COX3 pfam00510
Cytochrome c oxidase subunit III;
12-269 1.10e-135

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 382.91  E-value: 1.10e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578   12 HPFHMVMPSPWPIVVSFALLSLALSTALTMHGYIGNMNMVYLALFVLLTSSILWFRDIVAEATYLGDHTMAVRKGINLGF 91
Cdd:pfam00510   1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYSGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578   92 LMFVLSEVLIFAGLFWAYFHSAMSPDVTLGACWPPVGIEAVQPTELPLLNTIILLSSGATVTYSHHALIAGNRNKALSGL 171
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578  172 LITFWLIVIFVTCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMVMLAAMLGVNYWRMRNYHLTAGHHVGYETTIIYTH 251
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240

                         250
                  ....*....|....*...
gi 836643578  252 VLDVIWLFLYVTFYWWGV 269
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWGS 258
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 24-267 2.28e-105

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: 305.59  E-value: 2.28e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578  24 IVVSFALLSLALSTALTMHGYiGNMNMVYLALFVLLTSSILWFRDIVAEATYLGDHTMAVRKGINLGFLMFVLSEVLIFA 103
Cdd:cd01665    1 ILGSFGLLLLALGLVLWMHGY-GGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578 104 GLFWAYFHSAMSPDVTLGACWPPVGIEAVQPTELPLLNTIILLSSGATVTYSHHALIAGNRNKALSGLLITFWLIVIFVT 183
Cdd:cd01665   80 SFFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578 184 CQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMVMLAAMLGVNYWRMRNYHLTAGHHVGYETTIIYTHVLDVIWLFLYVT 263
Cdd:cd01665  160 LQAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVF 239


                 ....
gi 836643578 264 FYWW 267
Cdd:cd01665  240 VYWW 243
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 9-268 2.24e-91

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 270.69  E-value: 2.24e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578   9 HQQHPFHMVMPSPWPIVVSFALLSLALSTALTMHGYigNMNMVYLALFVLLTSSILWFRDIVAEATYLGDHTMAVRKGIN 88
Cdd:MTH00189   2 HQAHPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYN--SFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578  89 LGFLMFVLSEVLIFAGLFWAYFHSAMSPDVTLGACWPPVGIEAVQPTELPLLNTIILLSSGATVTYSHHALIAGNRNKAL 168
Cdd:MTH00189  80 YGMILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578 169 SGLLITFWLIVIFVTCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMVMLAAMLGVNYWRMRNYHLTAGHHVGYETTII 248
Cdd:MTH00189 160 QALTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAW 239

                        250       260
                 ....*....|....*....|
gi 836643578 249 YTHVLDVIWLFLYVTFYWWG 268
Cdd:MTH00189 240 YWHFVDVVWLFLYVSIYWWG 259
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
79-267 2.63e-40

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 138.06  E-value: 2.63e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578  79 HTMAVRKGINLGFLMFVLSEVLIFAGLFWAYF-HSAMSPDvtlgacWPPvGIEAVQPTeLPLLNTIILLSSGATVTYSHH 157
Cdd:COG1845    8 HAPERRSPGKLGMWLFLASEVMLFAALFAAYFvLRASAPD------WPA-GAELLDLP-LPLINTLLLLLSSFTVALAVR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578 158 ALIAGNRNKALSGLLITFWLIVIFVTCQYIEYTNAA---FTISDGVYGSVFYAGTGLHFLHMVMLAAMLGVNYWRMRNYH 234
Cdd:COG1845   80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHLIaegLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159

                        170       180       190
                 ....*....|....*....|....*....|...
gi 836643578 235 LTAGHHVGYETTIIYTHVLDVIWLFLYVTFYWW 267
Cdd:COG1845  160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
 
Name Accession Description Interval E-value
COX3 pfam00510
Cytochrome c oxidase subunit III;
12-269 1.10e-135

