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Conserved domains on  [gi|1933122355|gb|QPD01020|]
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cytochrome oxidase subunit II, partial (mitochondrion) [Orthochtha sp. Phlae_an8_1]

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
 1-169 6.46e-106

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 302.13  E-value: 6.46e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122355   1 FFHDHTMIVLLLITVIVGYSLSYMMVINYTNRNMLHGHMIETIWTALPAITLIFIALPSLRLLYLLDDSVDAMITIKTIG 80
Cdd:MTH00154   22 FFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIG 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122355  81 RQWYWSYEYSDFIDVEFDAYMTPEKELEQEGFRLLDVDNRTILPMNTEIRILTSASDVLHSWAVPALGIKIDATPGRLNQ 160
Cdd:MTH00154  102 HQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQ 181


                  ....*....
gi 1933122355 161 GTFTINRPG 169
Cdd:MTH00154  182 LNFLINRPG 190
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-169 6.46e-106

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 302.13  E-value: 6.46e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122355   1 FFHDHTMIVLLLITVIVGYSLSYMMVINYTNRNMLHGHMIETIWTALPAITLIFIALPSLRLLYLLDDSVDAMITIKTIG 80
Cdd:MTH00154   22 FFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIG 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122355  81 RQWYWSYEYSDFIDVEFDAYMTPEKELEQEGFRLLDVDNRTILPMNTEIRILTSASDVLHSWAVPALGIKIDATPGRLNQ 160
Cdd:MTH00154  102 HQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQ 181


                  ....*....
gi 1933122355 161 GTFTINRPG 169
Cdd:MTH00154  182 LNFLINRPG 190
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 74-169 8.43e-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: 184.31  E-value: 8.43e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122355  74 ITIKTIGRQWYWSYEYSDFIDVEFDAYMTPEKELEQEGFRLLDVDNRTILPMNTEIRILTSASDVLHSWAVPALGIKIDA 153
Cdd:cd13912     3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                          90
                  ....*....|....*.
gi 1933122355 154 TPGRLNQGTFTINRPG 169
Cdd:cd13912    83 VPGRLNQTSFFIERPG 98
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
74-169 4.60e-56

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 172.21  E-value: 4.60e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122355  74 ITIKTIGRQWYWSYEYSDFIDVEFDAYMTPEKELEQEGFRLLDVDNRTILPMNTEIRILTSASDVLHSWAVPALGIKIDA 153
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90
                  ....*....|....*.
gi 1933122355 154 TPGRLNQGTFTINRPG 169
Cdd:pfam00116  81 VPGRLNQTSFSIDREG 96
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
2-169 4.16e-28

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 104.14  E-value: 4.16e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122355   2 FHDHTMIVLLLITVIVGYSLSYMMV------INYTNRNMLHGHMIETIWTALPAITLIFIALPSLRLLYLLDDSVDAMIT 75
Cdd:COG1622    35 LFWVSLIIMLVIFVLVFGLLLYFAIryrrrkGDADPAQFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLT 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122355  76 IKTIGRQWYWSYEYsdfidvefdaymtpekeLEQEGfrllDVDNRTILPMNTEIRILTSASDVLHSWAVPALGIKIDATP 155
Cdd:COG1622   115 VEVTGYQWKWLFRY-----------------PDQGI----ATVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIP 173

                         170
                  ....*....|....
gi 1933122355 156 GRLNQGTFTINRPG 169
Cdd:COG1622   174 GRVTELWFTADKPG 187
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 36-169 1.08e-22

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: 89.36  E-value: 1.08e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122355  36 HGHMIETIWTALPAI--TLIFIALPSLRLLYLLDDSVDAMiTIKTIGRQWYWSYEYSDFidvefdaymtpekeleqeGFR 113
Cdd:TIGR02866  52 GNRRLEYVWTVIPLIivVGLFAATAKGLLYLERPIPKDAL-KVKVTGYQWWWDFEYPES------------------GFT 112

