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Conserved domains on  [gi|501416463|gb|AGL93566|]
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cytochrome oxidase subunit II, partial (mitochondrion) [Scaptomyza dentata]

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
 1-224 2.34e-160

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 442.35  E-value: 2.34e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463   1 STWANLGLQDSASPLMEQLTFFHDHALMILVMITVLVGYLMFMLFFNSYINRFLLHGQLIEVIWTILPAIILLFIALPSL 80
Cdd:MTH00154   2 ATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463  81 RLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNVEFDSYMIPTNELTNDGFRLLDVDNRIVLPMNSQIRILVTAADVIH 160
Cdd:MTH00154  82 RLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIH 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501416463 161 SWTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKWISN 224
Cdd:MTH00154 162 SWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKN 225
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-224 2.34e-160

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 442.35  E-value: 2.34e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463   1 STWANLGLQDSASPLMEQLTFFHDHALMILVMITVLVGYLMFMLFFNSYINRFLLHGQLIEVIWTILPAIILLFIALPSL 80
Cdd:MTH00154   2 ATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463  81 RLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNVEFDSYMIPTNELTNDGFRLLDVDNRIVLPMNSQIRILVTAADVIH 160
Cdd:MTH00154  82 RLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIH 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501416463 161 SWTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKWISN 224
Cdd:MTH00154 162 SWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKN 225
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 92-221 1.54e-94

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: 272.14  E-value: 1.54e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463  92 PSVTLKSIGHQWYWSYEYSDFNNVEFDSYMIPTNELTNDGFRLLDVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVKV 171
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 501416463 172 DGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKW 221
Cdd:cd13912   81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-213 6.70e-81

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 237.31  E-value: 6.70e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463   95 TLKSIGHQWYWSYEYSDFNNVEFDSYMIPTNELTNDGFRLLDVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDGT 174
Cdd:pfam00116   2 TIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDAV 81

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 501416463  175 PGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESV 213
Cdd:pfam00116  82 PGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
5-224 6.77e-52

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 167.31  E-value: 6.77e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463   5 NLGLQDSASPLMEQLTFFHDHALMILVMITVLVgylMFMLFFNSYINR---------FLLHGQLIEVIWTILPAIILLFI 75
Cdd:COG1622   18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLV---FGLLLYFAIRYRrrkgdadpaQFHHNTKLEIVWTVIPIIIVIVL 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463  76 ALPSLRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNVefdsymiptneltndgfrlldVDNRIVLPMNSQIRILVTA 155
Cdd:COG1622   95 AVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVNELVLPVGRPVRFLLTS 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501416463 156 ADVIHSWTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKWISN 224
Cdd:COG1622  154 ADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAE 222
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-223 4.23e-41

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: 138.67  E-value: 4.23e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463   12 ASPLMEQLTFFHDH--ALMILVMITVLVGYLMFMLFFNSY----INRFLLHGQLIEVIWTILPAIILL-FIALPSLRLLY 84
Cdd:TIGR02866   2 GGEIAQQIAFLFLFvlAVSTLISLLVAALLAYVVWKFRRKgdeeKPSQIHGNRRLEYVWTVIPLIIVVgLFAATAKGLLY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463   85 LLDEINEPSVTLKSIGHQWYWSYEYSdfnnvefdsymiptneltNDGFRlldVDNRIVLPMNSQIRILVTAADVIHSWTI 164
Cdd:TIGR02866  82 LERPIPKDALKVKVTGYQWWWDFEYP------------------ESGFT---TVNELVLPAGTPVELQVTSKDVIHSFWV 140

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 501416463  165 PALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKWIS 223
Cdd:TIGR02866 141 PELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-224 2.34e-160

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 442.35  E-value: 2.34e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463   1 STWANLGLQDSASPLMEQLTFFHDHALMILVMITVLVGYLMFMLFFNSYINRFLLHGQLIEVIWTILPAIILLFIALPSL 80
Cdd:MTH00154   2 ATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463  81 RLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNVEFDSYMIPTNELTNDGFRLLDVDNRIVLPMNSQIRILVTAADVIH 160
Cdd:MTH00154  82 RLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIH 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501416463 161 SWTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKWISN 224
Cdd:MTH00154 162 SWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKN 225
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-224 2.20e-128

