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Conserved domains on  [gi|2745726715|gb|XBW76993|]
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cytochrome c oxidase subunit II (mitochondrion) [Xenopsylla cheopis]

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 1.69e-133

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 374.55  E-value: 1.69e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715   1 MNTWMNFNLQNSNSPMMEQLMFFHNHSLLIILMITMLISYLMSSLFFNKINNRIMMESQTLEMVWTIIPMFLLIFIALPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715  81 LRLLYLLDDSNNPLITIKSIGHQWYWNYEYSDFKNINFDSYMISSNDLNLNSFRLLDVDNRIILPFNSHIRIIITASDVL 160
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2745726715 161 HSWTIPSLGIKVDASPGRLNQSNFYMNRPGLYFGQCSEICGANHSFMPIVIESISVNSFMKWVNLNS 227
Cdd:MTH00154  161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-227 1.69e-133

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 374.55  E-value: 1.69e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715   1 MNTWMNFNLQNSNSPMMEQLMFFHNHSLLIILMITMLISYLMSSLFFNKINNRIMMESQTLEMVWTIIPMFLLIFIALPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715  81 LRLLYLLDDSNNPLITIKSIGHQWYWNYEYSDFKNINFDSYMISSNDLNLNSFRLLDVDNRIILPFNSHIRIIITASDVL 160
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2745726715 161 HSWTIPSLGIKVDASPGRLNQSNFYMNRPGLYFGQCSEICGANHSFMPIVIESISVNSFMKWVNLNS 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 3.07e-88

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: 256.34  E-value: 3.07e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715  93 PLITIKSIGHQWYWNYEYSDFKNINFDSYMISSNDLNLNSFRLLDVDNRIILPFNSHIRIIITASDVLHSWTIPSLGIKV 172
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2745726715 173 DASPGRLNQSNFYMNRPGLYFGQCSEICGANHSFMPIVIESISVNSFMKW 222
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 6.35e-78

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 229.99  E-value: 6.35e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715  95 ITIKSIGHQWYWNYEYSDFKNINFDSYMISSNDLNLNSFRLLDVDNRIILPFNSHIRIIITASDVLHSWTIPSLGIKVDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2745726715 175 SPGRLNQSNFYMNRPGLYFGQCSEICGANHSFMPIVIESI 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-223 4.34e-47

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 154.99  E-value: 4.34e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715   6 NFNLQNSNSPMMEQLMFFHNHSLLIILMITMLISYLM--SSLFFNKINNRIMM----ESQTLEMVWTIIPMFLLIFIALP 79
Cdd:COG1622    18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLlyFAIRYRRRKGDADPaqfhHNTKLEIVWTVIPIIIVIVLAVP 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715  80 SLRLLYLLDDSNNPLITIKSIGHQWYWNYEYSDfKNInfdsymissndlnlnsfrllDVDNRIILPFNSHIRIIITASDV 159
Cdd:COG1622    98 TLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPD-QGI--------------------ATVNELVLPVGRPVRFLLTSADV 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2745726715 160 LHSWTIPSLGIKVDASPGRLNQSNFYMNRPGLYFGQCSEICGANHSFMPIVIESISVNSFMKWV 223
Cdd:COG1622   157 IHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWL 220
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 14-224 5.57e-38

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: 130.96  E-value: 5.57e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715  14 SPMMEQLMFFHNHSLLIILMITMLISYLMSSLFFnKINNRIMMESQT-------LEMVWTIIP--MFLLIFIALPSLRLL 84
Cdd:TIGR02866   3 GEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVW-KFRRKGDEEKPSqihgnrrLEYVWTVIPliIVVGLFAATAKGLLY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715  85 YLLDDSNNPLiTIKSIGHQWYWNYEYSDFkninfdsymissndlnlnsfrLLDVDNRIILPFNSHIRIIITASDVLHSWT 164
Cdd:TIGR02866  82 LERPIPKDAL-KVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFW 139

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715 165 IPSLGIKVDASPGRLNQSNFYMNRPGLYFGQCSEICGANHSFMPIVIESISVNSFMKWVN 224
Cdd:TIGR02866 140 VPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-227 1.69e-133