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1933122355 114 lldVDNRTILPMNTEIRILTSASDVLHSWAVPALGIKIDATPGRLNQGTFTINRPG 169
Cdd:TIGR02866 113 ---TVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPG 165
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-169 6.46e-106

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 302.13  E-value: 6.46e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122355   1 FFHDHTMIVLLLITVIVGYSLSYMMVINYTNRNMLHGHMIETIWTALPAITLIFIALPSLRLLYLLDDSVDAMITIKTIG 80
Cdd:MTH00154   22 FFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIG 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122355  81 RQWYWSYEYSDFIDVEFDAYMTPEKELEQEGFRLLDVDNRTILPMNTEIRILTSASDVLHSWAVPALGIKIDATPGRLNQ 160
Cdd:MTH00154  102 HQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQ 181


                  ....*....
gi 1933122355 161 GTFTINRPG 169
Cdd:MTH00154  182 LNFLINRPG 190
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-169 7.07e-78

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 230.96  E-value: 7.07e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122355   1 FFHDHTMIVLLLITVIVGYSLSYMMVINYTNRNMLHGHMIETIWTALPAITLIFIALPSLRLLYLLDDSVDAMITIKTIG 80
Cdd:MTH00117   22 FFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPSLRILYLMDEINNPHLTIKAIG 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122355  81 RQWYWSYEYSDFIDVEFDAYMTPEKELEQEGFRLLDVDNRTILPMNTEIRILTSASDVLHSWAVPALGIKIDATPGRLNQ 160
Cdd:MTH00117  102 HQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVPSLGVKTDAVPGRLNQ 181


                  ....*....
gi 1933122355 161 GTFTINRPG 169
Cdd:MTH00117  182 TSFITTRPG 190
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-169 5.06e-77

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 228.83  E-value: 5.06e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122355   1 FFHDHTMIVLLLITVIVGYSLSYMMVINYTNRNMLHGHMIETIWTALPAITLIFIALPSLRLLYLLDDSVDAMITIKTIG 80
Cdd:MTH00139   22 FFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPSLRLLYLMDEVSDPYLTFKAVG 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122355  81 RQWYWSYEYSDFIDVEFDAYMTPEKELEQEGFRLLDVDNRTILPMNTEIRILTSASDVLHSWAVPALGIKIDATPGRLNQ 160
Cdd:MTH00139  102 HQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSWTVPSLGVKIDAVPGRLNQ 181


                  ....*....
gi 1933122355 161 GTFTINRPG 169
Cdd:MTH00139  182 VGFFINRPG 190
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-169 4.33e-76

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 226.74  E-value: 4.33e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122355   1 FFHDHTMIVLLLITVIVGYSLSYMMVINYTNRNMLHGHMIETIWTALPAITLIFIALPSLRLLYLLDDSVDAMITIKTIG 80
Cdd:MTH00140   22 FFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPSLRLLYLLDETNNPLLTVKAIG 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122355  81 RQWYWSYEYSDFIDVEFDAYMTPEKELEQEGFRLLDVDNRTILPMNTEIRILTSASDVLHSWAVPALGIKIDATPGRLNQ 160
Cdd:MTH00140  102 HQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVPSLGVKVDAIPGRLNQ 181


                  ....*....
gi 1933122355 161 GTFTINRPG 169
Cdd:MTH00140  182 LSFEPKRPG 190
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 2-169 3.53e-74

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 222.04  E-value: 3.53e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122355   2 FHDHTMIVLLLITVIVGYSLSYMMVINYTNRNMLHGHMIETIWTALPAITLIFIALPSLRLLYLLDDSVDAMITIKTIGR 81
Cdd:MTH00008   23 FHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSLRLLYLMDEVSNPSITLKTIGH 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122355  82 QWYWSYEYSDFIDVEFDAYMTPEKELEQEGFRLLDVDNRTILPMNTEIRILTSASDVLHSWAVPALGIKIDATPGRLNQG 161
Cdd:MTH00008  103 QWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPGRLNQI 182


