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Conserved domains on  [gi|1904806548|ref|YP_009919797|]
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Cox3 (mitochondrion) [Metschnikowia agaves]

Protein Classification

cytochrome c oxidase subunit 3 family protein( domain architecture ID 201)

cytochrome c oxidase (CcO) subunit 3 family protein is not required for catalytic activity but may play a role in the assembly of the heme-copper oxidase (such as CcO and cytochrome bo(3) ubiquinol oxidase) multimer complex

CATH:  1.20.120.80
Gene Ontology:  GO:0070069|GO:0009055
PubMed:  8083153|12907296
SCOP:  3000671

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Heme_Cu_Oxidase_III_like super family cl00211
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 12-269 1.81e-102

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.


The actual alignment was detected with superfamily member pfam00510:

Pssm-ID: 444752  Cd Length: 258  Bit Score: 298.94  E-value: 1.81e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548  12 HPYHLVSSSPWPIYTSFALMNLAMSMGLTAHSYMNTNMYMLMNMFNVLYVLTLWFKDVMAESTYLGDHTKRVKTGLIQGF 91
Cdd:pfam00510   1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYSGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548  92 YLFVMSEMLMFASLFWAYLHSSLNPTIEMGMNWPPMGMEPISPSELPLLNTMILLASGVTITMGHHALINGNRNDTLYGF 171
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548 172 VFTTFFMILFVMLQGMEYMFSPFTISDGVYGSTFFSLTGLHGIHMIMLAIMLTICTWRVYNYDFTNTSHVFAETTVLYTH 251
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240

                         250
                  ....*....|....*...
gi 1904806548 252 VLDILWLFIYIMCYWWGS 269
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWGS 258
 
Name Accession Description Interval E-value
COX3 pfam00510
Cytochrome c oxidase subunit III;
12-269 1.81e-102

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 298.94  E-value: 1.81e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548  12 HPYHLVSSSPWPIYTSFALMNLAMSMGLTAHSYMNTNMYMLMNMFNVLYVLTLWFKDVMAESTYLGDHTKRVKTGLIQGF 91
Cdd:pfam00510   1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYSGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548  92 YLFVMSEMLMFASLFWAYLHSSLNPTIEMGMNWPPMGMEPISPSELPLLNTMILLASGVTITMGHHALINGNRNDTLYGF 171
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548 172 VFTTFFMILFVMLQGMEYMFSPFTISDGVYGSTFFSLTGLHGIHMIMLAIMLTICTWRVYNYDFTNTSHVFAETTVLYTH 251
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240

                         250
                  ....*....|....*...
gi 1904806548 252 VLDILWLFIYIMCYWWGS 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 2.49e-93

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: 275.16  E-value: 2.49e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548  24 IYTSFALMNLAMSMGLTAHSYMNTNMyMLMNMFNVLYVLTLWFKDVMAESTYLGDHTKRVKTGLIQGFYLFVMSEMLMFA 103
Cdd:cd01665     1 ILGSFGLLLLALGLVLWMHGYGGPLL-LFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548 104 SLFWAYLHSSLNPTIEMGMNWPPMGMEPISPSELPLLNTMILLASGVTITMGHHALINGNRNDTLYGFVFTTFFMILFVM 183
Cdd:cd01665    80 SFFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548 184 LQGMEYMFSPFTISDGVYGSTFFSLTGLHGIHMIMLAIMLTICTWRVYNYDFTNTSHVFAETTVLYTHVLDILWLFIYIM 263
Cdd:cd01665   160 LQAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVF 239


                  ....
gi 1904806548 264 CYWW 267
Cdd:cd01665   240 VYWW 243
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 9-269 9.72e-86

