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Conserved domains on  [gi|1939456643|gb|QPL15585|]
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cytochrome c oxidase subunit 2 (mitochondrion) [Promethis valgipes]

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
 1-227 4.85e-162

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 446.58  E-value: 4.85e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939456643   1 MATWKLLLLQDSASPLMEQLSFFHDHTLLILVMITILVGQMMAGLFFNKLTHRYLLEGQTIELIWTILPAITLIFIALPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939456643  81 LRLIYILDETNNPAITIKTIGHQWYWSYEYSDFKNIEFDSYMIPIQEMSSFNFRLLDVDNRMVVPFLSQIRMLVSAADVI 160
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1939456643 161 HSWTVPSLGVKIDATPGRLNQVSFTPTRTSILYGQCSEICGANHSFMPIVTETISPKYFIKWISKMI 227
Cdd:MTH00154  161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-227 4.85e-162

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 446.58  E-value: 4.85e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939456643   1 MATWKLLLLQDSASPLMEQLSFFHDHTLLILVMITILVGQMMAGLFFNKLTHRYLLEGQTIELIWTILPAITLIFIALPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939456643  81 LRLIYILDETNNPAITIKTIGHQWYWSYEYSDFKNIEFDSYMIPIQEMSSFNFRLLDVDNRMVVPFLSQIRMLVSAADVI 160
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1939456643 161 HSWTVPSLGVKIDATPGRLNQVSFTPTRTSILYGQCSEICGANHSFMPIVTETISPKYFIKWISKMI 227
Cdd:MTH00154  161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-222 4.62e-86

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: 250.95  E-value: 4.62e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939456643  93 PAITIKTIGHQWYWSYEYSDFKNIEFDSYMIPIQEMSSFNFRLLDVDNRMVVPFLSQIRMLVSAADVIHSWTVPSLGVKI 172
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1939456643 173 DATPGRLNQVSFTPTRTSILYGQCSEICGANHSFMPIVTETISPKYFIKW 222
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 3.63e-74

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 220.36  E-value: 3.63e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939456643  95 ITIKTIGHQWYWSYEYSDFKNIEFDSYMIPIQEMSSFNFRLLDVDNRMVVPFLSQIRMLVSAADVIHSWTVPSLGVKIDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1939456643 175 TPGRLNQVSFTPTRTSILYGQCSEICGANHSFMPIVTETI 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
7-226 7.24e-53

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 170.01  E-value: 7.24e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939456643   7 LLLQDSASPLMEQLSFFHDHTLLILVMITILVGQMMAGLFF------NKLTHRYLLEGQTIELIWTILPAITLIFIALPS 80
Cdd:COG1622    19 LSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIryrrrkGDADPAQFHHNTKLEIVWTVIPIIIVIVLAVPT 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939456643  81 LRLIYILDETNNPAITIKTIGHQWYWSYEYSDfKNIEfdsymipiqemssfnfrlldVDNRMVVPFLSQIRMLVSAADVI 160
Cdd:COG1622    99 LRVLHALDDAPEDPLTVEVTGYQWKWLFRYPD-QGIA--------------------TVNELVLPVGRPVRFLLTSADVI 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1939456643 161 HSWTVPSLGVKIDATPGRLNQVSFTPTRTSILYGQCSEICGANHSFMPIVTETISPKYFIKWISKM 226
Cdd:COG1622   158 HSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQ 223
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 13-224 1.09e-39

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: 135.20  E-value: 1.09e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939456643  13 ASPLMEQLSFFHDHTLLILVMITILVgqmMAGLFFNKLTHR---------YLLEGQTIELIWTILPA-ITLIFIALPSLR 82
Cdd:TIGR02866   2 GGEIAQQIAFLFLFVLAVSTLISLLV---AALLAYVVWKFRrkgdeekpsQIHGNRRLEYVWTVIPLiIVVGLFAATAKG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939456643  83 LIYILDETNNPAITIKTIGHQWYWSYEYSDFkniefdsymipiqemssfnfrLLDVDNRMVVPFLSQIRMLVSAADVIHS 162
Cdd:TIGR02866  79 LLYLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHS 137

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1939456643 163 WTVPSLGVKIDATPGRLNQVSFTPTRTSILYGQCSEICGANHSFMPIVTETISPKYFIKWIS 224
Cdd:TIGR02866 138 FWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-227 4.85e-162

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 446.58  E-value: 4.85e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939456643   1 MATWKLLLLQDSASPLMEQLSFFHDHTLLILVMITILVGQMMAGLFFNKLTHRYLLEGQTIELIWTILPAITLIFIALPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939456643  81 LRLIYILDETNNPAITIKTIGHQWYWSYEYSDFKNIEFDSYMIPIQEMSSFNFRLLDVDNRMVVPFLSQIRMLVSAADVI 160
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1939456643 161 HSWTVPSLGVKIDATPGRLNQVSFTPTRTSILYGQCSEICGANHSFMPIVTETISPKYFIKWISKMI 227
Cdd:MTH00154  161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-226 3.43e-128

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 360.96  E-value: 3.43e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939456643   1 MATWKLLLLQDSASPLMEQLSFFHDHTLLILVMITILVGQMMAGLFFNKLTHRYLLEGQTIELIWTILPAITLIFIALPS 80
Cdd:MTH00139    1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939456643  81 LRLIYILDETNNPAITIKTIGHQWYWSYEYSDFKNIEFDSYMIPIQEMSSFNFRLLDVDNRMVVPFLSQIRMLVSAADVI 160
Cdd:MTH00139   81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1939456643 161 HSWTVPSLGVKIDATPGRLNQVSFTPTRTSILYGQCSEICGANHSFMPIVTETISPKYFIKWISKM 226
Cdd:MTH00139  161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILEK 226
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-226 4.03e-128

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 360.79  E-value: 4.03e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939456643   1 MATWKLLLLQDSASPLMEQLSFFHDHTLLILVMITILVGQMMAGLFFNKLTHRYLLEGQTIELIWTILPAITLIFIALPS 80
Cdd:MTH00140    1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939456643  81 LRLIYILDETNNPAITIKTIGHQWYWSYEYSDFKNIEFDSYMIPIQEMSSFNFRLLDVDNRMVVPFLSQIRMLVSAADVI 160
Cdd:MTH00140   81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1939456643 161 HSWTVPSLGVKIDATPGRLNQVSFTPTRTSILYGQCSEICGANHSFMPIVTETISPKYFIKWISKM 226
Cdd:MTH00140  161 HSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELM 226
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-226 6.40e-127

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 358.07  E-value: 6.40e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939456643   1 MATWKLLLLQDSASPLMEQLSFFHDHTLLILVMITILVGQMMAGLFFNKLTHRYLLEGQTIELIWTILPAITLIFIALPS 80
Cdd:MTH00117    1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939456643  81 LRLIYILDETNNPAITIKTIGHQWYWSYEYSDFKNIEFDSYMIPIQEMSSFNFRLLDVDNRMVVPFLSQIRMLVSAADVI 160
Cdd:MTH00117   81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1939456643 161 HSWTVPSLGVKIDATPGRLNQVSFTPTRTSILYGQCSEICGANHSFMPIVTETISPKYFIKWISKM 226
Cdd:MTH00117  161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLL 226
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-225 1.06e-120

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 342.22  E-value: 1.06e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939456643   1 MATWKLLLLQDSASPLMEQLSFFHDHTLLILVMITILVGQMMAGLFFNKLTHRYLLEGQTIELIWTILPAITLIFIALPS 80
Cdd:MTH00008    1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939456643  81 LRLIYILDETNNPAITIKTIGHQWYWSYEYSDFKNIEFDSYMIPIQEMSSFNFRLLDVDNRMVVPFLSQIRMLVSAADVI 160
Cdd:MTH00008   81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1939456643 161 HSWTVPSLGVKIDATPGRLNQVSFTPTRTSILYGQCSEICGANHSFMPIVTETISPKYFIKWISK 225
Cdd:MTH00008  161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSS 225
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-229 2.53e-119

