NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1931731142|gb|QPB75159|]
View 

cytochrome c oxidase subunit III, partial (mitochondrion) [Zanclea sp. JP011]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 1-222 6.03e-108

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: 310.92  E-value: 6.03e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931731142   1 PWPYVMGCGAFLTTIGAVVYFHYSQLILVFIGLLMIVSCMFAWLKDVIRESTFQGHHTKIAVLGLKIGFLLFIVSEVLFF 80
Cdd:MTH00024   15 PWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGMLLFILSEVLFF 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931731142  81 FSFFWAFFHSSLSPSVEIGVIWPPVGIDPLNPFSVPLLNTAILLSSGATVTWAHHSIVSGNKSEAVQGLTLTVILGVLFT 160
Cdd:MTH00024   95 FSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFLTVFLGVLFT 174

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1931731142 161 ALQAMEYVEAPFCIADSVYGTTFFVATGFHGLHVIIGTIFLFICLLRLNLSHFTTSHHFGFE 222
Cdd:MTH00024  175 GLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFE 236
 
Name Accession Description Interval E-value
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 1-222 6.03e-108

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 310.92  E-value: 6.03e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931731142   1 PWPYVMGCGAFLTTIGAVVYFHYSQLILVFIGLLMIVSCMFAWLKDVIRESTFQGHHTKIAVLGLKIGFLLFIVSEVLFF 80
Cdd:MTH00024   15 PWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGMLLFILSEVLFF 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931731142  81 FSFFWAFFHSSLSPSVEIGVIWPPVGIDPLNPFSVPLLNTAILLSSGATVTWAHHSIVSGNKSEAVQGLTLTVILGVLFT 160
Cdd:MTH00024   95 FSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFLTVFLGVLFT 174

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1931731142 161 ALQAMEYVEAPFCIADSVYGTTFFVATGFHGLHVIIGTIFLFICLLRLNLSHFTTSHHFGFE 222
Cdd:MTH00024  175 GLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFE 236
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 5-222 1.98e-96

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: 280.94  E-value: 1.98e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931731142   5 VMGCGAFLTTIGAVVYFH-YSQLILVFIGLLMIVSCMFAWLKDVIRESTFQGHHTKIAVLGLKIGFLLFIVSEVLFFFSF 83
Cdd:cd01665     2 LGSFGLLLLALGLVLWMHgYGGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFSF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931731142  84 FWAFFHSSLSPSVEIGVIWPPVGIDPLNPFSVPLLNTAILLSSGATVTWAHHSIVSGNKSEAVQGLTLTVILGVLFTALQ 163
Cdd:cd01665    82 FWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGLQ 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1931731142 164 AMEYVEAPFCIADSVYGTTFFVATGFHGLHVIIGTIFLFICLLRLNLSHFTTSHHFGFE 222
Cdd:cd01665   162 AYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFE 220
COX3 pfam00510
Cytochrome c oxidase subunit III;
1-222 1.62e-88

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 261.58  E-value: 1.62e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931731142   1 PWPYVMGCGAFLTTIGAVVYFHYSQLI--LVFIGLLMIVSCMFAWLKDVIRESTFQGHHTKIAVLGLKIGFLLFIVSEVL 78
Cdd:pfam00510  10 PWPLFGSFALLLLTSGLVLWFHGYSGNmtLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGMILFIISEVF 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931731142  79 FFFSFFWAFFHSSLSPSVEIGVIWPPVGIDPLNPFSVPLLNTAILLSSGATVTWAHHSIVSGNKSEAVQGLTLTVILGVL 158
Cdd:pfam00510  90 FFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGLILTILLAVY 169

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1931731142 159 FTALQAMEYVEAPFCIADSVYGTTFFVATGFHGLHVIIGTIFLFICLLRLNLSHFTTSHHFGFE 222
Cdd:pfam00510 170 FTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFE 233
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
56-222 4.34e-31

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 112.64  E-value: 4.34e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931731142  56 HHTKIAVLGLKIGFLLFIVSEVLFFFSFFWAFFHSSLSpsveigVIWPPVGIDPLNPfSVPLLNTAILLSSGATVTWAHH 135
Cdd:COG1845     7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS------APDWPAGAELLDL-PLPLINTLLLLLSSFTVALAVR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931731142 136 SIVSGNKSEAVQGLTLTVILGVLFTALQAMEY---VEAPFCIADSVYGTTFFVATGFHGLHVIIGTIFLFICLLRLNLSH 212
Cdd:COG1845    80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159