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 382.91  E-value: 1.10e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578   12 HPFHMVMPSPWPIVVSFALLSLALSTALTMHGYIGNMNMVYLALFVLLTSSILWFRDIVAEATYLGDHTMAVRKGINLGF 91
Cdd:pfam00510   1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYSGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578   92 LMFVLSEVLIFAGLFWAYFHSAMSPDVTLGACWPPVGIEAVQPTELPLLNTIILLSSGATVTYSHHALIAGNRNKALSGL 171
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578  172 LITFWLIVIFVTCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMVMLAAMLGVNYWRMRNYHLTAGHHVGYETTIIYTH 251
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240

                         250
                  ....*....|....*...
gi 836643578  252 VLDVIWLFLYVTFYWWGV 269
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWGS 258
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 24-267 2.28e-105

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: 305.59  E-value: 2.28e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578  24 IVVSFALLSLALSTALTMHGYiGNMNMVYLALFVLLTSSILWFRDIVAEATYLGDHTMAVRKGINLGFLMFVLSEVLIFA 103
Cdd:cd01665    1 ILGSFGLLLLALGLVLWMHGY-GGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578 104 GLFWAYFHSAMSPDVTLGACWPPVGIEAVQPTELPLLNTIILLSSGATVTYSHHALIAGNRNKALSGLLITFWLIVIFVT 183
Cdd:cd01665   80 SFFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578 184 CQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMVMLAAMLGVNYWRMRNYHLTAGHHVGYETTIIYTHVLDVIWLFLYVT 263
Cdd:cd01665  160 LQAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVF 239


                 ....
gi 836643578 264 FYWW 267
Cdd:cd01665  240 VYWW 243
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 9-268 2.24e-91

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 270.69  E-value: 2.24e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578   9 HQQHPFHMVMPSPWPIVVSFALLSLALSTALTMHGYigNMNMVYLALFVLLTSSILWFRDIVAEATYLGDHTMAVRKGIN 88
Cdd:MTH00189   2 HQAHPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYN--SFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578  89 LGFLMFVLSEVLIFAGLFWAYFHSAMSPDVTLGACWPPVGIEAVQPTELPLLNTIILLSSGATVTYSHHALIAGNRNKAL 168
Cdd:MTH00189  80 YGMILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578 169 SGLLITFWLIVIFVTCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMVMLAAMLGVNYWRMRNYHLTAGHHVGYETTII 248
Cdd:MTH00189 160 QALTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAW 239

                        250       260
                 ....*....|....*....|
gi 836643578 249 YTHVLDVIWLFLYVTFYWWG 268
Cdd:MTH00189 240 YWHFVDVVWLFLYVSIYWWG 259
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 9-265 4.13e-90

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 267.43  E-value: 4.13e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578   9 HQQHPFHMVMPSPWPIVVSFALLSLALSTALTMHGYigNMNMVYLALFVLLTSSILWFRDIVAEATYLGDHTMAVRKGIN 88
Cdd:MTH00155   1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQF--NMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578  89 LGFLMFVLSEVLIFAGLFWAYFHSAMSPDVTLGACWPPVGIEAVQPTELPLLNTIILLSSGATVTYSHHALIAGNRNKAL 168
Cdd:MTH00155  79 WGMILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQAT 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578 169 SGLLITFWLIVIFVTCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMVMLAAMLGVNYWRMRNYHLTAGHHVGYETTII 248
Cdd:MTH00155 159 QSLFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAW 238

                        250
                 ....*....|....*..
gi 836643578 249 YTHVLDVIWLFLYVTFY 265
Cdd:MTH00155 239 YWHFVDVVWLFLYISIY 255
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 10-268 2.34e-88

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 262.90  E-value: 2.34e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578  10 QQHPFHMVMPSPWPIVVSFALLSLALSTALTMHGYigNMNMVYLALFVLLTSSILWFRDIVAEATYLGDHTMAVRKGINL 89
Cdd:MTH00141   2 TRNPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGG--SFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRW 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578  90 GFLMFVLSEVLIFAGLFWAYFHSAMSPDVTLGACWPPVGIEAVQPTELPLLNTIILLSSGATVTYSHHALIAGNRNKALS 169
Cdd:MTH00141  80 GFILFIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQ 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578 170 GLLITFWLIVIFVTCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMVMLAAMLGVNYWRMRNYHLTAGHHVGYETTIIY 249
Cdd:MTH00141 160 GLGLTIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWY 239