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 338.60  E-value: 2.53e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939456643   1 MATWKLLLLQDSASPLMEQLSFFHDHTLLILVMITILVGQMMAGLFFNKLTHRYLLEGQTIELIWTILPAITLIFIALPS 80
Cdd:MTH00038    1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939456643  81 LRLIYILDETNNPAITIKTIGHQWYWSYEYSDFKNIEFDSYMIPIQEMSSFNFRLLDVDNRMVVPFLSQIRMLVSAADVI 160
Cdd:MTH00038   81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1939456643 161 HSWTVPSLGVKIDATPGRLNQVSFTPTRTSILYGQCSEICGANHSFMPIVTETISPKYFIKWISKMIQA 229
Cdd:MTH00038  161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFLEE 229
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-224 1.11e-117

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 334.64  E-value: 1.11e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939456643   1 MATWKLLLLQDSASPLMEQLSFFHDHTLLILVMITILVGQMMAGLFFNKLTHRYLLEGQTIELIWTILPAITLIFIALPS 80
Cdd:MTH00168    1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939456643  81 LRLIYILDETNNPAITIKTIGHQWYWSYEYSDFKNIEFDSYMIPIQEMSSFNFRLLDVDNRMVVPFLSQIRMLVSAADVI 160
Cdd:MTH00168   81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1939456643 161 HSWTVPSLGVKIDATPGRLNQVSFTPTRTSILYGQCSEICGANHSFMPIVTETISPKYFIKWIS 224
Cdd:MTH00168  161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVD 224
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-228 4.27e-112

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 320.51  E-value: 4.27e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939456643   1 MATWKLLLLQDSASPLMEQLSFFHDHTLLILVMITILVGQMMAGLFFNKLTHRYLLEGQTIELIWTILPAITLIFIALPS 80
Cdd:MTH00129    1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939456643  81 LRLIYILDETNNPAITIKTIGHQWYWSYEYSDFKNIEFDSYMIPIQEMSSFNFRLLDVDNRMVVPFLSQIRMLVSAADVI 160
Cdd:MTH00129   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1939456643 161 HSWTVPSLGVKIDATPGRLNQVSFTPTRTSILYGQCSEICGANHSFMPIVTETISPKYFIKWISKMIQ 228
Cdd:MTH00129  161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLMLE 228
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-227 1.50e-109

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 313.96  E-value: 1.50e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939456643   1 MATWKLLLLQDSASPLMEQLSFFHDHTLLILVMITILVGQMMAGLFFNKLTHRYLLEGQTIELIWTILPAITLIFIALPS 80
Cdd:MTH00098    1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939456643  81 LRLIYILDETNNPAITIKTIGHQWYWSYEYSDFKNIEFDSYMIPIQEMSSFNFRLLDVDNRMVVPFLSQIRMLVSAADVI 160
Cdd:MTH00098   81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1939456643 161 HSWTVPSLGVKIDATPGRLNQVSFTPTRTSILYGQCSEICGANHSFMPIVTETISPKYFIKWISKMI 227
Cdd:MTH00098  161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASML 227
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-228 3.44e-106

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 305.66  E-value: 3.44e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939456643   1 MATWKLLLLQDSASPLMEQLSFFHDHTLLILVMITILVGQMMAGLFFNKLTHRYLLEGQTIELIWTILPAITLIFIALPS 80
Cdd:MTH00185    1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939456643  81 LRLIYILDETNNPAITIKTIGHQWYWSYEYSDFKNIEFDSYMIPIQEMSSFNFRLLDVDNRMVVPFLSQIRMLVSAADVI 160
Cdd:MTH00185   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1939456643 161 HSWTVPSLGVKIDATPGRLNQVSFTPTRTSILYGQCSEICGANHSFMPIVTETISPKYFIKWISKMIQ 228
Cdd:MTH00185  161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLMLE 228
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-226 2.18e-105

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 303.62  E-value: 2.18e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939456643   1 MATWKLLLLQDSASPLMEQLSFFHDHTLLILVMITILVGQMMAGLFFNKLTHRYLLEGQTIELIWTILPAITLIFIALPS 80
Cdd:MTH00076    1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939456643  81 LRLIYILDETNNPAITIKTIGHQWYWSYEYSDFKNIEFDSYMIPIQEMSSFNFRLLDVDNRMVVPFLSQIRMLVSAADVI 160
Cdd:MTH00076   81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1939456643 161 HSWTVPSLGVKIDATPGRLNQVSFTPTRTSILYGQCSEICGANHSFMPIVTETISPKYFIKWISKM 226
Cdd:MTH00076  161 HSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSM 226
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 7-228 4.46e-103

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 298.20  E-value: 4.46e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939456643   7 LLLQDSASPLMEQLSFFHDHTLLILVMITILVGQMMAGLFFNKLTHRYLLEGQTIELIWTILPAITLIFIALPSLRLIYI 86
Cdd:MTH00023   16 LGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939456643  87 LDETNNPAITIKTIGHQWYWSYEYSDFK--NIEFDSYMIPIQEMSSFNFRLLDVDNRMVVPFLSQIRMLVSAADVIHSWT 164
Cdd:MTH00023   96 MDEVVSPALTIKAIGHQWYWSYEYSDYEgeTLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFA 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1939456643 165 VPSLGVKIDATPGRLNQVSFTPTRTSILYGQCSEICGANHSFMPIVTETISPKYFIKWISKMIQ 228
Cdd:MTH00023  176 VPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLSLSN 239
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 7-228 1.38e-99

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 288.99  E-value: 1.38e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939456643   7 LLLQDSASPLMEQLSFFHDHTLLILVMITILVGQMMAGLFFNKLTHRYLLEGQTIELIWTILPAITLIFIALPSLRLIYI 86
Cdd:MTH00051    9 LGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939456643  87 LDETNNPAITIKTIGHQWYWSYEYSDF--KNIEFDSYMIPIQEMSSFNFRLLDVDNRMVVPFLSQIRMLVSAADVIHSWT 164
Cdd:MTH00051   89 MDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFA 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1939456643 165 VPSLGVKIDATPGRLNQVSFTPTRTSILYGQCSEICGANHSFMPIVTETISPKYFIKWISKMIQ 228
Cdd:MTH00051  169 VPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQSE 232
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-222 4.62e-86

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: 250.95  E-value: 4.62e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939456643  93 PAITIKTIGHQWYWSYEYSDFKNIEFDSYMIPIQEMSSFNFRLLDVDNRMVVPFLSQIRMLVSAADVIHSWTVPSLGVKI 172
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1939456643 173 DATPGRLNQVSFTPTRTSILYGQCSEICGANHSFMPIVTETISPKYFIKW 222
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 7-225 8.39e-77

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 232.22  E-value: 8.39e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939456643   7 LLLQDSASPLMEQLSFFHDHTLLILVMITILVGQMMAGLFFNKLTHRYL---LEGQTIELIWTILPAITLIFIALPSLRL 83
Cdd:MTH00027   35 LGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLGNNYYSYYwnkLDGSLIEVIWTLIPAFILILIAFPSLRL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939456643  84 IYILDETNNPA-ITIKTIGHQWYWSYEYSDF--KNIEFDSYMIPIQEMSSFNFRLLDVDNRMVVPFLSQIRMLVSAADVI 160
Cdd:MTH00027  115 LYIMDECGFSAnITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVL 194

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1939456643 161 HSWTVPSLGVKIDATPGRLNQVSFTPTRTSILYGQCSEICGANHSFMPIVTETISPKYFIKWISK 225
Cdd:MTH00027  195 HSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWIGR 259
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 3.63e-74

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 220.36  E-value: 3.63e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939456643  95 ITIKTIGHQWYWSYEYSDFKNIEFDSYMIPIQEMSSFNFRLLDVDNRMVVPFLSQIRMLVSAADVIHSWTVPSLGVKIDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1939456643 175 TPGRLNQVSFTPTRTSILYGQCSEICGANHSFMPIVTETI 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 4-223 2.09e-68

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 209.87  E-value: 2.09e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939456643   4 WKLLLLQDSASPLMEQLSFFHDHTLLILVMITILVGQMMAGLFFNKLTHRYLLEGQTIELIWTILPAITLIFIALPSLRL 83
Cdd:MTH00080    6 YNLNFSNSLFSSYMDWFHNFNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939456643  84 IYILDETN-NPAITIKTIGHQWYWSYEYSDFKNIEFDSYMIPIQEMSSFNFRLLDVDNRMVVPFLSQIRMLVSAADVIHS 162
Cdd:MTH00080   86 LYYYGLMNlDSNLTVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHS 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1939456643 163 WTVPSLGVKIDATPGRLNQVSFTPTRTSILYGQCSEICGANHSFMPIVTETISPKYFIKWI 223
Cdd:MTH00080  166 WALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWC 226
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
7-226 7.24e-53

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 170.01  E-value: 7.24e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939456643   7 LLLQDSASPLMEQLSFFHDHTLLILVMITILVGQMMAGLFF------NKLTHRYLLEGQTIELIWTILPAITLIFIALPS 80
Cdd:COG1622    19 LSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIryrrrkGDADPAQFHHNTKLEIVWTVIPIIIVIVLAVPT 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939456643  81 LRLIYILDETNNPAITIKTIGHQWYWSYEYSDfKNIEfdsymipiqemssfnfrlldVDNRMVVPFLSQIRMLVSAADVI 160
Cdd:COG1622    99 LRVLHALDDAPEDPLTVEVTGYQWKWLFRYPD-QGIA--------------------TVNELVLPVGRPVRFLLTSADVI 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1939456643 161 HSWTVPSLGVKIDATPGRLNQVSFTPTRTSILYGQCSEICGANHSFMPIVTETISPKYFIKWISKM 226
Cdd:COG1622   158 HSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQ 223
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 57-218 3.38e-48

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 157.04  E-value: 3.38e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939456643  57 EGQTIELIWTILPaiTLIFIALPSLRLIYIL-DETNNPAITIKTIGHQWYWSYEYSDfkNIEFDSYMipiqemSSFNFrl 135
Cdd:MTH00047   45 ENQVLELLWTVVP--TLLVLVLCFLNLNFITsDLDCFSSETIKVIGHQWYWSYEYSF--GGSYDSFM------TDDIF-- 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939456643 136 lDVDNRMVVPFLSQIRMLVSAADVIHSWTVPSLGVKIDATPGRLNQVSFTPTRTSILYGQCSEICGANHSFMPIVTETIS 215
Cdd:MTH00047  113 -GVDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVVD 191


                  ...
gi 1939456643 216 PKY 218
Cdd:MTH00047  192 VDS 194
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 13-224 1.09e-39

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: 135.20  E-value: 1.09e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939456643  13 ASPLMEQLSFFHDHTLLILVMITILVgqmMAGLFFNKLTHR---------YLLEGQTIELIWTILPA-ITLIFIALPSLR 82
Cdd:TIGR02866   2 GGEIAQQIAFLFLFVLAVSTLISLLV---AALLAYVVWKFRrkgdeekpsQIHGNRRLEYVWTVIPLiIVVGLFAATAKG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939456643  83 LIYILDETNNPAITIKTIGHQWYWSYEYSDFkniefdsymipiqemssfnfrLLDVDNRMVVPFLSQIRMLVSAADVIHS 162
Cdd:TIGR02866  79 LLYLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHS 137

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1939456643 163 WTVPSLGVKIDATPGRLNQVSFTPTRTSILYGQCSEICGANHSFMPIVTETISPKYFIKWIS 224
Cdd:TIGR02866 138 FWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 118-219 3.27e-36

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 125.32  E-value: 3.27e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939456643 118 FDSYMIPIQEMSSFNFRLLDVDNRMVVPFLSQIRMLVSAADVIHSWTVPSLGVKIDATPGRLNQVSFTPTRTSILYGQCS 197
Cdd:PTZ00047   51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                          90       100
                  ....*....|....*....|..
gi 1939456643 198 EICGANHSFMPIVTETISPKYF 219
Cdd:PTZ00047  131 EMCGTLHGFMPIVVEAVSPEAY 152
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 94-207 5.61e-25

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: 94.22  E-value: 5.61e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939456643  94 AITIKTIGHQWYWSYEYSDFKNIEFDSymipiqemssfnfrlldvDNRMVVPFLSQIRMLVSAADVIHSWTVPSLGVKID 173
Cdd:cd04213     1 ALTIEVTGHQWWWEFRYPDEPGRGIVT------------------ANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMD 62

