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Conserved domains on  [gi|941488632|gb|ALK80383|]
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cytochrome oxidase subunit 3, partial (mitochondrion) [Epiactis japonica]

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 ...
 1-173 1.54e-101

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 MTH00024:

Pssm-ID: 444752  Cd Length: 261  Bit Score: 292.43  E-value: 1.54e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488632   1 HTVVVKQGLKYGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGAVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHA 80
Cdd:MTH00024  71 HSLIVKQGLKYGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHA 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488632  81 LISGKKTEAINGLTATVILGLIFTGLQAMEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLAVCLARLVYHQFTRH 160
Cdd:MTH00024 151 IISGKRKEAILGLFLTVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRR 230

                        170
                 ....*....|...
gi 941488632 161 HHLGFEAASWYWH 173
Cdd:MTH00024 231 QHVGFEAASWYWH 243
 
Name Accession Description Interval E-value
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 1-173 1.54e-101

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 292.43  E-value: 1.54e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488632   1 HTVVVKQGLKYGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGAVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHA 80
Cdd:MTH00024  71 HSLIVKQGLKYGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHA 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488632  81 LISGKKTEAINGLTATVILGLIFTGLQAMEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLAVCLARLVYHQFTRH 160
Cdd:MTH00024 151 IISGKRKEAILGLFLTVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRR 230

                        170
                 ....*....|...
gi 941488632 161 HHLGFEAASWYWH 173
Cdd:MTH00024 231 QHVGFEAASWYWH 243
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-173 6.05e-89

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: 260.14  E-value: 6.05e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488632   1 HTVVVKQGLKYGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGAVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHA 80
Cdd:cd01665   55 HTKKVQKGLRLGMILFILSEVMFFFSFFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHA 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488632  81 LISGKKTEAINGLTATVILGLIFTGLQAMEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLAVCLARLVYHQFTRH 160
Cdd:cd01665  135 LLLGNRKKAILGLILTILLGVYFTGLQAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSN 214

                        170
                 ....*....|...
gi 941488632 161 HHLGFEAASWYWH 173
Cdd:cd01665  215 HHLGFEAAIWYWH 227
COX3 pfam00510
Cytochrome c oxidase subunit III;
1-173 2.38e-78

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 233.84  E-value: 2.38e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488632    1 HTVVVKQGLKYGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGAVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHA 80
Cdd:pfam00510  68 HTFAVQKGLNLGMILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHS 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488632   81 LISGKKTEAINGLTATVILGLIFTGLQAMEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLAVCLARLVYHQFTRH 160
Cdd:pfam00510 148 LIEGNRKQALQGLILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDN 227

                         170
                  ....*....|...
gi 941488632  161 HHLGFEAASWYWH 173
Cdd:pfam00510 228 HHFGFEAAILYWH 240
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
1-173 1.42e-39

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 132.67  E-value: 1.42e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488632   1 HTVVVKQGLKYGMLLFILSEVLFFFSFFWAFFHSSLApavelGAVWPpQGINPLNPfSVPLLNTAVLLSSGATVTWAHHA 80
Cdd:COG1845    8 HAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS-----APDWP-AGAELLDL-PLPLINTLLLLLSSFTVALAVRA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488632  81 LISGKKTEAINGLTATVILGLIFTGLQAMEYYE---APFAISDSVYGSTFFVATGFHGLHVIIGTTFLAVCLARLVYHQF 157
Cdd:COG1845   81 ARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHliaEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGF 160

                        170
                 ....*....|....*.
gi 941488632 158 TRHHHLGFEAASWYWH 173
Cdd:COG1845  161 TPENHTGVEAAALYWH 176
 
Name Accession Description Interval E-value
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 1-173 1.54e-101

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 292.43  E-value: 1.54e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488632   1 HTVVVKQGLKYGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGAVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHA 80
Cdd:MTH00024  71 HSLIVKQGLKYGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHA 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488632  81 LISGKKTEAINGLTATVILGLIFTGLQAMEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLAVCLARLVYHQFTRH 160
Cdd:MTH00024 151 IISGKRKEAILGLFLTVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRR 230