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 374.55  E-value: 1.69e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715   1 MNTWMNFNLQNSNSPMMEQLMFFHNHSLLIILMITMLISYLMSSLFFNKINNRIMMESQTLEMVWTIIPMFLLIFIALPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715  81 LRLLYLLDDSNNPLITIKSIGHQWYWNYEYSDFKNINFDSYMISSNDLNLNSFRLLDVDNRIILPFNSHIRIIITASDVL 160
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2745726715 161 HSWTIPSLGIKVDASPGRLNQSNFYMNRPGLYFGQCSEICGANHSFMPIVIESISVNSFMKWVNLNS 227
Cdd:MTH00154  161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 5-227 8.27e-113

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 322.25  E-value: 8.27e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715   5 MNFNLQNSNSPMMEQLMFFHNHSLLIILMITMLISYLMSSLFFNKINNRIMMESQTLEMVWTIIPMFLLIFIALPSLRLL 84
Cdd:MTH00117    5 SQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPSLRIL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715  85 YLLDDSNNPLITIKSIGHQWYWNYEYSDFKNINFDSYMISSNDLNLNSFRLLDVDNRIILPFNSHIRIIITASDVLHSWT 164
Cdd:MTH00117   85 YLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWA 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2745726715 165 IPSLGIKVDASPGRLNQSNFYMNRPGLYFGQCSEICGANHSFMPIVIESISVNSFMKWVNLNS 227
Cdd:MTH00117  165 VPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLLS 227
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-224 4.50e-112

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 320.35  E-value: 4.50e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715   1 MNTWMNFNLQNSNSPMMEQLMFFHNHSLLIILMITMLISYLMSSLFFNKINNRIMMESQTLEMVWTIIPMFLLIFIALPS 80
Cdd:MTH00140    1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715  81 LRLLYLLDDSNNPLITIKSIGHQWYWNYEYSDFKNINFDSYMISSNDLNLNSFRLLDVDNRIILPFNSHIRIIITASDVL 160
Cdd:MTH00140   81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2745726715 161 HSWTIPSLGIKVDASPGRLNQSNFYMNRPGLYFGQCSEICGANHSFMPIVIESISVNSFMKWVN 224
Cdd:MTH00140  161 HSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLE 224
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-223 6.12e-111

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 317.43  E-value: 6.12e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715   1 MNTWMNFNLQNSNSPMMEQLMFFHNHSLLIILMITMLISYLMSSLFFNKINNRIMMESQTLEMVWTIIPMFLLIFIALPS 80
Cdd:MTH00139    1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715  81 LRLLYLLDDSNNPLITIKSIGHQWYWNYEYSDFKNINFDSYMISSNDLNLNSFRLLDVDNRIILPFNSHIRIIITASDVL 160
Cdd:MTH00139   81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2745726715 161 HSWTIPSLGIKVDASPGRLNQSNFYMNRPGLYFGQCSEICGANHSFMPIVIESISVNSFMKWV 223
Cdd:MTH00139  161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWI 223
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-224 7.36e-106

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 304.70  E-value: 7.36e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715   1 MNTWMNFNLQNSNSPMMEQLMFFHNHSLLIILMITMLISYLMSSLFFNKINNRIMMESQTLEMVWTIIPMFLLIFIALPS 80
Cdd:MTH00038    1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715  81 LRLLYLLDDSNNPLITIKSIGHQWYWNYEYSDFKNINFDSYMISSNDLNLNSFRLLDVDNRIILPFNSHIRIIITASDVL 160
Cdd:MTH00038   81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2745726715 161 HSWTIPSLGIKVDASPGRLNQSNFYMNRPGLYFGQCSEICGANHSFMPIVIESISVNSFMKWVN 224
Cdd:MTH00038  161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVS 224
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-224 1.22e-103

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 298.82  E-value: 1.22e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715   1 MNTWMNFNLQNSNSPMMEQLMFFHNHSLLIILMITMLISYLMSSLFFNKINNRIMMESQTLEMVWTIIPMFLLIFIALPS 80
Cdd:MTH00168    1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715  81 LRLLYLLDDSNNPLITIKSIGHQWYWNYEYSDFKNINFDSYMISSNDLNLNSFRLLDVDNRIILPFNSHIRIIITASDVL 160
Cdd:MTH00168   81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2745726715 161 HSWTIPSLGIKVDASPGRLNQSNFYMNRPGLYFGQCSEICGANHSFMPIVIESISVNSFMKWVN 224
Cdd:MTH00168  161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVD 224
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-227 8.63e-102