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 361.56  E-value: 2.20e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463   1 STWANLGLQDSASPLMEQLTFFHDHALMILVMITVLVGYLMFMLFFNSYINRFLLHGQLIEVIWTILPAIILLFIALPSL 80
Cdd:MTH00140   2 SYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPSL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463  81 RLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNVEFDSYMIPTNELTNDGFRLLDVDNRIVLPMNSQIRILVTAADVIH 160
Cdd:MTH00140  82 RLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIH 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501416463 161 SWTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKWISN 224
Cdd:MTH00140 162 SWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLEL 225
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-224 5.79e-128

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 360.19  E-value: 5.79e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463   1 STWANLGLQDSASPLMEQLTFFHDHALMILVMITVLVGYLMFMLFFNSYINRFLLHGQLIEVIWTILPAIILLFIALPSL 80
Cdd:MTH00139   2 AYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPSL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463  81 RLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNVEFDSYMIPTNELTNDGFRLLDVDNRIVLPMNSQIRILVTAADVIH 160
Cdd:MTH00139  82 RLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLH 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501416463 161 SWTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKWISN 224
Cdd:MTH00139 162 SWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILE 225
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 4-224 1.10e-124

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 351.91  E-value: 1.10e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463   4 ANLGLQDSASPLMEQLTFFHDHALMILVMITVLVGY-LMFMLFFNSYINRfLLHGQLIEVIWTILPAIILLFIALPSLRL 82
Cdd:MTH00117   5 SQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYlLTLMLTTKLTHTN-TVDAQEVELIWTILPAIVLILLALPSLRI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463  83 LYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNVEFDSYMIPTNELTNDGFRLLDVDNRIVLPMNSQIRILVTAADVIHSW 162
Cdd:MTH00117  84 LYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSW 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501416463 163 TIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKWISN 224
Cdd:MTH00117 164 AVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSL 225
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-224 1.08e-121

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 344.27  E-value: 1.08e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463   1 STWANLGLQDSASPLMEQLTFFHDHALMILVMITVLVGYLMFMLFFNSYINRFLLHGQLIEVIWTILPAIILLFIALPSL 80
Cdd:MTH00168   2 ATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPSL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463  81 RLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNVEFDSYMIPTNELTNDGFRLLDVDNRIVLPMNSQIRILVTAADVIH 160
Cdd:MTH00168  82 RLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLH 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501416463 161 SWTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKWISN 224
Cdd:MTH00168 162 SWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVDS 225
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-224 3.13e-121

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 343.38  E-value: 3.13e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463   1 STWANLGLQDSASPLMEQLTFFHDHALMILVMITVLVGYLMFMLFFNSYINRFLLHGQLIEVIWTILPAIILLFIALPSL 80
Cdd:MTH00008   2 PHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463  81 RLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNVEFDSYMIPTNELTNDGFRLLDVDNRIVLPMNSQIRILVTAADVIH 160
Cdd:MTH00008  82 RLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIH 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501416463 161 SWTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKWISN 224
Cdd:MTH00008 162 SWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSS 225
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-224 3.38e-121

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 343.22  E-value: 3.38e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463   1 STWANLGLQDSASPLMEQLTFFHDHALMILVMITVLVGYLMFMLFFNSYINRFLLHGQLIEVIWTILPAIILLFIALPSL 80
Cdd:MTH00038   2 ATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPSL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463  81 RLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNVEFDSYMIPTNELTNDGFRLLDVDNRIVLPMNSQIRILVTAADVIH 160
Cdd:MTH00038  82 QLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLH 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501416463 161 SWTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKWISN 224
Cdd:MTH00038 162 SWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSN 225
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 4-223 5.69e-112

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 320.12  E-value: 5.69e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463   4 ANLGLQDSASPLMEQLTFFHDHALMILVMITVLVGYLMFMLFFNSYINRFLLHGQLIEVIWTILPAIILLFIALPSLRLL 83
Cdd:MTH00129   5 SQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRIL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463  84 YLLDEINEPSVTLKSIGHQWYWSYEYSDFNNVEFDSYMIPTNELTNDGFRLLDVDNRIVLPMNSQIRILVTAADVIHSWT 163
Cdd:MTH00129  85 YLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWA 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463 164 IPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKWIS 223
Cdd:MTH00129 165 VPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSS 224
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 4-223 4.45e-110

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 315.29  E-value: 4.45e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463   4 ANLGLQDSASPLMEQLTFFHDHALMILVMITVLVGYLMFMLFFNSYINRFLLHGQLIEVIWTILPAIILLFIALPSLRLL 83
Cdd:MTH00185   5 SQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLRIL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463  84 YLLDEINEPSVTLKSIGHQWYWSYEYSDFNNVEFDSYMIPTNELTNDGFRLLDVDNRIVLPMNSQIRILVTAADVIHSWT 163
Cdd:MTH00185  85 YLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWT 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463 164 IPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKWIS 223
Cdd:MTH00185 165 VPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSS 224
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 6-223 3.03e-109