                  ....*...
gi 1933122355 162 TFTINRPG 169
Cdd:MTH00008  183 GFTITRPG 190
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-169 3.03e-73

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 219.57  E-value: 3.03e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122355   1 FFHDHTMIVLLLITVIVGYSLSYMMVINYTNRNMLHGHMIETIWTALPAITLIFIALPSLRLLYLLDDSVDAMITIKTIG 80
Cdd:MTH00038   22 YFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPSLQLLYLMDEVNNPFLTIKAIG 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122355  81 RQWYWSYEYSDFIDVEFDAYMTPEKELEQEGFRLLDVDNRTILPMNTEIRILTSASDVLHSWAVPALGIKIDATPGRLNQ 160
Cdd:MTH00038  102 HQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLHSWAVPSLGVKMDAVPGRLNQ 181


                  ....*....
gi 1933122355 161 GTFTINRPG 169
Cdd:MTH00038  182 TTFFISRTG 190
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-169 8.02e-73

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 218.31  E-value: 8.02e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122355   1 FFHDHTMIVLLLITVIVGYSLSYMMVINYTNRNMLHGHMIETIWTALPAITLIFIALPSLRLLYLLDDSVDAMITIKTIG 80
Cdd:MTH00168   22 LFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPSLRLLYLMDEIDKPDLTIKAVG 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122355  81 RQWYWSYEYSDFIDVEFDAYMTPEKELEQEGFRLLDVDNRTILPMNTEIRILTSASDVLHSWAVPALGIKIDATPGRLNQ 160
Cdd:MTH00168  102 HQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSWTLPSLGLKMDAVPGRLNQ 181


                  ....*....
gi 1933122355 161 GTFTINRPG 169
Cdd:MTH00168  182 LAFLSSRPG 190
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-169 2.47e-66

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 201.87  E-value: 2.47e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122355   1 FFHDHTMIVLLLITVIVGYSLSYMMVINYTNRNMLHGHMIETIWTALPAITLIFIALPSLRLLYLLDDSVDAMITIKTIG 80
Cdd:MTH00098   22 HFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRILYMMDEINNPSLTVKTMG 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122355  81 RQWYWSYEYSDFIDVEFDAYMTPEKELEQEGFRLLDVDNRTILPMNTEIRILTSASDVLHSWAVPALGIKIDATPGRLNQ 160
Cdd:MTH00098  102 HQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQ 181


                  ....*....
gi 1933122355 161 GTFTINRPG 169
Cdd:MTH00098  182 TTLMSTRPG 190
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 2-169 1.20e-65

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 200.01  E-value: 1.20e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122355   2 FHDHTMIVLLLITVIVGYSLSYMMVINYTNRNMLHGHMIETIWTALPAITLIFIALPSLRLLYLLDDSVDAMITIKTIGR 81
Cdd:MTH00076   23 FHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRILYLMDEINDPHLTVKAIGH 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122355  82 QWYWSYEYSDFIDVEFDAYMTPEKELEQEGFRLLDVDNRTILPMNTEIRILTSASDVLHSWAVPALGIKIDATPGRLNQG 161
Cdd:MTH00076  103 QWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSLGIKTDAIPGRLNQT 182


                  ....*...
gi 1933122355 162 TFTINRPG 169
Cdd:MTH00076  183 SFIASRPG 190
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 2-169 5.78e-65

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 198.57  E-value: 5.78e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122355   2 FHDHTMIVLLLITVIVGYSLSYMMVINYTNRNMLHGHMIETIWTALPAITLIFIALPSLRLLYLLDDSVDAMITIKTIGR 81
Cdd:MTH00185   23 FHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLRILYLMDEINDPHLTIKAMGH 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122355  82 QWYWSYEYSDFIDVEFDAYMTPEKELEQEGFRLLDVDNRTILPMNTEIRILTSASDVLHSWAVPALGIKIDATPGRLNQG 161
Cdd:MTH00185  103 QWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVPALGVKMDAVPGRLNQA 182


                  ....*...
gi 1933122355 162 TFTINRPG 169
Cdd:MTH00185  183 TFIISRPG 190
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 1-169 3.02e-63

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 194.58  E-value: 3.02e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122355   1 FFHDHTMIVLLLITVIVGYSLSYMMVINYTNRNMLHGHMIETIWTALPAITLIFIALPSLRLLYLLDDSVDAMITIKTIG 80
Cdd:MTH00023   31 FFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYLMDEVVSPALTIKAIG 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122355  81 RQWYWSYEYSDFID--VEFDAYMTPEKELEQEGFRLLDVDNRTILPMNTEIRILTSASDVLHSWAVPALGIKIDATPGRL 158
Cdd:MTH00023  111 HQWYWSYEYSDYEGetLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVPSLGLKIDAVPGRL 190

                         170
                  ....*....|.
gi 1933122355 159 NQGTFTINRPG 169
Cdd:MTH00023  191 NQTGFFIKRPG 201
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 2-169 3.98e-63

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 193.78  E-value: 3.98e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122355   2 FHDHTMIVLLLITVIVGYSLSYMMVINYTNRNMLHGHMIETIWTALPAITLIFIALPSLRLLYLLDDSVDAMITIKTIGR 81
Cdd:MTH00129   23 FHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRILYLMDEINDPHLTIKAMGH 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122355  82 QWYWSYEYSDFIDVEFDAYMTPEKELEQEGFRLLDVDNRTILPMNTEIRILTSASDVLHSWAVPALGIKIDATPGRLNQG 161
Cdd:MTH00129  103 QWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVPALGVKMDAVPGRLNQT 182


                  ....*...
gi 1933122355 162 TFTINRPG 169
Cdd:MTH00129  183 AFIASRPG 190
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 1-169 1.39e-61

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 189.99  E-value: 1.39e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122355   1 FFHDHTMIVLLLITVIVGYSLSYMMVINYTNRNMLHGHMIETIWTALPAITLIFIALPSLRLLYLLDDSVDAMITIKTIG 80
Cdd:MTH00051   24 FFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYLMDEVIDPALTIKAIG 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122355  81 RQWYWSYEYSDF--IDVEFDAYMTPEKELEQEGFRLLDVDNRTILPMNTEIRILTSASDVLHSWAVPALGIKIDATPGRL 158
Cdd:MTH00051  104 HQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPSLSVKIDAVPGRL 183

                         170
                  ....*....|.
gi 1933122355 159 NQGTFTINRPG 169
Cdd:MTH00051  184 NQTSFFIKRPG 194
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 74-169 8.43e-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: 184.31  E-value: 8.43e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122355  74 ITIKTIGRQWYWSYEYSDFIDVEFDAYMTPEKELEQEGFRLLDVDNRTILPMNTEIRILTSASDVLHSWAVPALGIKIDA 153
Cdd:cd13912     3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                          90
                  ....*....|....*.
gi 1933122355 154 TPGRLNQGTFTINRPG 169
Cdd:cd13912    83 VPGRLNQTSFFIERPG 98
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
74-169 4.60e-56

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 172.21  E-value: 4.60e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122355  74 ITIKTIGRQWYWSYEYSDFIDVEFDAYMTPEKELEQEGFRLLDVDNRTILPMNTEIRILTSASDVLHSWAVPALGIKIDA 153
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90
                  ....*....|....*.
gi 1933122355 154 TPGRLNQGTFTINRPG 169
Cdd:pfam00116  81 VPGRLNQTSFSIDREG 96
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 9-169 5.58e-44

