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Conserved domains on  [gi|2310909992|gb|UXO31190|]
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cytochrome c oxidase subunit III, partial (mitochondrion) [Scophthalmus maximus]

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

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 ...
 1-187 3.74e-131

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 MTH00118:

Pssm-ID: 444752  Cd Length: 261  Bit Score: 368.12  E-value: 3.74e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310909992   1 QWWRDVVREATFQGLHTPPVQKGLRYGMILFIASEVLFFLGFFWAFYHSSLAPTPELGGFWPPAGITPLDPFEVPLLNTT 80
Cdd:MTH00118   56 QWWRDIVRESTFQGHHTPTVQKGLRYGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTA 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310909992  81 VLLASGVTVTWAHHSIIEGERKQAIQALTLTILLGGYFTFLQAMEYCEAPFTIADGVYGATFFVATGFHGLHVLIGSTFL 160
Cdd:MTH00118  136 VLLASGVTVTWAHHSIMEGNRKQAIQALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFL 215

                         170       180
                  ....*....|....*....|....*..
gi 2310909992 161 GICHLRQVQNHFTSTHHFGFEAAAWYW 187
Cdd:MTH00118  216 IVCLLRLIKFHFTTNHHFGFEAAAWYW 242
 
Name Accession Description Interval E-value
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 1-187 3.74e-131

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 368.12  E-value: 3.74e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310909992   1 QWWRDVVREATFQGLHTPPVQKGLRYGMILFIASEVLFFLGFFWAFYHSSLAPTPELGGFWPPAGITPLDPFEVPLLNTT 80
Cdd:MTH00118   56 QWWRDIVRESTFQGHHTPTVQKGLRYGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTA 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310909992  81 VLLASGVTVTWAHHSIIEGERKQAIQALTLTILLGGYFTFLQAMEYCEAPFTIADGVYGATFFVATGFHGLHVLIGSTFL 160
Cdd:MTH00118  136 VLLASGVTVTWAHHSIMEGNRKQAIQALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFL 215

                         170       180
                  ....*....|....*....|....*..
gi 2310909992 161 GICHLRQVQNHFTSTHHFGFEAAAWYW 187
Cdd:MTH00118  216 IVCLLRLIKFHFTTNHHFGFEAAAWYW 242
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-187 2.19e-110

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: 314.84  E-value: 2.19e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310909992   1 QWWRDVVREATFQGLHTPPVQKGLRYGMILFIASEVLFFLGFFWAFYHSSLAPTPELGGFWPPAGITPLDPFEVPLLNTT 80
Cdd:cd01665    40 LWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFSFFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTI 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310909992  81 VLLASGVTVTWAHHSIIEGERKQAIQALTLTILLGGYFTFLQAMEYCEAPFTIADGVYGATFFVATGFHGLHVLIGSTFL 160
Cdd:cd01665   120 ILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGLQAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFL 199

                         170       180
                  ....*....|....*....|....*..
gi 2310909992 161 GICHLRQVQNHFTSTHHFGFEAAAWYW 187
Cdd:cd01665   200 TVCLIRLLKGHFSSNHHLGFEAAIWYW 226
COX3 pfam00510
Cytochrome c oxidase subunit III;
1-187 3.44e-106

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 304.72  E-value: 3.44e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310909992   1 QWWRDVVREATFQGLHTPPVQKGLRYGMILFIASEVLFFLGFFWAFYHSSLAPTPELGGFWPPAGITPLDPFEVPLLNTT 80
Cdd:pfam00510  53 LWFRDIIREGTFLGDHTFAVQKGLNLGMILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTI 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310909992  81 VLLASGVTVTWAHHSIIEGERKQAIQALTLTILLGGYFTFLQAMEYCEAPFTIADGVYGATFFVATGFHGLHVLIGSTFL 160
Cdd:pfam00510 133 ILLSSGVTVTYAHHSLIEGNRKQALQGLILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFL 212