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 294.46  E-value: 8.63e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715   1 MNTWMNFNLQNSNSPMMEQLMFFHNHSLLIILMITMLISYLMSSLFFNKINNRIMMESQTLEMVWTIIPMFLLIFIALPS 80
Cdd:MTH00008    1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715  81 LRLLYLLDDSNNPLITIKSIGHQWYWNYEYSDFKNINFDSYMISSNDLNLNSFRLLDVDNRIILPFNSHIRIIITASDVL 160
Cdd:MTH00008   81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2745726715 161 HSWTIPSLGIKVDASPGRLNQSNFYMNRPGLYFGQCSEICGANHSFMPIVIESISVNSFMKWVNLNS 227
Cdd:MTH00008  161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSSFA 227
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-222 1.54e-97

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 283.53  E-value: 1.54e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715   1 MNTWMNFNLQNSNSPMMEQLMFFHNHSLLIILMITMLISYLMSSLFFNKINNRIMMESQTLEMVWTIIPMFLLIFIALPS 80
Cdd:MTH00098    1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715  81 LRLLYLLDDSNNPLITIKSIGHQWYWNYEYSDFKNINFDSYMISSNDLNLNSFRLLDVDNRIILPFNSHIRIIITASDVL 160
Cdd:MTH00098   81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2745726715 161 HSWTIPSLGIKVDASPGRLNQSNFYMNRPGLYFGQCSEICGANHSFMPIVIESISVNSFMKW 222
Cdd:MTH00098  161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKW 222
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 9-226 8.74e-96

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 278.97  E-value: 8.74e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715   9 LQNSNSPMMEQLMFFHNHSLLIILMITMLISYLMSSLFFNKINNRIMMESQTLEMVWTIIPMFLLIFIALPSLRLLYLLD 88
Cdd:MTH00076    9 FQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRILYLMD 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715  89 DSNNPLITIKSIGHQWYWNYEYSDFKNINFDSYMISSNDLNLNSFRLLDVDNRIILPFNSHIRIIITASDVLHSWTIPSL 168
Cdd:MTH00076   89 EINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSL 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2745726715 169 GIKVDASPGRLNQSNFYMNRPGLYFGQCSEICGANHSFMPIVIESISVNSFMKWVNLN 226
Cdd:MTH00076  169 GIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSM 226
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 9-225 1.70e-94

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 276.00  E-value: 1.70e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715   9 LQNSNSPMMEQLMFFHNHSLLIILMITMLISYLMSSLFFNKINNRIMMESQTLEMVWTIIPMFLLIFIALPSLRLLYLLD 88
Cdd:MTH00185    9 LQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLRILYLMD 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715  89 DSNNPLITIKSIGHQWYWNYEYSDFKNINFDSYMISSNDLNLNSFRLLDVDNRIILPFNSHIRIIITASDVLHSWTIPSL 168
Cdd:MTH00185   89 EINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVPAL 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2745726715 169 GIKVDASPGRLNQSNFYMNRPGLYFGQCSEICGANHSFMPIVIESISVNSFMKWVNL 225
Cdd:MTH00185  169 GVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSL 225
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 9-225 2.46e-94

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 275.44  E-value: 2.46e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715   9 LQNSNSPMMEQLMFFHNHSLLIILMITMLISYLMSSLFFNKINNRIMMESQTLEMVWTIIPMFLLIFIALPSLRLLYLLD 88
Cdd:MTH00129    9 FQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRILYLMD 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715  89 DSNNPLITIKSIGHQWYWNYEYSDFKNINFDSYMISSNDLNLNSFRLLDVDNRIILPFNSHIRIIITASDVLHSWTIPSL 168
Cdd:MTH00129   89 EINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVPAL 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2745726715 169 GIKVDASPGRLNQSNFYMNRPGLYFGQCSEICGANHSFMPIVIESISVNSFMKWVNL 225
Cdd:MTH00129  169 GVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSL 225
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 9-223 1.39e-91

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 268.93  E-value: 1.39e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715   9 LQNSNSPMMEQLMFFHNHSLLIILMITMLISYLMSSLFFNKINNRIMMESQTLEMVWTIIPMFLLIFIALPSLRLLYLLD 88
Cdd:MTH00023   18 FQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYLMD 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715  89 DSNNPLITIKSIGHQWYWNYEYSDFK--NINFDSYMISSNDLNLNSFRLLDVDNRIILPFNSHIRIIITASDVLHSWTIP 166
Cdd:MTH00023   98 EVVSPALTIKAIGHQWYWSYEYSDYEgeTLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVP 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2745726715 167 SLGIKVDASPGRLNQSNFYMNRPGLYFGQCSEICGANHSFMPIVIESISVNSFMKWV 223
Cdd:MTH00023  178 SLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWL 234
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-222 3.07e-88

