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Conserved domains on  [gi|1511931889|gb|AYV60938|]
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cytochrome c oxidase subunit II, partial (mitochondrion) [Nocaracris citripes]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11475927)

cytochrome c oxidase subunit II, part of the functional core of the enzyme, transfers the electrons from cytochrome c via its binuclear copper A center to the bimetallic center of the catalytic subunit I

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-173 1.71e-108

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 308.68  E-value: 1.71e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931889   1 TVLMLITIVVGYSLAYMLTINYSNRHVLHGHLIETIWTTLPAITLIFIALPSLRLLYLLDDSIDSMITIKTIGRQWYWSY 80
Cdd:MTH00154   29 MILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSY 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931889  81 EYSDFVDVEFDTYMTPEMDLEVDGFRLLDVDNRTILPMNTEIRVLTSASDVLHSWAVPSLGIKIDATPGRLNQGTFTMNR 160
Cdd:MTH00154  109 EYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINR 188

                         170
                  ....*....|...
gi 1511931889 161 PGLFFGQCSEICG 173
Cdd:MTH00154  189 PGLFFGQCSEICG 201
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-173 1.71e-108

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 308.68  E-value: 1.71e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931889   1 TVLMLITIVVGYSLAYMLTINYSNRHVLHGHLIETIWTTLPAITLIFIALPSLRLLYLLDDSIDSMITIKTIGRQWYWSY 80
Cdd:MTH00154   29 MILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSY 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931889  81 EYSDFVDVEFDTYMTPEMDLEVDGFRLLDVDNRTILPMNTEIRVLTSASDVLHSWAVPSLGIKIDATPGRLNQGTFTMNR 160
Cdd:MTH00154  109 EYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINR 188

                         170
                  ....*....|...
gi 1511931889 161 PGLFFGQCSEICG 173
Cdd:MTH00154  189 PGLFFGQCSEICG 201
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 65-173 1.47e-71

C-terminal domain of Cytochrome c Oxidase subunit II; 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. It 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. 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 II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the binuclear center (active site) in subunit I.


Pssm-ID: 259979 [Multi-domain]  Cd Length: 130  Bit Score: 211.66  E-value: 1.47e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931889  65 SMITIKTIGRQWYWSYEYSDFVDVEFDTYMTPEMDLEVDGFRLLDVDNRTILPMNTEIRVLTSASDVLHSWAVPSLGIKI 144
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100
                  ....*....|....*....|....*....
gi 1511931889 145 DATPGRLNQGTFTMNRPGLFFGQCSEICG 173
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICG 109
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
67-173 1.35e-66

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 198.79  E-value: 1.35e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931889  67 ITIKTIGRQWYWSYEYSDFVDVEFDTYMTPEMDLEVDGFRLLDVDNRTILPMNTEIRVLTSASDVLHSWAVPSLGIKIDA 146
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100
                  ....*....|....*....|....*..
gi 1511931889 147 TPGRLNQGTFTMNRPGLFFGQCSEICG 173
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICG 107
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
2-173 7.24e-34

Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 119.16  E-value: 7.24e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931889   2 VLMLITIVVGYSLAYMLtINYSNR-------HVLHGHLIETIWTTLPAITLIFIALPSLRLLYLLDDSIDSMITIKTIGR 74
Cdd:COG1622    42 IMLVIFVLVFGLLLYFA-IRYRRRkgdadpaQFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGY 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931889  75 QWYWSYEYsdfvdvefdtymtPEMDLEVDgfrlldvdNRTILPMNTEIRVLTSASDVLHSWAVPSLGIKIDATPGRLNQG 154
Cdd:COG1622   121 QWKWLFRY-------------PDQGIATV--------NELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTEL 179

                         170
                  ....*....|....*....
gi 1511931889 155 TFTMNRPGLFFGQCSEICG 173
Cdd:COG1622   180 WFTADKPGTYRGQCAELCG 198
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 2-173 2.96e-29

cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions. [Energy metabolism, Electron transport]