                         170
                  ....*....|
gi 1931731142 213 FTTSHHFGFE 222
Cdd:COG1845   160 FTPENHTGVE 169
 
Name Accession Description Interval E-value
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 1-222 6.03e-108

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 310.92  E-value: 6.03e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931731142   1 PWPYVMGCGAFLTTIGAVVYFHYSQLILVFIGLLMIVSCMFAWLKDVIRESTFQGHHTKIAVLGLKIGFLLFIVSEVLFF 80
Cdd:MTH00024   15 PWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGMLLFILSEVLFF 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931731142  81 FSFFWAFFHSSLSPSVEIGVIWPPVGIDPLNPFSVPLLNTAILLSSGATVTWAHHSIVSGNKSEAVQGLTLTVILGVLFT 160
Cdd:MTH00024   95 FSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFLTVFLGVLFT 174

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1931731142 161 ALQAMEYVEAPFCIADSVYGTTFFVATGFHGLHVIIGTIFLFICLLRLNLSHFTTSHHFGFE 222
Cdd:MTH00024  175 GLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFE 236
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 1-222 3.93e-105

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 303.64  E-value: 3.93e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931731142   1 PWPYVMGCGAFLTTIGAVVYFHYSQLILVFIGLLMIVSCMFAWLKDVIRESTFQGHHTKIAVLGLKIGFLLFIVSEVLFF 80
Cdd:MTH00155   13 PWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGMILFIVSEVFFF 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931731142  81 FSFFWAFFHSSLSPSVEIGVIWPPVGIDPLNPFSVPLLNTAILLSSGATVTWAHHSIVSGNKSEAVQGLTLTVILGVLFT 160
Cdd:MTH00155   93 ISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSLFFTIILGIYFT 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1931731142 161 ALQAMEYVEAPFCIADSVYGTTFFVATGFHGLHVIIGTIFLFICLLRLNLSHFTTSHHFGFE 222
Cdd:MTH00155  173 MLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFE 234
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 1-222 2.77e-104

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 301.49  E-value: 2.77e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931731142   1 PWPYVMGCGAFLTTIGAVVYFHYSQLILVFIGLLMIVSCMFAWLKDVIRESTFQGHHTKIAVLGLKIGFLLFIVSEVLFF 80
Cdd:MTH00118   15 PWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRYGMILFITSEVFFF 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931731142  81 FSFFWAFFHSSLSPSVEIGVIWPPVGIDPLNPFSVPLLNTAILLSSGATVTWAHHSIVSGNKSEAVQGLTLTVILGVLFT 160
Cdd:MTH00118   95 LGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQALTLTILLGLYFT 174

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1931731142 161 ALQAMEYVEAPFCIADSVYGTTFFVATGFHGLHVIIGTIFLFICLLRLNLSHFTTSHHFGFE 222
Cdd:MTH00118  175 ALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFE 236
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 1-222 8.23e-102

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 295.34  E-value: 8.23e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931731142   1 PWPYVMGCGAFLTTIGAVVYFHYSQLILVFIGLLMIVSCMFAWLKDVIRESTFQGHHTKIAVLGLKIGFLLFIVSEVLFF 80
Cdd:MTH00189   14 PWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRYGMILFITSEVFFF 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931731142  81 FSFFWAFFHSSLSPSVEIGVIWPPVGIDPLNPFSVPLLNTAILLSSGATVTWAHHSIVSGNKSEAVQGLTLTVILGVLFT 160
Cdd:MTH00189   94 LGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQALTLTVILGVYFT 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1931731142 161 ALQAMEYVEAPFCIADSVYGTTFFVATGFHGLHVIIGTIFLFICLLRLNLSHFTTSHHFGFE 222
Cdd:MTH00189  174 LLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFE 235
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 1-222 1.49e-101

