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Conserved domains on  [gi|237682780|gb|ACR10437|]
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cytochrome c oxidase subunit II (mitochondrion) [Apalacris sp. LZ-2009]

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 4.44e-147

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 408.83  E-value: 4.44e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780   1 MSTWSNFSLQDSASPMMEQLLFFHDHTMTMLIMITVIVSYSIIYMMKINYTNQNFLHEHMIEMIWTTLPAITLIFIAMPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780  81 LRLLYLFDDSMNTMMTIKTIGRQWYWSYEYSDFNNIEFDTYMMPEKELKNGGFRLLEVDNRTILPMNLEIRVMVTASDVI 160
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 237682780 161 HSWTIPSLGIKIDAMPGRLNQSTFSINRPGLFMGQCSEICGTNHSFMPITIESTSVNLFIKWLSKMI 227
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-227 4.44e-147

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 408.83  E-value: 4.44e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780   1 MSTWSNFSLQDSASPMMEQLLFFHDHTMTMLIMITVIVSYSIIYMMKINYTNQNFLHEHMIEMIWTTLPAITLIFIAMPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780  81 LRLLYLFDDSMNTMMTIKTIGRQWYWSYEYSDFNNIEFDTYMMPEKELKNGGFRLLEVDNRTILPMNLEIRVMVTASDVI 160
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 237682780 161 HSWTIPSLGIKIDAMPGRLNQSTFSINRPGLFMGQCSEICGTNHSFMPITIESTSVNLFIKWLSKMI 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 ...
 95-222 2.22e-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: 251.72  E-value: 2.22e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780  95 MTIKTIGRQWYWSYEYSDFNNIEFDTYMMPEKELKNGGFRLLEVDNRTILPMNLEIRVMVTASDVIHSWTIPSLGIKIDA 174
Cdd:cd13912    3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 237682780 175 MPGRLNQSTFSINRPGLFMGQCSEICGTNHSFMPITIESTSVNLFIKW 222
Cdd:cd13912   83 VPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 8.62e-78

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 229.60  E-value: 8.62e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780   95 MTIKTIGRQWYWSYEYSDFNNIEFDTYMMPEKELKNGGFRLLEVDNRTILPMNLEIRVMVTASDVIHSWTIPSLGIKIDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 237682780  175 MPGRLNQSTFSINRPGLFMGQCSEICGTNHSFMPITIEST 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-226 1.85e-52

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 168.85  E-value: 1.85e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780   6 NFSLQDSASPMMEQLLFFHDHTMTMLIMITVIVSYSIIYMM------KINYTNQNFLHEHMIEMIWTTLPAITLIFIAMP 79
Cdd:COG1622   18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAiryrrrKGDADPAQFHHNTKLEIVWTVIPIIIVIVLAVP 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780  80 SLRLLYLFDDSMNTMMTIKTIGRQWYWSYEYSDFNNiefdtymmpekelknggfrllEVDNRTILPMNLEIRVMVTASDV 159
Cdd:COG1622   98 TLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGI---------------------ATVNELVLPVGRPVRFLLTSADV 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 237682780 160 IHSWTIPSLGIKIDAMPGRLNQSTFSINRPGLFMGQCSEICGTNHSFMPITIESTSVNLFIKWLSKM 226
Cdd:COG1622  157 IHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQ 223
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 13-224 4.03e-40

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: 136.36  E-value: 4.03e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780   13 ASPMMEQLLFFHDHTMTMLIMITVIVSYSIIYMM-----KINYTNQNFLHEHM-IEMIWTTLPA-ITLIFIAMPSLRLLY 85
Cdd:TIGR02866   2 GGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVwkfrrKGDEEKPSQIHGNRrLEYVWTVIPLiIVVGLFAATAKGLLY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780   86 LFDDSMNTMMTIKTIGRQWYWSYEYsdfnniefdtymmpekelKNGGFRlleVDNRTILPMNLEIRVMVTASDVIHSWTI 165
Cdd:TIGR02866  82 LERPIPKDALKVKVTGYQWWWDFEY------------------PESGFT---TVNELVLPAGTPVELQVTSKDVIHSFWV 140

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 237682780  166 PSLGIKIDAMPGRLNQSTFSINRPGLFMGQCSEICGTNHSFMPITIESTSVNLFIKWLS 224
Cdd:TIGR02866 141 PELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-227 4.44e-147

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 408.83  E-value: 4.44e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780   1 MSTWSNFSLQDSASPMMEQLLFFHDHTMTMLIMITVIVSYSIIYMMKINYTNQNFLHEHMIEMIWTTLPAITLIFIAMPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780  81 LRLLYLFDDSMNTMMTIKTIGRQWYWSYEYSDFNNIEFDTYMMPEKELKNGGFRLLEVDNRTILPMNLEIRVMVTASDVI 160
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 237682780 161 HSWTIPSLGIKIDAMPGRLNQSTFSINRPGLFMGQCSEICGTNHSFMPITIESTSVNLFIKWLSKMI 227
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-226 7.87e-120