                         170       180
                  ....*....|....*....|....*..
gi 2310909992 161 GICHLRQVQNHFTSTHHFGFEAAAWYW 187
Cdd:pfam00510 213 AVCFLRLLKYHLTDNHHFGFEAAILYW 239
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
15-187 5.91e-44

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 144.61  E-value: 5.91e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310909992  15 LHTPPVQKGLRYGMILFIASEVLFFLGFFWA-FYHSSLAPtpelggfWPPAGITPLDPFeVPLLNTTVLLASGVTVTWAH 93
Cdd:COG1845     7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAyFVLRASAP-------DWPAGAELLDLP-LPLINTLLLLLSSFTVALAV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310909992  94 HSIIEGERKQAIQALTLTILLGGYFTFLQAMEYCE---APFTIADGVYGATFFVATGFHGLHVLIGSTFLGICHLRQVQN 170
Cdd:COG1845    79 RAARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHliaEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRG 158

                         170
                  ....*....|....*..
gi 2310909992 171 HFTSTHHFGFEAAAWYW 187
Cdd:COG1845   159 GFTPENHTGVEAAALYW 175
 
Name Accession Description Interval E-value
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 1-187 3.74e-131

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 368.12  E-value: 3.74e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310909992   1 QWWRDVVREATFQGLHTPPVQKGLRYGMILFIASEVLFFLGFFWAFYHSSLAPTPELGGFWPPAGITPLDPFEVPLLNTT 80
Cdd:MTH00118   56 QWWRDIVRESTFQGHHTPTVQKGLRYGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTA 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310909992  81 VLLASGVTVTWAHHSIIEGERKQAIQALTLTILLGGYFTFLQAMEYCEAPFTIADGVYGATFFVATGFHGLHVLIGSTFL 160
Cdd:MTH00118  136 VLLASGVTVTWAHHSIMEGNRKQAIQALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFL 215

                         170       180
                  ....*....|....*....|....*..
gi 2310909992 161 GICHLRQVQNHFTSTHHFGFEAAAWYW 187
Cdd:MTH00118  216 IVCLLRLIKFHFTTNHHFGFEAAAWYW 242
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 1-187 1.86e-127

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 358.69  E-value: 1.86e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310909992   1 QWWRDVVREATFQGLHTPPVQKGLRYGMILFIASEVLFFLGFFWAFYHSSLAPTPELGGFWPPAGITPLDPFEVPLLNTT 80
Cdd:MTH00130   56 QWWRDIVREGTFQGHHTPPVQKGLRYGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTA 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310909992  81 VLLASGVTVTWAHHSIIEGERKQAIQALTLTILLGGYFTFLQAMEYCEAPFTIADGVYGATFFVATGFHGLHVLIGSTFL 160
Cdd:MTH00130  136 VLLASGVTVTWAHHSIMEGERKQAIQSLTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFL 215

                         170       180
                  ....*....|....*....|....*..
gi 2310909992 161 GICHLRQVQNHFTSTHHFGFEAAAWYW 187
Cdd:MTH00130  216 AVCLLRQIQYHFTSEHHFGFEAAAWYW 242
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 1-187 4.57e-120

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 340.03  E-value: 4.57e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310909992   1 QWWRDVVREATFQGLHTPPVQKGLRYGMILFIASEVLFFLGFFWAFYHSSLAPTPELGGFWPPAGITPLDPFEVPLLNTT 80
Cdd:MTH00189   55 QWWRDVVRESTFQGFHTPPVQKGLRYGMILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTA 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310909992  81 VLLASGVTVTWAHHSIIEGERKQAIQALTLTILLGGYFTFLQAMEYCEAPFTIADGVYGATFFVATGFHGLHVLIGSTFL 160
Cdd:MTH00189  135 VLLSSGVTVTWAHHSLMEGNRKEAIQALTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFL 214

                         170       180
                  ....*....|....*....|....*..
gi 2310909992 161 GICHLRQVQNHFTSTHHFGFEAAAWYW 187
Cdd:MTH00189  215 LVCLLRQIQGHFTSSHHFGFEAAAWYW 241
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 1-187 4.73e-119

