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Conserved domains on  [gi|1213499666|gb|ASG92044|]
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cytochrome oxidase subunit II, partial (mitochondrion) [Prosphena scudderi]

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
 1-162 2.62e-93

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 269.78  E-value: 2.62e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499666   1 IMITIIVGYNLSYIILIKFKARNMLHGHMIEMIWTLIPAITLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWSYEYS 80
Cdd:MTH00154   32 IMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499666  81 DFMNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLNLGTFSINRPGL 160
Cdd:MTH00154  112 DFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGL 191


                  ..
gi 1213499666 161 YF 162
Cdd:MTH00154  192 FF 193
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-162 2.62e-93

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 269.78  E-value: 2.62e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499666   1 IMITIIVGYNLSYIILIKFKARNMLHGHMIEMIWTLIPAITLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWSYEYS 80
Cdd:MTH00154   32 IMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499666  81 DFMNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLNLGTFSINRPGL 160
Cdd:MTH00154  112 DFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGL 191


                  ..
gi 1213499666 161 YF 162
Cdd:MTH00154  192 FF 193
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 64-162 3.17e-61

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: 185.08  E-value: 3.17e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499666  64 ITIKTIGRQWYWSYEYSDFMNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDA 143
Cdd:cd13912     3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                          90
                  ....*....|....*....
gi 1213499666 144 TPGRLNLGTFSINRPGLYF 162
Cdd:cd13912    83 VPGRLNQTSFFIERPGVYY 101
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
64-162 1.06e-56

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 173.36  E-value: 1.06e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499666  64 ITIKTIGRQWYWSYEYSDFMNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDA 143
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90
                  ....*....|....*....
gi 1213499666 144 TPGRLNLGTFSINRPGLYF 162
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFY 99
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
20-161 8.62e-27

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 100.29  E-value: 8.62e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499666  20 KARNMLHGHMIEMIWTLIPAITLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWSYEYsdfmnvefdtymlPEKElks 99
Cdd:COG1622    69 DPAQFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRY-------------PDQG--- 132

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1213499666 100 nnfrlLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLNLGTFSINRPGLY 161
Cdd:COG1622   133 -----IATVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTY 189
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 13-161 2.27e-23

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: 90.90  E-value: 2.27e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499666  13 YIILIKFKARN--------MLHGHM-IEMIWTLIPA-ITLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWSYEYSDF 82
Cdd:TIGR02866  30 LLAYVVWKFRRkgdeekpsQIHGNRrLEYVWTVIPLiIVVGLFAATAKGLLYLERPIPKDALKVKVTGYQWWWDFEYPES 109

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1213499666  83 mnvefdtymlpekelksnnfrLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLNLGTFSINRPGLY 161
Cdd:TIGR02866 110 ---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVY 167
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-162 2.62e-93

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 269.78  E-value: 2.62e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499666   1 IMITIIVGYNLSYIILIKFKARNMLHGHMIEMIWTLIPAITLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWSYEYS 80
Cdd:MTH00154   32 IMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499666  81 DFMNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLNLGTFSINRPGL 160
Cdd:MTH00154  112 DFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGL 191


                  ..
gi 1213499666 161 YF 162
Cdd:MTH00154  192 FF 193
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-162 4.75e-69

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 208.61  E-value: 4.75e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499666   1 IMITIIVGYNLSYIILIKFKARNMLHGHMIEMIWTLIPAITLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWSYEYS 80
Cdd:MTH00117   32 LLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPSLRILYLMDEINNPHLTIKAIGHQWYWSYEYT 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499666  81 DFMNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLNLGTFSINRPGL 160
Cdd:MTH00117  112 DYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVPSLGVKTDAVPGRLNQTSFITTRPGV 191


                  ..
gi 1213499666 161 YF 162
Cdd:MTH00117  192 FY 193
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-162 3.40e-67

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 203.80  E-value: 3.40e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499666   1 IMITIIVGYNLSYIILIKFKARNMLHGHMIEMIWTLIPAITLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWSYEYS 80
Cdd:MTH00139   32 IMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPSLRLLYLMDEVSDPYLTFKAVGHQWYWSYEYS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499666  81 DFMNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLNLGTFSINRPGL 160
Cdd:MTH00139  112 DFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSWTVPSLGVKIDAVPGRLNQVGFFINRPGV 191


                  ..
gi 1213499666 161 YF 162
Cdd:MTH00139  192 FY 193
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-162 5.05e-67

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 203.25  E-value: 5.05e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499666   1 IMITIIVGYNLSYIILIKFKARNMLHGHMIEMIWTLIPAITLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWSYEYS 80
Cdd:MTH00140   32 VLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPSLRLLYLLDETNNPLLTVKAIGHQWYWSYEYS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499666  81 DFMNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLNLGTFSINRPGL 160
Cdd:MTH00140  112 DFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGV 191


                  ..
gi 1213499666 161 YF 162
Cdd:MTH00140  192 FY 193
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-162 4.37e-65

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 198.54  E-value: 4.37e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499666   1 IMITIIVGYNLSYIILIKFKARNMLHGHMIEMIWTLIPAITLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWSYEYS 80
Cdd:MTH00008   32 TLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSLRLLYLMDEVSNPSITLKTIGHQWYWSYEYS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499666  81 DFMNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLNLGTFSINRPGL 160
Cdd:MTH00008  112 DFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPGRLNQIGFTITRPGV 191


                  ..
gi 1213499666 161 YF 162
Cdd:MTH00008  192 FY 193
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-162 3.92e-63

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 193.27  E-value: 3.92e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499666   1 IMITIIVGYNLSYIILIKFKARNMLHGHMIEMIWTLIPAITLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWSYEYS 80
Cdd:MTH00168   32 VLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPSLRLLYLMDEIDKPDLTIKAVGHQWYWSYEYT 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499666  81 DFMNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLNLGTFSINRPGL 160
Cdd:MTH00168  112 DYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSWTLPSLGLKMDAVPGRLNQLAFLSSRPGS 191


                  ..
gi 1213499666 161 YF 162
Cdd:MTH00168  192 FY 193
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-162 2.26e-62

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 191.45  E-value: 2.26e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499666   1 IMITIIVGYNLSYIILIKFKARNMLHGHMIEMIWTLIPAITLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWSYEYS 80
Cdd:MTH00038   32 TLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPSLQLLYLMDEVNNPFLTIKAIGHQWYWSYEYT 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499666  81 DFMNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLNLGTFSINRPGL 160
Cdd:MTH00038  112 DYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFISRTGL 191


                  ..
gi 1213499666 161 YF 162
Cdd:MTH00038  192 FY 193
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 64-162 3.17e-61

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: 185.08  E-value: 3.17e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499666  64 ITIKTIGRQWYWSYEYSDFMNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDA 143
Cdd:cd13912     3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                          90
                  ....*....|....*....
gi 1213499666 144 TPGRLNLGTFSINRPGLYF 162
Cdd:cd13912    83 VPGRLNQTSFFIERPGVYY 101
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 2-162 3.72e-59

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 183.55  E-value: 3.72e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499666   2 MITIIVGYNLSYIILIKFKARNMLHGHMIEMIWTLIPAITLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWSYEYSD 81
Cdd:MTH00185   33 LISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLRILYLMDEINDPHLTIKAMGHQWYWSYEYTD 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499666  82 FMNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLNLGTFSINRPGLY 161
Cdd:MTH00185  113 YEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVPALGVKMDAVPGRLNQATFIISRPGLY 192


                  .
gi 1213499666 162 F 162
Cdd:MTH00185  193 Y 193
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-162 1.39e-58

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 181.90  E-value: 1.39e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499666   1 IMITIIVGYNLSYIILIKFKARNMLHGHMIEMIWTLIPAITLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWSYEYS 80
Cdd:MTH00076   32 FLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRILYLMDEINDPHLTVKAIGHQWYWSYEYT 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499666  81 DFMNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLNLGTFSINRPGL 160
Cdd:MTH00076  112 DYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSLGIKTDAIPGRLNQTSFIASRPGV 191


                  ..
gi 1213499666 161 YF 162
Cdd:MTH00076  192 YY 193
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 2-162 6.84e-58

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 180.30  E-value: 6.84e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499666   2 MITIIVGYNLSYIILIKFKARNMLHGHMIEMIWTLIPAITLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWSYEYSD 81
Cdd:MTH00098   33 LISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRILYMMDEINNPSLTVKTMGHQWYWSYEYTD 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499666  82 FMNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLNLGTFSINRPGLY 161
Cdd:MTH00098  113 YEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLY 192


                  .
gi 1213499666 162 F 162
Cdd:MTH00098  193 Y 193
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-162 3.31e-57

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 178.37  E-value: 3.31e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499666   1 IMITIIVGYNLSYIIL----IKFKARNMLHGHMIEMIWTLIPAITLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWS 76
Cdd:MTH00129   28 LMIVFLISTLVLYIIVamvsTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRILYLMDEINDPHLTIKAMGHQWYWS 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499666  77 YEYSDFMNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLNLGTFSIN 156
Cdd:MTH00129  108 YEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVPALGVKMDAVPGRLNQTAFIAS 187


                  ....*.
gi 1213499666 157 RPGLYF 162
Cdd:MTH00129  188 RPGVFY 193
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 1-162 4.03e-57

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 178.79  E-value: 4.03e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499666   1 IMITIIVGYNLSYIILIKFKARNMLHGHMIEMIWTLIPAITLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWSYEYS 80
Cdd:MTH00023   41 IIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYLMDEVVSPALTIKAIGHQWYWSYEYS 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499666  81 DFM--NVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLNLGTFSINRP 158
Cdd:MTH00023  121 DYEgeTLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRP 200


                  ....
gi 1213499666 159 GLYF 162
Cdd:MTH00023  201 GVFY 204
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
64-162 1.06e-56

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 173.36  E-value: 1.06e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499666  64 ITIKTIGRQWYWSYEYSDFMNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDA 143
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90
                  ....*....|....*....
gi 1213499666 144 TPGRLNLGTFSINRPGLYF 162
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFY 99
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 1-162 7.83e-54

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 169.96  E-value: 7.83e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499666   1 IMITIIVGYNLSYIILIKFKARNMLHGHMIEMIWTLIPAITLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWSYEYS 80
Cdd:MTH00051   34 TIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYLMDEVIDPALTIKAIGHQWYWSYEYS 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499666  81 DF--MNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLNLGTFSINRP 158
Cdd:MTH00051  114 DYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRP 193


                  ....
gi 1213499666 159 GLYF 162
Cdd:MTH00051  194 GVFY 197
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 2-162 3.42e-44

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 146.32  E-value: 3.42e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499666   2 MITIIVGYNLSYIILIKFKAR------NMLHGHMIEMIWTLIPAITLIFIALPSLRLLYLLDDSN-ETMITIKTIGRQWY 74
Cdd:MTH00027   58 ILTIIVGVVLWLIIRILLGNNyysyywNKLDGSLIEVIWTLIPAFILILIAFPSLRLLYIMDECGfSANITIKVTGHQWY 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499666  75 WSYEYSDF--MNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLNLGT 152
Cdd:MTH00027  138 WSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVLHSWTVPSLAVKMDAVPGRINETG 217

                         170
                  ....*....|
gi 1213499666 153 FSINRPGLYF 162
Cdd:MTH00027  218 FLIKRPGIFY 227
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 2-162 2.36e-40

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 135.52  E-value: 2.36e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499666   2 MITIIVGYNLSYIILIKFKARNMLHGHMIEMIWTLIPAITLIFIALPSLRLLYLLDDSN-ETMITIKTIGRQWYWSYEYS 80
Cdd:MTH00080   35 VLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMNlDSNLTVKVTGHQWYWSYEFS 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499666  81 DFMNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLNLGTFSINRPGL 160
Cdd:MTH00080  115 DIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILSTLCYSFPMPGV 194


                  ..
gi 1213499666 161 YF 162
Cdd:MTH00080  195 FY 196
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
20-161 8.62e-27

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 100.29  E-value: 8.62e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499666  20 KARNMLHGHMIEMIWTLIPAITLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWSYEYsdfmnvefdtymlPEKElks 99
Cdd:COG1622    69 DPAQFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRY-------------PDQG--- 132

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1213499666 100 nnfrlLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLNLGTFSINRPGLY 161
Cdd:COG1622   133 -----IATVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTY 189
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 13-161 2.27e-23

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: 90.90  E-value: 2.27e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499666  13 YIILIKFKARN--------MLHGHM-IEMIWTLIPA-ITLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWSYEYSDF 82
Cdd:TIGR02866  30 LLAYVVWKFRRkgdeekpsQIHGNRrLEYVWTVIPLiIVVGLFAATAKGLLYLERPIPKDALKVKVTGYQWWWDFEYPES 109

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1213499666  83 mnvefdtymlpekelksnnfrLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLNLGTFSINRPGLY 161
Cdd:TIGR02866 110 ---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVY 167
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 30-161 1.08e-21

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 86.55  E-value: 1.08e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499666  30 IEMIWTLIPAItLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWSYEYSDfmNVEFDTYMlpekelksNNFRLLdVDN 109
Cdd:MTH00047   49 LELLWTVVPTL-LVLVLCFLNLNFITSDLDCFSSETIKVIGHQWYWSYEYSF--GGSYDSFM--------TDDIFG-VDK 116

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1213499666 110 RTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLNLGTFSINRPGLY 161
Cdd:MTH00047  117 PLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVF 168
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 87-162 2.09e-20

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 82.18  E-value: 2.09e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1213499666  87 FDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLN-LGTFsINRPGLYF 162
Cdd:PTZ00047   51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHkINTF-ILREGVFY 126
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 64-161 1.87e-16

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: 70.02  E-value: 1.87e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499666  64 ITIKTIGRQWYWSYEYSDfmnvefdtymlpekelksnnfrlLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDA 143
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                          90
                  ....*....|....*...
gi 1213499666 144 TPGRLNLGTFSINRPGLY 161
Cdd:cd13842    58 VPGYTSELWFVADKPGTY 75
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 64-161 5.31e-14

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: 63.80  E-value: 5.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499666  64 ITIKTIGRQWYWSYEYSdfmnvefdtymlpekelksNNFRlldVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDA 143
Cdd:cd13915     2 LEIQVTGRQWMWEFTYP-------------------NGKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDV 59

                          90
                  ....*....|....*...
gi 1213499666 144 TPGRLNLGTFSINRPGLY 161
Cdd:cd13915    60 VPGRYTYLWFEATKPGEY 77
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 64-161 7.52e-13

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: 61.12  E-value: 7.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499666  64 ITIKTIGRQWYWSYEYsdfmnvefdtymlPEKELKSNNFRLLDVdNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDA 143
Cdd:cd13919     2 LVVEVTAQQWAWTFRY-------------PGGDGKLGTDDDVTS-PELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                          90
                  ....*....|....*...
gi 1213499666 144 TPGRLNLGTFSINRPGLY 161
Cdd:cd13919    68 VPGRTTRLWFTPTREGEY 85
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 64-162 1.23e-12

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: 60.33  E-value: 1.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499666  64 ITIKTIGRQWYWSYEYSDFMNVEFDTymlpekelksnnfrlldvDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDA 143
Cdd:cd04213     2 LTIEVTGHQWWWEFRYPDEPGRGIVT------------------ANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDM 63

                          90
                  ....*....|....*....
gi 1213499666 144 TPGRLNLGTFSINRPGLYF 162
Cdd:cd04213    64 IPGRTNRLWLQADEPGVYR 82
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 64-161 2.29e-10

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: 54.72  E-value: 2.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499666  64 ITIKTIGRQWYWSYEYSDfmnvefdtymlpekelkSNNFRlldvDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDA 143
Cdd:cd13914     1 VEIEVEAYQWGWEFSYPE-----------------ANVTT----SEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDA 59

                          90
                  ....*....|....*...
gi 1213499666 144 TPGRLNLGTFSINRPGLY 161
Cdd:cd13914    60 FPGQYNTIKTEATEEGEY 77
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 57-161 1.45e-07

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: 47.84  E-value: 1.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499666  57 DDSNETMITIKTIGRQWYWSYEYSDfmNVEFDTYMlpekelksnnfrlldvdnrtVVPMNSEIRMLTSASDVLHSWTIPA 136
Cdd:cd13918    26 DEADEDALEVEVEGFQFGWQFEYPN--GVTTGNTL--------------------RVPADTPIALRVTSTDVFHTFGIPE 83

                          90       100
                  ....*....|....*....|....*
gi 1213499666 137 LGIKVDATPGRLNLGTFSINRPGLY 161
Cdd:cd13918    84 LRVKADAIPGEYTSTWFEADEPGTY 108
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-46 1.25e-06

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: 44.24  E-value: 1.25e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1213499666   1 IMITIIVGYNLSYIIL------IKFKARNMLHGHMIEMIWTLIPAITLIFIA 46
Cdd:pfam02790  32 TLILILVLYILVTCLIrfnrrkNPITARYTTHGQTIEIIWTIIPAVILILIA 83
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 109-161 6.18e-03

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: 34.47  E-value: 6.18e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1213499666 109 NRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLNLGTFSINRPGLY 161
Cdd:cd13913    25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEY 77
 
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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