                        250
                 ....*....|....*....
gi 836643578 250 THVLDVIWLFLYVTFYWWG 268
Cdd:MTH00141 240 WHFVDVVWLFLYLSIYWWG 258
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 9-268 1.30e-87

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 261.42  E-value: 1.30e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578   9 HQQHPFHMVMPSPWPIVVSFALLSLALSTALTMHgyIGNMNMVYLALFVLLTSSILWFRDIVAEATYLGDHTMAVRKGIN 88
Cdd:MTH00118   3 HQAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFH--YNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578  89 LGFLMFVLSEVLIFAGLFWAYFHSAMSPDVTLGACWPPVGIEAVQPTELPLLNTIILLSSGATVTYSHHALIAGNRNKAL 168
Cdd:MTH00118  81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578 169 SGLLITFWLIVIFVTCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMVMLAAMLGVNYWRMRNYHLTAGHHVGYETTII 248
Cdd:MTH00118 161 QALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAW 240

                        250       260
                 ....*....|....*....|
gi 836643578 249 YTHVLDVIWLFLYVTFYWWG 268
Cdd:MTH00118 241 YWHFVDVVWLFLYISIYWWG 260
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 10-268 2.68e-86

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 257.73  E-value: 2.68e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578  10 QQHPFHMVMPSPWPIVVSFALLSLALSTALTMHGyiGNMNMVYLALFVLLTSSILWFRDIVAEATYLGDHTMAVRKGINL 89
Cdd:MTH00039   3 HQHPYHLVDQSPWPLTAAIGALIMTSGLVLWFHG--DSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578  90 GFLMFVLSEVLIFAGLFWAYFHSAMSPDVTLGACWPPVGIEAVQPTELPLLNTIILLSSGATVTYSHHALIAGNRNKALS 169
Cdd:MTH00039  81 GMILFITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578 170 GLLITFWLIVIFVTCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMVMLAAMLGVNYWRMRNYHLTAGHHVGYETTIIY 249
Cdd:MTH00039 161 ALFLTVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWY 240

                        250
                 ....*....|....*....
gi 836643578 250 THVLDVIWLFLYVTFYWWG 268
Cdd:MTH00039 241 WHFVDVVWLFLYVCIYWWG 259
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 12-268 1.69e-80

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 243.12  E-value: 1.69e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578  12 HPFHMVMPSPWPIVVSFALLSLALSTALTMHgyIGNMNMVYLALFVLLTSSILWFRDIVAEATYLGDHTMAVRKGINLGF 91
Cdd:MTH00024   6 HPYHLVEPSPWPFLGAGGAFFITVGSVVYFH--YGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGM 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578  92 LMFVLSEVLIFAGLFWAYFHSAMSPDVTLGACWPPVGIEAVQPTELPLLNTIILLSSGATVTYSHHALIAGNRNKALSGL 171
Cdd:MTH00024  84 LLFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGL 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578 172 LITFWLIVIFVTCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMVMLAAMLGVNYWRMRNYHLTAGHHVGYETTIIYTH 251
Cdd:MTH00024 164 FLTVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASWYWH 243

                        250
                 ....*....|....*..
gi 836643578 252 VLDVIWLFLYVTFYWWG 268
Cdd:MTH00024 244 FVDVVWLFLYLCIYWWG 260
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 9-268 3.41e-79

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 240.05  E-value: 3.41e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578   9 HQQHPFHMVMPSPWPIVVSFALLSLALSTALTMHgyIGNMNMVYLALFVLLTSSILWFRDIVAEATYLGDHTMAVRKGIN 88
Cdd:MTH00130   3 HQAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFH--FHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578  89 LGFLMFVLSEVLIFAGLFWAYFHSAMSPDVTLGACWPPVGIEAVQPTELPLLNTIILLSSGATVTYSHHALIAGNRNKAL 168
Cdd:MTH00130  81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578 169 SGLLITFWLIVIFVTCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMVMLAAMLGVNYWRMRNYHLTAGHHVGYETTII 248
Cdd:MTH00130 161 QSLTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAW 240

                        250       260
                 ....*....|....*....|
gi 836643578 249 YTHVLDVIWLFLYVTFYWWG 268
Cdd:MTH00130 241 YWHFVDVVWLFLYISIYWWG 260
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 9-268 8.37e-79