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 337.47  E-value: 4.73e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310909992   1 QWWRDVVREATFQGLHTPPVQKGLRYGMILFIASEVLFFLGFFWAFYHSSLAPTPELGGFWPPAGITPLDPFEVPLLNTT 80
Cdd:MTH00099   56 QWWRDIIRESTFQGHHTPIVQKGLRYGMILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTS 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310909992  81 VLLASGVTVTWAHHSIIEGERKQAIQALTLTILLGGYFTFLQAMEYCEAPFTIADGVYGATFFVATGFHGLHVLIGSTFL 160
Cdd:MTH00099  136 VLLASGVSITWAHHSLMEGNRKHMLQALFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFL 215

                         170       180
                  ....*....|....*....|....*..
gi 2310909992 161 GICHLRQVQNHFTSTHHFGFEAAAWYW 187
Cdd:MTH00099  216 IVCFLRQLKFHFTSNHHFGFEAAAWYW 242
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 1-187 1.04e-118

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 336.72  E-value: 1.04e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310909992   1 QWWRDVVREATFQGLHTPPVQKGLRYGMILFIASEVLFFLGFFWAFYHSSLAPTPELGGFWPPAGITPLDPFEVPLLNTT 80
Cdd:MTH00075   56 QWWRDIVREGTFQGHHTPPVQKGLRYGMILFITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTA 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310909992  81 VLLASGVTVTWAHHSIIEGERKQAIQALTLTILLGGYFTFLQAMEYCEAPFTIADGVYGATFFVATGFHGLHVLIGSTFL 160
Cdd:MTH00075  136 VLLASGVTVTWAHHSIMQGNRKEAIQSLALTIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFL 215

                         170       180
                  ....*....|....*....|....*..
gi 2310909992 161 GICHLRQVQNHFTSTHHFGFEAAAWYW 187
Cdd:MTH00075  216 LVCLLRQINFHFTSQHHFGFEAAAWYW 242
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 1-187 8.34e-117

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 331.37  E-value: 8.34e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310909992   1 QWWRDVVREATFQGLHTPPVQKGLRYGMILFIASEVLFFLGFFWAFYHSSLAPTPELGGFWPPAGITPLDPFEVPLLNTT 80
Cdd:MTH00155   54 QWWRDVIREGTFQGLHTKKVTKGLRWGMILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTI 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310909992  81 VLLASGVTVTWAHHSIIEGERKQAIQALTLTILLGGYFTFLQAMEYCEAPFTIADGVYGATFFVATGFHGLHVLIGSTFL 160
Cdd:MTH00155  134 ILLSSGVTVTWAHHSLMENNYKQATQSLFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFL 213

                         170       180
                  ....*....|....*....|....*..
gi 2310909992 161 GICHLRQVQNHFTSTHHFGFEAAAWYW 187
Cdd:MTH00155  214 LVCLIRHLNNHFSSNHHFGFEAAAWYW 240
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-187 2.19e-110

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: 314.84  E-value: 2.19e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310909992   1 QWWRDVVREATFQGLHTPPVQKGLRYGMILFIASEVLFFLGFFWAFYHSSLAPTPELGGFWPPAGITPLDPFEVPLLNTT 80
Cdd:cd01665    40 LWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFSFFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTI 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310909992  81 VLLASGVTVTWAHHSIIEGERKQAIQALTLTILLGGYFTFLQAMEYCEAPFTIADGVYGATFFVATGFHGLHVLIGSTFL 160
Cdd:cd01665   120 ILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGLQAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFL 199

                         170       180
                  ....*....|....*....|....*..
gi 2310909992 161 GICHLRQVQNHFTSTHHFGFEAAAWYW 187
Cdd:cd01665   200 TVCLIRLLKGHFSSNHHLGFEAAIWYW 226
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 1-187 2.27e-108

