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Conserved domains on  [gi|148728375|gb|ABR08662|]
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cytochrome oxidase subunit II, partial (mitochondrion) [Deracantha onos]

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
 1-182 6.69e-120

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 337.96  E-value: 6.69e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728375   1 MEQLIFFHDHTLFILLMITILVAYIMVSLLFNKFTHRYLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPLIT 80
Cdd:MTH00154  17 MEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSIT 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728375  81 IKTVGHQWYWSYEYTDFSTpYEFDSYMLPYNEMPTSGFRLLDVDNRTTLPVNTQIRMLVTAADVLHSWTIPAFGVKVDAT 160
Cdd:MTH00154  97 LKTIGHQWYWSYEYSDFKN-IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAV 175

                        170       180
                 ....*....|....*....|..
gi 148728375 161 PGRLNQTSFFMNRPGLFYGQCS 182
Cdd:MTH00154 176 PGRLNQLNFLINRPGLFFGQCS 197
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-182 6.69e-120

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 337.96  E-value: 6.69e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728375   1 MEQLIFFHDHTLFILLMITILVAYIMVSLLFNKFTHRYLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPLIT 80
Cdd:MTH00154  17 MEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSIT 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728375  81 IKTVGHQWYWSYEYTDFSTpYEFDSYMLPYNEMPTSGFRLLDVDNRTTLPVNTQIRMLVTAADVLHSWTIPAFGVKVDAT 160
Cdd:MTH00154  97 LKTIGHQWYWSYEYSDFKN-IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAV 175

                        170       180
                 ....*....|....*....|..
gi 148728375 161 PGRLNQTSFFMNRPGLFYGQCS 182
Cdd:MTH00154 176 PGRLNQLNFLINRPGLFFGQCS 197
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 77-182 6.74e-69

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: 205.50  E-value: 6.74e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728375  77 PLITIKTVGHQWYWSYEYTDFSTpYEFDSYMLPYNEMPTSGFRLLDVDNRTTLPVNTQIRMLVTAADVLHSWTIPAFGVK 156
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFND-LEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIK 79

                         90       100
                 ....*....|....*....|....*.
gi 148728375 157 VDATPGRLNQTSFFMNRPGLFYGQCS 182
Cdd:cd13912   80 VDAVPGRLNQTSFFIERPGVYYGQCS 105
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
79-182 1.29e-60

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 184.15  E-value: 1.29e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728375   79 ITIKTVGHQWYWSYEYTDFSTpYEFDSYMLPYNEMPTSGFRLLDVDNRTTLPVNTQIRMLVTAADVLHSWTIPAFGVKVD 158
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGD-LEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTD 79

                          90       100
                  ....*....|....*....|....
gi 148728375  159 ATPGRLNQTSFFMNRPGLFYGQCS 182
Cdd:pfam00116  80 AVPGRLNQTSFSIDREGVFYGQCS 103
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
10-182 1.15e-35

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 124.17  E-value: 1.15e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728375  10 HTLFILLMITILVAYIMVSLLF-----------NKFTHRYLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPL 78
Cdd:COG1622   33 DDLFWVSLIIMLVIFVLVFGLLlyfairyrrrkGDADPAQFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDP 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728375  79 ITIKTVGHQWYWSYEYTDFSTpyefdsymlpynemptsgfrllDVDNRTTLPVNTQIRMLVTAADVLHSWTIPAFGVKVD 158
Cdd:COG1622  113 LTVEVTGYQWKWLFRYPDQGI----------------------ATVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQD 170

                        170       180
                 ....*....|....*....|....
gi 148728375 159 ATPGRLNQTSFFMNRPGLFYGQCS 182
Cdd:COG1622  171 AIPGRVTELWFTADKPGTYRGQCA 194
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 1-181 7.60e-29