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 339.97  E-value: 7.87e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780   1 MSTWSNFSLQDSASPMMEQLLFFHDHTMTMLIMITVIVSYSIIYMMKINYTNQNFLHEHMIEMIWTTLPAITLIFIAMPS 80
Cdd:MTH00117   1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780  81 LRLLYLFDDSMNTMMTIKTIGRQWYWSYEYSDFNNIEFDTYMMPEKELKNGGFRLLEVDNRTILPMNLEIRVMVTASDVI 160
Cdd:MTH00117  81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 237682780 161 HSWTIPSLGIKIDAMPGRLNQSTFSINRPGLFMGQCSEICGTNHSFMPITIESTSVNLFIKWLSKM 226
Cdd:MTH00117 161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLL 226
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-226 1.00e-115

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 329.37  E-value: 1.00e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780   1 MSTWSNFSLQDSASPMMEQLLFFHDHTMTMLIMITVIVSYSIIYMMKINYTNQNFLHEHMIEMIWTTLPAITLIFIAMPS 80
Cdd:MTH00139   1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780  81 LRLLYLFDDSMNTMMTIKTIGRQWYWSYEYSDFNNIEFDTYMMPEKELKNGGFRLLEVDNRTILPMNLEIRVMVTASDVI 160
Cdd:MTH00139  81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 237682780 161 HSWTIPSLGIKIDAMPGRLNQSTFSINRPGLFMGQCSEICGTNHSFMPITIESTSVNLFIKWLSKM 226
Cdd:MTH00139 161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILEK 226
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-226 8.63e-114

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 324.58  E-value: 8.63e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780   1 MSTWSNFSLQDSASPMMEQLLFFHDHTMTMLIMITVIVSYSIIYMMKINYTNQNFLHEHMIEMIWTTLPAITLIFIAMPS 80
Cdd:MTH00140   1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780  81 LRLLYLFDDSMNTMMTIKTIGRQWYWSYEYSDFNNIEFDTYMMPEKELKNGGFRLLEVDNRTILPMNLEIRVMVTASDVI 160
Cdd:MTH00140  81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 237682780 161 HSWTIPSLGIKIDAMPGRLNQSTFSINRPGLFMGQCSEICGTNHSFMPITIESTSVNLFIKWLSKM 226
Cdd:MTH00140 161 HSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELM 226
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-227 2.05e-110

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 316.26  E-value: 2.05e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780   1 MSTWSNFSLQDSASPMMEQLLFFHDHTMTMLIMITVIVSYSIIYMMKINYTNQNFLHEHMIEMIWTTLPAITLIFIAMPS 80
Cdd:MTH00038   1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780  81 LRLLYLFDDSMNTMMTIKTIGRQWYWSYEYSDFNNIEFDTYMMPEKELKNGGFRLLEVDNRTILPMNLEIRVMVTASDVI 160
Cdd:MTH00038  81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 237682780 161 HSWTIPSLGIKIDAMPGRLNQSTFSINRPGLFMGQCSEICGTNHSFMPITIESTSVNLFIKWLSKMI 227
Cdd:MTH00038 161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFL 227
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-224 7.98e-110

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 314.61  E-value: 7.98e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780   1 MSTWSNFSLQDSASPMMEQLLFFHDHTMTMLIMITVIVSYSIIYMMKINYTNQNFLHEHMIEMIWTTLPAITLIFIAMPS 80
Cdd:MTH00168   1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780  81 LRLLYLFDDSMNTMMTIKTIGRQWYWSYEYSDFNNIEFDTYMMPEKELKNGGFRLLEVDNRTILPMNLEIRVMVTASDVI 160
Cdd:MTH00168  81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 237682780 161 HSWTIPSLGIKIDAMPGRLNQSTFSINRPGLFMGQCSEICGTNHSFMPITIESTSVNLFIKWLS 224
Cdd:MTH00168 161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVD 224
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-225 2.43e-108

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 311.02  E-value: 2.43e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780   1 MSTWSNFSLQDSASPMMEQLLFFHDHTMTMLIMITVIVSYSIIYMMKINYTNQNFLHEHMIEMIWTTLPAITLIFIAMPS 80
Cdd:MTH00008   1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780  81 LRLLYLFDDSMNTMMTIKTIGRQWYWSYEYSDFNNIEFDTYMMPEKELKNGGFRLLEVDNRTILPMNLEIRVMVTASDVI 160
Cdd:MTH00008  81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 237682780 161 HSWTIPSLGIKIDAMPGRLNQSTFSINRPGLFMGQCSEICGTNHSFMPITIESTSVNLFIKWLSK 225
Cdd:MTH00008 161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSS 225
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-227 1.12e-100

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 291.24  E-value: 1.12e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780   1 MSTWSNFSLQDSASPMMEQLLFFHDHTMTMLIMITVIVSYSIIYMMKINYTNQNFLHEHMIEMIWTTLPAITLIFIAMPS 80
Cdd:MTH00098   1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780  81 LRLLYLFDDSMNTMMTIKTIGRQWYWSYEYSDFNNIEFDTYMMPEKELKNGGFRLLEVDNRTILPMNLEIRVMVTASDVI 160
Cdd:MTH00098  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 237682780 161 HSWTIPSLGIKIDAMPGRLNQSTFSINRPGLFMGQCSEICGTNHSFMPITIESTSVNLFIKWLSKMI 227
Cdd:MTH00098 161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASML 227
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-227 1.43e-100

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 291.23  E-value: 1.43e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780   1 MSTWSNFSLQDSASPMMEQLLFFHDHTMTMLIMITVIVSYSIIYMMKINYTNQNFLHEHMIEMIWTTLPAITLIFIAMPS 80
Cdd:MTH00129   1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780  81 LRLLYLFDDSMNTMMTIKTIGRQWYWSYEYSDFNNIEFDTYMMPEKELKNGGFRLLEVDNRTILPMNLEIRVMVTASDVI 160
Cdd:MTH00129  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 237682780 161 HSWTIPSLGIKIDAMPGRLNQSTFSINRPGLFMGQCSEICGTNHSFMPITIESTSVNLFIKWLSKMI 227
Cdd:MTH00129 161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLML 227
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-226 3.41e-100

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 290.14  E-value: 3.41e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780   1 MSTWSNFSLQDSASPMMEQLLFFHDHTMTMLIMITVIVSYSIIYMMKINYTNQNFLHEHMIEMIWTTLPAITLIFIAMPS 80
Cdd:MTH00076   1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780  81 LRLLYLFDDSMNTMMTIKTIGRQWYWSYEYSDFNNIEFDTYMMPEKELKNGGFRLLEVDNRTILPMNLEIRVMVTASDVI 160
Cdd:MTH00076  81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 237682780 161 HSWTIPSLGIKIDAMPGRLNQSTFSINRPGLFMGQCSEICGTNHSFMPITIESTSVNLFIKWLSKM 226
Cdd:MTH00076 161 HSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSM 226
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-227 6.75e-100

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 289.48  E-value: 6.75e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780   1 MSTWSNFSLQDSASPMMEQLLFFHDHTMTMLIMITVIVSYSIIYMMKINYTNQNFLHEHMIEMIWTTLPAITLIFIAMPS 80
Cdd:MTH00185   1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780  81 LRLLYLFDDSMNTMMTIKTIGRQWYWSYEYSDFNNIEFDTYMMPEKELKNGGFRLLEVDNRTILPMNLEIRVMVTASDVI 160
Cdd:MTH00185  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 237682780 161 HSWTIPSLGIKIDAMPGRLNQSTFSINRPGLFMGQCSEICGTNHSFMPITIESTSVNLFIKWLSKMI 227
Cdd:MTH00185 161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLML 227
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 8-227 1.96e-99

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 288.96  E-value: 1.96e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780   8 SLQDSASPMMEQLLFFHDHTMTMLIMITVIVSYSIIYMMKINYTNQNFLHEHMIEMIWTTLPAITLIFIAMPSLRLLYLF 87
Cdd:MTH00023  17 GFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYLM 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780  88 DDSMNTMMTIKTIGRQWYWSYEYSDFN--NIEFDTYMMPEKELKNGGFRLLEVDNRTILPMNLEIRVMVTASDVIHSWTI 165
Cdd:MTH00023  97 DEVVSPALTIKAIGHQWYWSYEYSDYEgeTLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAV 176

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 237682780 166 PSLGIKIDAMPGRLNQSTFSINRPGLFMGQCSEICGTNHSFMPITIESTSVNLFIKWLSKMI 227
Cdd:MTH00023 177 PSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLSLS 238
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 10-224 6.26e-98

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 284.75  E-value: 6.26e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780  10 QDSASPMMEQLLFFHDHTMTMLIMITVIVSYSIIYMMKINYTNQNFLHEHMIEMIWTTLPAITLIFIAMPSLRLLYLFDD 89
Cdd:MTH00051  12 QDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYLMDE 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780  90 SMNTMMTIKTIGRQWYWSYEYSDF--NNIEFDTYMMPEKELKNGGFRLLEVDNRTILPMNLEIRVMVTASDVIHSWTIPS 167
Cdd:MTH00051  92 VIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPS 171