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 238.86  E-value: 8.37e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578   9 HQQHPFHMVMPSPWPIVVSFALLSLALSTALTMHGYigNMNMVYLALFVLLTSSILWFRDIVAEATYLGDHTMAVRKGIN 88
Cdd:MTH00099   3 HQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHFN--STTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578  89 LGFLMFVLSEVLIFAGLFWAYFHSAMSPDVTLGACWPPVGIEAVQPTELPLLNTIILLSSGATVTYSHHALIAGNRNKAL 168
Cdd:MTH00099  81 YGMILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHML 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578 169 SGLLITFWLIVIFVTCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMVMLAAMLGVNYWRMRNYHLTAGHHVGYETTII 248
Cdd:MTH00099 161 QALFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAW 240

                        250       260
                 ....*....|....*....|
gi 836643578 249 YTHVLDVIWLFLYVTFYWWG 268
Cdd:MTH00099 241 YWHFVDVVWLFLYVSIYWWG 260
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 9-268 5.52e-77

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 234.25  E-value: 5.52e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578   9 HQQHPFHMVMPSPWPIVVSFALLSLALSTALTMHgyIGNMNMVYLALFVLLTSSILWFRDIVAEATYLGDHTMAVRKGIN 88
Cdd:MTH00075   3 HQAHAFHMVDPSPWPLTGAIAALLLTSGLAMWFH--FGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578  89 LGFLMFVLSEVLIFAGLFWAYFHSAMSPDVTLGACWPPVGIEAVQPTELPLLNTIILLSSGATVTYSHHALIAGNRNKAL 168
Cdd:MTH00075  81 YGMILFITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578 169 SGLLITFWLIVIFVTCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMVMLAAMLGVNYWRMRNYHLTAGHHVGYETTII 248
Cdd:MTH00075 161 QSLALTIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAW 240

                        250       260
                 ....*....|....*....|
gi 836643578 249 YTHVLDVIWLFLYVTFYWWG 268
Cdd:MTH00075 241 YWHFVDVVWLFLYVSIYWWG 260
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 9-268 2.45e-76

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 232.76  E-value: 2.45e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578   9 HQQHPFHMVMPSPWPIVVSFALLSLALSTALTMHgyIGNMNMVYLALFVLLTSSILWFRDIVAEATYLGDHTMAVRKGIN 88
Cdd:MTH00052   4 QYYHPYHLVDPSPWPYIGGCGALFTTVGGVMYFH--YSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGLK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578  89 LGFLMFVLSEVLIFAGLFWAYFHSAMSPDVTLGACWPPVGIEAVQPTELPLLNTIILLSSGATVTYSHHALIAGNRNKAL 168
Cdd:MTH00052  82 YGMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEAI 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578 169 SGLLITFWLIVIFVTCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMVMLAAMLGVNYWRMRNYHLTAGHHVGYETTII 248
Cdd:MTH00052 162 IGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAAW 241

                        250       260
                 ....*....|....*....|
gi 836643578 249 YTHVLDVIWLFLYVTFYWWG 268
Cdd:MTH00052 242 YWHFVDVVWLFLFIFMYWWG 261
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 10-268 1.51e-75

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 230.44  E-value: 1.51e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578  10 QQHPFHMVMPSPWPIVVSFALLSLALSTALTMHGYigNMNMVYLALFVLLTSSILWFRDIVAEATYLGDHTMAVRKGINL 89
Cdd:MTH00219   5 QTNPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHY--NLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLRI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578  90 GFLMFVLSEVLIFAGLFWAYFHSAMSPDVTLGACWPPVGIEAVQPTELPLLNTIILLSSGATVTYSHHALIAGNRNKALS 169
Cdd:MTH00219  83 GMILFIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQQ 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578 170 GLLITFWLIVIFVTCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMVMLAAMLGVNYWRMRNYHLTAGHHVGYETTIIY 249
Cdd:MTH00219 163 GLLFTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAAWY 242