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 256.36  E-value: 9.72e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548   9 MQLHPYHLVSSSPWPIYTSFALmnLAMSMGLTAHSYMNTNMYMLMNMFNVLYVLTLWFKDVMAESTYLGDHTKRVKTGLI 88
Cdd:MTH00141    1 MTRNPFHLVEFSPWPLTGSIGA--LFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548  89 QGFYLFVMSEMLMFASLFWAYLHSSLNPTIEMGMNWPPMGMEPISPSELPLLNTMILLASGVTITMGHHALINGNRNDTL 168
Cdd:MTH00141   79 WGFILFIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSAL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548 169 YGFVFTTFFMILFVMLQGMEYMFSPFTISDGVYGSTFFSLTGLHGIHMIMLAIMLTICTWRVYNYDFTNTSHVFAETTVL 248
Cdd:MTH00141  159 QGLGLTIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAW 238

                         250       260
                  ....*....|....*....|.
gi 1904806548 249 YTHVLDILWLFIYIMCYWWGS 269
Cdd:MTH00141  239 YWHFVDVVWLFLYLSIYWWGS 259
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
79-267 3.43e-40

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 137.67  E-value: 3.43e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548  79 HTKRVKTGLIQGFYLFVMSEMLMFASLFWAYLhsslnpTIEMGMNWPPMGMEPISPSeLPLLNTMILLASGVTITMGHHA 158
Cdd:COG1845     8 HAPERRSPGKLGMWLFLASEVMLFAALFAAYF------VLRASAPDWPAGAELLDLP-LPLINTLLLLLSSFTVALAVRA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548 159 LINGNRNDTLYGFVFTTFFMILFVMLQGMEYM---FSPFTISDGVYGSTFFSLTGLHGIHMIMLAIMLTICTWRVYNYDF 235
Cdd:COG1845    81 ARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYShliAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGF 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1904806548 236 TNTSHVFAETTVLYTHVLDILWLFIYIMCYWW 267
Cdd:COG1845   161 TPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
 
Name Accession Description Interval E-value
COX3 pfam00510
Cytochrome c oxidase subunit III;
12-269 1.81e-102

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 298.94  E-value: 1.81e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548  12 HPYHLVSSSPWPIYTSFALMNLAMSMGLTAHSYMNTNMYMLMNMFNVLYVLTLWFKDVMAESTYLGDHTKRVKTGLIQGF 91
Cdd:pfam00510   1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYSGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548  92 YLFVMSEMLMFASLFWAYLHSSLNPTIEMGMNWPPMGMEPISPSELPLLNTMILLASGVTITMGHHALINGNRNDTLYGF 171
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548 172 VFTTFFMILFVMLQGMEYMFSPFTISDGVYGSTFFSLTGLHGIHMIMLAIMLTICTWRVYNYDFTNTSHVFAETTVLYTH 251
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240

                         250
                  ....*....|....*...
gi 1904806548 252 VLDILWLFIYIMCYWWGS 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 2.49e-93

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: 275.16  E-value: 2.49e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548  24 IYTSFALMNLAMSMGLTAHSYMNTNMyMLMNMFNVLYVLTLWFKDVMAESTYLGDHTKRVKTGLIQGFYLFVMSEMLMFA 103
Cdd:cd01665     1 ILGSFGLLLLALGLVLWMHGYGGPLL-LFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548 104 SLFWAYLHSSLNPTIEMGMNWPPMGMEPISPSELPLLNTMILLASGVTITMGHHALINGNRNDTLYGFVFTTFFMILFVM 183
Cdd:cd01665    80 SFFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548 184 LQGMEYMFSPFTISDGVYGSTFFSLTGLHGIHMIMLAIMLTICTWRVYNYDFTNTSHVFAETTVLYTHVLDILWLFIYIM 263
Cdd:cd01665   160 LQAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVF 239


                  ....
gi 1904806548 264 CYWW 267
Cdd:cd01665   240 VYWW 243
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 9-269 9.72e-86