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 106.31  E-value: 2.96e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931889   2 VLMLITIVVGYSLAYMlTINYSNR-------HVLHGHLIETIWTTLPAITLIFIALPSLRLLYLLDDSID-SMITIKTIG 73
Cdd:TIGR02866  19 VSTLISLLVAALLAYV-VWKFRRKgdeekpsQIHGNRRLEYVWTVIPLIIVVGLFAATAKGLLYLERPIPkDALKVKVTG 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931889  74 RQWYWSYEYSDFvdvefdtymtpemdlevdGFRlldVDNRTILPMNTEIRVLTSASDVLHSWAVPSLGIKIDATPGRLNQ 153
Cdd:TIGR02866  98 YQWWWDFEYPES------------------GFT---TVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNA 156

                         170       180
                  ....*....|....*....|
gi 1511931889 154 GTFTMNRPGLFFGQCSEICG 173
Cdd:TIGR02866 157 LWFNADEPGVYYGFCAELCG 176
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-173 1.71e-108

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 308.68  E-value: 1.71e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931889   1 TVLMLITIVVGYSLAYMLTINYSNRHVLHGHLIETIWTTLPAITLIFIALPSLRLLYLLDDSIDSMITIKTIGRQWYWSY 80
Cdd:MTH00154   29 MILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSY 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931889  81 EYSDFVDVEFDTYMTPEMDLEVDGFRLLDVDNRTILPMNTEIRVLTSASDVLHSWAVPSLGIKIDATPGRLNQGTFTMNR 160
Cdd:MTH00154  109 EYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINR 188

                         170
                  ....*....|...
gi 1511931889 161 PGLFFGQCSEICG 173
Cdd:MTH00154  189 PGLFFGQCSEICG 201
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 2-173 1.33e-81

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 240.59  E-value: 1.33e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931889   2 VLMLITIVVGYSLAYMLTINYSNRHVLHGHLIETIWTTLPAITLIFIALPSLRLLYLLDDSIDSMITIKTIGRQWYWSYE 81
Cdd:MTH00117   30 VALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPSLRILYLMDEINNPHLTIKAIGHQWYWSYE 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931889  82 YSDFVDVEFDTYMTPEMDLEVDGFRLLDVDNRTILPMNTEIRVLTSASDVLHSWAVPSLGIKIDATPGRLNQGTFTMNRP 161
Cdd:MTH00117  110 YTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVPSLGVKTDAVPGRLNQTSFITTRP 189

                         170
                  ....*....|..
gi 1511931889 162 GLFFGQCSEICG 173
Cdd:MTH00117  190 GVFYGQCSEICG 201
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 2-173 3.75e-80

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 237.14  E-value: 3.75e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931889   2 VLMLITIVVGYSLAYMLTINYSNRHVLHGHLIETIWTTLPAITLIFIALPSLRLLYLLDDSIDSMITIKTIGRQWYWSYE 81
Cdd:MTH00140   30 VLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPSLRLLYLLDETNNPLLTVKAIGHQWYWSYE 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931889  82 YSDFVDVEFDTYMTPEMDLEVDGFRLLDVDNRTILPMNTEIRVLTSASDVLHSWAVPSLGIKIDATPGRLNQGTFTMNRP 161
Cdd:MTH00140  110 YSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVPSLGVKVDAIPGRLNQLSFEPKRP 189

                         170
                  ....*....|..
gi 1511931889 162 GLFFGQCSEICG 173
Cdd:MTH00140  190 GVFYGQCSEICG 201
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 2-173 3.43e-79

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 234.60  E-value: 3.43e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931889   2 VLMLITIVVGYSLAYMLTINYSNRHVLHGHLIETIWTTLPAITLIFIALPSLRLLYLLDDSIDSMITIKTIGRQWYWSYE 81
Cdd:MTH00038   30 ILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPSLQLLYLMDEVNNPFLTIKAIGHQWYWSYE 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931889  82 YSDFVDVEFDTYMTPEMDLEVDGFRLLDVDNRTILPMNTEIRVLTSASDVLHSWAVPSLGIKIDATPGRLNQGTFTMNRP 161
Cdd:MTH00038  110 YTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFISRT 189