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 294.78  E-value: 1.49e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931731142   1 PWPYVMGCGAFLTTIGAVVYFHYSQLILVFIGLLMIVSCMFAWLKDVIRESTFQGHHTKIAVLGLKIGFLLFIVSEVLFF 80
Cdd:MTH00052   16 PWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGLKYGMILFIVSEVCLF 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931731142  81 FSFFWAFFHSSLSPSVEIGVIWPPVGIDPLNPFSVPLLNTAILLSSGATVTWAHHSIVSGNKSEAVQGLTLTVILGVLFT 160
Cdd:MTH00052   96 FSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEAIIGLALTVALGLLFT 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1931731142 161 ALQAMEYVEAPFCIADSVYGTTFFVATGFHGLHVIIGTIFLFICLLRLNLSHFTTSHHFGFE 222
Cdd:MTH00052  176 GLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFE 237
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 1-222 7.43e-101

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 292.79  E-value: 7.43e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931731142   1 PWPYVMGCGAFLTTIGAVVYFHYSQLILVFIGLLMIVSCMFAWLKDVIRESTFQGHHTKIAVLGLKIGFLLFIVSEVLFF 80
Cdd:MTH00039   14 PWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRYGMILFITSEVCFF 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931731142  81 FSFFWAFFHSSLSPSVEIGVIWPPVGIDPLNPFSVPLLNTAILLSSGATVTWAHHSIVSGNKSEAVQGLTLTVILGVLFT 160
Cdd:MTH00039   94 FAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQALFLTVLLGLYFT 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1931731142 161 ALQAMEYVEAPFCIADSVYGTTFFVATGFHGLHVIIGTIFLFICLLRLNLSHFTTSHHFGFE 222
Cdd:MTH00039  174 ALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFE 235
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 1-222 1.34e-97

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 284.48  E-value: 1.34e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931731142   1 PWPYVMGCGAFLTTIGAVVYFHYSQLILVFIGLLMIVSCMFAWLKDVIRESTFQGHHTKIAVLGLKIGFLLFIVSEVLFF 80
Cdd:MTH00141   13 PWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFILFIVSEVCFF 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931731142  81 FSFFWAFFHSSLSPSVEIGVIWPPVGIDPLNPFSVPLLNTAILLSSGATVTWAHHSIVSGNKSEAVQGLTLTVILGVLFT 160
Cdd:MTH00141   93 FAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGLTIILGVYFT 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1931731142 161 ALQAMEYVEAPFCIADSVYGTTFFVATGFHGLHVIIGTIFLFICLLRLNLSHFTTSHHFGFE 222
Cdd:MTH00141  173 FLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFE 234
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 5-222 1.98e-96

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: 280.94  E-value: 1.98e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931731142   5 VMGCGAFLTTIGAVVYFH-YSQLILVFIGLLMIVSCMFAWLKDVIRESTFQGHHTKIAVLGLKIGFLLFIVSEVLFFFSF 83
Cdd:cd01665     2 LGSFGLLLLALGLVLWMHgYGGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFSF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931731142  84 FWAFFHSSLSPSVEIGVIWPPVGIDPLNPFSVPLLNTAILLSSGATVTWAHHSIVSGNKSEAVQGLTLTVILGVLFTALQ 163
Cdd:cd01665    82 FWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGLQ 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1931731142 164 AMEYVEAPFCIADSVYGTTFFVATGFHGLHVIIGTIFLFICLLRLNLSHFTTSHHFGFE 222
Cdd:cd01665   162 AYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFE 220
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 1-222 1.05e-92

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 272.39  E-value: 1.05e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931731142   1 PWPYVMGCGAFLTTIGAVVYFHYSQLILVFIGLLMIVSCMFAWLKDVIRESTFQGHHTKIAVLGLKIGFLLFIVSEVLFF 80
Cdd:MTH00075   15 PWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRYGMILFITSEVFFF 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931731142  81 FSFFWAFFHSSLSPSVEIGVIWPPVGIDPLNPFSVPLLNTAILLSSGATVTWAHHSIVSGNKSEAVQGLTLTVILGVLFT 160
Cdd:MTH00075   95 LGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQSLALTIILGLYFT 174

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1931731142 161 ALQAMEYVEAPFCIADSVYGTTFFVATGFHGLHVIIGTIFLFICLLRLNLSHFTTSHHFGFE 222
Cdd:MTH00075  175 LLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFE 236
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 1-222 2.40e-92