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 312.81  E-value: 3.03e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463   6 LGLQDSASPLMEQLTFFHDHALMILVMITVLVGYLMFMLFFNSYINRFLLHGQLIEVIWTILPAIILLFIALPSLRLLYL 85
Cdd:MTH00098   7 LGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRILYM 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463  86 LDEINEPSVTLKSIGHQWYWSYEYSDFNNVEFDSYMIPTNELTNDGFRLLDVDNRIVLPMNSQIRILVTAADVIHSWTIP 165
Cdd:MTH00098  87 MDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVP 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 501416463 166 ALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKWIS 223
Cdd:MTH00098 167 SLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSA 224
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 6-224 5.04e-108

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 310.53  E-value: 5.04e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463   6 LGLQDSASPLMEQLTFFHDHALMILVMITVLVGYLMFMLFFNSYINRFLLHGQLIEVIWTILPAIILLFIALPSLRLLYL 85
Cdd:MTH00023  16 LGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463  86 LDEINEPSVTLKSIGHQWYWSYEYSDFN--NVEFDSYMIPTNELTNDGFRLLDVDNRIVLPMNSQIRILVTAADVIHSWT 163
Cdd:MTH00023  96 MDEVVSPALTIKAIGHQWYWSYEYSDYEgeTLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFA 175

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501416463 164 IPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKWISN 224
Cdd:MTH00023 176 VPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLS 236
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 6-224 1.65e-106

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 305.94  E-value: 1.65e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463   6 LGLQDSASPLMEQLTFFHDHALMILVMITVLVGYLMFMLFFNSYINRFLLHGQLIEVIWTILPAIILLFIALPSLRLLYL 85
Cdd:MTH00076   7 LGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRILYL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463  86 LDEINEPSVTLKSIGHQWYWSYEYSDFNNVEFDSYMIPTNELTNDGFRLLDVDNRIVLPMNSQIRILVTAADVIHSWTIP 165
Cdd:MTH00076  87 MDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVP 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 501416463 166 ALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKWISN 224
Cdd:MTH00076 167 SLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSS 225
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 6-224 3.84e-102

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 295.15  E-value: 3.84e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463   6 LGLQDSASPLMEQLTFFHDHALMILVMITVLVGYLMFMLFFNSYINRFLLHGQLIEVIWTILPAIILLFIALPSLRLLYL 85
Cdd:MTH00051   9 LGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463  86 LDEINEPSVTLKSIGHQWYWSYEYSDF--NNVEFDSYMIPTNELTNDGFRLLDVDNRIVLPMNSQIRILVTAADVIHSWT 163
Cdd:MTH00051  89 MDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFA 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501416463 164 IPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKWISN 224
Cdd:MTH00051 169 VPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVAT 229
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 92-221 1.54e-94

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: 272.14  E-value: 1.54e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463  92 PSVTLKSIGHQWYWSYEYSDFNNVEFDSYMIPTNELTNDGFRLLDVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVKV 171
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 501416463 172 DGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKW 221
Cdd:cd13912   81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-213 6.70e-81

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 237.31  E-value: 6.70e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463   95 TLKSIGHQWYWSYEYSDFNNVEFDSYMIPTNELTNDGFRLLDVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDGT 174
Cdd:pfam00116   2 TIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDAV 81

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 501416463  175 PGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESV 213
Cdd:pfam00116  82 PGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 6-222 1.29e-77

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 234.15  E-value: 1.29e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463   6 LGLQDSASPLMEQLTFFHDHALMILVMITVLVGYLMF-MLFFNSYINRFL--LHGQLIEVIWTILPAIILLFIALPSLRL 82
Cdd:MTH00027  35 LGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIrILLGNNYYSYYWnkLDGSLIEVIWTLIPAFILILIAFPSLRL 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463  83 LYLLDE-INEPSVTLKSIGHQWYWSYEYSDF--NNVEFDSYMIPTNELTNDGFRLLDVDNRIVLPMNSQIRILVTAADVI 159
Cdd:MTH00027 115 LYIMDEcGFSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVL 194

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501416463 160 HSWTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKWI 222
Cdd:MTH00027 195 HSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWI 257
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 5-224 1.13e-66

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 205.24  E-value: 1.13e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463   5 NLGLQDSA-SPLMEQLTFFHDHALMILVMITVLVGYLMFMLFFNSYINRFLLHGQLIEVIWTILPAIILLFIALPSLRLL 83
Cdd:MTH00080   7 NLNFSNSLfSSYMDWFHNFNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463  84 YLLDEIN-EPSVTLKSIGHQWYWSYEYSDFNNVEFDSYMIPTNELTNDGFRLLDVDNRIVLPMNSQIRILVTAADVIHSW 162
Cdd:MTH00080  87 YYYGLMNlDSNLTVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSW 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501416463 163 TIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKWISN 224
Cdd:MTH00080 167 ALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWCKL 228
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
5-224 6.77e-52

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 167.31  E-value: 6.77e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463   5 NLGLQDSASPLMEQLTFFHDHALMILVMITVLVgylMFMLFFNSYINR---------FLLHGQLIEVIWTILPAIILLFI 75
Cdd:COG1622   18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLV---FGLLLYFAIRYRrrkgdadpaQFHHNTKLEIVWTVIPIIIVIVL 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463  76 ALPSLRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNVefdsymiptneltndgfrlldVDNRIVLPMNSQIRILVTA 155
Cdd:COG1622   95 AVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVNELVLPVGRPVRFLLTS 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501416463 156 ADVIHSWTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKWISN 224
Cdd:COG1622  154 ADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAE 222
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 16-217 1.21e-46

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 152.80  E-value: 1.21e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463  16 MEQLTFFHDHALMILVMITVLVGYLMFMLFFNSYI-NRFLLHG---QLIEVIWTILPAIILLFIALPSLRLLYLlDEINE 91
Cdd:MTH00047   1 MNLSLLYYDIVCYILALCVFIPCWVYIMLCWQVVSgNGSVNFGsenQVLELLWTVVPTLLVLVLCFLNLNFITS-DLDCF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463  92 PSVTLKSIGHQWYWSYEYSDfnNVEFDSYMiptnelTNDGFrllDVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVKV 171
Cdd:MTH00047  80 SSETIKVIGHQWYWSYEYSF--GGSYDSFM------TDDIF---GVDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKM 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 501416463 172 DGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESVPVNY 217
Cdd:MTH00047 149 DAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVVDVDS 194
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 117-213 1.27e-41

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 138.80  E-value: 1.27e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463 117 FDSYMIPTNELTNDGFRLLDVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCS 196
Cdd:PTZ00047  51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                         90
                 ....*....|....*..
gi 501416463 197 EICGANHSFMPIVIESV 213
Cdd:PTZ00047 131 EMCGTLHGFMPIVVEAV 147
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-223 4.23e-41

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: 138.67  E-value: 4.23e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463   12 ASPLMEQLTFFHDH--ALMILVMITVLVGYLMFMLFFNSY----INRFLLHGQLIEVIWTILPAIILL-FIALPSLRLLY 84
Cdd:TIGR02866   2 GGEIAQQIAFLFLFvlAVSTLISLLVAALLAYVVWKFRRKgdeeKPSQIHGNRRLEYVWTVIPLIIVVgLFAATAKGLLY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463   85 LLDEINEPSVTLKSIGHQWYWSYEYSdfnnvefdsymiptneltNDGFRlldVDNRIVLPMNSQIRILVTAADVIHSWTI 164
Cdd:TIGR02866  82 LERPIPKDALKVKVTGYQWWWDFEYP------------------ESGFT---TVNELVLPAGTPVELQVTSKDVIHSFWV 140

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 501416463  165 PALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKWIS 223
Cdd:TIGR02866 141 PELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 94-211 3.98e-27

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: 99.68  E-value: 3.98e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463  94 VTLKSIGHQWYWSYEYSDFNnvefdsymiptneltndgfrlldVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDG 173
Cdd:cd13842    1 LTVYVTGVQWSWTFIYPNVR-----------------------TPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 501416463 174 TPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIE 211
Cdd:cd13842   58 VPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-76 7.77e-25

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: 93.55  E-value: 7.77e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463    1 STWANLGLQDSASPLMEQLTFFHDHALMILVMITVLVGYLMFMLFF------NSYINRFLLHGQLIEVIWTILPAIILLF 74
Cdd:pfam02790   2 PTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIrfnrrkNPITARYTTHGQTIEIIWTIIPAVILIL 81