                        170
                 ....*....|...
gi 941488632 161 HHLGFEAASWYWH 173
Cdd:MTH00024 231 QHVGFEAASWYWH 243
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 1-173 1.31e-95

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 277.44  E-value: 1.31e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488632   1 HTVVVKQGLKYGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGAVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHA 80
Cdd:MTH00052  72 HTLIVKQGLKYGMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHG 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488632  81 LISGKKTEAINGLTATVILGLIFTGLQAMEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLAVCLARLVYHQFTRH 160
Cdd:MTH00052 152 IISGKRKEAIIGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRH 231

                        170
                 ....*....|...
gi 941488632 161 HHLGFEAASWYWH 173
Cdd:MTH00052 232 HHFGFEAAAWYWH 244
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 1-173 3.13e-92

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 269.13  E-value: 3.13e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488632   1 HTVVVKQGLKYGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGAVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHA 80
Cdd:MTH00118  71 HTPTVQKGLRYGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHS 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488632  81 LISGKKTEAINGLTATVILGLIFTGLQAMEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLAVCLARLVYHQFTRH 160
Cdd:MTH00118 151 IMEGNRKQAIQALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTN 230

                        170
                 ....*....|...
gi 941488632 161 HHLGFEAASWYWH 173
Cdd:MTH00118 231 HHFGFEAAAWYWH 243
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-173 6.05e-89

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: 260.14  E-value: 6.05e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488632   1 HTVVVKQGLKYGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGAVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHA 80
Cdd:cd01665   55 HTKKVQKGLRLGMILFILSEVMFFFSFFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHA 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488632  81 LISGKKTEAINGLTATVILGLIFTGLQAMEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLAVCLARLVYHQFTRH 160
Cdd:cd01665  135 LLLGNRKKAILGLILTILLGVYFTGLQAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSN 214

                        170
                 ....*....|...
gi 941488632 161 HHLGFEAASWYWH 173
Cdd:cd01665  215 HHLGFEAAIWYWH 227
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 1-173 2.82e-88

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 258.89  E-value: 2.82e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488632   1 HTVVVKQGLKYGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGAVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHA 80
Cdd:MTH00039  70 HTLIVINGLRYGMILFITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHS 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488632  81 LISGKKTEAINGLTATVILGLIFTGLQAMEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLAVCLARLVYHQFTRH 160
Cdd:MTH00039 150 ILEGNRTEAIQALFLTVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNN 229

                        170
                 ....*....|...
gi 941488632 161 HHLGFEAASWYWH 173
Cdd:MTH00039 230 HHFGFEAAAWYWH 242
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 1-173 3.08e-88

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 258.57  E-value: 3.08e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488632   1 HTVVVKQGLKYGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGAVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHA 80
Cdd:MTH00155  69 HTKKVTKGLRWGMILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHS 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488632  81 LISGKKTEAINGLTATVILGLIFTGLQAMEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLAVCLARLVYHQFTRH 160
Cdd:MTH00155 149 LMENNYKQATQSLFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSN 228

                        170
                 ....*....|...
gi 941488632 161 HHLGFEAASWYWH 173
Cdd:MTH00155 229 HHFGFEAAAWYWH 241
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 1-173 1.07e-87

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 257.59  E-value: 1.07e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488632   1 HTVVVKQGLKYGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGAVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHA 80
Cdd:MTH00189  70 HTPPVQKGLRYGMILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHS 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488632  81 LISGKKTEAINGLTATVILGLIFTGLQAMEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLAVCLARLVYHQFTRH 160
Cdd:MTH00189 150 LMEGNRKEAIQALTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSS 229

                        170
                 ....*....|...
gi 941488632 161 HHLGFEAASWYWH 173
Cdd:MTH00189 230 HHFGFEAAAWYWH 242
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 1-173 6.99e-82