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 256.36  E-value: 9.72e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548   9 MQLHPYHLVSSSPWPIYTSFALmnLAMSMGLTAHSYMNTNMYMLMNMFNVLYVLTLWFKDVMAESTYLGDHTKRVKTGLI 88
Cdd:MTH00141    1 MTRNPFHLVEFSPWPLTGSIGA--LFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548  89 QGFYLFVMSEMLMFASLFWAYLHSSLNPTIEMGMNWPPMGMEPISPSELPLLNTMILLASGVTITMGHHALINGNRNDTL 168
Cdd:MTH00141   79 WGFILFIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSAL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548 169 YGFVFTTFFMILFVMLQGMEYMFSPFTISDGVYGSTFFSLTGLHGIHMIMLAIMLTICTWRVYNYDFTNTSHVFAETTVL 248
Cdd:MTH00141  159 QGLGLTIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAW 238

                         250       260
                  ....*....|....*....|.
gi 1904806548 249 YTHVLDILWLFIYIMCYWWGS 269
Cdd:MTH00141  239 YWHFVDVVWLFLYLSIYWWGS 259
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 9-269 1.14e-85

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 256.44  E-value: 1.14e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548   9 MQLHPYHLVSSSPWPIYTSFALMNLAMSMGLTAHsyMNTNMYMLMNMFNVLYVLTLWFKDVMAESTYLGDHTKRVKTGLI 88
Cdd:MTH00189    2 HQAHPFHLVDPSPWPLTGAIAALLLTSGLAMWFH--YNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548  89 QGFYLFVMSEMLMFASLFWAYLHSSLNPTIEMGMNWPPMGMEPISPSELPLLNTMILLASGVTITMGHHALINGNRNDTL 168
Cdd:MTH00189   80 YGMILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548 169 YGFVFTTFFMILFVMLQGMEYMFSPFTISDGVYGSTFFSLTGLHGIHMIMLAIMLTICTWRVYNYDFTNTSHVFAETTVL 248
Cdd:MTH00189  160 QALTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAW 239

                         250       260
                  ....*....|....*....|.
gi 1904806548 249 YTHVLDILWLFIYIMCYWWGS 269
Cdd:MTH00189  240 YWHFVDVVWLFLYVSIYWWGS 260
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 10-269 1.55e-85

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 256.03  E-value: 1.55e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548  10 QLHPYHLVSSSPWPIYTSFALMNLAMsmGLTAHSYMNTNMYMLMNMFNVLYVLTLWFKDVMAESTYLGDHTKRVKTGLIQ 89
Cdd:MTH00118    4 QAHPYHMVDPSPWPLTGAMAALLLTS--GLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548  90 GFYLFVMSEMLMFASLFWAYLHSSLNPTIEMGMNWPPMGMEPISPSELPLLNTMILLASGVTITMGHHALINGNRNDTLY 169
Cdd:MTH00118   82 GMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548 170 GFVFTTFFMILFVMLQGMEYMFSPFTISDGVYGSTFFSLTGLHGIHMIMLAIMLTICTWRVYNYDFTNTSHVFAETTVLY 249
Cdd:MTH00118  162 ALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWY 241

                         250       260
                  ....*....|....*....|
gi 1904806548 250 THVLDILWLFIYIMCYWWGS 269
Cdd:MTH00118  242 WHFVDVVWLFLYISIYWWGS 261
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 9-265 7.47e-85

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 253.95  E-value: 7.47e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548   9 MQLHPYHLVSSSPWPIYTSFALMNLAMSMGLTAHSYMNtnMYMLMNMFNVLYVLTLWFKDVMAESTYLGDHTKRVKTGLI 88
Cdd:MTH00155    1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNM--NLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548  89 QGFYLFVMSEMLMFASLFWAYLHSSLNPTIEMGMNWPPMGMEPISPSELPLLNTMILLASGVTITMGHHALINGNRNDTL 168
Cdd:MTH00155   79 WGMILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQAT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548 169 YGFVFTTFFMILFVMLQGMEYMFSPFTISDGVYGSTFFSLTGLHGIHMIMLAIMLTICTWRVYNYDFTNTSHVFAETTVL 248
Cdd:MTH00155  159 QSLFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAW 238

                         250
                  ....*....|....*..
gi 1904806548 249 YTHVLDILWLFIYIMCY 265
Cdd:MTH00155  239 YWHFVDVVWLFLYISIY 255
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 12-269 3.38e-83