                        250
                 ....*....|....*....
gi 836643578 250 THVLDVIWLFLYVTFYWWG 268
Cdd:MTH00219 243 WHFVDVVWLFLYVSIYWWG 261
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 12-268 6.69e-71

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 219.94  E-value: 6.69e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578  12 HPFHMVMPSPWPIVVSFALLSLALSTALTMHgyIGNMNMVYLALFVLLTSSILWFRDIVAEATYLGDHTMAVRKGINLGF 91
Cdd:MTH00028   6 HPYHLVDPSPWPFVGASGAFLFTSGAVILFH--YSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGM 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578  92 LMFVLSEVLIFAGLFWAYFHSAMSPDVTLGACWPPVGIEAVQPTELPLLNTIILLSSGATVTYSHHALIAGN-------- 163
Cdd:MTH00028  84 LLFILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTGnpaslekg 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578 164 ----------------------------RNKALSGLLITFWLIVIFVTCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLH 215
Cdd:MTH00028 164 tqgiegpnpsngappdpqkgptfllsdfRTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLH 243

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 836643578 216 MVMLAAMLGVNYWRMRNYHLTAGHHVGYETTIIYTHVLDVIWLFLYVTFYWWG 268
Cdd:MTH00028 244 VLVGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWG 296
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 11-268 1.17e-68

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 212.77  E-value: 1.17e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578  11 QHPFHMVMPSPWPIVVSFALLSLALSTALTMHGYigNMNMVYLALFVLLTSSILWFRDIVAEATYLGDHTMAVRKGINLG 90
Cdd:MTH00009   3 RQPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGY--GTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578  91 FLMFVLSEVLIFAGLFWAYFHSAMSPDVTLGACWPPVGIEAVQPTELPLLNTIILLSSGATVTYSHHALIAGNRNKALSG 170
Cdd:MTH00009  81 MILFIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578 171 LLITFWLIVIFVTCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMVMLAAMLGVNYWRMRNYHLTAGHHVGYETTIIYT 250
Cdd:MTH00009 161 LILTVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYW 240

                        250
                 ....*....|....*...
gi 836643578 251 HVLDVIWLFLYVTFYWWG 268
Cdd:MTH00009 241 HFVDVVWIFLYLCIYWWG 258
PLN02194 PLN02194
cytochrome-c oxidase
 10-268 7.87e-63

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 198.35  E-value: 7.87e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578  10 QQHPFHMVMPSPWPIVVSFALLSLALSTALTMHGYIGNMNMVYLALFVLLTSSILWFRDIVAEATYLGDHTMAVRKGINL 89
Cdd:PLN02194   5 QRHSYHLVDPSPWPISGSLGALATTVGGVMYMHPFQGGARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGPRY 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578  90 GFLMFVLSEVLIFAGLFWAYFHSAMSPDVTLGACWPPVGIEAVQPTELPLLNTIILLSSGATVTYSHHALIAGNRNKALS 169
Cdd:PLN02194  85 GSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEKRAVY 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578 170 GLLITFWLIVIFVTCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMVMLAAMLGVNYWRMRNYHLTAGHHVGYETTIIY 249
Cdd:PLN02194 165 ALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWY 244

                        250
                 ....*....|....*....
gi 836643578 250 THVLDVIWLFLYVTFYWWG 268
Cdd:PLN02194 245 WHFVDVVWLFLFVSIYWWG 263
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
 12-268 1.56e-61

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 194.40  E-value: 1.56e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578  12 HPFHMVMPSPWPIVVSFALLSLALSTALTMhgYIGNMNMVYLALFVLLTSSILWFRDIVAEAtYLGDHTMAVRKGINLGF 91
Cdd:MTH00083   3 HNFHILSLSSYPYMMFFSSLGLTSSLVVFF--KYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGM 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578  92 LMFVLSEVLIFAGLFWAYFHSAMSPDVTLGACWPPVGIEAVQPTELPLLNTIILLSSGATVTYSHHALIAGNrNKALSGL 171
Cdd:MTH00083  80 ILFIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSN-KSCTNSL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578 172 LITFWLIVIFVTCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMVMLAAMLGVNYWRMRNYHLTAGHHVGYETTIIYTH 251
Cdd:MTH00083 159 LLTCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWH 238