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 242.49  E-value: 6.99e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488632   1 HTVVVKQGLKYGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGAVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHA 80
Cdd:MTH00141  69 HTSKVQRGLRWGFILFIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHS 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488632  81 LISGKKTEAINGLTATVILGLIFTGLQAMEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLAVCLARLVYHQFTRH 160
Cdd:MTH00141 149 LMEGDYKSALQGLGLTIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTN 228

                        170
                 ....*....|...
gi 941488632 161 HHLGFEAASWYWH 173
Cdd:MTH00141 229 HHFGFEAAAWYWH 241
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 1-173 2.24e-81

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 241.59  E-value: 2.24e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488632   1 HTVVVKQGLKYGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGAVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHA 80
Cdd:MTH00130  71 HTPPVQKGLRYGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHS 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488632  81 LISGKKTEAINGLTATVILGLIFTGLQAMEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLAVCLARLVYHQFTRH 160
Cdd:MTH00130 151 IMEGERKQAIQSLTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSE 230

                        170
                 ....*....|...
gi 941488632 161 HHLGFEAASWYWH 173
Cdd:MTH00130 231 HHFGFEAAAWYWH 243
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 1-173 3.29e-80

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 238.49  E-value: 3.29e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488632   1 HTVVVKQGLKYGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGAVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHA 80
Cdd:MTH00075  71 HTPPVQKGLRYGMILFITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHS 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488632  81 LISGKKTEAINGLTATVILGLIFTGLQAMEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLAVCLARLVYHQFTRH 160
Cdd:MTH00075 151 IMQGNRKEAIQSLALTIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQ 230

                        170
                 ....*....|...
gi 941488632 161 HHLGFEAASWYWH 173
Cdd:MTH00075 231 HHFGFEAAAWYWH 243
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 1-173 2.21e-78

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 233.85  E-value: 2.21e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488632   1 HTVVVKQGLKYGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGAVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHA 80
Cdd:MTH00099  71 HTPIVQKGLRYGMILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHS 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488632  81 LISGKKTEAINGLTATVILGLIFTGLQAMEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLAVCLARLVYHQFTRH 160
Cdd:MTH00099 151 LMEGNRKHMLQALFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSN 230

                        170
                 ....*....|...
gi 941488632 161 HHLGFEAASWYWH 173
Cdd:MTH00099 231 HHFGFEAAAWYWH 243
COX3 pfam00510
Cytochrome c oxidase subunit III;
1-173 2.38e-78

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 233.84  E-value: 2.38e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488632    1 HTVVVKQGLKYGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGAVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHA 80
Cdd:pfam00510  68 HTFAVQKGLNLGMILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHS 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488632   81 LISGKKTEAINGLTATVILGLIFTGLQAMEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLAVCLARLVYHQFTRH 160
Cdd:pfam00510 148 LIEGNRKQALQGLILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDN 227

                         170
                  ....*....|...
gi 941488632  161 HHLGFEAASWYWH 173
Cdd:pfam00510 228 HHFGFEAAILYWH 240
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 1-173 2.05e-76

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 228.90  E-value: 2.05e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488632   1 HTVVVKQGLKYGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGAVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHA 80
Cdd:MTH00219  72 HTSKVSTGLRIGMILFIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHS 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488632  81 LISGKKTEAINGLTATVILGLIFTGLQAMEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLAVCLARLVYHQFTRH 160
Cdd:MTH00219 152 LMESNHKEAQQGLLFTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKN 231

                        170
                 ....*....|...
gi 941488632 161 HHLGFEAASWYWH 173
Cdd:MTH00219 232 HHFGFEAAAWYWH 244
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 1-173 5.98e-73