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 271.27  E-value: 2.40e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931731142   1 PWPYVMGCGAFLTTIGAVVYFHYSQLILVFIGLLMIVSCMFAWLKDVIRESTFQGHHTKIAVLGLKIGFLLFIVSEVLFF 80
Cdd:MTH00219   16 PWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLRIGMILFIVSEILFF 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931731142  81 FSFFWAFFHSSLSPSVEIGVIWPPVGIDPLNPFSVPLLNTAILLSSGATVTWAHHSIVSGNKSEAVQGLTLTVILGVLFT 160
Cdd:MTH00219   96 FAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQQGLLFTILLGLYFT 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1931731142 161 ALQAMEYVEAPFCIADSVYGTTFFVATGFHGLHVIIGTIFLFICLLRLNLSHFTTSHHFGFE 222
Cdd:MTH00219  176 MLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFE 237
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 1-222 9.98e-91

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 267.40  E-value: 9.98e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931731142   1 PWPYVMGCGAFLTTIGAVVYFHYSQLILVFIGLLMIVSCMFAWLKDVIRESTFQGHHTKIAVLGLKIGFLLFIVSEVLFF 80
Cdd:MTH00130   15 PWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRYGMILFITSEVFFF 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931731142  81 FSFFWAFFHSSLSPSVEIGVIWPPVGIDPLNPFSVPLLNTAILLSSGATVTWAHHSIVSGNKSEAVQGLTLTVILGVLFT 160
Cdd:MTH00130   95 LGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQSLTLTILLGFYFT 174

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1931731142 161 ALQAMEYVEAPFCIADSVYGTTFFVATGFHGLHVIIGTIFLFICLLRLNLSHFTTSHHFGFE 222
Cdd:MTH00130  175 FLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFE 236
COX3 pfam00510
Cytochrome c oxidase subunit III;
1-222 1.62e-88

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 261.58  E-value: 1.62e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931731142   1 PWPYVMGCGAFLTTIGAVVYFHYSQLI--LVFIGLLMIVSCMFAWLKDVIRESTFQGHHTKIAVLGLKIGFLLFIVSEVL 78
Cdd:pfam00510  10 PWPLFGSFALLLLTSGLVLWFHGYSGNmtLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGMILFIISEVF 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931731142  79 FFFSFFWAFFHSSLSPSVEIGVIWPPVGIDPLNPFSVPLLNTAILLSSGATVTWAHHSIVSGNKSEAVQGLTLTVILGVL 158
Cdd:pfam00510  90 FFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGLILTILLAVY 169

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1931731142 159 FTALQAMEYVEAPFCIADSVYGTTFFVATGFHGLHVIIGTIFLFICLLRLNLSHFTTSHHFGFE 222
Cdd:pfam00510 170 FTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFE 233
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 1-222 9.97e-88

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 259.66  E-value: 9.97e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931731142   1 PWPYVMGCGAFLTTIGAVVYFHYSQLILVFIGLLMIVSCMFAWLKDVIRESTFQGHHTKIAVLGLKIGFLLFIVSEVLFF 80
Cdd:MTH00099   15 PWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRYGMILFIISEVFFF 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931731142  81 FSFFWAFFHSSLSPSVEIGVIWPPVGIDPLNPFSVPLLNTAILLSSGATVTWAHHSIVSGNKSEAVQGLTLTVILGVLFT 160
Cdd:MTH00099   95 AGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQALFITILLGLYFT 174

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1931731142 161 ALQAMEYVEAPFCIADSVYGTTFFVATGFHGLHVIIGTIFLFICLLRLNLSHFTTSHHFGFE 222
Cdd:MTH00099  175 LLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFE 236
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 1-222 6.90e-85

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 252.45  E-value: 6.90e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931731142   1 PWPYVMGCGAFLTTIGAVVYFHYSQLILVFIGLLMIVSCMFAWLKDVIRESTFQGHHTKIAVLGLKIGFLLFIVSEVLFF 80
Cdd:MTH00009   13 PWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMILFIASEVMFF 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931731142  81 FSFFWAFFHSSLSPSVEIGVIWPPVGIDPLNPFSVPLLNTAILLSSGATVTWAHHSIVSGNKSEAVQGLTLTVILGVLFT 160
Cdd:MTH00009   93 FAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALILTVLLGAYFT 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1931731142 161 ALQAMEYVEAPFCIADSVYGTTFFVATGFHGLHVIIGTIFLFICLLRLNLSHFTTSHHFGFE 222
Cdd:MTH00009  173 FLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFE 234
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 1-222 1.92e-80