                         170
                  ....*....|..
gi 1511931889 162 GLFFGQCSEICG 173
Cdd:MTH00038  190 GLFYGQCSEICG 201
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-173 2.65e-78

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 232.30  E-value: 2.65e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931889   1 TVLMLITIVVGYSLAYMLTINYSNRHVLHGHLIETIWTTLPAITLIFIALPSLRLLYLLDDSIDSMITIKTIGRQWYWSY 80
Cdd:MTH00139   29 VILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPSLRLLYLMDEVSDPYLTFKAVGHQWYWSY 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931889  81 EYSDFVDVEFDTYMTPEMDLEVDGFRLLDVDNRTILPMNTEIRVLTSASDVLHSWAVPSLGIKIDATPGRLNQGTFTMNR 160
Cdd:MTH00139  109 EYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSWTVPSLGVKIDAVPGRLNQVGFFINR 188

                         170
                  ....*....|...
gi 1511931889 161 PGLFFGQCSEICG 173
Cdd:MTH00139  189 PGVFYGQCSEICG 201
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-173 5.81e-78

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 231.41  E-value: 5.81e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931889   1 TVLMLITIVVGYSLAYMLTINYSNRHVLHGHLIETIWTTLPAITLIFIALPSLRLLYLLDDSIDSMITIKTIGRQWYWSY 80
Cdd:MTH00168   29 LILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPSLRLLYLMDEIDKPDLTIKAVGHQWYWSY 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931889  81 EYSDFVDVEFDTYMTPEMDLEVDGFRLLDVDNRTILPMNTEIRVLTSASDVLHSWAVPSLGIKIDATPGRLNQGTFTMNR 160
Cdd:MTH00168  109 EYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSWTLPSLGLKMDAVPGRLNQLAFLSSR 188

                         170
                  ....*....|...
gi 1511931889 161 PGLFFGQCSEICG 173
Cdd:MTH00168  189 PGSFYGQCSEICG 201
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 2-173 6.59e-78

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 231.67  E-value: 6.59e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931889   2 VLMLITIVVGYSLAYMLTINYSNRHVLHGHLIETIWTTLPAITLIFIALPSLRLLYLLDDSIDSMITIKTIGRQWYWSYE 81
Cdd:MTH00008   30 ILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSLRLLYLMDEVSNPSITLKTIGHQWYWSYE 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931889  82 YSDFVDVEFDTYMTPEMDLEVDGFRLLDVDNRTILPMNTEIRVLTSASDVLHSWAVPSLGIKIDATPGRLNQGTFTMNRP 161
Cdd:MTH00008  110 YSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPGRLNQIGFTITRP 189

                         170
                  ....*....|..
gi 1511931889 162 GLFFGQCSEICG 173
Cdd:MTH00008  190 GVFYGQCSEICG 201
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 65-173 1.47e-71

C-terminal domain of Cytochrome c Oxidase subunit II; 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. It 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. 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 II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the binuclear center (active site) in subunit I.


Pssm-ID: 259979 [Multi-domain]  Cd Length: 130  Bit Score: 211.66  E-value: 1.47e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931889  65 SMITIKTIGRQWYWSYEYSDFVDVEFDTYMTPEMDLEVDGFRLLDVDNRTILPMNTEIRVLTSASDVLHSWAVPSLGIKI 144
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100
                  ....*....|....*....|....*....
gi 1511931889 145 DATPGRLNQGTFTMNRPGLFFGQCSEICG 173
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICG 109
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 2-173 4.94e-71