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 220.09  E-value: 5.98e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488632   1 HTVVVKQGLKYGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGAVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHA 80
Cdd:MTH00009  69 HTSYVTKGLRWGMILFIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHS 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488632  81 LISGKKTEAINGLTATVILGLIFTGLQAMEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLAVCLARLVYHQFTRH 160
Cdd:MTH00009 149 LIEGDRPEATQALILTVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTG 228

                        170
                 ....*....|...
gi 941488632 161 HHLGFEAASWYWH 173
Cdd:MTH00009 229 HHFGFEAAAWYWH 241
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 1-173 3.06e-69

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 211.85  E-value: 3.06e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488632   1 HTVVVKQGLKYGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGAVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHA 80
Cdd:MTH00028  71 HTQIVVRGLKLGMLLFILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHA 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488632  81 LISGK------------------------------------KTEAINGLTATVILGLIFTGLQAMEYYEAPFAISDSVYG 124
Cdd:MTH00028 151 IIGTGnpaslekgtqgiegpnpsngappdpqkgptfllsdfRTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYG 230

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 941488632 125 STFFVATGFHGLHVIIGTTFLAVCLARLVYHQFTRHHHLGFEAASWYWH 173
Cdd:MTH00028 231 STFFMLTGTHGLHVLVGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWH 279
PLN02194 PLN02194
cytochrome-c oxidase
 1-173 7.09e-62

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 192.19  E-value: 7.09e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488632   1 HTVVVKQGLKYGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGAVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHA 80
Cdd:PLN02194  74 HTKVVQLGPRYGSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHA 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488632  81 LISGKKTEAINGLTATVILGLIFTGLQAMEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLAVCLARLVYHQFTRH 160
Cdd:PLN02194 154 ILAGKEKRAVYALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKE 233

                        170
                 ....*....|...
gi 941488632 161 HHLGFEAASWYWH 173
Cdd:PLN02194 234 HHVGFEAAAWYWH 246
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
 1-173 1.11e-55

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 175.91  E-value: 1.11e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488632   1 HTVVVKQGLKYGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGAVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHA 80
Cdd:MTH00083  67 HNFFVMDGFKFGMILFIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHS 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488632  81 L-ISGKKTEaiNGLTATVILGLIFTGLQAMEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLAVCLARLVYHQFTR 159
Cdd:MTH00083 147 LcLSNKSCT--NSLLLTCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNY 224

                        170
                 ....*....|....
gi 941488632 160 HHHLGFEAASWYWH 173
Cdd:MTH00083 225 NHHLGLEFAILYWH 238
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 1-173 1.79e-54

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: 170.46  E-value: 1.79e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488632   1 HTVVVKQGLKYGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGAvwppqginPLNPFSVPLLNTAVLLSSGATVTWAHHA 80
Cdd:cd00386    1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFGA--------GLDPLDLPLLNTNTLLLSGSSVTWAHAS 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488632  81 LI--SGKKTEAINGLTATVILGLIFTGLQAMEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLAVCLARLVYHQFT 158
Cdd:cd00386   73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152

                        170
                 ....*....|....*
gi 941488632 159 RHHHLGFEAASWYWH 173
Cdd:cd00386  153 PRHHLGLEAAALYWH 167
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
1-173 1.42e-39

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 132.67  E-value: 1.42e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488632   1 HTVVVKQGLKYGMLLFILSEVLFFFSFFWAFFHSSLApavelGAVWPpQGINPLNPfSVPLLNTAVLLSSGATVTWAHHA 80
Cdd:COG1845    8 HAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS-----APDWP-AGAELLDL-PLPLINTLLLLLSSFTVALAVRA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488632  81 LISGKKTEAINGLTATVILGLIFTGLQAMEYYE---APFAISDSVYGSTFFVATGFHGLHVIIGTTFLAVCLARLVYHQF 157
Cdd:COG1845   81 ARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHliaEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGF 160

                        170
                 ....*....|....*.
gi 941488632 158 TRHHHLGFEAASWYWH 173
Cdd:COG1845  161 TPENHTGVEAAALYWH 176
NorE_like cd02862
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ...
 61-173 9.53e-18