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: 256.34  E-value: 3.07e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715  93 PLITIKSIGHQWYWNYEYSDFKNINFDSYMISSNDLNLNSFRLLDVDNRIILPFNSHIRIIITASDVLHSWTIPSLGIKV 172
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2745726715 173 DASPGRLNQSNFYMNRPGLYFGQCSEICGANHSFMPIVIESISVNSFMKW 222
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 8-223 1.98e-86

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 255.48  E-value: 1.98e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715   8 NLQNSNSPMMEQLMFFHNHSLLIILMITMLISYLMSSLFFNKINNRIMMESQTLEMVWTIIPMFLLIFIALPSLRLLYLL 87
Cdd:MTH00051   10 GFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYLM 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715  88 DDSNNPLITIKSIGHQWYWNYEYSDF--KNINFDSYMISSNDLNLNSFRLLDVDNRIILPFNSHIRIIITASDVLHSWTI 165
Cdd:MTH00051   90 DEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAV 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2745726715 166 PSLGIKVDASPGRLNQSNFYMNRPGLYFGQCSEICGANHSFMPIVIESISVNSFMKWV 223
Cdd:MTH00051  170 PSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWV 227
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 6.35e-78

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 229.99  E-value: 6.35e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715  95 ITIKSIGHQWYWNYEYSDFKNINFDSYMISSNDLNLNSFRLLDVDNRIILPFNSHIRIIITASDVLHSWTIPSLGIKVDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2745726715 175 SPGRLNQSNFYMNRPGLYFGQCSEICGANHSFMPIVIESI 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 9-223 7.82e-69

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 211.81  E-value: 7.82e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715   9 LQNSNSPMMEQLMFFHNHSLLIILMIT-----MLISYLMSSLFFNKINNRimMESQTLEMVWTIIPMFLLIFIALPSLRL 83
Cdd:MTH00027   37 FQDAGSPVMEEIIMLHDQILFILTIIVgvvlwLIIRILLGNNYYSYYWNK--LDGSLIEVIWTLIPAFILILIAFPSLRL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715  84 LYLLDDSN-NPLITIKSIGHQWYWNYEYSDF--KNINFDSYMISSNDLNLNSFRLLDVDNRIILPFNSHIRIIITASDVL 160
Cdd:MTH00027  115 LYIMDECGfSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVL 194

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2745726715 161 HSWTIPSLGIKVDASPGRLNQSNFYMNRPGLYFGQCSEICGANHSFMPIVIESISVNSFMKWV 223
Cdd:MTH00027  195 HSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWI 257
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 6-226 7.97e-62

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 192.92  E-value: 7.97e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715   6 NFNLQNSNSPMMEQLMFFHN---HSLLIILMITMLISYLMSSLFFNKINNRIMMESQTLEMVWTIIPMFLLIFIALPSLR 82
Cdd:MTH00080    5 GYNLNFSNSLFSSYMDWFHNfncSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715  83 LLYLLD----DSNnplITIKSIGHQWYWNYEYSDFKNINFDSYMISSNDLNLNSFRLLDVDNRIILPFNSHIRIIITASD 158
Cdd:MTH00080   85 LLYYYGlmnlDSN---LTVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSD 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2745726715 159 VLHSWTIPSLGIKVDASPGRLNQSNFYMNRPGLYFGQCSEICGANHSFMPIVIESISVNSFMKWVNLN 226
Cdd:MTH00080  162 VIHSWALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWCKLL 229
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-223 4.34e-47

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 154.99  E-value: 4.34e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715   6 NFNLQNSNSPMMEQLMFFHNHSLLIILMITMLISYLM--SSLFFNKINNRIMM----ESQTLEMVWTIIPMFLLIFIALP 79
Cdd:COG1622    18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLlyFAIRYRRRKGDADPaqfhHNTKLEIVWTVIPIIIVIVLAVP 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715  80 SLRLLYLLDDSNNPLITIKSIGHQWYWNYEYSDfKNInfdsymissndlnlnsfrllDVDNRIILPFNSHIRIIITASDV 159
Cdd:COG1622    98 TLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPD-QGI--------------------ATVNELVLPVGRPVRFLLTSADV 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2745726715 160 LHSWTIPSLGIKVDASPGRLNQSNFYMNRPGLYFGQCSEICGANHSFMPIVIESISVNSFMKWV 223
Cdd:COG1622   157 IHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWL 220
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 30-218 3.76e-44

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 146.64  E-value: 3.76e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715  30 IILMITMLISYLMSSLFFNkinnrimmESQTLEMVWTIIPMFLLIFIALPSLRLLYLlDDSNNPLITIKSIGHQWYWNYE 109
Cdd:MTH00047   26 YIMLCWQVVSGNGSVNFGS--------ENQVLELLWTVVPTLLVLVLCFLNLNFITS-DLDCFSSETIKVIGHQWYWSYE 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715 110 YSDfkNINFDSYMISSNDLnlnsfrlldVDNRIILPFNSHIRIIITASDVLHSWTIPSLGIKVDASPGRLNQSNFYMNRP 189
Cdd:MTH00047   97 YSF--GGSYDSFMTDDIFG---------VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRH 165

                         170       180
                  ....*....|....*....|....*....
gi 2745726715 190 GLYFGQCSEICGANHSFMPIVIESISVNS 218
Cdd:MTH00047  166 GVFVGYCSELCGVGHSYMPIVIEVVDVDS 194
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 118-219 3.27e-42

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 140.73  E-value: 3.27e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715 118 FDSYMISSNDLNLNSFRLLDVDNRIILPFNSHIRIIITASDVLHSWTIPSLGIKVDASPGRLNQSNFYMNRPGLYFGQCS 197
Cdd:PTZ00047   51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                          90       100
                  ....*....|....*....|..
gi 2745726715 198 EICGANHSFMPIVIESISVNSF 219
Cdd:PTZ00047  131 EMCGTLHGFMPIVVEAVSPEAY 152
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 14-224 5.57e-38

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: 130.96  E-value: 5.57e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715  14 SPMMEQLMFFHNHSLLIILMITMLISYLMSSLFFnKINNRIMMESQT-------LEMVWTIIP--MFLLIFIALPSLRLL 84
Cdd:TIGR02866   3 GEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVW-KFRRKGDEEKPSqihgnrrLEYVWTVIPliIVVGLFAATAKGLLY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715  85 YLLDDSNNPLiTIKSIGHQWYWNYEYSDFkninfdsymissndlnlnsfrLLDVDNRIILPFNSHIRIIITASDVLHSWT 164
Cdd:TIGR02866  82 LERPIPKDAL-KVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFW 139

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715 165 IPSLGIKVDASPGRLNQSNFYMNRPGLYFGQCSEICGANHSFMPIVIESISVNSFMKWVN 224
Cdd:TIGR02866 140 VPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-212 1.24e-26

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: 98.14  E-value: 1.24e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715  95 ITIKSIGHQWYWNYEYSDfkninfdsymissndlnlnsfrlLDVDNRIILPFNSHIRIIITASDVLHSWTIPSLGIKVDA 174
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2745726715 175 SPGRLNQSNFYMNRPGLYFGQCSEICGANHSFMPIVIE 212
Cdd:cd13842    58 VPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 95-207 9.20e-26

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: 96.15  E-value: 9.20e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715  95 ITIKSIGHQWYWNYEYSDFKNINFdsymISSNDlnlnsfrlldvdnrIILPFNSHIRIIITASDVLHSWTIPSLGIKVDA 174
Cdd:cd04213     2 LTIEVTGHQWWWEFRYPDEPGRGI----VTANE--------------LHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDM 63

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2745726715 175 SPGRLNQSNFYMNRPGLYFGQCSEICGANHSFM 207
Cdd:cd04213    64 IPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-207 7.86e-20

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: 80.75  E-value: 7.86e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715  95 ITIKSIGHQWYWNYEYSDFKNInfdsymissndlnlnsfrlldvDNRIILPFNSHIRIIITASDVLHSWTIPSLGIKVDA 174
Cdd:cd13915     2 LEIQVTGRQWMWEFTYPNGKRE----------------------INELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDV 59

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2745726715 175 SPGRLNQSNFYMNRPGLYFGQCSEICGANHSFM 207
Cdd:cd13915    60 VPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-207 7.51e-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: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 78.45  E-value: 7.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715  95 ITIKSIGHQWYWNYEY--SDFKNINFDSymISSNDLNLnsfrlldvdnriilPFNSHIRIIITASDVLHSWTIPSLGIKV 172
Cdd:cd13919     2 LVVEVTAQQWAWTFRYpgGDGKLGTDDD--VTSPELHL--------------PVGRPVLFNLRSKDVIHSFWVPEFRVKQ 65