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 310.28  E-value: 2.27e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310909992   1 QWWRDVVREATFQGLHTPPVQKGLRYGMILFIASEVLFFLGFFWAFYHSSLAPTPELGGFWPPAGITPLDPFEVPLLNTT 80
Cdd:MTH00141   54 QWWRDIVRESTFQGFHTSKVQRGLRWGFILFIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTA 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310909992  81 VLLASGVTVTWAHHSIIEGERKQAIQALTLTILLGGYFTFLQAMEYCEAPFTIADGVYGATFFVATGFHGLHVLIGSTFL 160
Cdd:MTH00141  134 VLLASGVTVTWAHHSLMEGDYKSALQGLGLTIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFL 213

                         170       180
                  ....*....|....*....|....*..
gi 2310909992 161 GICHLRQVQNHFTSTHHFGFEAAAWYW 187
Cdd:MTH00141  214 LVCLVRLLLGHFSTNHHFGFEAAAWYW 240
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 2-187 3.48e-107

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 307.42  E-value: 3.48e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310909992   2 WWRDVVREATFQGLHTPPVQKGLRYGMILFIASEVLFFLGFFWAFYHSSLAPTPELGGFWPPAGITPLDPFEVPLLNTTV 81
Cdd:MTH00039   56 WWRDVIREATFQGMHTLIVINGLRYGMILFITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAV 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310909992  82 LLASGVTVTWAHHSIIEGERKQAIQALTLTILLGGYFTFLQAMEYCEAPFTIADGVYGATFFVATGFHGLHVLIGSTFLG 161
Cdd:MTH00039  136 LLSSGVTITWSHHSILEGNRTEAIQALFLTVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLA 215

                         170       180
                  ....*....|....*....|....*.
gi 2310909992 162 ICHLRQVQNHFTSTHHFGFEAAAWYW 187
Cdd:MTH00039  216 VCLFRLINHHFSNNHHFGFEAAAWYW 241
COX3 pfam00510
Cytochrome c oxidase subunit III;
1-187 3.44e-106

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 304.72  E-value: 3.44e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310909992   1 QWWRDVVREATFQGLHTPPVQKGLRYGMILFIASEVLFFLGFFWAFYHSSLAPTPELGGFWPPAGITPLDPFEVPLLNTT 80
Cdd:pfam00510  53 LWFRDIIREGTFLGDHTFAVQKGLNLGMILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTI 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310909992  81 VLLASGVTVTWAHHSIIEGERKQAIQALTLTILLGGYFTFLQAMEYCEAPFTIADGVYGATFFVATGFHGLHVLIGSTFL 160
Cdd:pfam00510 133 ILLSSGVTVTYAHHSLIEGNRKQALQGLILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFL 212

                         170       180
                  ....*....|....*....|....*..
gi 2310909992 161 GICHLRQVQNHFTSTHHFGFEAAAWYW 187
Cdd:pfam00510 213 AVCFLRLLKYHLTDNHHFGFEAAILYW 239
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 1-187 1.56e-102

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 295.54  E-value: 1.56e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310909992   1 QWWRDVVREATFQGLHTPPVQKGLRYGMILFIASEVLFFLGFFWAFYHSSLAPTPELGGFWPPAGITPLDPFEVPLLNTT 80
Cdd:MTH00219   57 QWWRDVIRESTFMGLHTSKVSTGLRIGMILFIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTA 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310909992  81 VLLASGVTVTWAHHSIIEGERKQAIQALTLTILLGGYFTFLQAMEYCEAPFTIADGVYGATFFVATGFHGLHVLIGSTFL 160
Cdd:MTH00219  137 VLLASGVTVTWAHHSLMESNHKEAQQGLLFTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFL 216

                         170       180
                  ....*....|....*....|....*..
gi 2310909992 161 GICHLRQVQNHFTSTHHFGFEAAAWYW 187
Cdd:MTH00219  217 FVCFMRGLMLHFSKNHHFGFEAAAWYW 243
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 1-187 7.46e-101