                        250
                 ....*....|....*..
gi 836643578 252 VLDVIWLFLYVTFYWWG 268
Cdd:MTH00083 239 FVDVVWLFLFVFVYWWS 255
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 79-267 5.02e-59

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: 185.48  E-value: 5.02e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578  79 HTMAVRKGINLGFLMFVLSEVLIFAGLFWAYFHSAMSPDVTLGAcwppvgieAVQPTELPLLNTIILLSSGATVTYSHHA 158
Cdd:cd00386    1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFGA--------GLDPLDLPLLNTNTLLLSGSSVTWAHAS 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578 159 LIA--GNRNKALSGLLITFWLIVIFVTCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMVMLAAMLGVNYWRMRNYHLT 236
Cdd:cd00386   73 LAArrGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152

                        170       180       190
                 ....*....|....*....|....*....|.
gi 836643578 237 AGHHVGYETTIIYTHVLDVIWLFLYVTFYWW 267
Cdd:cd00386  153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
79-267 2.63e-40

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 138.06  E-value: 2.63e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578  79 HTMAVRKGINLGFLMFVLSEVLIFAGLFWAYF-HSAMSPDvtlgacWPPvGIEAVQPTeLPLLNTIILLSSGATVTYSHH 157
Cdd:COG1845    8 HAPERRSPGKLGMWLFLASEVMLFAALFAAYFvLRASAPD------WPA-GAELLDLP-LPLINTLLLLLSSFTVALAVR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578 158 ALIAGNRNKALSGLLITFWLIVIFVTCQYIEYTNAA---FTISDGVYGSVFYAGTGLHFLHMVMLAAMLGVNYWRMRNYH 234
Cdd:COG1845   80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHLIaegLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159

                        170       180       190
                 ....*....|....*....|....*....|...
gi 836643578 235 LTAGHHVGYETTIIYTHVLDVIWLFLYVTFYWW 267
Cdd:COG1845  160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
Heme_Cu_Oxidase_III_2 cd02865
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 94-267 2.51e-10

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: 58.15  E-value: 2.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578  94 FVLSEVLIFAGLFWAYFHSAMSPDVtlgacWPPVGIEAVQpteLPLLNTIILLSSGATVTYSHHALIAGNRNKALSGLLI 173
Cdd:cd02865   16 FMAVEGTLFALLISAYFMRMTSGDW-----QPGAPLPLPN---LLSLNTAVLAASSVAMQWARRAARRNRRVLARLGLAL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578 174 TFWLIVIFVTCQYIEY---TNAAFTISDGVYGSVFYAGTGLHFLHMVM-LAAMLGVNYWRMRNyHLTAGHHVGYETTIIY 249
Cdd:cd02865   88 AGALALAFLAGQLLAWhalNDAGYGPTSNPAGSFFYLLTGLHGLHVIGgLVALAIVLAGLIRG-HYGPRRRLPVELCALY 166

                        170
                 ....*....|....*...
gi 836643578 250 THVLDVIWLFLYVTFYWW 267
Cdd:cd02865  167 WHFLLLVWLVLLALLYGT 184
COX3 MTH00049
cytochrome c oxidase subunit III; Validated
 90-265 2.98e-08

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177124  Cd Length: 215  Bit Score: 52.61  E-value: 2.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578  90 GFLMFVLSEVLIFAGLFWAYFHSAMSPDVTLGAcwppvgieavqPTELPLLNTIILLSSGATVTYSHHaLIAGNRNKALs 169
Cdd:MTH00049  56 AFWLFILSEVIIFGSLLVCCLWFDDWSYISLSS-----------SLEIPFVGCFLLLGSSITVTAYHH-LLGWKYCDLF- 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836643578 170 gLLITFWLIVIFVTCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMVM----LAAMLGVNYWRMRNYHLTaghhvgyeT 245
Cdd:MTH00049 123 -LYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHFSHVVLgvvgLSTLLLVGSSSFGVYRST--------V 193

                        170       180
                 ....*....|....*....|
gi 836643578 246 TIIYTHVLDVIWLFLYVTFY 265
Cdd:MTH00049 194 LTWYWHFVDYIWLLVYLIVY 213
 
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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