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 213.81  E-value: 4.94e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931889   2 VLMLITIVVGYSLAYMLTINYSNRHVLHGHLIETIWTTLPAITLIFIALPSLRLLYLLDDSIDSMITIKTIGRQWYWSYE 81
Cdd:MTH00098   30 IVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRILYMMDEINNPSLTVKTMGHQWYWSYE 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931889  82 YSDFVDVEFDTYMTPEMDLEVDGFRLLDVDNRTILPMNTEIRVLTSASDVLHSWAVPSLGIKIDATPGRLNQGTFTMNRP 161
Cdd:MTH00098  110 YTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMSTRP 189

                         170
                  ....*....|..
gi 1511931889 162 GLFFGQCSEICG 173
Cdd:MTH00098  190 GLYYGQCSEICG 201
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-173 6.94e-71

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 213.59  E-value: 6.94e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931889   1 TVLMLITIVVGYSLAYMLTINYSNRHVLHGHLIETIWTTLPAITLIFIALPSLRLLYLLDDSIDSMITIKTIGRQWYWSY 80
Cdd:MTH00185   29 MIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLRILYLMDEINDPHLTIKAMGHQWYWSY 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931889  81 EYSDFVDVEFDTYMTPEMDLEVDGFRLLDVDNRTILPMNTEIRVLTSASDVLHSWAVPSLGIKIDATPGRLNQGTFTMNR 160
Cdd:MTH00185  109 EYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVPALGVKMDAVPGRLNQATFIISR 188

                         170
                  ....*....|...
gi 1511931889 161 PGLFFGQCSEICG 173
Cdd:MTH00185  189 PGLYYGQCSEICG 201
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 2-173 8.98e-70

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 211.15  E-value: 8.98e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931889   2 VLMLITIVVGYSLAYMLTINYSNRHVLHGHLIETIWTTLPAITLIFIALPSLRLLYLLDDSIDSMITIKTIGRQWYWSYE 81
Cdd:MTH00023   39 LLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYLMDEVVSPALTIKAIGHQWYWSYE 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931889  82 YSDFVD--VEFDTYMTPEMDLEVDGFRLLDVDNRTILPMNTEIRVLTSASDVLHSWAVPSLGIKIDATPGRLNQGTFTMN 159
Cdd:MTH00023  119 YSDYEGetLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIK 198

                         170
                  ....*....|....
gi 1511931889 160 RPGLFFGQCSEICG 173
Cdd:MTH00023  199 RPGVFYGQCSEICG 212
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 2-173 3.17e-69

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 209.57  E-value: 3.17e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931889   2 VLMLITIVVGYSLAYMLTINYSNRHVLHGHLIETIWTTLPAITLIFIALPSLRLLYLLDDSIDSMITIKTIGRQWYWSYE 81
Cdd:MTH00129   30 IVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRILYLMDEINDPHLTIKAMGHQWYWSYE 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931889  82 YSDFVDVEFDTYMTPEMDLEVDGFRLLDVDNRTILPMNTEIRVLTSASDVLHSWAVPSLGIKIDATPGRLNQGTFTMNRP 161
Cdd:MTH00129  110 YTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVPALGVKMDAVPGRLNQTAFIASRP 189

                         170
                  ....*....|..
gi 1511931889 162 GLFFGQCSEICG 173
Cdd:MTH00129  190 GVFYGQCSEICG 201
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 2-173 1.14e-68

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 208.10  E-value: 1.14e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931889   2 VLMLITIVVGYSLAYMLTINYSNRHVLHGHLIETIWTTLPAITLIFIALPSLRLLYLLDDSIDSMITIKTIGRQWYWSYE 81
Cdd:MTH00051   32 ILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYLMDEVIDPALTIKAIGHQWYWSYE 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931889  82 YSDF--VDVEFDTYMTPEMDLEVDGFRLLDVDNRTILPMNTEIRVLTSASDVLHSWAVPSLGIKIDATPGRLNQGTFTMN 159
Cdd:MTH00051  112 YSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPSLSVKIDAVPGRLNQTSFFIK 191

                         170
                  ....*....|....
gi 1511931889 160 RPGLFFGQCSEICG 173
Cdd:MTH00051  192 RPGVFYGQCSEICG 205
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 4-173 2.31e-67