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: 76.12  E-value: 9.53e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488632  61 LLNTAVLLSSGATVTWAHHALISGKKTEAINGLTATVILGLIFTGLQAMEYYE---APFAISDSVYGSTFFVATGFHGLH 137
Cdd:cd02862   55 ALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYAHkiaAGIDPDAGLFFTLYFLLTGFHLLH 134

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 941488632 138 VIIGTTFLAVCLARLVYHQFTRHHHLGFEAASWYWH 173
Cdd:cd02862  135 VLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWH 170
Ubiquinol_oxidase_III cd02863
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ...
 61-173 6.19e-16

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: 6.19e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488632  61 LLNTAVLLSSGATVTWAHHALISGKKTEAINGLTATVILGLIFTGLQAME---YYEAPFAISDSVYGSTFFVATGFHGLH 137
Cdd:cd02863   54 FIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLVGTHGLH 133

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 941488632 138 VIIGTTFLAVCLARLVYHQFTRHHHLGFEAASWYWH 173
Cdd:cd02863  134 VTFGLIWILVMIIQLKKRGLTPDTARRLFCLSLFWH 169
Heme_Cu_Oxidase_III_2 cd02865
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 43-173 1.83e-14

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: 67.39  E-value: 1.83e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488632  43 GAVWPPQGINPLNpfsVPLLNTAVLLSSGATVTWAHHALISGKKTEAINGLTATVILGLIFTGLQAMEYYEAPFAI---S 119
Cdd:cd02865   38 GDWQPGAPLPLPN---LLSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWHALNDAGygpT 114

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 941488632 120 DSVYGSTFFVATGFHGLHVIIGTTFLAVCLARLVYHQFTRHHHLGFEAASWYWH 173
Cdd:cd02865  115 SNPAGSFFYLLTGLHGLHVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYWH 168
Heme_Cu_Oxidase_III_1 cd02864
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 10-173 1.56e-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: 239215  Cd Length: 202  Bit Score: 57.51  E-value: 1.56e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488632  10 KYGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGAVWPPQGInPLNPFSVPL----LNTAVLLSSGATVTWAHHALISGK 85
Cdd:cd02864   10 KAMMWFFLLSDAFIFSSFLIAYMTARISTTEPWPLPSDVFAL-RIGHFNIPLvliaIMTFILITSSGTMAMAVNFGYRGN 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488632  86 KTEAINGLTATVILGLIFTGLQAMEYYE---------APFAISDSVYGSTFFVATGFHGLHVIIGTTFLAVCLARLVYHQ 156
Cdd:cd02864   89 RKAAARLMLATALLGATFVGMQAFEWTKliveegvrpWGNPWGAAQFGASFFMITGFHGTHVTIGVIYLIIIARKVWRGK 168

                        170
                 ....*....|....*...
gi 941488632 157 FTRH-HHLGFEAASWYWH 173
Cdd:cd02864  169 YQRIgRYEIVEIAGLYWH 186
COX3 MTH00049
cytochrome c oxidase subunit III; Validated
 15-173 4.12e-06

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177124  Cd Length: 215  Bit Score: 45.29  E-value: 4.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488632  15 LFILSEVLFFFSFFwaffhsslapaveLGAVW--PPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHALisGKKTEAINg 92
Cdd:MTH00049  59 LFILSEVIIFGSLL-------------VCCLWfdDWSYISLSSSLEIPFVGCFLLLGSSITVTAYHHLL--GWKYCDLF- 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941488632  93 LTATVILGLIFTGLQAMEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTtflaVCLARLVYHQFTRHHHLGFEAASWYW 172
Cdd:MTH00049 123 LYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHFSHVVLGV----VGLSTLLLVGSSSFGVYRSTVLTWYW 198


                 .
gi 941488632 173 H 173
Cdd:MTH00049 199 H 199
 
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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