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1939456643 174 ATPGRLNQVSFTPTRTSILYGQCSEICGANHSFM 207
Cdd:cd04213    63 MIPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-83 7.91e-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: 7.91e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939456643   1 MATWKLLLLQDSASPLMEQLSFFHDHTLLILVMITILVGQMMAGLFF------NKLTHRYLLEGQTIELIWTILPAITLI 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIrfnrrkNPITARYTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 1939456643  75 FIALPSLRL 83
Cdd:pfam02790  81 LIALPSFKL 89
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-208 3.54e-24

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: 91.97  E-value: 3.54e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939456643  95 ITIKTIGHQWYWSYEYSDfkniefdsymipiqemssfnfrlLDVDNRMVVPFLSQIRMLVSAADVIHSWTVPSLGVKIDA 174
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1939456643 175 TPGRLNQVSFTPTRTSILYGQCSEICGANHSFMP 208
Cdd:cd13842    58 VPGYTSELWFVADKPGTYTIICAEYCGLGHSYML 91
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 94-207 6.46e-22

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: 86.54  E-value: 6.46e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939456643  94 AITIKTIGHQWYWSYEYsdfkniefdsymipIQEMSSFNFRLLDVDNRMVVPFLSQIRMLVSAADVIHSWTVPSLGVKID 173
Cdd:cd13919     1 ALVVEVTAQQWAWTFRY--------------PGGDGKLGTDDDVTSPELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQD 66

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1939456643 174 ATPGRLNQVSFTPTRTSILYGQCSEICGANHSFM 207
Cdd:cd13919    67 AVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 94-207 3.36e-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: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 79.21  E-value: 3.36e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939456643  94 AITIKTIGHQWYWSYEYSDFKNIefdsymipiqemssfnfrlldvDNRMVVPFLSQIRMLVSAADVIHSWTVPSLGVKID 173
Cdd:cd13915     1 ALEIQVTGRQWMWEFTYPNGKRE----------------------INELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQD 58

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1939456643 174 ATPGRLNQVSFTPTRTSILYGQCSEICGANHSFM 207
Cdd:cd13915    59 VVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-207 3.74e-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: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 71.67  E-value: 3.74e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939456643  95 ITIKTIGHQWYWSYEYSDfKNIefdsymipiqemssfnfrllDVDNRMVVPFLSQIRMLVSAADVIHSWTVPSLGVKIDA 174
Cdd:cd13914     1 VEIEVEAYQWGWEFSYPE-ANV--------------------TTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDA 59

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1939456643 175 TPGRLNQVSFTPTRTSILYGQCSEICGANHSFM 207
Cdd:cd13914    60 FPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQM 92
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 83-207 3.81e-15

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: 69.79  E-value: 3.81e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939456643  83 LIYILD---ETNNPAITIKTIGHQWYWSYEYSDfkniefdsymipiqEMSSFNFrlldvdnrMVVPFLSQIRMLVSAADV 159
Cdd:cd13918    18 LLYVEDppdEADEDALEVEVEGFQFGWQFEYPN--------------GVTTGNT--------LRVPADTPIALRVTSTDV 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1939456643 160 IHSWTVPSLGVKIDATPGRLNQVSFTPTRTSILYGQCSEICGANHSFM 207
Cdd:cd13918    76 FHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLM 123
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 140-207 2.07e-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: 44.87  E-value: 2.07e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1939456643 140 NRMVVPFLSQIRMLVSAADVIHSWTVPSLGVKIDATPGRLNQVSFTPTRTSILYGQCSEICGANHSFM 207
Cdd:cd13913    25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 97-210 2.22e-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: 2.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939456643  97 IKTIGHQWYWSYEYSDFKNIEFDSYMIPIQEMSSFNFrlldvdnrmvvpflsqirmlVSAADVIHSWTVPSLGVKIDA-- 174
Cdd:cd00920     1 ITVTASDWGWSFTYNGVLLFGPPVLVVPVGDTVRVQF--------------------VNKLGENHSVTIAGFGVPVVAma 60

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1939456643 175 -------------TPGRLNQVSFTPTRTSILYGQCSEICGaNHSFMPIV 210
Cdd:cd00920    61 gganpglvntlviGPGESAEVTFTTDQAGVYWFYCTIPGH-NHAGMVGT 108
 
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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