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 242.66  E-value: 1.92e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931731142   1 PWPYVMGCGAFLTTIGAVVYFHYSQLILVFIGLLMIVSCMFAWLKDVIRESTFQGHHTKIAVLGLKIGFLLFIVSEVLFF 80
Cdd:MTH00028   15 PWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLLFILSEVCLF 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931731142  81 FSFFWAFFHSSLSPSVEIGVIWPPVGIDPLNPFSVPLLNTAILLSSGATVTWAHHSIVSGN------------------- 141
Cdd:MTH00028   95 FAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTGnpaslekgtqgiegpnpsn 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931731142 142 -----------------KSEAVQGLTLTVILGVLFTALQAMEYVEAPFCIADSVYGTTFFVATGFHGLHVIIGTIFLFIC 204
Cdd:MTH00028  175 gappdpqkgptfllsdfRTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVLVGTTFLIVC 254

                         250
                  ....*....|....*...
gi 1931731142 205 LLRLNLSHFTTSHHFGFE 222
Cdd:MTH00028  255 FIRLLSNQFTNSHHLGLE 272
PLN02194 PLN02194
cytochrome-c oxidase
 1-222 4.17e-69

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 212.60  E-value: 4.17e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931731142   1 PWPYVMGCGAFLTTIGAVVYFHYSQ--LILVFIGLLMIVSCMFAWLKDVIRESTFQGHHTKIAVLGLKIGFLLFIVSEVL 78
Cdd:PLN02194   16 PWPISGSLGALATTVGGVMYMHPFQggARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGPRYGSILFIVSEVM 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931731142  79 FFFSFFWAFFHSSLSPSVEIGVIWPPVGIDPLNPFSVPLLNTAILLSSGATVTWAHHSIVSGNKSEAVQGLTLTVILGVL 158
Cdd:PLN02194   96 FFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEKRAVYALVATVLLALV 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1931731142 159 FTALQAMEYVEAPFCIADSVYGTTFFVATGFHGLHVIIGTIFLFICLLRLNLSHFTTSHHFGFE 222
Cdd:PLN02194  176 FTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFE 239
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
 2-222 4.08e-54

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 173.99  E-value: 4.08e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931731142   2 WPYVMGCGAFLTTIGAVVYFHYSQLILVFIGLLMIVSCMFAWLKDVIREStFQGHHTKIAVLGLKIGFLLFIVSEVLFFF 81
Cdd:MTH00083   13 YPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMILFIFSEFMFFF 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931731142  82 SFFWAFFHSSLSPSVEIGVIWPPVGIDPLNPFSVPLLNTAILLSSGATVTWAHHSIVSGNKSeAVQGLTLTVILGVLFTA 161
Cdd:MTH00083   92 SIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSNKS-CTNSLLLTCFLGLYFTS 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1931731142 162 LQAMEYVEAPFCIADSVYGTTFFVATGFHGLHVIIGTIFLFICLLRLNLSHFTTSHHFGFE 222
Cdd:MTH00083  171 FQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLE 231
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 57-222 9.85e-44

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: 145.04  E-value: 9.85e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931731142  57 HTKIAVLGLKIGFLLFIVSEVLFFFSFFWAFFHSSLSPSVEIGViwppvgidPLNPFSVPLLNTAILLSSGATVTWAHHS 136
Cdd:cd00386     1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFGA--------GLDPLDLPLLNTNTLLLSGSSVTWAHAS 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931731142 137 IV--SGNKSEAVQGLTLTVILGVLFTALQAMEYVEAPFCIADSVYGTTFFVATGFHGLHVIIGTIFLFICLLRLNLSHFT 214
Cdd:cd00386    73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152


                  ....*...
gi 1931731142 215 TSHHFGFE 222
Cdd:cd00386   153 PRHHLGLE 160
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
56-222 4.34e-31

