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Conserved domains on  [gi|295388246|gb|ADG03027|]
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cytochrome c oxidase subunit III, partial (mitochondrion) [Drosophila guttifera]

Protein Classification

cytochrome c oxidase subunit 3( domain architecture ID 10009592)

cytochrome c oxidase subunit 3 is one of main transmembrane subunits of cytochrome c oxidase, the last enzyme in the respiratory electron transport chain of mitochondria or bacteria located in the mitochondrial or bacterial membrane

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 11-148 5.24e-92

cytochrome c oxidase subunit III; Provisional


:

Pssm-ID: 214439  Cd Length: 255  Bit Score: 267.05  E-value: 5.24e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295388246  11 FHSSLSPAIELGASWPPMGIISFNPFQIPLLNTAILLASGVTVTWAHHSLMENNHSQTTQALFFTVLLGVYFTMLQAYEY 90
Cdd:MTH00155 100 FHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSLFFTIILGIYFTMLQAYEY 179

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 295388246  91 IEAPFTIADSVYGSTFFMATGFHGIHVLIGTTFLLICLLRHLNNHFSKNHHFGFEAAA 148
Cdd:MTH00155 180 YEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAA 237
 
Name Accession Description Interval E-value
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 11-148 5.24e-92

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 267.05  E-value: 5.24e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295388246  11 FHSSLSPAIELGASWPPMGIISFNPFQIPLLNTAILLASGVTVTWAHHSLMENNHSQTTQALFFTVLLGVYFTMLQAYEY 90
Cdd:MTH00155 100 FHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSLFFTIILGIYFTMLQAYEY 179

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 295388246  91 IEAPFTIADSVYGSTFFMATGFHGIHVLIGTTFLLICLLRHLNNHFSKNHHFGFEAAA 148
Cdd:MTH00155 180 YEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAA 237
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 12-148 2.83e-77

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: 229.32  E-value: 2.83e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295388246  12 HSSLSPAIELGASWPPMGIISFNPFQIPLLNTAILLASGVTVTWAHHSLMENNHSQTTQALFFTVLLGVYFTMLQAYEYI 91
Cdd:cd01665   87 HSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGLQAYEYY 166

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 295388246  92 EAPFTIADSVYGSTFFMATGFHGIHVLIGTTFLLICLLRHLNNHFSKNHHFGFEAAA 148
Cdd:cd01665  167 EASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAI 223
COX3 pfam00510
Cytochrome c oxidase subunit III;
12-148 2.15e-70

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 212.27  E-value: 2.15e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295388246   12 HSSLSPAIELGASWPPMGIISFNPFQIPLLNTAILLASGVTVTWAHHSLMENNHSQTTQALFFTVLLGVYFTMLQAYEYI 91
Cdd:pfam00510 100 HSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGLILTILLAVYFTGLQAMEYT 179

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 295388246   92 EAPFTIADSVYGSTFFMATGFHGIHVLIGTTFLLICLLRHLNNHFSKNHHFGFEAAA 148
Cdd:pfam00510 180 EASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAI 236
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
27-148 3.80e-35

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 120.34  E-value: 3.80e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295388246  27 PMGIISFNPFqIPLLNTAILLASGVTVTWAHHSLMENNHSQTTQALFFTVLLGVYFTMLQAYEY---IEAPFTIADSVYG 103
Cdd:COG1845   49 PAGAELLDLP-LPLINTLLLLLSSFTVALAVRAARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFG 127

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 295388246 104 STFFMATGFHGIHVLIGTTFLLICLLRHLNNHFSKNHHFGFEAAA 148
Cdd:COG1845  128 SFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGFTPENHTGVEAAA 172
 
Name Accession Description Interval E-value
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 11-148 5.24e-92