                  ..
gi 501416463   75 IA 76
Cdd:pfam02790  82 IA 83
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 93-206 9.60e-24

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: 91.14  E-value: 9.60e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463  93 SVTLKSIGHQWYWSYEYSDfnnvefdsymiptneltnDGFRLLDVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVKVD 172
Cdd:cd04213    1 ALTIEVTGHQWWWEFRYPD------------------EPGRGIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMD 62

                         90       100       110
                 ....*....|....*....|....*....|....
gi 501416463 173 GTPGRLNQTNFFINRPGLFYGQCSEICGANHSFM 206
Cdd:cd04213   63 MIPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 94-206 4.39e-21

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: 84.23  E-value: 4.39e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463  94 VTLKSIGHQWYWSYEYSDFNNVEFDSYMIPTNELtndgfrlldvdnriVLPMNSQIRILVTAADVIHSWTIPALGVKVDG 173
Cdd:cd13919    2 LVVEVTAQQWAWTFRYPGGDGKLGTDDDVTSPEL--------------HLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                         90       100       110
                 ....*....|....*....|....*....|...
gi 501416463 174 TPGRLNQTNFFINRPGLFYGQCSEICGANHSFM 206
Cdd:cd13919   68 VPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 87-221 9.04e-19

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: 79.04  E-value: 9.04e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463  87 DEINEPSVTLKSIGHQWYWSYEYSdfNNVEFDSYMiptneltndgfrlldvdnriVLPMNSQIRILVTAADVIHSWTIPA 166
Cdd:cd13918   26 DEADEDALEVEVEGFQFGWQFEYP--NGVTTGNTL--------------------RVPADTPIALRVTSTDVFHTFGIPE 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 501416463 167 LGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKW 221
Cdd:cd13918   84 LRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAW 138
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 94-222 1.16e-18

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


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 77.83  E-value: 1.16e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463  94 VTLKSIGHQWYWSYEYSDFNNVEFdsymiptneltndgfrlldvdNRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDG 173
Cdd:cd13914    1 VEIEVEAYQWGWEFSYPEANVTTS---------------------EQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDA 59

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 501416463 174 TPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKWI 222
Cdd:cd13914   60 FPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 99-206 2.08e-18

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


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 76.90  E-value: 2.08e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463  99 IGHQWYWSYEYSDfnnvefdsymiptneltndGFRlldVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDGTPGRL 178
Cdd:cd13915    7 TGRQWMWEFTYPN-------------------GKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDVVPGRY 64

                         90       100
                 ....*....|....*....|....*...
gi 501416463 179 NQTNFFINRPGLFYGQCSEICGANHSFM 206
Cdd:cd13915   65 TYLWFEATKPGEYDLFCTEYCGTGHSGM 92
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 139-206 1.88e-10

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: 56.04  E-value: 1.88e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501416463 139 NRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFM 206
Cdd:cd13913   25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 139-206 1.66e-06

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: 45.23  E-value: 1.66e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501416463 139 NRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFM 206
Cdd:cd04212   25 NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDM 92
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 100-206 1.45e-03

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: 259983 [Multi-domain]  Cd Length: 93  Bit Score: 36.59  E-value: 1.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463 100 GHQWYWsyeysdfnnvefdsymiptnELTndgfrlldvdnRIVLPMNSQIRILVTAADVIHSWTI--PALGV--KVDGTP 175
Cdd:cd13916    7 GHQWYW--------------------ELS-----------RTEIPAGKPVEFRVTSADVNHGFGIydPDMRLlaQTQAMP 55

                         90       100       110
                 ....*....|....*....|....*....|.
gi 501416463 176 GRLNQTNFFINRPGLFYGQCSEICGANHSFM 206
Cdd:cd13916   56 GYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 114-211 2.03e-03

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: 36.83  E-value: 2.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416463 114 NVEFDSYMIPTNELTNDGFrlldVDNRIVLPMNSQIR-ILVTAADVIHSWTIPALGVKVDG---------------TPGR 177
Cdd:cd00920    2 TVTASDWGWSFTYNGVLLF----GPPVLVVPVGDTVRvQFVNKLGENHSVTIAGFGVPVVAmagganpglvntlviGPGE 77

                         90       100       110
                 ....*....|....*....|....*....|....
gi 501416463 178 LNQTNFFINRPGLFYGQCSEICGaNHSFMPIVIE 211
Cdd:cd00920   78 SAEVTFTTDQAGVYWFYCTIPGH-NHAGMVGTIN 110
 
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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