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 112.64  E-value: 4.34e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931731142  56 HHTKIAVLGLKIGFLLFIVSEVLFFFSFFWAFFHSSLSpsveigVIWPPVGIDPLNPfSVPLLNTAILLSSGATVTWAHH 135
Cdd:COG1845     7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS------APDWPAGAELLDL-PLPLINTLLLLLSSFTVALAVR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931731142 136 SIVSGNKSEAVQGLTLTVILGVLFTALQAMEY---VEAPFCIADSVYGTTFFVATGFHGLHVIIGTIFLFICLLRLNLSH 212
Cdd:COG1845    80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159

                         170
                  ....*....|
gi 1931731142 213 FTTSHHFGFE 222
Cdd:COG1845   160 FTPENHTGVE 169
NorE_like cd02862
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ...
 117-222 2.57e-13

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: 65.72  E-value: 2.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931731142 117 LLNTAILLSSGATVTWAHHSIVSGNKSEAVQGLTLTVILGVLFTALQAMEY---VEAPFCIADSVYGTTFFVATGFHGLH 193
Cdd:cd02862    55 ALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYahkIAAGIDPDAGLFFTLYFLLTGFHLLH 134

                          90       100
                  ....*....|....*....|....*....
gi 1931731142 194 VIIGTIFLFICLLRLNLSHFTTSHHFGFE 222
Cdd:cd02862   135 VLIGLGILLWVAWRARRGRYSARDYEGVE 163
Heme_Cu_Oxidase_III_2 cd02865
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 102-222 2.92e-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: 57.38  E-value: 2.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931731142 102 WPPVGIDPLNpfsVPLLNTAILLSSGATVTWAHHSIVSGNKSEAVQGLTLTVILGVLFTALQAMEYVEAPFCI---ADSV 178
Cdd:cd02865    41 QPGAPLPLPN---LLSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWHALNDAGygpTSNP 117

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1931731142 179 YGTTFFVATGFHGLHVIIGTIFLFICLLRLNLSHFTTSHHFGFE 222
Cdd:cd02865   118 AGSFFYLLTGLHGLHVIGGLVALAIVLAGLIRGHYGPRRRLPVE 161
Ubiquinol_oxidase_III cd02863
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ...
 117-208 6.49e-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: 56.48  E-value: 6.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931731142 117 LLNTAILLSSGATVTWAHHSIVSGNKSEAVQGLTLTVILGVLFTALQAME---YVEAPFCIADSVYGTTFFVATGFHGLH 193
Cdd:cd02863    54 FIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLVGTHGLH 133

                          90
                  ....*....|....*
gi 1931731142 194 VIIGTIFLFICLLRL 208
Cdd:cd02863   134 VTFGLIWILVMIIQL 148
Heme_Cu_Oxidase_III_1 cd02864
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 102-203 4.17e-07

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: 48.65  E-value: 4.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931731142 102 WPP---VGIDPLNPFSVPL----LNTAILLSSGATVTWAHHSIVSGNKSEAVQGLTLTVILGVLFTALQAMEYVE----- 169
Cdd:cd02864    42 WPLpsdVFALRIGHFNIPLvliaIMTFILITSSGTMAMAVNFGYRGNRKAAARLMLATALLGATFVGMQAFEWTKlivee 121

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1931731142 170 ------APFCIAdsVYGTTFFVATGFHGLHVIIGTIFLFI 203
Cdd:cd02864   122 gvrpwgNPWGAA--QFGASFFMITGFHGTHVTIGVIYLII 159
COX3 MTH00049
cytochrome c oxidase subunit III; Validated
 66-206 1.01e-06

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177124  Cd Length: 215  Bit Score: 47.60  E-value: 1.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931731142  66 KIGFLLFIVSEVLFFFSFFWAFFHSSLSPSVEIGviwppvgidplNPFSVPLLNTAILLSSGATVTWAHHSIVSgnkSEA 145
Cdd:MTH00049   54 ESAFWLFILSEVIIFGSLLVCCLWFDDWSYISLS-----------SSLEIPFVGCFLLLGSSITVTAYHHLLGW---KYC 119

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1931731142 146 VQGLTLTVILGVLFTALQAMEYVEAPFCIADSVYGTTFFVATGFHGLHVIIGTIFLFICLL 206
Cdd:MTH00049  120 DLFLYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHFSHVVLGVVGLSTLLL 180
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH