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Conserved domains on  [gi|970839875|gb|ALU66371|]
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cytochrome c 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 970839875   1 IMITIIVGYNLSYIILIKFKARNMLHGHMIEMIWTLIPAITLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWSYEYS 80
Cdd:MTH00154  32 IMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839875  81 DFMNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLNLGTFSINRPGL 160
Cdd:MTH00154 112 DFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGL 191


                 ..
gi 970839875 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 970839875   1 IMITIIVGYNLSYIILIKFKARNMLHGHMIEMIWTLIPAITLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWSYEYS 80
Cdd:MTH00154  32 IMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839875  81 DFMNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLNLGTFSINRPGL 160
Cdd:MTH00154 112 DFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGL 191


                 ..
gi 970839875 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 970839875  64 ITIKTIGRQWYWSYEYSDFMNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDA 143
Cdd:cd13912    3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                         90
                 ....*....|....*....
gi 970839875 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 970839875   64 ITIKTIGRQWYWSYEYSDFMNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDA 143
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90
                  ....*....|....*....
gi 970839875  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 970839875  20 KARNMLHGHMIEMIWTLIPAITLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWSYEYsdfmnvefdtymlPEKElks 99
Cdd:COG1622   69 DPAQFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRY-------------PDQG--- 132

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 970839875 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 970839875   13 YIILIKFKARN--------MLHGHM-IEMIWTLIPA-ITLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWSYEYSDF 82
Cdd:TIGR02866  30 LLAYVVWKFRRkgdeekpsQIHGNRrLEYVWTVIPLiIVVGLFAATAKGLLYLERPIPKDALKVKVTGYQWWWDFEYPES 109

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 970839875   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 970839875   1 IMITIIVGYNLSYIILIKFKARNMLHGHMIEMIWTLIPAITLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWSYEYS 80
Cdd:MTH00154  32 IMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839875  81 DFMNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLNLGTFSINRPGL 160
Cdd:MTH00154 112 DFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGL 191


                 ..
gi 970839875 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 970839875   1 IMITIIVGYNLSYIILIKFKARNMLHGHMIEMIWTLIPAITLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWSYEYS 80
Cdd:MTH00117  32 LLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPSLRILYLMDEINNPHLTIKAIGHQWYWSYEYT 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839875  81 DFMNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLNLGTFSINRPGL 160
Cdd:MTH00117 112 DYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVPSLGVKTDAVPGRLNQTSFITTRPGV 191


                 ..
gi 970839875 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 970839875   1 IMITIIVGYNLSYIILIKFKARNMLHGHMIEMIWTLIPAITLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWSYEYS 80
Cdd:MTH00139  32 IMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPSLRLLYLMDEVSDPYLTFKAVGHQWYWSYEYS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839875  81 DFMNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLNLGTFSINRPGL 160
Cdd:MTH00139 112 DFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSWTVPSLGVKIDAVPGRLNQVGFFINRPGV 191


                 ..
gi 970839875 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 970839875   1 IMITIIVGYNLSYIILIKFKARNMLHGHMIEMIWTLIPAITLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWSYEYS 80
Cdd:MTH00140  32 VLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPSLRLLYLLDETNNPLLTVKAIGHQWYWSYEYS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839875  81 DFMNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLNLGTFSINRPGL 160
Cdd:MTH00140 112 DFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGV 191


                 ..
gi 970839875 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 970839875   1 IMITIIVGYNLSYIILIKFKARNMLHGHMIEMIWTLIPAITLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWSYEYS 80
Cdd:MTH00008  32 TLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSLRLLYLMDEVSNPSITLKTIGHQWYWSYEYS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839875  81 DFMNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLNLGTFSINRPGL 160
Cdd:MTH00008 112 DFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPGRLNQIGFTITRPGV 191


                 ..
gi 970839875 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 970839875   1 IMITIIVGYNLSYIILIKFKARNMLHGHMIEMIWTLIPAITLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWSYEYS 80
Cdd:MTH00168  32 VLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPSLRLLYLMDEIDKPDLTIKAVGHQWYWSYEYT 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839875  81 DFMNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLNLGTFSINRPGL 160
Cdd:MTH00168 112 DYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSWTLPSLGLKMDAVPGRLNQLAFLSSRPGS 191


                 ..
gi 970839875 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 970839875   1 IMITIIVGYNLSYIILIKFKARNMLHGHMIEMIWTLIPAITLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWSYEYS 80
Cdd:MTH00038  32 TLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPSLQLLYLMDEVNNPFLTIKAIGHQWYWSYEYT 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839875  81 DFMNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLNLGTFSINRPGL 160
Cdd:MTH00038 112 DYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFISRTGL 191


                 ..
gi 970839875 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 970839875  64 ITIKTIGRQWYWSYEYSDFMNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDA 143
Cdd:cd13912    3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                         90
                 ....*....|....*....
gi 970839875 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 970839875   2 MITIIVGYNLSYIILIKFKARNMLHGHMIEMIWTLIPAITLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWSYEYSD 81
Cdd:MTH00185  33 LISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLRILYLMDEINDPHLTIKAMGHQWYWSYEYTD 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839875  82 FMNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLNLGTFSINRPGLY 161
Cdd:MTH00185 113 YEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVPALGVKMDAVPGRLNQATFIISRPGLY 192


                 .
gi 970839875 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 970839875   1 IMITIIVGYNLSYIILIKFKARNMLHGHMIEMIWTLIPAITLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWSYEYS 80
Cdd:MTH00076  32 FLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRILYLMDEINDPHLTVKAIGHQWYWSYEYT 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839875  81 DFMNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLNLGTFSINRPGL 160
Cdd:MTH00076 112 DYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSLGIKTDAIPGRLNQTSFIASRPGV 191


                 ..
gi 970839875 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 970839875   2 MITIIVGYNLSYIILIKFKARNMLHGHMIEMIWTLIPAITLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWSYEYSD 81
Cdd:MTH00098  33 LISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRILYMMDEINNPSLTVKTMGHQWYWSYEYTD 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839875  82 FMNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLNLGTFSINRPGLY 161
Cdd:MTH00098 113 YEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLY 192


                 .
gi 970839875 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 970839875   1 IMITIIVGYNLSYIIL----IKFKARNMLHGHMIEMIWTLIPAITLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWS 76
Cdd:MTH00129  28 LMIVFLISTLVLYIIVamvsTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRILYLMDEINDPHLTIKAMGHQWYWS 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839875  77 YEYSDFMNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLNLGTFSIN 156
Cdd:MTH00129 108 YEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVPALGVKMDAVPGRLNQTAFIAS 187


                 ....*.
gi 970839875 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 970839875   1 IMITIIVGYNLSYIILIKFKARNMLHGHMIEMIWTLIPAITLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWSYEYS 80
Cdd:MTH00023  41 IIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYLMDEVVSPALTIKAIGHQWYWSYEYS 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839875  81 DFM--NVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLNLGTFSINRP 158
Cdd:MTH00023 121 DYEgeTLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRP 200


                 ....
gi 970839875 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 970839875   64 ITIKTIGRQWYWSYEYSDFMNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDA 143
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90
                  ....*....|....*....
gi 970839875  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 970839875   1 IMITIIVGYNLSYIILIKFKARNMLHGHMIEMIWTLIPAITLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWSYEYS 80
Cdd:MTH00051  34 TIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYLMDEVIDPALTIKAIGHQWYWSYEYS 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839875  81 DF--MNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLNLGTFSINRP 158
Cdd:MTH00051 114 DYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRP 193


                 ....
gi 970839875 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 970839875   2 MITIIVGYNLSYIILIKFKAR------NMLHGHMIEMIWTLIPAITLIFIALPSLRLLYLLDDSN-ETMITIKTIGRQWY 74
Cdd:MTH00027  58 ILTIIVGVVLWLIIRILLGNNyysyywNKLDGSLIEVIWTLIPAFILILIAFPSLRLLYIMDECGfSANITIKVTGHQWY 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839875  75 WSYEYSDF--MNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLNLGT 152
Cdd:MTH00027 138 WSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVLHSWTVPSLAVKMDAVPGRINETG 217

                        170
                 ....*....|
gi 970839875 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 970839875   2 MITIIVGYNLSYIILIKFKARNMLHGHMIEMIWTLIPAITLIFIALPSLRLLYLLDDSN-ETMITIKTIGRQWYWSYEYS 80
Cdd:MTH00080  35 VLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMNlDSNLTVKVTGHQWYWSYEFS 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839875  81 DFMNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLNLGTFSINRPGL 160
Cdd:MTH00080 115 DIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILSTLCYSFPMPGV 194


                 ..
gi 970839875 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 970839875  20 KARNMLHGHMIEMIWTLIPAITLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWSYEYsdfmnvefdtymlPEKElks 99
Cdd:COG1622   69 DPAQFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRY-------------PDQG--- 132

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 970839875 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 970839875   13 YIILIKFKARN--------MLHGHM-IEMIWTLIPA-ITLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWSYEYSDF 82
Cdd:TIGR02866  30 LLAYVVWKFRRkgdeekpsQIHGNRrLEYVWTVIPLiIVVGLFAATAKGLLYLERPIPKDALKVKVTGYQWWWDFEYPES 109

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 970839875   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 970839875  30 IEMIWTLIPAItLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWSYEYSDfmNVEFDTYMlpekelksNNFRLLdVDN 109
Cdd:MTH00047  49 LELLWTVVPTL-LVLVLCFLNLNFITSDLDCFSSETIKVIGHQWYWSYEYSF--GGSYDSFM--------TDDIFG-VDK 116

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 970839875 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 970839875  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 970839875  64 ITIKTIGRQWYWSYEYSDfmnvefdtymlpekelksnnfrlLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDA 143
Cdd:cd13842    1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                         90
                 ....*....|....*...
gi 970839875 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 970839875  64 ITIKTIGRQWYWSYEYSdfmnvefdtymlpekelksNNFRlldVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDA 143
Cdd:cd13915    2 LEIQVTGRQWMWEFTYP-------------------NGKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDV 59

                         90
                 ....*....|....*...
gi 970839875 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 970839875  64 ITIKTIGRQWYWSYEYsdfmnvefdtymlPEKELKSNNFRLLDVdNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDA 143
Cdd:cd13919    2 LVVEVTAQQWAWTFRY-------------PGGDGKLGTDDDVTS-PELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                         90
                 ....*....|....*...
gi 970839875 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 970839875  64 ITIKTIGRQWYWSYEYSDFMNVEFDTymlpekelksnnfrlldvDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDA 143
Cdd:cd04213    2 LTIEVTGHQWWWEFRYPDEPGRGIVT------------------ANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDM 63

                         90
                 ....*....|....*....
gi 970839875 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 970839875  64 ITIKTIGRQWYWSYEYSDfmnvefdtymlpekelkSNNFRlldvDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDA 143
Cdd:cd13914    1 VEIEVEAYQWGWEFSYPE-----------------ANVTT----SEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDA 59

                         90
                 ....*....|....*...
gi 970839875 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 970839875  57 DDSNETMITIKTIGRQWYWSYEYSDfmNVEFDTYMlpekelksnnfrlldvdnrtVVPMNSEIRMLTSASDVLHSWTIPA 136
Cdd:cd13918   26 DEADEDALEVEVEGFQFGWQFEYPN--GVTTGNTL--------------------RVPADTPIALRVTSTDVFHTFGIPE 83

                         90       100
                 ....*....|....*....|....*
gi 970839875 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 970839875    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 970839875 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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