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2745726715 173 DASPGRLNQSNFYMNRPGLYFGQCSEICGANHSFM 207
Cdd:cd13919    66 DAVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-223 2.00e-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: 77.45  E-value: 2.00e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715  95 ITIKSIGHQWYWNYEYsdfkninfdsymissNDLNLNSFrlldvdNRIILPFNSHIRIIITASDVLHSWTIPSLGIKVDA 174
Cdd:cd13914     1 VEIEVEAYQWGWEFSY---------------PEANVTTS------EQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDA 59

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2745726715 175 SPGRLNQSNFYMNRPGLYFGQCSEICGANHSFMPIVIESISVNSFMKWV 223
Cdd:cd13914    60 FPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 88-207 6.52e-17

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: 74.41  E-value: 6.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715  88 DDSNNPLITIKSIGHQWYWNYEYSdfkninfdsymissndlNLNSFRlldvdNRIILPFNSHIRIIITASDVLHSWTIPS 167
Cdd:cd13918    26 DEADEDALEVEVEGFQFGWQFEYP-----------------NGVTTG-----NTLRVPADTPIALRVTSTDVFHTFGIPE 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2745726715 168 LGIKVDASPGRLNQSNFYMNRPGLYFGQCSEICGANHSFM 207
Cdd:cd13918    84 LRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLM 123
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-77 3.21e-16

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: 71.21  E-value: 3.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715   1 MNTWMNFNLQNSNSPMMEQLMFFHNHSLLIILMITMLISYLMSSLFF------NKINNRIMMESQTLEMVWTIIPMFLLI 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIrfnrrkNPITARYTTHGQTIEIIWTIIPAVILI 80


                  ...
gi 2745726715  75 FIA 77
Cdd:pfam02790  81 LIA 83
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 140-207 1.48e-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: 1.48e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2745726715 140 NRIILPFNSHIRIIITASDVLHSWTIPSLGIKVDASPGRLNQSNFYMNRPGLYFGQCSEICGANHSFM 207
Cdd:cd13913    25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-207 2.03e-04

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: 39.29  E-value: 2.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745726715  95 ITIKSIGHQWYWnyEYSdfkninfdsymissndlnlnsfrlldvdnRIILPFNSHIRIIITASDVLHSWTI--PSLGI-- 170
Cdd:cd13916     1 QVVAVTGHQWYW--ELS-----------------------------RTEIPAGKPVEFRVTSADVNHGFGIydPDMRLla 49

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2745726715 171 KVDASPGRLNQSNFYMNRPGLYFGQCSEICGANHSFM 207
Cdd:cd13916    50 QTQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 140-207 3.15e-04

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: 38.68  E-value: 3.15e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2745726715 140 NRIILPFNSHIRIIITASDVLHSWTIPSLGIKVDASPGRLNQSNFYMNRPGLYFGQCSEICGANHSFM 207
Cdd:cd04212    25 NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDM 92
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 149-207 5.97e-04

The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase participates in nitrogen metabolism and catalyzes the last step in dissimilatory nitrate reduction, the two-electron reduction of N2O to N2. It contains copper ions as cofactors in the form of a binuclear CuA center at the site of electron entry and a tetranuclear CuZ centre at the active site. The C-terminus of Nitrous-oxide reductase is a cupredoxin domain.


Pssm-ID: 259885 [Multi-domain]  Cd Length: 95  Bit Score: 37.98  E-value: 5.97e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2745726715 149 HIRIIIT----ASDVLHSWTIPSLGIKVDASPGRLNQSNFYMNRPGLYFGQCSEICGANHSFM 207
Cdd:cd04223    25 EVTVHLTnleqDEDITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALHLEM 87
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 152-212 8.26e-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: 34.90  E-value: 8.26e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2745726715 152 IIITASDVLHSWTIPSLGIKVDAS---------------PGRLNQSNFYMNRPGLYFGQCSEICGaNHSFMPIVIE 212
Cdd:cd00920    36 QFVNKLGENHSVTIAGFGVPVVAMagganpglvntlvigPGESAEVTFTTDQAGVYWFYCTIPGH-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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