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 250.03  E-value: 3.38e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548  12 HPYHLVSSSPWPIYTSFAlmNLAMSMGLTAHSYMNTNMYMLMNMFNVLYVLTLWFKDVMAESTYLGDHTKRVKTGLIQGF 91
Cdd:MTH00039    5 HPYHLVDQSPWPLTAAIG--ALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRYGM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548  92 YLFVMSEMLMFASLFWAYLHSSLNPTIEMGMNWPPMGMEPISPSELPLLNTMILLASGVTITMGHHALINGNRNDTLYGF 171
Cdd:MTH00039   83 ILFITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQAL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548 172 VFTTFFMILFVMLQGMEYMFSPFTISDGVYGSTFFSLTGLHGIHMIMLAIMLTICTWRVYNYDFTNTSHVFAETTVLYTH 251
Cdd:MTH00039  163 FLTVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWYWH 242

                         250
                  ....*....|....*...
gi 1904806548 252 VLDILWLFIYIMCYWWGS 269
Cdd:MTH00039  243 FVDVVWLFLYVCIYWWGS 260
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 9-269 4.04e-83

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 249.67  E-value: 4.04e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548   9 MQLHPYHLVSSSPWPIYTSFALmnLAMSMGLTAHSYMNTNMYMLMNMFNVLYVLTLWFKDVMAESTYLGDHTKRVKTGLI 88
Cdd:MTH00024    3 KLYHPYHLVEPSPWPFLGAGGA--FFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548  89 QGFYLFVMSEMLMFASLFWAYLHSSLNPTIEMGMNWPPMGMEPISPSELPLLNTMILLASGVTITMGHHALINGNRNDTL 168
Cdd:MTH00024   81 YGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548 169 YGFVFTTFFMILFVMLQGMEYMFSPFTISDGVYGSTFFSLTGLHGIHMIMLAIMLTICTWRVYNYDFTNTSHVFAETTVL 248
Cdd:MTH00024  161 LGLFLTVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASW 240

                         250       260
                  ....*....|....*....|.
gi 1904806548 249 YTHVLDILWLFIYIMCYWWGS 269
Cdd:MTH00024  241 YWHFVDVVWLFLYLCIYWWGS 261
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 10-269 7.44e-78

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 236.61  E-value: 7.44e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548  10 QLHPYHLVSSSPWPIYTSFAlmNLAMSMGLTAHSYMNTNMYMLMNMFNVLYVLTLWFKDVMAESTYLGDHTKRVKTGLIQ 89
Cdd:MTH00052    5 YYHPYHLVDPSPWPYIGGCG--ALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGLKY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548  90 GFYLFVMSEMLMFASLFWAYLHSSLNPTIEMGMNWPPMGMEPISPSELPLLNTMILLASGVTITMGHHALINGNRNDTLY 169
Cdd:MTH00052   83 GMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEAII 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548 170 GFVFTTFFMILFVMLQGMEYMFSPFTISDGVYGSTFFSLTGLHGIHMIMLAIMLTICTWRVYNYDFTNTSHVFAETTVLY 249
Cdd:MTH00052  163 GLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAAWY 242

                         250       260
                  ....*....|....*....|
gi 1904806548 250 THVLDILWLFIYIMCYWWGS 269
Cdd:MTH00052  243 WHFVDVVWLFLFIFMYWWGS 262
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 10-269 5.99e-76

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 231.54  E-value: 5.99e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548  10 QLHPYHLVSSSPWPIytSFALMNLAMSMGLTAHSYMNTNMYMLMNMFNVLYVLTLWFKDVMAESTYLGDHTKRVKTGLIQ 89
Cdd:MTH00099    4 QTHAYHMVNPSPWPL--TGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548  90 GFYLFVMSEMLMFASLFWAYLHSSLNPTIEMGMNWPPMGMEPISPSELPLLNTMILLASGVTITMGHHALINGNRNDTLY 169
Cdd:MTH00099   82 GMILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548 170 GFVFTTFFMILFVMLQGMEYMFSPFTISDGVYGSTFFSLTGLHGIHMIMLAIMLTICTWRVYNYDFTNTSHVFAETTVLY 249
Cdd:MTH00099  162 ALFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWY 241