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 204.63  E-value: 2.31e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931889   4 MLITIVVGYSLAYMLTINYSNRHVLHGHLIETIWTTLPAITLIFIALPSLRLLYLLDDSIDSMITIKTIGRQWYWSYEYS 83
Cdd:MTH00076   32 FLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRILYLMDEINDPHLTVKAIGHQWYWSYEYT 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931889  84 DFVDVEFDTYMTPEMDLEVDGFRLLDVDNRTILPMNTEIRVLTSASDVLHSWAVPSLGIKIDATPGRLNQGTFTMNRPGL 163
Cdd:MTH00076  112 DYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSLGIKTDAIPGRLNQTSFIASRPGV 191

                         170
                  ....*....|
gi 1511931889 164 FFGQCSEICG 173
Cdd:MTH00076  192 YYGQCSEICG 201
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
67-173 1.35e-66

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 198.79  E-value: 1.35e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931889  67 ITIKTIGRQWYWSYEYSDFVDVEFDTYMTPEMDLEVDGFRLLDVDNRTILPMNTEIRVLTSASDVLHSWAVPSLGIKIDA 146
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100
                  ....*....|....*....|....*..
gi 1511931889 147 TPGRLNQGTFTMNRPGLFFGQCSEICG 173
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICG 107
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 2-173 8.89e-54

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 171.36  E-value: 8.89e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931889   2 VLMLITIVVGYSLAYMLTINYSNRHV------LHGHLIETIWTTLPAITLIFIALPSLRLLYLLDDSIDSM-ITIKTIGR 74
Cdd:MTH00027   55 ILFILTIIVGVVLWLIIRILLGNNYYsyywnkLDGSLIEVIWTLIPAFILILIAFPSLRLLYIMDECGFSAnITIKVTGH 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931889  75 QWYWSYEYSDF--VDVEFDTYMTPEMDLEVDGFRLLDVDNRTILPMNTEIRVLTSASDVLHSWAVPSLGIKIDATPGRLN 152
Cdd:MTH00027  135 QWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVLHSWTVPSLAVKMDAVPGRIN 214

                         170       180
                  ....*....|....*....|.
gi 1511931889 153 QGTFTMNRPGLFFGQCSEICG 173
Cdd:MTH00027  215 ETGFLIKRPGIFYGQCSEICG 235
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 3-173 2.08e-51

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 164.03  E-value: 2.08e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931889   3 LMLITIVVGYSLAYMLTINYSNRHVlHGHLIETIWTTLPAITLIFIALPSLRLLYLLD-DSIDSMITIKTIGRQWYWSYE 81
Cdd:MTH00080   34 FVLAFVVFLFLYLISNNFYFKSKKI-EYQFGELLCSVFPVLILLMQMVPSLSLLYYYGlMNLDSNLTVKVTGHQWYWSYE 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931889  82 YSDFVDVEFDTYMTPEMDLEVDGFRLLDVDNRTILPMNTEIRVLTSASDVLHSWAVPSLGIKIDATPGRLNQGTFTMNRP 161
Cdd:MTH00080  113 FSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILSTLCYSFPMP 192

                         170
                  ....*....|..
gi 1511931889 162 GLFFGQCSEICG 173
Cdd:MTH00080  193 GVFYGQCSEICG 204
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
2-173 7.24e-34

Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 119.16  E-value: 7.24e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931889   2 VLMLITIVVGYSLAYMLtINYSNR-------HVLHGHLIETIWTTLPAITLIFIALPSLRLLYLLDDSIDSMITIKTIGR 74
Cdd:COG1622    42 IMLVIFVLVFGLLLYFA-IRYRRRkgdadpaQFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGY 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931889  75 QWYWSYEYsdfvdvefdtymtPEMDLEVDgfrlldvdNRTILPMNTEIRVLTSASDVLHSWAVPSLGIKIDATPGRLNQG 154
Cdd:COG1622   121 QWKWLFRY-------------PDQGIATV--------NELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTEL 179