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 267.05  E-value: 5.24e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295388246  11 FHSSLSPAIELGASWPPMGIISFNPFQIPLLNTAILLASGVTVTWAHHSLMENNHSQTTQALFFTVLLGVYFTMLQAYEY 90
Cdd:MTH00155 100 FHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSLFFTIILGIYFTMLQAYEY 179

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 295388246  91 IEAPFTIADSVYGSTFFMATGFHGIHVLIGTTFLLICLLRHLNNHFSKNHHFGFEAAA 148
Cdd:MTH00155 180 YEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAA 237
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 12-148 5.70e-78

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 231.76  E-value: 5.70e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295388246  12 HSSLSPAIELGASWPPMGIISFNPFQIPLLNTAILLASGVTVTWAHHSLMENNHSQTTQALFFTVLLGVYFTMLQAYEYI 91
Cdd:MTH00118 103 HSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQALTLTILLGLYFTALQAMEYY 182

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 295388246  92 EAPFTIADSVYGSTFFMATGFHGIHVLIGTTFLLICLLRHLNNHFSKNHHFGFEAAA 148
Cdd:MTH00118 183 EAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAA 239
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 12-148 1.52e-77

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 230.63  E-value: 1.52e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295388246  12 HSSLSPAIELGASWPPMGIISFNPFQIPLLNTAILLASGVTVTWAHHSLMENNHSQTTQALFFTVLLGVYFTMLQAYEYI 91
Cdd:MTH00189 102 HSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQALTLTVILGVYFTLLQAMEYY 181

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 295388246  92 EAPFTIADSVYGSTFFMATGFHGIHVLIGTTFLLICLLRHLNNHFSKNHHFGFEAAA 148
Cdd:MTH00189 182 EAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAA 238
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 12-148 2.83e-77

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: 229.32  E-value: 2.83e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295388246  12 HSSLSPAIELGASWPPMGIISFNPFQIPLLNTAILLASGVTVTWAHHSLMENNHSQTTQALFFTVLLGVYFTMLQAYEYI 91
Cdd:cd01665   87 HSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGLQAYEYY 166

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 295388246  92 EAPFTIADSVYGSTFFMATGFHGIHVLIGTTFLLICLLRHLNNHFSKNHHFGFEAAA 148
Cdd:cd01665  167 EASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAI 223
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 11-148 7.37e-76

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 226.31  E-value: 7.37e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295388246  11 FHSSLSPAIELGASWPPMGIISFNPFQIPLLNTAILLASGVTVTWAHHSLMENNHSQTTQALFFTVLLGVYFTMLQAYEY 90
Cdd:MTH00141 100 FHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGLTIILGVYFTFLQAGEY 179

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 295388246  91 IEAPFTIADSVYGSTFFMATGFHGIHVLIGTTFLLICLLRHLNNHFSKNHHFGFEAAA 148
Cdd:MTH00141 180 YEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAA 237
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 12-148 3.74e-75

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 224.61  E-value: 3.74e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295388246  12 HSSLSPAIELGASWPPMGIISFNPFQIPLLNTAILLASGVTVTWAHHSLMENNHSQTTQALFFTVLLGVYFTMLQAYEYI 91
Cdd:MTH00039 102 HSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQALFLTVLLGLYFTALQAWEYY 181

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 295388246  92 EAPFTIADSVYGSTFFMATGFHGIHVLIGTTFLLICLLRHLNNHFSKNHHFGFEAAA 148
Cdd:MTH00039 182 DAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAA 238
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 12-148 7.96e-72

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 216.13  E-value: 7.96e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295388246  12 HSSLSPAIELGASWPPMGIISFNPFQIPLLNTAILLASGVTVTWAHHSLMENNHSQTTQALFFTVLLGVYFTMLQAYEYI 91
Cdd:MTH00099 103 HSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQALFITILLGLYFTLLQASEYY 182

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 295388246  92 EAPFTIADSVYGSTFFMATGFHGIHVLIGTTFLLICLLRHLNNHFSKNHHFGFEAAA 148
Cdd:MTH00099 183 EAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAA 239
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 12-148 1.15e-70

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 213.09  E-value: 1.15e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295388246  12 HSSLSPAIELGASWPPMGIISFNPFQIPLLNTAILLASGVTVTWAHHSLMENNHSQTTQALFFTVLLGVYFTMLQAYEYI 91
Cdd:MTH00130 103 HSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQSLTLTILLGFYFTFLQAMEYY 182

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 295388246  92 EAPFTIADSVYGSTFFMATGFHGIHVLIGTTFLLICLLRHLNNHFSKNHHFGFEAAA 148
Cdd:MTH00130 183 EAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAA 239
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 13-148 1.63e-70

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 212.68  E-value: 1.63e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295388246  13 SSLSPAIELGASWPPMGIISFNPFQIPLLNTAILLASGVTVTWAHHSLMENNHSQTTQALFFTVLLGVYFTMLQAYEYIE 92
Cdd:MTH00075 104 SSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQSLALTIILGLYFTLLQAMEYYE 183

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 295388246  93 APFTIADSVYGSTFFMATGFHGIHVLIGTTFLLICLLRHLNNHFSKNHHFGFEAAA 148
Cdd:MTH00075 184 APFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAA 239
COX3 pfam00510
Cytochrome c oxidase subunit III;
12-148 2.15e-70

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 212.27  E-value: 2.15e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295388246   12 HSSLSPAIELGASWPPMGIISFNPFQIPLLNTAILLASGVTVTWAHHSLMENNHSQTTQALFFTVLLGVYFTMLQAYEYI 91
Cdd:pfam00510 100 HSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGLILTILLAVYFTGLQAMEYT 179

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 295388246   92 EAPFTIADSVYGSTFFMATGFHGIHVLIGTTFLLICLLRHLNNHFSKNHHFGFEAAA 148
Cdd:pfam00510 180 EASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAI 236
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 11-148 1.20e-69

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 210.80  E-value: 1.20e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295388246  11 FHSSLSPAIELGASWPPMGIISFNPFQIPLLNTAILLASGVTVTWAHHSLMENNHSQTTQALFFTVLLGVYFTMLQAYEY 90
Cdd:MTH00219 103 FHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQQGLLFTILLGLYFTMLQGMEY 182

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 295388246  91 IEAPFTIADSVYGSTFFMATGFHGIHVLIGTTFLLICLLRHLNNHFSKNHHFGFEAAA 148
Cdd:MTH00219 183 LEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAA 240
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 12-148 7.07e-68

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 205.84  E-value: 7.07e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295388246  12 HSSLSPAIELGASWPPMGIISFNPFQIPLLNTAILLASGVTVTWAHHSLMENNHSQTTQALFFTVLLGVYFTMLQAYEYI 91
Cdd:MTH00009 101 HSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALILTVLLGAYFTFLQAGEYI 180

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 295388246  92 EAPFTIADSVYGSTFFMATGFHGIHVLIGTTFLLICLLRHLNNHFSKNHHFGFEAAA 148
Cdd:MTH00009 181 EAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAA 237
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 11-148 8.13e-67

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 203.45  E-value: 8.13e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295388246  11 FHSSLSPAIELGASWPPMGIISFNPFQIPLLNTAILLASGVTVTWAHHSLMENNHSQTTQALFFTVLLGVYFTMLQAYEY 90
Cdd:MTH00024 102 FHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFLTVFLGVLFTGLQAIEY 181

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 295388246  91 IEAPFTIADSVYGSTFFMATGFHGIHVLIGTTFLLICLLRHLNNHFSKNHHFGFEAAA 148
Cdd:MTH00024 182 YEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAAS 239
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 11-148 1.98e-61

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 189.62  E-value: 1.98e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295388246  11 FHSSLSPAIELGASWPPMGIISFNPFQIPLLNTAILLASGVTVTWAHHSLMENNHSQTTQALFFTVLLGVYFTMLQAYEY 90
Cdd:MTH00052 103 FHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEAIIGLALTVALGLLFTGLQAMEY 182

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 295388246  91 IEAPFTIADSVYGSTFFMATGFHGIHVLIGTTFLLICLLRHLNNHFSKNHHFGFEAAA 148
Cdd:MTH00052 183 YEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAA 240
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 12-147 2.75e-48

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 157.15  E-value: 2.75e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295388246  12 HSSLSPAIELGASWPPMGIISFNPFQIPLLNTAILLASGVTVTWAHH--------------------------------- 58
Cdd:MTH00028 103 HSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHaiigtgnpaslekgtqgiegpnpsngappdpqk 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295388246  59 ---SLMENNHSQTTQALFFTVLLGVYFTMLQAYEYIEAPFTIADSVYGSTFFMATGFHGIHVLIGTTFLLICLLRHLNNH 135
Cdd:MTH00028 183 gptFLLSDFRTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVLVGTTFLIVCFIRLLSNQ 262

                        170
                 ....*....|..
gi 295388246 136 FSKNHHFGFEAA 147
Cdd:MTH00028 263 FTNSHHLGLEAA 274
PLN02194 PLN02194
cytochrome-c oxidase
 12-148 2.71e-46

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 151.35  E-value: 2.71e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295388246  12 HSSLSPAIELGASWPPMGIISFNPFQIPLLNTAILLASGVTVTWAHHSLMENNHSQTTQALFFTVLLGVYFTMLQAYEYI 91
Cdd:PLN02194 106 HSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEKRAVYALVATVLLALVFTGFQGMEYY 185

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 295388246  92 EAPFTIADSVYGSTFFMATGFHGIHVLIGTTFLLICLLRHLNNHFSKNHHFGFEAAA 148
Cdd:PLN02194 186 QAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAA 242
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
 12-148 4.43e-46

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 150.49  E-value: 4.43e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295388246  12 HSSLSPAIELGASWPPMGIISFNPFQIPLLNTAILLASGVTVTWAHHSLMENNhSQTTQALFFTVLLGVYFTMLQAYEYI 91
Cdd:MTH00083  99 DAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSN-KSCTNSLLLTCFLGLYFTSFQLMEYK 177

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 295388246  92 EAPFTIADSVYGSTFFMATGFHGIHVLIGTTFLLICLLRHLNNHFSKNHHFGFEAAA 148
Cdd:MTH00083 178 EASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAI 234
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 12-148 2.77e-43

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: 140.80  E-value: 2.77e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295388246  12 HSSLSPAIELGASwppmgiisFNPFQIPLLNTAILLASGVTVTWAHHSLM--ENNHSQTTQALFFTVLLGVYFTMLQAYE 89
Cdd:cd00386   33 HSRLSPPVEFGAG--------LDPLDLPLLNTNTLLLSGSSVTWAHASLAarRGNRKKARLWLLLTILLGLAFLGLQAYE 104

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 295388246  90 YIEAPFTIADSVYGSTFFMATGFHGIHVLIGTTFLLICLLRHLNNHFSKNHHFGFEAAA 148
Cdd:cd00386  105 YSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFTPRHHLGLEAAA 163
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
27-148 3.80e-35

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 120.34  E-value: 3.80e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295388246  27 PMGIISFNPFqIPLLNTAILLASGVTVTWAHHSLMENNHSQTTQALFFTVLLGVYFTMLQAYEY---IEAPFTIADSVYG 103
Cdd:COG1845   49 PAGAELLDLP-LPLINTLLLLLSSFTVALAVRAARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFG 127