                         250       260
                  ....*....|....*....|
gi 1904806548 250 THVLDILWLFIYIMCYWWGS 269
Cdd:MTH00099  242 WHFVDVVWLFLYVSIYWWGS 261
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 10-269 7.44e-75

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 228.88  E-value: 7.44e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548  10 QLHPYHLVSSSPWPIytSFALMNLAMSMGLTAHSYMNTNMYMLMNMFNVLYVLTLWFKDVMAESTYLGDHTKRVKTGLIQ 89
Cdd:MTH00130    4 QAHAYHMVDPSPWPL--TGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548  90 GFYLFVMSEMLMFASLFWAYLHSSLNPTIEMGMNWPPMGMEPISPSELPLLNTMILLASGVTITMGHHALINGNRNDTLY 169
Cdd:MTH00130   82 GMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548 170 GFVFTTFFMILFVMLQGMEYMFSPFTISDGVYGSTFFSLTGLHGIHMIMLAIMLTICTWRVYNYDFTNTSHVFAETTVLY 249
Cdd:MTH00130  162 SLTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWY 241

                         250       260
                  ....*....|....*....|
gi 1904806548 250 THVLDILWLFIYIMCYWWGS 269
Cdd:MTH00130  242 WHFVDVVWLFLYISIYWWGS 261
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 8-269 9.82e-75

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 228.52  E-value: 9.82e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548   8 YMQLHPYHLVSSSPWPIYTSfaLMNLAMSMGLTAHSYMNTNMYMLMNMFNVLYVLTLWFKDVMAESTYLGDHTKRVKTGL 87
Cdd:MTH00219    3 FFQTNPYHLVDYSPWPLTGS--LGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548  88 IQGFYLFVMSEMLMFASLFWAYLHSSLNPTIEMGMNWPPMGMEPISPSELPLLNTMILLASGVTITMGHHALINGNRNDT 167
Cdd:MTH00219   81 RIGMILFIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548 168 LYGFVFTTFFMILFVMLQGMEYMFSPFTISDGVYGSTFFSLTGLHGIHMIMLAIMLTICTWRVYNYDFTNTSHVFAETTV 247
Cdd:MTH00219  161 QQGLLFTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAA 240

                         250       260
                  ....*....|....*....|..
gi 1904806548 248 LYTHVLDILWLFIYIMCYWWGS 269
Cdd:MTH00219  241 WYWHFVDVVWLFLYVSIYWWGS 262
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 10-269 2.13e-72

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 222.70  E-value: 2.13e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548  10 QLHPYHLVSSSPWPIytSFALMNLAMSMGLTAHSYMNTNMYMLMNMFNVLYVLTLWFKDVMAESTYLGDHTKRVKTGLIQ 89
Cdd:MTH00075    4 QAHAFHMVDPSPWPL--TGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548  90 GFYLFVMSEMLMFASLFWAYLHSSLNPTIEMGMNWPPMGMEPISPSELPLLNTMILLASGVTITMGHHALINGNRNDTLY 169
Cdd:MTH00075   82 GMILFITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548 170 GFVFTTFFMILFVMLQGMEYMFSPFTISDGVYGSTFFSLTGLHGIHMIMLAIMLTICTWRVYNYDFTNTSHVFAETTVLY 249
Cdd:MTH00075  162 SLALTIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWY 241

                         250       260
                  ....*....|....*....|
gi 1904806548 250 THVLDILWLFIYIMCYWWGS 269
Cdd:MTH00075  242 WHFVDVVWLFLYVSIYWWGS 261
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 9-269 7.32e-69