                         170
                  ....*....|....*....
gi 1511931889 155 TFTMNRPGLFFGQCSEICG 173
Cdd:COG1622   180 WFTADKPGTYRGQCAELCG 198
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 32-173 7.87e-31

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 110.43  E-value: 7.87e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931889  32 LIETIWTTLPAITLIFIALPSLRLLYLLDDSIDSMiTIKTIGRQWYWSYEYSDfvDVEFDTYMTPEMDLevdgfrlldVD 111
Cdd:MTH00047   48 VLELLWTVVPTLLVLVLCFLNLNFITSDLDCFSSE-TIKVIGHQWYWSYEYSF--GGSYDSFMTDDIFG---------VD 115

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1511931889 112 NRTILPMNTEIRVLTSASDVLHSWAVPSLGIKIDATPGRLNQGTFTMNRPGLFFGQCSEICG 173
Cdd:MTH00047  116 KPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCG 177
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 90-173 4.94e-30

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 107.60  E-value: 4.94e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931889  90 FDTYMTPEMDLEVDGFRLLDVDNRTILPMNTEIRVLTSASDVLHSWAVPSLGIKIDATPGRLNQGTFTMNRPGLFFGQCS 169
Cdd:PTZ00047   51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130


                  ....
gi 1511931889 170 EICG 173
Cdd:PTZ00047  131 EMCG 134
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 2-173 2.96e-29

cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions. [Energy metabolism, Electron transport]


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 106.31  E-value: 2.96e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931889   2 VLMLITIVVGYSLAYMlTINYSNR-------HVLHGHLIETIWTTLPAITLIFIALPSLRLLYLLDDSID-SMITIKTIG 73
Cdd:TIGR02866  19 VSTLISLLVAALLAYV-VWKFRRKgdeekpsQIHGNRRLEYVWTVIPLIIVVGLFAATAKGLLYLERPIPkDALKVKVTG 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931889  74 RQWYWSYEYSDFvdvefdtymtpemdlevdGFRlldVDNRTILPMNTEIRVLTSASDVLHSWAVPSLGIKIDATPGRLNQ 153
Cdd:TIGR02866  98 YQWWWDFEYPES------------------GFT---TVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNA 156

                         170       180
                  ....*....|....*....|
gi 1511931889 154 GTFTMNRPGLFFGQCSEICG 173
Cdd:TIGR02866 157 LWFNADEPGVYYGFCAELCG 176
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 67-173 3.85e-21

The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of most bacteria, is a multi-chain transmembrane protein located in the inner membrane the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. Caa3 type of CcO Subunit II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the cytochromes a, a3 and CuB active site in subunit I.


Pssm-ID: 259875 [Multi-domain]  Cd Length: 103  Bit Score: 82.67  E-value: 3.85e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931889  67 ITIKTIGRQWYWSYEYSDFVDVEFDTymtpemdlevdgfrlldvDNRTILPMNTEIRVLTSASDVLHSWAVPSLGIKIDA 146
Cdd:cd04213     2 LTIEVTGHQWWWEFRYPDEPGRGIVT------------------ANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDM 63

                          90       100
                  ....*....|....*....|....*..
gi 1511931889 147 TPGRLNQGTFTMNRPGLFFGQCSEICG 173
Cdd:cd04213    64 IPGRTNRLWLQADEPGVYRGQCAEFCG 90
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 67-173 1.04e-20

Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259911 [Multi-domain]  Cd Length: 95  Bit Score: 81.57  E-value: 1.04e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931889  67 ITIKTIGRQWYWSYEYSDfvdvefdtymtpemdlevdgfrlLDVDNRTILPMNTEIRVLTSASDVLHSWAVPSLGIKIDA 146
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                          90       100
                  ....*....|....*....|....*..
gi 1511931889 147 TPGRLNQGTFTMNRPGLFFGQCSEICG 173
Cdd:cd13842    58 VPGYTSELWFVADKPGTYTIICAEYCG 84
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 67-173 5.49e-18