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


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 105.93  E-value: 7.60e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728375    1 MEQLIFFHDHTLFILLMITILVAYIMVSLLFnKFTHR-------YLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDE 73
Cdd:TIGR02866   6 AQQIAFLFLFVLAVSTLISLLVAALLAYVVW-KFRRKgdeekpsQIHGNRRLEYVWTVIPLIIVVGLFAATAKGLLYLER 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728375   74 SMDP-LITIKTVGHQWYWSYEYtdfstpyefdsymlpynemPTSGFRlldVDNRTTLPVNTQIRMLVTAADVLHSWTIPA 152
Cdd:TIGR02866  85 PIPKdALKVKVTGYQWWWDFEY-------------------PESGFT---TVNELVLPAGTPVELQVTSKDVIHSFWVPE 142

                         170       180
                  ....*....|....*....|....*....
gi 148728375  153 FGVKVDATPGRLNQTSFFMNRPGLFYGQC 181
Cdd:TIGR02866 143 LGGKIDAIPGQTNALWFNADEPGVYYGFC 171
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-182 6.69e-120

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 337.96  E-value: 6.69e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728375   1 MEQLIFFHDHTLFILLMITILVAYIMVSLLFNKFTHRYLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPLIT 80
Cdd:MTH00154  17 MEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSIT 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728375  81 IKTVGHQWYWSYEYTDFSTpYEFDSYMLPYNEMPTSGFRLLDVDNRTTLPVNTQIRMLVTAADVLHSWTIPAFGVKVDAT 160
Cdd:MTH00154  97 LKTIGHQWYWSYEYSDFKN-IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAV 175

                        170       180
                 ....*....|....*....|..
gi 148728375 161 PGRLNQTSFFMNRPGLFYGQCS 182
Cdd:MTH00154 176 PGRLNQLNFLINRPGLFFGQCS 197
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-182 1.81e-93

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 271.43  E-value: 1.81e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728375   1 MEQLIFFHDHTLFILLMITILVAYIMVSLLFNKFTHRYLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPLIT 80
Cdd:MTH00140  17 MEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPSLRLLYLLDETNNPLLT 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728375  81 IKTVGHQWYWSYEYTDFSTpYEFDSYMLPYNEMPTSGFRLLDVDNRTTLPVNTQIRMLVTAADVLHSWTIPAFGVKVDAT 160
Cdd:MTH00140  97 VKAIGHQWYWSYEYSDFSV-IEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVPSLGVKVDAI 175

                        170       180
                 ....*....|....*....|..
gi 148728375 161 PGRLNQTSFFMNRPGLFYGQCS 182
Cdd:MTH00140 176 PGRLNQLSFEPKRPGVFYGQCS 197
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-182 1.17e-92

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 269.28  E-value: 1.17e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728375   1 MEQLIFFHDHTLFILLMITILVAYIMVSLLFNKFTHRYLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPLIT 80
Cdd:MTH00139  17 MEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPSLRLLYLMDEVSDPYLT 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728375  81 IKTVGHQWYWSYEYTDFSTpYEFDSYMLPYNEMPTSGFRLLDVDNRTTLPVNTQIRMLVTAADVLHSWTIPAFGVKVDAT 160
Cdd:MTH00139  97 FKAVGHQWYWSYEYSDFKN-LSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSWTVPSLGVKIDAV 175

                        170       180
                 ....*....|....*....|..
gi 148728375 161 PGRLNQTSFFMNRPGLFYGQCS 182
Cdd:MTH00139 176 PGRLNQVGFFINRPGVFYGQCS 197
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-182 4.73e-89

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 259.85  E-value: 4.73e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728375   1 MEQLIFFHDHTLFILLMITILVAYIMVSLLFNKFTHRYLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPLIT 80
Cdd:MTH00117  17 MEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPSLRILYLMDEINNPHLT 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728375  81 IKTVGHQWYWSYEYTDFSTpYEFDSYMLPYNEMPTSGFRLLDVDNRTTLPVNTQIRMLVTAADVLHSWTIPAFGVKVDAT 160
Cdd:MTH00117  97 IKAIGHQWYWSYEYTDYKD-LSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVPSLGVKTDAV 175

                        170       180
                 ....*....|....*....|..
gi 148728375 161 PGRLNQTSFFMNRPGLFYGQCS 182
Cdd:MTH00117 176 PGRLNQTSFITTRPGVFYGQCS 197
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-182 1.69e-88

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 258.63  E-value: 1.69e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728375   1 MEQLIFFHDHTLFILLMITILVAYIMVSLLFNKFTHRYLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPLIT 80
Cdd:MTH00008  17 MLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSLRLLYLMDEVSNPSIT 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728375  81 IKTVGHQWYWSYEYTDFSTpYEFDSYMLPYNEMPTSGFRLLDVDNRTTLPVNTQIRMLVTAADVLHSWTIPAFGVKVDAT 160
Cdd:MTH00008  97 LKTIGHQWYWSYEYSDFSN-LEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDAV 175

                        170       180
                 ....*....|....*....|..
gi 148728375 161 PGRLNQTSFFMNRPGLFYGQCS 182
Cdd:MTH00008 176 PGRLNQIGFTITRPGVFYGQCS 197
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-182 1.24e-86

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 253.86  E-value: 1.24e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728375   1 MEQLIFFHDHTLFILLMITILVAYIMVSLLFNKFTHRYLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPLIT 80
Cdd:MTH00038  17 MEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPSLQLLYLMDEVNNPFLT 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728375  81 IKTVGHQWYWSYEYTDFSTpYEFDSYMLPYNEMPTSGFRLLDVDNRTTLPVNTQIRMLVTAADVLHSWTIPAFGVKVDAT 160
Cdd:MTH00038  97 IKAIGHQWYWSYEYTDYND-LEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLHSWAVPSLGVKMDAV 175

                        170       180
                 ....*....|....*....|..
gi 148728375 161 PGRLNQTSFFMNRPGLFYGQCS 182
Cdd:MTH00038 176 PGRLNQTTFFISRTGLFYGQCS 197
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-182 2.38e-84

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 247.97  E-value: 2.38e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728375   1 MEQLIFFHDHTLFILLMITILVAYIMVSLLFNKFTHRYLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPLIT 80
Cdd:MTH00168  17 MEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPSLRLLYLMDEIDKPDLT 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728375  81 IKTVGHQWYWSYEYTDFSTpYEFDSYMLPYNEMPTSGFRLLDVDNRTTLPVNTQIRMLVTAADVLHSWTIPAFGVKVDAT 160
Cdd:MTH00168  97 IKAVGHQWYWSYEYTDYND-LEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSWTLPSLGLKMDAV 175

                        170       180
                 ....*....|....*....|..
gi 148728375 161 PGRLNQTSFFMNRPGLFYGQCS 182
Cdd:MTH00168 176 PGRLNQLAFLSSRPGSFYGQCS 197
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 1-182 3.15e-84

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 248.13  E-value: 3.15e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728375   1 MEQLIFFHDHTLFILLMITILVAYIMVSLLFNKFTHRYLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPLIT 80
Cdd:MTH00023  26 MEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYLMDEVVSPALT 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728375  81 IKTVGHQWYWSYEYTDFSTP-YEFDSYMLPYNEMPTSGFRLLDVDNRTTLPVNTQIRMLVTAADVLHSWTIPAFGVKVDA 159
Cdd:MTH00023 106 IKAIGHQWYWSYEYSDYEGEtLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVPSLGLKIDA 185

                        170       180
                 ....*....|....*....|...
gi 148728375 160 TPGRLNQTSFFMNRPGLFYGQCS 182
Cdd:MTH00023 186 VPGRLNQTGFFIKRPGVFYGQCS 208
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 1-182 1.01e-80

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 239.30  E-value: 1.01e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728375   1 MEQLIFFHDHTLFILLMITILVAYIMVSLLFNKFTHRYLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPLIT 80
Cdd:MTH00051  19 MEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYLMDEVIDPALT 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728375  81 IKTVGHQWYWSYEYTDFSTP-YEFDSYMLPYNEMPTSGFRLLDVDNRTTLPVNTQIRMLVTAADVLHSWTIPAFGVKVDA 159
Cdd:MTH00051  99 IKAIGHQWYWSYEYSDYGTDtIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPSLSVKIDA 178

                        170       180
                 ....*....|....*....|...
gi 148728375 160 TPGRLNQTSFFMNRPGLFYGQCS 182
Cdd:MTH00051 179 VPGRLNQTSFFIKRPGVFYGQCS 201
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-182 5.20e-80

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 237.30  E-value: 5.20e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728375   1 MEQLIFFHDHTLFILLMITILVAYIMVSLLFNKFTHRYLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPLIT 80
Cdd:MTH00129  17 MEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRILYLMDEINDPHLT 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728375  81 IKTVGHQWYWSYEYTDFSTpYEFDSYMLPYNEMPTSGFRLLDVDNRTTLPVNTQIRMLVTAADVLHSWTIPAFGVKVDAT 160
Cdd:MTH00129  97 IKAMGHQWYWSYEYTDYED-LGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVPALGVKMDAV 175

                        170       180
                 ....*....|....*....|..
gi 148728375 161 PGRLNQTSFFMNRPGLFYGQCS 182
Cdd:MTH00129 176 PGRLNQTAFIASRPGVFYGQCS 197
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-182 1.81e-79

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 235.94  E-value: 1.81e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728375   1 MEQLIFFHDHTLFILLMITILVAYIMVSLLFNKFTHRYLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPLIT 80
Cdd:MTH00185  17 MEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLRILYLMDEINDPHLT 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728375  81 IKTVGHQWYWSYEYTDFSTpYEFDSYMLPYNEMPTSGFRLLDVDNRTTLPVNTQIRMLVTAADVLHSWTIPAFGVKVDAT 160
Cdd:MTH00185  97 IKAMGHQWYWSYEYTDYEQ-LEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVPALGVKMDAV 175

                        170       180
                 ....*....|....*....|..
gi 148728375 161 PGRLNQTSFFMNRPGLFYGQCS 182
Cdd:MTH00185 176 PGRLNQATFIISRPGLYYGQCS 197
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-182 1.07e-78

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 233.84  E-value: 1.07e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728375   1 MEQLIFFHDHTLFILLMITILVAYIMVSLLFNKFTHRYLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPLIT 80
Cdd:MTH00098  17 MEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRILYMMDEINNPSLT 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728375  81 IKTVGHQWYWSYEYTDFSTpYEFDSYMLPYNEMPTSGFRLLDVDNRTTLPVNTQIRMLVTAADVLHSWTIPAFGVKVDAT 160
Cdd:MTH00098  97 VKTMGHQWYWSYEYTDYED-LSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDAI 175

                        170       180
                 ....*....|....*....|..
gi 148728375 161 PGRLNQTSFFMNRPGLFYGQCS 182
Cdd:MTH00098 176 PGRLNQTTLMSTRPGLYYGQCS 197
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-182 2.59e-75

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 225.43  E-value: 2.59e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728375   1 MEQLIFFHDHTLFILLMITILVAYIMVSLLFNKFTHRYLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPLIT 80
Cdd:MTH00076  17 MEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRILYLMDEINDPHLT 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728375  81 IKTVGHQWYWSYEYTDFSTpYEFDSYMLPYNEMPTSGFRLLDVDNRTTLPVNTQIRMLVTAADVLHSWTIPAFGVKVDAT 160
Cdd:MTH00076  97 VKAIGHQWYWSYEYTDYED-LSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSLGIKTDAI 175

                        170       180
                 ....*....|....*....|..
gi 148728375 161 PGRLNQTSFFMNRPGLFYGQCS 182
Cdd:MTH00076 176 PGRLNQTSFIASRPGVYYGQCS 197
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 77-182 6.74e-69

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: 205.50  E-value: 6.74e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728375  77 PLITIKTVGHQWYWSYEYTDFSTpYEFDSYMLPYNEMPTSGFRLLDVDNRTTLPVNTQIRMLVTAADVLHSWTIPAFGVK 156
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFND-LEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIK 79

                         90       100
                 ....*....|....*....|....*.
gi 148728375 157 VDATPGRLNQTSFFMNRPGLFYGQCS 182
Cdd:cd13912   80 VDAVPGRLNQTSFFIERPGVYYGQCS 105
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
79-182 1.29e-60

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 184.15  E-value: 1.29e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728375   79 ITIKTVGHQWYWSYEYTDFSTpYEFDSYMLPYNEMPTSGFRLLDVDNRTTLPVNTQIRMLVTAADVLHSWTIPAFGVKVD 158
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGD-LEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTD 79

                          90       100
                  ....*....|....*....|....
gi 148728375  159 ATPGRLNQTSFFMNRPGLFYGQCS 182
Cdd:pfam00116  80 AVPGRLNQTSFSIDREGVFYGQCS 103
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 1-182 6.48e-58

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 182.15  E-value: 6.48e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728375   1 MEQLIFFHDHTLFILLMITILVAYIMVSLLFNKFTHRYL---LEGQTIEVIWTILPAITLIFIALPSLRLLYLLDES-MD 76
Cdd:MTH00027  45 MEEIIMLHDQILFILTIIVGVVLWLIIRILLGNNYYSYYwnkLDGSLIEVIWTLIPAFILILIAFPSLRLLYIMDECgFS 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728375  77 PLITIKTVGHQWYWSYEYTDFSTP-YEFDSYMLPYNEMPTSGFRLLDVDNRTTLPVNTQIRMLVTAADVLHSWTIPAFGV 155
Cdd:MTH00027 125 ANITIKVTGHQWYWSYSYEDYGEKnIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVLHSWTVPSLAV 204

                        170       180
                 ....*....|....*....|....*..
gi 148728375 156 KVDATPGRLNQTSFFMNRPGLFYGQCS 182
Cdd:MTH00027 205 KMDAVPGRINETGFLIKRPGIFYGQCS 231
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 7-182 2.01e-45

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 149.39  E-value: 2.01e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728375   7 FHDHTLFILLMITILVAYIMVSLLFNKFTHRYLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLD-ESMDPLITIKTVG 85
Cdd:MTH00080  25 FNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGlMNLDSNLTVKVTG 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728375  86 HQWYWSYEYTDFSTpYEFDSYMLPYNEMPTSGFRLLDVDNRTTLPVNTQIRMLVTAADVLHSWTIPAFGVKVDATPGRLN 165
Cdd:MTH00080 105 HQWYWSYEFSDIPG-LEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILS 183

                        170
                 ....*....|....*..
gi 148728375 166 QTSFFMNRPGLFYGQCS 182
Cdd:MTH00080 184 TLCYSFPMPGVFYGQCS 200
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
10-182 1.15e-35

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 124.17  E-value: 1.15e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728375  10 HTLFILLMITILVAYIMVSLLF-----------NKFTHRYLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPL 78
Cdd:COG1622   33 DDLFWVSLIIMLVIFVLVFGLLlyfairyrrrkGDADPAQFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDP 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728375  79 ITIKTVGHQWYWSYEYTDFSTpyefdsymlpynemptsgfrllDVDNRTTLPVNTQIRMLVTAADVLHSWTIPAFGVKVD 158
Cdd:COG1622  113 LTVEVTGYQWKWLFRYPDQGI----------------------ATVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQD 170

                        170       180
                 ....*....|....*....|....
gi 148728375 159 ATPGRLNQTSFFMNRPGLFYGQCS 182
Cdd:COG1622  171 AIPGRVTELWFTADKPGTYRGQCA 194
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 1-182 6.92e-31

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 110.81  E-value: 6.92e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728375   1 MEQLIFFHDHTLFILLMITILVAYIMVSLLFNKFTHRYLL----EGQTIEVIWTILPAItLIFIALPSLRLLYLLDESMD 76
Cdd:MTH00047   1 MNLSLLYYDIVCYILALCVFIPCWVYIMLCWQVVSGNGSVnfgsENQVLELLWTVVPTL-LVLVLCFLNLNFITSDLDCF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728375  77 PLITIKTVGHQWYWSYEYTDFStpyEFDSYMlpynemptSGFRLLdVDNRTTLPVNTQIRMLVTAADVLHSWTIPAFGVK 156
Cdd:MTH00047  80 SSETIKVIGHQWYWSYEYSFGG---SYDSFM--------TDDIFG-VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLK 147

                        170       180
                 ....*....|....*....|....*.
gi 148728375 157 VDATPGRLNQTSFFMNRPGLFYGQCS 182
Cdd:MTH00047 148 MDAIPGRINHLFFCPDRHGVFVGYCS 173
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 1-181 7.60e-29

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


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 105.93  E-value: 7.60e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728375    1 MEQLIFFHDHTLFILLMITILVAYIMVSLLFnKFTHR-------YLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDE 73
Cdd:TIGR02866   6 AQQIAFLFLFVLAVSTLISLLVAALLAYVVW-KFRRKgdeekpsQIHGNRRLEYVWTVIPLIIVVGLFAATAKGLLYLER 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728375   74 SMDP-LITIKTVGHQWYWSYEYtdfstpyefdsymlpynemPTSGFRlldVDNRTTLPVNTQIRMLVTAADVLHSWTIPA 152
Cdd:TIGR02866  85 PIPKdALKVKVTGYQWWWDFEY-------------------PESGFT---TVNELVLPAGTPVELQVTSKDVIHSFWVPE 142

                         170       180
                  ....*....|....*....|....*....
gi 148728375  153 FGVKVDATPGRLNQTSFFMNRPGLFYGQC 181
Cdd:TIGR02866 143 LGGKIDAIPGQTNALWFNADEPGVYYGFC 171
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 101-182 3.23e-28

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 102.98  E-value: 3.23e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728375 101 YEFDSYMLPYNEMPTSGFRLLDVDNRTTLPVNTQIRMLVTAADVLHSWTIPAFGVKVDATPGRLNQTSFFMNRPGLFYGQ 180
Cdd:PTZ00047  49 YSFQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQ 128


                 ..
gi 148728375 181 CS 182
Cdd:PTZ00047 129 CS 130
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-61 2.10e-19

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: 78.14  E-value: 2.10e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148728375    1 MEQLIFFHDHTLFILLMITILVAYIMVSLLF------NKFTHRYLLEGQTIEVIWTILPAITLIFIA 61
Cdd:pfam02790  17 MEGLLELHDYIMFILTLILILVLYILVTCLIrfnrrkNPITARYTTHGQTIEIIWTIIPAVILILIA 83
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 79-182 2.88e-19

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: 78.11  E-value: 2.88e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728375  79 ITIKTVGHQWYWSYEYTDFSTPyefdsymlpynemptsgfrlldvdNRTTLPVNTQIRMLVTAADVLHSWTIPAFGVKVD 158
Cdd:cd13842    1 LTVYVTGVQWSWTFIYPNVRTP------------------------NEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVD 56

                         90       100
                 ....*....|....*....|....
gi 148728375 159 ATPGRLNQTSFFMNRPGLFYGQCS 182
Cdd:cd13842   57 AVPGYTSELWFVADKPGTYTIICA 80
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 79-182 5.96e-16

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: 69.59  E-value: 5.96e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728375  79 ITIKTVGHQWYWSYEYtdfstpyefdsymlpynemPTSGFRLLDVDNRTT----LPVNTQIRMLVTAADVLHSWTIPAFG 154
Cdd:cd13919    2 LVVEVTAQQWAWTFRY-------------------PGGDGKLGTDDDVTSpelhLPVGRPVLFNLRSKDVIHSFWVPEFR 62

                         90       100
                 ....*....|....*....|....*...
gi 148728375 155 VKVDATPGRLNQTSFFMNRPGLFYGQCS 182
Cdd:cd13919   63 VKQDAVPGRTTRLWFTPTREGEYEVRCA 90
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 79-182 1.67e-15

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: 68.42  E-value: 1.67e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728375  79 ITIKTVGHQWYWSYEYtdfstpyefdsymlpynemPTSGFRLLDVDNRTTLPVNTQIRMLVTAADVLHSWTIPAFGVKVD 158
Cdd:cd04213    2 LTIEVTGHQWWWEFRY-------------------PDEPGRGIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMD 62

                         90       100
                 ....*....|....*....|....
gi 148728375 159 ATPGRLNQTSFFMNRPGLFYGQCS 182
Cdd:cd04213   63 MIPGRTNRLWLQADEPGVYRGQCA 86
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 79-182 1.14e-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: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 63.42  E-value: 1.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728375  79 ITIKTVGHQWYWSYEYTDfstpyefdsymlpynemptsGFRlldVDNRTTLPVNTQIRMLVTAADVLHSWTIPAFGVKVD 158
Cdd:cd13915    2 LEIQVTGRQWMWEFTYPN--------------------GKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQD 58

                         90       100
                 ....*....|....*....|....
gi 148728375 159 ATPGRLNQTSFFMNRPGLFYGQCS 182
Cdd:cd13915   59 VVPGRYTYLWFEATKPGEYDLFCT 82
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 76-181 3.78e-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: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 55.15  E-value: 3.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728375  76 DPLiTIKTVGHQWYWSYEYtdfSTPYEFDSYMLpynemptsgfrlldvdnrttLPVNTQIRMLVTAADVLHSWTIPAFGV 155
Cdd:cd13918   31 DAL-EVEVEGFQFGWQFEY---PNGVTTGNTLR--------------------VPADTPIALRVTSTDVFHTFGIPELRV 86

                         90       100
                 ....*....|....*....|....*.
gi 148728375 156 KVDATPGRLNQTSFFMNRPGLFYGQC 181
Cdd:cd13918   87 KADAIPGEYTSTWFEADEPGTYEAKC 112
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 79-182 9.98e-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: 53.57  E-value: 9.98e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728375  79 ITIKTVGHQWYWSYEYTDFStpyefdsymlpynemptsgfrlLDVDNRTTLPVNTQIRMLVTAADVLHSWTIPAFGVKVD 158
Cdd:cd13914    1 VEIEVEAYQWGWEFSYPEAN----------------------VTTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQD 58

                         90       100
                 ....*....|....*....|....
gi 148728375 159 ATPGRLNQTSFFMNRPGLFYGQCS 182
Cdd:cd13914   59 AFPGQYNTIKTEATEEGEYQLYCA 82
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 125-181 9.30e-06

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: 42.56  E-value: 9.30e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 148728375 125 NRTTLPVNTQIRMLVTAADVLHSWTIPAFGVKVDATPGRLNQTSFFMNRPGLFYGQC 181
Cdd:cd13913   25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIIC 81
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 125-180 8.42e-05

The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase in the respiratory chains of aerobic bacteria, is a multi-chain transmembrane protein located in the cell membrane. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits in ubiquinol oxidase varies from two to five. Although subunit II of ubiquinol oxidase lacks the binuclear CuA site found in cytochrome c oxidases, the structure is conserved.


Pssm-ID: 259874 [Multi-domain]  Cd Length: 99  Bit Score: 39.84  E-value: 8.42e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 148728375 125 NRTTLPVNTQIRMLVTAADVLHSWTIPAFGVKVDATPGRLNQTSFFMNRPGLFYGQ 180
Cdd:cd04212   25 NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGL 80
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 106-182 7.34e-04

Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in inter-molecular electron transfer reactions. Cupredoxins are blue copper proteins, having an intense blue color due to the presence of a mononuclear type 1 (T1) copper site. Structurally, the cupredoxin-like fold consists of a beta-sandwich with 7 strands in 2 beta-sheets, which is arranged in a Greek-key beta-barrel. Some of these proteins have lost the ability to bind copper. The majority of family members contain multiple cupredoxin domain repeats: ceruloplasmin and the coagulation factors V/VIII have six repeats; laccase, ascorbate oxidase, spore coat protein A, and multicopper oxidase CueO contain three repeats; and nitrite reductase has two repeats. Others are mono-domain cupredoxins, such as plastocyanin, pseudoazurin, plantacyanin, azurin, rusticyanin, stellacyanin, quinol oxidase, and the periplasmic domain of cytochrome c oxidase subunit II.


Pssm-ID: 259860 [Multi-domain]  Cd Length: 110  Bit Score: 37.60  E-value: 7.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728375 106 YMLPYNEMPTSGFRLLDVDNRTTLPVNTQIRM-LVTAADVLHSWTIPAFGVKVDA---------------TPGRLNQTSF 169
Cdd:cd00920    4 TASDWGWSFTYNGVLLFGPPVLVVPVGDTVRVqFVNKLGENHSVTIAGFGVPVVAmagganpglvntlviGPGESAEVTF 83

                         90
                 ....*....|...
gi 148728375 170 FMNRPGLFYGQCS 182
Cdd:cd00920   84 TTDQAGVYWFYCT 96
 
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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