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 145.94  E-value: 5.58e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122355   9 VLLLITVIVGYSLSYMMVINYTNR------NMLHGHMIETIWTALPAITLIFIALPSLRLLYLLDDSV-DAMITIKTIGR 81
Cdd:MTH00027   55 ILFILTIIVGVVLWLIIRILLGNNyysyywNKLDGSLIEVIWTLIPAFILILIAFPSLRLLYIMDECGfSANITIKVTGH 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122355  82 QWYWSYEYSDF--IDVEFDAYMTPEKELEQEGFRLLDVDNRTILPMNTEIRILTSASDVLHSWAVPALGIKIDATPGRLN 159
Cdd:MTH00027  135 QWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVLHSWTVPSLAVKMDAVPGRIN 214

                         170
                  ....*....|
gi 1933122355 160 QGTFTINRPG 169
Cdd:MTH00027  215 ETGFLIKRPG 224
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 1-169 1.96e-42

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 140.92  E-value: 1.96e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122355   1 FFHDHTMIVLLLITVIVGYSLSYMMVINYT---NRNMLHGHMIETIWTALPAITLIFIALPSLRLLYLLD-DSVDAMITI 76
Cdd:MTH00080   21 WFHNFNCSLLFGEFVLAFVVFLFLYLISNNfyfKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGlMNLDSNLTV 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122355  77 KTIGRQWYWSYEYSDFIDVEFDAYMTPEKELEQEGFRLLDVDNRTILPMNTEIRILTSASDVLHSWAVPALGIKIDATPG 156
Cdd:MTH00080  101 KVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSG 180

                         170
                  ....*....|...
gi 1933122355 157 RLNQGTFTINRPG 169
Cdd:MTH00080  181 ILSTLCYSFPMPG 193
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
2-169 4.16e-28

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 104.14  E-value: 4.16e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122355   2 FHDHTMIVLLLITVIVGYSLSYMMV------INYTNRNMLHGHMIETIWTALPAITLIFIALPSLRLLYLLDDSVDAMIT 75
Cdd:COG1622    35 LFWVSLIIMLVIFVLVFGLLLYFAIryrrrkGDADPAQFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLT 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122355  76 IKTIGRQWYWSYEYsdfidvefdaymtpekeLEQEGfrllDVDNRTILPMNTEIRILTSASDVLHSWAVPALGIKIDATP 155
Cdd:COG1622   115 VEVTGYQWKWLFRY-----------------PDQGI----ATVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIP 173

                         170
                  ....*....|....
gi 1933122355 156 GRLNQGTFTINRPG 169
Cdd:COG1622   174 GRVTELWFTADKPG 187
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 7-169 4.03e-24

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 93.10  E-value: 4.03e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122355   7 MIVLLLITVIVGYSL-SYMMVINYTNRNMLhghmIETIWTALPaiTLIFIALPSLRLLYLLDDSVDAMI-TIKTIGRQWY 84
Cdd:MTH00047   19 VFIPCWVYIMLCWQVvSGNGSVNFGSENQV----LELLWTVVP--TLLVLVLCFLNLNFITSDLDCFSSeTIKVIGHQWY 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122355  85 WSYEYSDfiDVEFDAYMTpekeleqeGFRLLdVDNRTILPMNTEIRILTSASDVLHSWAVPALGIKIDATPGRLNQGTFT 164
Cdd:MTH00047   93 WSYEYSF--GGSYDSFMT--------DDIFG-VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFC 161


                  ....*
gi 1933122355 165 INRPG 169
Cdd:MTH00047  162 PDRHG 166
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 36-169 1.08e-22

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: 89.36  E-value: 1.08e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122355  36 HGHMIETIWTALPAI--TLIFIALPSLRLLYLLDDSVDAMiTIKTIGRQWYWSYEYSDFidvefdaymtpekeleqeGFR 113
Cdd:TIGR02866  52 GNRRLEYVWTVIPLIivVGLFAATAKGLLYLERPIPKDAL-KVKVTGYQWWWDFEYPES------------------GFT 112

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1933122355 114 lldVDNRTILPMNTEIRILTSASDVLHSWAVPALGIKIDATPGRLNQGTFTINRPG 169
Cdd:TIGR02866 113 ---TVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPG 165
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 97-169 1.85e-19