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 74.60  E-value: 5.49e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931889  67 ITIKTIGRQWYWSYEYSDFVDVEFDTYMTPEMDLEvdgfrlldvdnrtiLPMNTEIRVLTSASDVLHSWAVPSLGIKIDA 146
Cdd:cd13919     2 LVVEVTAQQWAWTFRYPGGDGKLGTDDDVTSPELH--------------LPVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                          90       100
                  ....*....|....*....|....*..
gi 1511931889 147 TPGRLNQGTFTMNRPGLFFGQCSEICG 173
Cdd:cd13919    68 VPGRTTRLWFTPTREGEYEVRCAELCG 94
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 67-173 5.10e-17

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 71.89  E-value: 5.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931889  67 ITIKTIGRQWYWSYEYsdfvdvefdtymtpemdleVDGFRlldVDNRTILPMNTEIRVLTSASDVLHSWAVPSLGIKIDA 146
Cdd:cd13915     2 LEIQVTGRQWMWEFTY-------------------PNGKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDV 59

                          90       100
                  ....*....|....*....|....*..
gi 1511931889 147 TPGRLNQGTFTMNRPGLFFGQCSEICG 173
Cdd:cd13915    60 VPGRYTYLWFEATKPGEYDLFCTEYCG 86
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 67-173 2.97e-12

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 59.73  E-value: 2.97e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931889  67 ITIKTIGRQWYWSYEYSDfvdvefdtymtpemdLEVDGFrlldvdNRTILPMNTEIRVLTSASDVLHSWAVPSLGIKIDA 146
Cdd:cd13914     1 VEIEVEAYQWGWEFSYPE---------------ANVTTS------EQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDA 59

                          90       100
                  ....*....|....*....|....*..
gi 1511931889 147 TPGRLNQGTFTMNRPGLFFGQCSEICG 173
Cdd:cd13914    60 FPGQYNTIKTEATEEGEYQLYCAEYCG 86
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 60-173 8.87e-11

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 56.69  E-value: 8.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931889  60 DDSIDSMITIKTIGRQWYWSYEYSDFVDvefdtymtpemdlEVDGFRLldvdnrtilPMNTEIRVLTSASDVLHSWAVPS 139
Cdd:cd13918    26 DEADEDALEVEVEGFQFGWQFEYPNGVT-------------TGNTLRV---------PADTPIALRVTSTDVFHTFGIPE 83

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1511931889 140 LGIKIDATPGRLNQGTFTMNRPGLFFGQCSEICG 173
Cdd:cd13918    84 LRVKADAIPGEYTSTWFEADEPGTYEAKCYELCG 117
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-49 3.78e-07

Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C oxidase contains two transmembrane alpha-helices.


Pssm-ID: 397083 [Multi-domain]  Cd Length: 89  Bit Score: 45.79  E-value: 3.78e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1511931889   1 TVLMLITIVVGYSLAYMLtINY-------SNRHVLHGHLIETIWTTLPAITLIFIA 49
Cdd:pfam02790  29 FILTLILILVLYILVTCL-IRFnrrknpiTARYTTHGQTIEIIWTIIPAVILILIA 83
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 116-173 5.25e-05

C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and some archaea, which catalyze the reduction of O2 and simultaneously pump protons across the membrane. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. The ba3 family contains oxidases that lack the conserved residues that form the D- and K-pathways in CcO and ubiquinol oxidase. Instead, they contain a potential alternative K-pathway. Additional proton channels have been proposed for this family of oxidases but none have been identified definitively.


Pssm-ID: 259980 [Multi-domain]  Cd Length: 99  Bit Score: 40.25  E-value: 5.25e-05
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gi 1511931889 116 LPMNTEIRVLTSASDVLHSWAVPSLGIKIDATPGRLNQGTFTMNRPGLFFGQCSEICG 173
Cdd:cd13913    29 VPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCG 86
 
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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