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 213.54  E-value: 7.32e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548   9 MQLHPYHLVSSSPWPIYTSFALmnLAMSMGLTAHSYMNTNMYMLMNMFNVLYVLTLWFKDVMAESTYLGDHTKRVKTGLI 88
Cdd:MTH00009    1 MIRQPFHLVEYSPWPLTGSIGA--FTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548  89 QGFYLFVMSEMLMFASLFWAYLHSSLNPTIEMGMNWPPMGMEPISPSELPLLNTMILLASGVTITMGHHALINGNRNDTL 168
Cdd:MTH00009   79 WGMILFIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEAT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548 169 YGFVFTTFFMILFVMLQGMEYMFSPFTISDGVYGSTFFSLTGLHGIHMIMLAIMLTICTWRVYNYDFTNTSHVFAETTVL 248
Cdd:MTH00009  159 QALILTVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAW 238

                         250       260
                  ....*....|....*....|.
gi 1904806548 249 YTHVLDILWLFIYIMCYWWGS 269
Cdd:MTH00009  239 YWHFVDVVWIFLYLCIYWWGS 259
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 12-269 1.87e-64

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 203.37  E-value: 1.87e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548  12 HPYHLVSSSPWP-IYTSFALMnlaMSMGLTAHSYMNTNMYMLMNMFNVLYVLTLWFKDVMAESTYLGDHTKRVKTGLIQG 90
Cdd:MTH00028    6 HPYHLVDPSPWPfVGASGAFL---FTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548  91 FYLFVMSEMLMFASLFWAYLHSSLNPTIEMGMNWPPMGMEPISPSELPLLNTMILLASGVTITMGHHALINGN------- 163
Cdd:MTH00028   83 MLLFILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTGnpaslek 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548 164 -----------------------------RNDTLYGFVFTTFFMILFVMLQGMEYMFSPFTISDGVYGSTFFSLTGLHGI 214
Cdd:MTH00028  163 gtqgiegpnpsngappdpqkgptfllsdfRTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGL 242

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1904806548 215 HMIMLAIMLTICTWRVYNYDFTNTSHVFAETTVLYTHVLDILWLFIYIMCYWWGS 269
Cdd:MTH00028  243 HVLVGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWGS 297
PLN02194 PLN02194
cytochrome-c oxidase
 10-268 2.89e-62

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 196.81  E-value: 2.89e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548  10 QLHPYHLVSSSPWPIYTSFALMNLAMSMGLTAHSYMNTNMYMLMNMFNVLYVLTLWFKDVMAESTYLGDHTKRVKTGLIQ 89
Cdd:PLN02194    5 QRHSYHLVDPSPWPISGSLGALATTVGGVMYMHPFQGGARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGPRY 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548  90 GFYLFVMSEMLMFASLFWAYLHSSLNPTIEMGMNWPPMGMEPISPSELPLLNTMILLASGVTITMGHHALINGNRNDTLY 169
Cdd:PLN02194   85 GSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEKRAVY 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548 170 GFVFTTFFMILFVMLQGMEYMFSPFTISDGVYGSTFFSLTGLHGIHMIMLAIMLTICTWRVYNYDFTNTSHVFAETTVLY 249
Cdd:PLN02194  165 ALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWY 244

                         250
                  ....*....|....*....
gi 1904806548 250 THVLDILWLFIYIMCYWWG 268
Cdd:PLN02194  245 WHFVDVVWLFLFVSIYWWG 263
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 79-267 4.63e-52

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: 167.77  E-value: 4.63e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548  79 HTKRVKTGLIQGFYLFVMSEMLMFASLFWAYLHSSLNPTIEMGmnwppmgmEPISPSELPLLNTMILLASGVTITMGHHA 158
Cdd:cd00386     1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFG--------AGLDPLDLPLLNTNTLLLSGSSVTWAHAS 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548 159 LI--NGNRNDTLYGFVFTTFFMILFVMLQGMEYMFSPFTISDGVYGSTFFSLTGLHGIHMIMLAIMLTICTWRVYNYDFT 236
Cdd:cd00386    73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1904806548 237 NTSHVFAETTVLYTHVLDILWLFIYIMCYWW 267
Cdd:cd00386   153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
 10-269 1.34e-43