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 291.35  E-value: 7.46e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310909992   1 QWWRDVVREATFQGLHTPPVQKGLRYGMILFIASEVLFFLGFFWAFYHSSLAPTPELGGFWPPAGITPLDPFEVPLLNTT 80
Cdd:MTH00009   54 QWWRDVIREGTYMGHHTSYVTKGLRWGMILFIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTA 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310909992  81 VLLASGVTVTWAHHSIIEGERKQAIQALTLTILLGGYFTFLQAMEYCEAPFTIADGVYGATFFVATGFHGLHVLIGSTFL 160
Cdd:MTH00009  134 VLLASGVTVTWAHHSLIEGDRPEATQALILTVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFL 213

                         170       180
                  ....*....|....*....|....*..
gi 2310909992 161 GICHLRQVQNHFTSTHHFGFEAAAWYW 187
Cdd:MTH00009  214 FVCLLRTWSHHFSTGHHFGFEAAAWYW 240
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 2-187 1.58e-98

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 285.49  E-value: 1.58e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310909992   2 WWRDVVREATFQGLHTPPVQKGLRYGMILFIASEVLFFLGFFWAFYHSSLAPTPELGGFWPPAGITPLDPFEVPLLNTTV 81
Cdd:MTH00024   57 WWQDVIRESTFQGHHSLIVKQGLKYGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAV 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310909992  82 LLASGVTVTWAHHSIIEGERKQAIQALTLTILLGGYFTFLQAMEYCEAPFTIADGVYGATFFVATGFHGLHVLIGSTFLG 161
Cdd:MTH00024  137 LLSSGATVTWAHHAIISGKRKEAILGLFLTVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLF 216

                         170       180
                  ....*....|....*....|....*.
gi 2310909992 162 ICHLRQVQNHFTSTHHFGFEAAAWYW 187
Cdd:MTH00024  217 VCLLRLLSNQFTRRQHVGFEAASWYW 242
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 2-187 2.85e-95

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 277.44  E-value: 2.85e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310909992   2 WWRDVVREATFQGLHTPPVQKGLRYGMILFIASEVLFFLGFFWAFYHSSLAPTPELGGFWPPAGITPLDPFEVPLLNTTV 81
Cdd:MTH00052   58 WWRDVIRESTYQGHHTLIVKQGLKYGMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAV 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310909992  82 LLASGVTVTWAHHSIIEGERKQAIQALTLTILLGGYFTFLQAMEYCEAPFTIADGVYGATFFVATGFHGLHVLIGSTFLG 161
Cdd:MTH00052  138 LLSSGATVTWAHHGIISGKRKEAIIGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLL 217

                         170       180
                  ....*....|....*....|....*.
gi 2310909992 162 ICHLRQVQNHFTSTHHFGFEAAAWYW 187
Cdd:MTH00052  218 VCLFRLINHQFTRHHHFGFEAAAWYW 243
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 2-187 4.18e-76

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 229.95  E-value: 4.18e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310909992   2 WWRDVVREATFQGLHTPPVQKGLRYGMILFIASEVLFFLGFFWAFYHSSLAPTPELGGFWPPAGITPLDPFEVPLLNTTV 81
Cdd:MTH00028   57 WWRDVIREGTHQGHHTQIVVRGLKLGMLLFILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTI 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310909992  82 LLASGVTVTWAHHSIIEGE------------------------------------RKQAIQALTLTILLGGYFTFLQAME 125
Cdd:MTH00028  137 LLSSGATVTWAHHAIIGTGnpaslekgtqgiegpnpsngappdpqkgptfllsdfRTNAVIGLLMTILLGIIFTGLQAFE 216

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2310909992 126 YCEAPFTIADGVYGATFFVATGFHGLHVLIGSTFLGICHLRQVQNHFTSTHHFGFEAAAWYW 187
Cdd:MTH00028  217 YKEASFAISDSVYGSTFFMLTGTHGLHVLVGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYW 278
PLN02194 PLN02194
cytochrome-c oxidase
 2-187 1.11e-71