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 79.86  E-value: 1.85e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1933122355  97 FDAYMTPEKELEQEGFRLLDVDNRTILPMNTEIRILTSASDVLHSWAVPALGIKIDATPGRLNQGTFTINRPG 169
Cdd:PTZ00047   51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREG 123
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 74-169 1.12e-15

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: 68.48  E-value: 1.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122355  74 ITIKTIGRQWYWSYEYSDfidvefdaymtpekeleqegfrlLDVDNRTILPMNTEIRILTSASDVLHSWAVPALGIKIDA 153
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                          90
                  ....*....|....*.
gi 1933122355 154 TPGRLNQGTFTINRPG 169
Cdd:cd13842    58 VPGYTSELWFVADKPG 73
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 74-169 9.48e-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: 63.42  E-value: 9.48e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122355  74 ITIKTIGRQWYWSYEYSDfidvefdaymtpekeleqeGFRlldVDNRTILPMNTEIRILTSASDVLHSWAVPALGIKIDA 153
Cdd:cd13915     2 LEIQVTGRQWMWEFTYPN-------------------GKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDV 59

                          90
                  ....*....|....*.
gi 1933122355 154 TPGRLNQGTFTINRPG 169
Cdd:cd13915    60 VPGRYTYLWFEATKPG 75
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 74-169 1.53e-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: 63.04  E-value: 1.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122355  74 ITIKTIGRQWYWSYEYsdfidvefdaymtpEKELEQEGFRLLDVDNRTILPMNTEIRILTSASDVLHSWAVPALGIKIDA 153
Cdd:cd13919     2 LVVEVTAQQWAWTFRY--------------PGGDGKLGTDDDVTSPELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                          90
                  ....*....|....*.
gi 1933122355 154 TPGRLNQGTFTINRPG 169
Cdd:cd13919    68 VPGRTTRLWFTPTREG 83
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-56 3.50e-12

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: 58.88  E-value: 3.50e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1933122355   1 FFHDHTMIVLLLITVIVGYSLsYMMVINY-------TNRNMLHGHMIETIWTALPAITLIFIA 56
Cdd:pfam02790  22 ELHDYIMFILTLILILVLYIL-VTCLIRFnrrknpiTARYTTHGQTIEIIWTIIPAVILILIA 83
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 74-169 5.52e-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: 58.79  E-value: 5.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122355  74 ITIKTIGRQWYWSYEYSDfidvefdaymtpekeLEQEGFRLLdvdNRTILPMNTEIRILTSASDVLHSWAVPALGIKIDA 153
Cdd:cd04213     2 LTIEVTGHQWWWEFRYPD---------------EPGRGIVTA---NELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDM 63

                          90
                  ....*....|....*.
gi 1933122355 154 TPGRLNQGTFTINRPG 169
Cdd:cd04213    64 IPGRTNRLWLQADEPG 79
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 74-159 4.64e-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: 53.95  E-value: 4.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122355  74 ITIKTIGRQWYWSYEYsdfidvefdaymtPEKELeqegfrllDVDNRTILPMNTEIRILTSASDVLHSWAVPALGIKIDA 153
Cdd:cd13914     1 VEIEVEAYQWGWEFSY-------------PEANV--------TTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDA 59


                  ....*.
gi 1933122355 154 TPGRLN 159
Cdd:cd13914    60 FPGQYN 65
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 67-169 1.29e-06

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: 45.52  E-value: 1.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122355  67 DDSVDAMITIKTIGRQWYWSYEYSDfiDVEFDAYMtpekeleqegfrlldvdnrtILPMNTEIRILTSASDVLHSWAVPA 146
Cdd:cd13918    26 DEADEDALEVEVEGFQFGWQFEYPN--GVTTGNTL--------------------RVPADTPIALRVTSTDVFHTFGIPE 83

                          90       100
                  ....*....|....*....|...
gi 1933122355 147 LGIKIDATPGRLNQGTFTINRPG 169
Cdd:cd13918    84 LRVKADAIPGEYTSTWFEADEPG 106
 
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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