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 148.57  E-value: 1.34e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548  10 QLHPYHLVSSSPWPIYTSFALMNLAMSMGLtahsYMNTNMYM--LMNMFNVLYVLTLWFKDVMAEStYLGDHTKRVKTGL 87
Cdd:MTH00083    1 MFHNFHILSLSSYPYMMFFSSLGLTSSLVV----FFKYGLFYsfFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548  88 IQGFYLFVMSEMLMFASLFWAYLHSSLNPTIEMGMNWPPMGMEPISPSELPLLNTMILLASGVTITMGHHALINGNRNDT 167
Cdd:MTH00083   76 KFGMILFIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSNKSCT 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548 168 LYgFVFTTFFMILFVMLQGMEYMFSPFTISDGVYGSTFFSLTGLHGIHMIMLAIMLTICTWRVYNYDFTNTSHVFAETTV 247
Cdd:MTH00083  156 NS-LLLTCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAI 234

                         250       260
                  ....*....|....*....|..
gi 1904806548 248 LYTHVLDILWLFIYIMCYWWGS 269
Cdd:MTH00083  235 LYWHFVDVVWLFLFVFVYWWSY 256
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
79-267 3.43e-40

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 137.67  E-value: 3.43e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548  79 HTKRVKTGLIQGFYLFVMSEMLMFASLFWAYLhsslnpTIEMGMNWPPMGMEPISPSeLPLLNTMILLASGVTITMGHHA 158
Cdd:COG1845     8 HAPERRSPGKLGMWLFLASEVMLFAALFAAYF------VLRASAPDWPAGAELLDLP-LPLINTLLLLLSSFTVALAVRA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548 159 LINGNRNDTLYGFVFTTFFMILFVMLQGMEYM---FSPFTISDGVYGSTFFSLTGLHGIHMIMLAIMLTICTWRVYNYDF 235
Cdd:COG1845    81 ARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYShliAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGF 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1904806548 236 TNTSHVFAETTVLYTHVLDILWLFIYIMCYWW 267
Cdd:COG1845   161 TPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
Ubiquinol_oxidase_III cd02863
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ...
 77-265 4.35e-15

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: 71.50  E-value: 4.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548  77 GDHTKRVKTGLiqGFYLFVMSEMLMFASLFWAY--LHSSLNPtiemgmnwppmGMEPISPSELPL--LNTMILLASGVTI 152
Cdd:cd02863     1 HHTNTGSKKIL--GFWIYLMSDCILFATLFATYavLSGNTAG-----------GPPGHELFELPLvfIETFLLLLSSFTC 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548 153 TMGHHALINGNRNDTLYGFVFTTFFMILFVMLQGME---YMFSPFTISDGVYGSTFFSLTGLHGIHMIMLAIMLTICTWR 229
Cdd:cd02863    68 GLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLVGTHGLHVTFGLIWILVMIIQ 147

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1904806548 230 VYNYDFTNTSHVFAETTVLYTHVLDILWLFIYIMCY 265
Cdd:cd02863   148 LKKRGLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
Heme_Cu_Oxidase_III_1 cd02864
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 90-267 4.96e-12

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: 63.29  E-value: 4.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548  90 GFYLFVMSEMLMFASLFWAYLHSSLNPTiemgmNWPPMGME----PISPSELPL----LNTMILLASGVTITMGHHALIN 161
Cdd:cd02864    12 MMWFFLLSDAFIFSSFLIAYMTARISTT-----EPWPLPSDvfalRIGHFNIPLvliaIMTFILITSSGTMAMAVNFGYR 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548 162 GNRNDTLYGFVFTTFFMILFVMLQGMEYmfSPFTISDGV-----------YGSTFFSLTGLHGIHMIMLAIMLTICTWRV 230
Cdd:cd02864    87 GNRKAAARLMLATALLGATFVGMQAFEW--TKLIVEEGVrpwgnpwgaaqFGASFFMITGFHGTHVTIGVIYLIIIARKV 164