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 217.61  E-value: 1.11e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310909992   2 WWRDVVREATFQGLHTPPVQKGLRYGMILFIASEVLFFLGFFWAFYHSSLAPTPELGGFWPPAGITPLDPFEVPLLNTTV 81
Cdd:PLN02194   60 WWRDVLRESTLEGHHTKVVQLGPRYGSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPI 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310909992  82 LLASGVTVTWAHHSIIEGERKQAIQALTLTILLGGYFTFLQAMEYCEAPFTIADGVYGATFFVATGFHGLHVLIGSTFLG 161
Cdd:PLN02194  140 LPSSGAAVTWAHHAILAGKEKRAVYALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLI 219

                         170       180
                  ....*....|....*....|....*.
gi 2310909992 162 ICHLRQVQNHFTSTHHFGFEAAAWYW 187
Cdd:PLN02194  220 ICGIRQYLGHLTKEHHVGFEAAAWYW 245
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
 2-187 5.60e-63

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 195.17  E-value: 5.60e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310909992   2 WWRDVVREAtFQGLHTPPVQKGLRYGMILFIASEVLFFLGFFWAFYHSSLAPTPELGGFWPPAGITPLDPFEVPLLNTTV 81
Cdd:MTH00083   54 WGKDISMEG-LSGYHNFFVMDGFKFGMILFIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTII 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310909992  82 LLASGVTVTWAHHSIIEgERKQAIQALTLTILLGGYFTFLQAMEYCEAPFTIADGVYGATFFVATGFHGLHVLIGSTFLG 161
Cdd:MTH00083  133 LLSSGVSVTWSHHSLCL-SNKSCTNSLLLTCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLL 211

                         170       180
                  ....*....|....*....|....*.
gi 2310909992 162 ICHLRQVQNHFTSTHHFGFEAAAWYW 187
Cdd:MTH00083  212 FNLLRLLKSHFNYNHHLGLEFAILYW 237
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 16-187 2.89e-62

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: 190.88  E-value: 2.89e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310909992  16 HTPPVQKGLRYGMILFIASEVLFFLGFFWAFYHSSLAPTPELGgfwppagiTPLDPFEVPLLNTTVLLASGVTVTWAHHS 95
Cdd:cd00386     1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFG--------AGLDPLDLPLLNTNTLLLSGSSVTWAHAS 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310909992  96 II--EGERKQAIQALTLTILLGGYFTFLQAMEYCEAPFTIADGVYGATFFVATGFHGLHVLIGSTFLGICHLRQVQNHFT 173
Cdd:cd00386    73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152

                         170
                  ....*....|....
gi 2310909992 174 STHHFGFEAAAWYW 187
Cdd:cd00386   153 PRHHLGLEAAALYW 166
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
15-187 5.91e-44

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 144.61  E-value: 5.91e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310909992  15 LHTPPVQKGLRYGMILFIASEVLFFLGFFWA-FYHSSLAPtpelggfWPPAGITPLDPFeVPLLNTTVLLASGVTVTWAH 93
Cdd:COG1845     7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAyFVLRASAP-------DWPAGAELLDLP-LPLINTLLLLLSSFTVALAV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310909992  94 HSIIEGERKQAIQALTLTILLGGYFTFLQAMEYCE---APFTIADGVYGATFFVATGFHGLHVLIGSTFLGICHLRQVQN 170
Cdd:COG1845    79 RAARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHliaEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRG 158

                         170
                  ....*....|....*..
gi 2310909992 171 HFTSTHHFGFEAAAWYW 187
Cdd:COG1845   159 GFTPENHTGVEAAALYW 175
NorE_like cd02862
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ...
 27-187 6.68e-22

NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include cytochrome c and ubiquinol oxidases. Alcaligenes faecalis norE is found in a gene cluster containing norCB. norCB encodes the cytochrome c and cytochrome b subunits of nitric oxide reductase (NOR). Based on this and on its similarity to subunit III of cytochrome c oxidase (CcO) and ubiquinol oxidase, NorE has been speculated to be a subunit of NOR.