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 295388246 104 STFFMATGFHGIHVLIGTTFLLICLLRHLNNHFSKNHHFGFEAAA 148
Cdd:COG1845  128 SFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGFTPENHTGVEAAA 172
NorE_like cd02862
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ...
 40-148 4.04e-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: 63.41  E-value: 4.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295388246  40 LLNTAILLASGVTVTWAHHSLMENNHSQTTQALFFTVLLGVYFTMLQAYEY---IEAPFTIADSVYGSTFFMATGFHGIH 116
Cdd:cd02862   55 ALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYahkIAAGIDPDAGLFFTLYFLLTGFHLLH 134

                         90       100       110
                 ....*....|....*....|....*....|..
gi 295388246 117 VLIGTTFLLICLLRHLNNHFSKNHHFGFEAAA 148
Cdd:cd02862  135 VLIGLGILLWVAWRARRGRYSARDYEGVEAAA 166
COX3 MTH00049
cytochrome c oxidase subunit III; Validated
 35-129 1.08e-11

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177124  Cd Length: 215  Bit Score: 59.93  E-value: 1.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295388246  35 PFQIPLLNTAILLASGVTVTWAHHSL-MENNHSQttqaLFFTVLLGVYFTMLQAYEYIEAPFTIADSVYGSTFFMATGFH 113
Cdd:MTH00049  89 SLEIPFVGCFLLLGSSITVTAYHHLLgWKYCDLF----LYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLH 164

                         90
                 ....*....|....*.
gi 295388246 114 GIHVLIGTTFLLICLL 129
Cdd:MTH00049 165 FSHVVLGVVGLSTLLL 180
Ubiquinol_oxidase_III cd02863
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ...
 36-132 7.23e-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: 54.55  E-value: 7.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295388246  36 FQIPL--LNTAILLASGVTVTWAHHSLMENNHSQTTQALFFTVLLGVYFTMLQAYE---YIEAPFTIADSVYGSTFFMAT 110
Cdd:cd02863   48 FELPLvfIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLV 127

                         90       100
                 ....*....|....*....|..
gi 295388246 111 GFHGIHVLIGtTFLLICLLRHL 132
Cdd:cd02863  128 GTHGLHVTFG-LIWILVMIIQL 148
Heme_Cu_Oxidase_III_1 cd02864
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 31-126 3.17e-09

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: 52.89  E-value: 3.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295388246  31 ISFNPFQIPL----LNTAILLASGVTVTWAHHSLMENNHSQTTQALFFTVLLGVYFTMLQAYEY-----------IEAPF 95
Cdd:cd02864   51 LRIGHFNIPLvliaIMTFILITSSGTMAMAVNFGYRGNRKAAARLMLATALLGATFVGMQAFEWtkliveegvrpWGNPW 130

                         90       100       110
                 ....*....|....*....|....*....|.
gi 295388246  96 TIAdsVYGSTFFMATGFHGIHVLIGTTFLLI 126
Cdd:cd02864  131 GAA--QFGASFFMITGFHGTHVTIGVIYLII 159
ACR_tran pfam00873
AcrB/AcrD/AcrF family; Members of this family are integral membrane proteins. Some are ...
 12-97 9.98e-04

AcrB/AcrD/AcrF family; Members of this family are integral membrane proteins. Some are involved in drug resistance. AcrB cooperates with a membrane fusion protein, AcrA, and an outer membrane channel TolC. The structure shows the AcrB forms a homotrimer.


Pssm-ID: 395701 [Multi-domain]  Cd Length: 1021  Bit Score: 38.04  E-value: 9.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295388246    12 HSSLSPAIELGASWPPMGIISFNPFQIPLLNTAILLASGVTVTWAHHSLMENNHSQTTQALFFTVLLGVYFTMLQAYEYI 91
Cdd:pfam00873  807 RYNGFRSIVISGNVAAGDSLGDAMEAMAQIAKQVKLPPGYGYTWTGQFEQEQLAGNSLPILIALALLVVFLVLAALYESW 886


                   ....*.
gi 295388246    92 EAPFTI 97
Cdd:pfam00873  887 SDPLSI 892
 
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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