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1904806548 231 YNYDFTNT-SHVFAETTVLYTHVLDILWLFIYIMCYWW 267
Cdd:cd02864   165 WRGKYQRIgRYEIVEIAGLYWHFVDLVWVFIFAFFYLW 202
COX3 MTH00049
cytochrome c oxidase subunit III; Validated
 58-265 1.30e-11

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177124  Cd Length: 215  Bit Score: 62.24  E-value: 1.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548  58 VLYVLTLWFKDVMaesTYLGDHTKRVKTGLIQGFYLFVMSEMLMFASLFWAYLhsslnptieMGMNWppmGMEPISPS-E 136
Cdd:MTH00049   27 LLVFLILWVLLIV---IFVSDGLVQVKHHYESAFWLFILSEVIIFGSLLVCCL---------WFDDW---SYISLSSSlE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548 137 LPLLNTMILLASGVTITMGHHALinGNRNDTLYGFVfTTFFMILFVMLQGMEYMFSPFTISDGVYGSTFFSLTGLHGIHM 216
Cdd:MTH00049   92 IPFVGCFLLLGSSITVTAYHHLL--GWKYCDLFLYL-TILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHFSHV 168

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1904806548 217 IMLAIMLTIctwrVYNYDFTNTSHVFAETTVLYTHVLDILWLFIYIMCY 265
Cdd:MTH00049  169 VLGVVGLST----LLLVGSSSFGVYRSTVLTWYWHFVDYIWLLVYLIVY 213
Heme_Cu_Oxidase_III_2 cd02865
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 85-267 1.18e-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: 59.31  E-value: 1.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548  85 TGLIQGFYLFVMSEMLMFASLFWAYLHSSLnptieMGMNWPPmgmEPISPSELPLLNTMILLASGVTITMGHHALINGNR 164
Cdd:cd02865     7 SPGWWGLWVFMAVEGTLFALLISAYFMRMT-----SGDWQPG---APLPLPNLLSLNTAVLAASSVAMQWARRAARRNRR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548 165 NDTLYGFVFTTFFMILFVMLQGMEY---MFSPFTISDGVYGSTFFSLTGLHGIHMIMLAIMLTICTWRVYNYDFTNTSHV 241
Cdd:cd02865    79 VLARLGLALAGALALAFLAGQLLAWhalNDAGYGPTSNPAGSFFYLLTGLHGLHVIGGLVALAIVLAGLIRGHYGPRRRL 158

                         170       180
                  ....*....|....*....|....*.
gi 1904806548 242 FAETTVLYTHVLDILWLFIYIMCYWW 267
Cdd:cd02865   159 PVELCALYWHFLLLVWLVLLALLYGT 184
PRK10663 PRK10663
cytochrome o ubiquinol oxidase subunit III; Provisional
 90-269 2.47e-07

cytochrome o ubiquinol oxidase subunit III; Provisional


Pssm-ID: 182628  Cd Length: 204  Bit Score: 50.16  E-value: 2.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548  90 GFYLFVMSEMLMFASLFWAYlhsslnPTIEMGMNWPPMGMEPIspsELP--LLNTMILLASGVTITMGHHALINGNRNDT 167
Cdd:PRK10663   28 GFWIYLMSDCILFSILFATY------AVLVNGTAGGPTGKDIF---ELPfvLVETFLLLFSSITYGMAAIAMYKNNKSQV 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806548 168 LYGFVFTTFFMILFVmlqGMEYMFSPFTISDGvYG-------STFFSLTGLHGIHMIMLAIMLTICTWRVYNYDFTNTSH 240
Cdd:PRK10663   99 ISWLALTFLFGAGFI---GMEIYEFHHLIVEG-MGpdrsgflSAFFALVGTHGLHVTSGLIWMAVLMVQVARRGLTSTNR 174

                         170       180
                  ....*....|....*....|....*....
gi 1904806548 241 VFAETTVLYTHVLDILWLFIYIMCYWWGS 269
Cdd:PRK10663  175 TRIMCLSLFWHFLDVVWICVFTVVYLMGA 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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