Pssm-ID: 239213  Cd Length: 186  Bit Score: 87.68  E-value: 6.68e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310909992  27 GMILFIASEVLFFLGFFwAFYHSSLAPTPELggFwpPAGITPLDPFeVPLLNTTVLLASGVTVTWAHHSIIEGERKQAIQ 106
Cdd:cd02862    12 GMWVFILSELLAFGALF-IAYAVYRALYPEL--F--AAGSAHLDLL-LGALNTLVLLTSSFTVALAVRAARAGRRRRARR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310909992 107 ALTLTILLGGYFTFLQAMEYCE---APFTIADGVYGATFFVATGFHGLHVLIGSTFLGICHLRQVQNHFTSTHHFGFEAA 183
Cdd:cd02862    86 WLAAAVLLGLVFLVIKYFEYAHkiaAGIDPDAGLFFTLYFLLTGFHLLHVLIGLGILLWVAWRARRGRYSARDYEGVEAA 165


                  ....
gi 2310909992 184 AWYW 187
Cdd:cd02862   166 ALYW 169
Heme_Cu_Oxidase_III_1 cd02864
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 25-187 5.56e-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: 61.75  E-value: 5.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310909992  25 RYGMILFIASEVLFFLGFFWAfYHSSLAPTPELGGFWPPAGITPLDPFEVPL----LNTTVLLASGVTVTWAHHSIIEGE 100
Cdd:cd02864    10 KAMMWFFLLSDAFIFSSFLIA-YMTARISTTEPWPLPSDVFALRIGHFNIPLvliaIMTFILITSSGTMAMAVNFGYRGN 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310909992 101 RKQAIQALTLTILLGGYFTFLQAMEYCEAPFTIADG---------VYGATFFVATGFHGLHVLIGSTFLGICHLRQVQNH 171
Cdd:cd02864    89 RKAAARLMLATALLGATFVGMQAFEWTKLIVEEGVRpwgnpwgaaQFGASFFMITGFHGTHVTIGVIYLIIIARKVWRGK 168

                         170
                  ....*....|....*..
gi 2310909992 172 FTSTHHF-GFEAAAWYW 187
Cdd:cd02864   169 YQRIGRYeIVEIAGLYW 185
Ubiquinol_oxidase_III cd02863
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ...
 26-156 2.03e-10

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: 56.86  E-value: 2.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310909992  26 YGMILFIASEVLFFLGFFWAF--YHSSLAPTPelggfwppagiTPLDPFEVPL--LNTTVLLASGVTVTWAHHSIIEGER 101
Cdd:cd02863    11 LGFWIYLMSDCILFATLFATYavLSGNTAGGP-----------PGHELFELPLvfIETFLLLLSSFTCGLAMIAMNKNNK 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2310909992 102 KQAIQALTLTILLGGYFTFLQAME---YCEAPFTIADGVYGATFFVATGFHGLHVLIG 156
Cdd:cd02863    80 KKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLVGTHGLHVTFG 137
COX3 MTH00049
cytochrome c oxidase subunit III; Validated
 30-157 1.02e-09

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177124  Cd Length: 215  Bit Score: 55.69  E-value: 1.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310909992  30 LFIASEVLFFLGFFwafyhsslaptpeLGGFW--PPAGITPLDPFEVPLLNTTVLLASGVTVTWAHHSIieGERKQAIQa 107
Cdd:MTH00049   59 LFILSEVIIFGSLL-------------VCCLWfdDWSYISLSSSLEIPFVGCFLLLGSSITVTAYHHLL--GWKYCDLF- 122

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2310909992 108 LTLTILLGGYFTFLQAMEYCEAPFTIADGVYGATFFVATGFHGLHVLIGS 157
Cdd:MTH00049  123 LYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHFSHVVLGV 172
 
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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