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 237682780 168 LGIKIDAMPGRLNQSTFSINRPGLFMGQCSEICGTNHSFMPITIESTSVNLFIKWLS 224
Cdd:MTH00051 172 LSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVA 228
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 95-222 2.22e-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: 251.72  E-value: 2.22e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780  95 MTIKTIGRQWYWSYEYSDFNNIEFDTYMMPEKELKNGGFRLLEVDNRTILPMNLEIRVMVTASDVIHSWTIPSLGIKIDA 174
Cdd:cd13912    3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 237682780 175 MPGRLNQSTFSINRPGLFMGQCSEICGTNHSFMPITIESTSVNLFIKW 222
Cdd:cd13912   83 VPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 8.62e-78

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 229.60  E-value: 8.62e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780   95 MTIKTIGRQWYWSYEYSDFNNIEFDTYMMPEKELKNGGFRLLEVDNRTILPMNLEIRVMVTASDVIHSWTIPSLGIKIDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 237682780  175 MPGRLNQSTFSINRPGLFMGQCSEICGTNHSFMPITIEST 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 9-225 3.49e-75

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 227.99  E-value: 3.49e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780   9 LQDSASPMMEQLLFFHDHTMTMLIMITVIVSYSII-YMMKINYTNQ--NFLHEHMIEMIWTTLPAITLIFIAMPSLRLLY 85
Cdd:MTH00027  37 FQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIrILLGNNYYSYywNKLDGSLIEVIWTLIPAFILILIAFPSLRLLY 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780  86 LFDDS-MNTMMTIKTIGRQWYWSYEYSDF--NNIEFDTYMMPEKELKNGGFRLLEVDNRTILPMNLEIRVMVTASDVIHS 162
Cdd:MTH00027 117 IMDECgFSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVLHS 196

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 237682780 163 WTIPSLGIKIDAMPGRLNQSTFSINRPGLFMGQCSEICGTNHSFMPITIESTSVNLFIKWLSK 225
Cdd:MTH00027 197 WTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWIGR 259
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 23-223 2.17e-69

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 212.18  E-value: 2.17e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780  23 FHDHTMTMLIMITVIVSYSIIYMMKINYTNQNFLHEHMIEMIWTTLPAITLIFIAMPSLRLLYLFDdSMNTM--MTIKTI 100
Cdd:MTH00080  25 FNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYG-LMNLDsnLTVKVT 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780 101 GRQWYWSYEYSDFNNIEFDTYMMPEKELKNGGFRLLEVDNRTILPMNLEIRVMVTASDVIHSWTIPSLGIKIDAMPGRLN 180
Cdd:MTH00080 104 GHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILS 183

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 237682780 181 QSTFSINRPGLFMGQCSEICGTNHSFMPITIESTSVNLFIKWL 223
Cdd:MTH00080 184 TLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWC 226
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-226 1.85e-52

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 168.85  E-value: 1.85e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780   6 NFSLQDSASPMMEQLLFFHDHTMTMLIMITVIVSYSIIYMM------KINYTNQNFLHEHMIEMIWTTLPAITLIFIAMP 79
Cdd:COG1622   18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAiryrrrKGDADPAQFHHNTKLEIVWTVIPIIIVIVLAVP 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780  80 SLRLLYLFDDSMNTMMTIKTIGRQWYWSYEYSDFNNiefdtymmpekelknggfrllEVDNRTILPMNLEIRVMVTASDV 159
Cdd:COG1622   98 TLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGI---------------------ATVNELVLPVGRPVRFLLTSADV 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 237682780 160 IHSWTIPSLGIKIDAMPGRLNQSTFSINRPGLFMGQCSEICGTNHSFMPITIESTSVNLFIKWLSKM 226
Cdd:COG1622  157 IHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQ 223
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 32-212 9.66e-43

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 142.79  E-value: 9.66e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780  32 IMITVIVSYSIIYMMKINYTNQNFLHE-HMIEMIWTTLPaiTLIFIAMPSLRLLYLFDDSMNTMM-TIKTIGRQWYWSYE 109
Cdd:MTH00047  19 VFIPCWVYIMLCWQVVSGNGSVNFGSEnQVLELLWTVVP--TLLVLVLCFLNLNFITSDLDCFSSeTIKVIGHQWYWSYE 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780 110 YSdfNNIEFDTYMMpekELKNGgfrlleVDNRTILPMNLEIRVMVTASDVIHSWTIPSLGIKIDAMPGRLNQSTFSINRP 189
Cdd:MTH00047  97 YS--FGGSYDSFMT---DDIFG------VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRH 165

                        170       180
                 ....*....|....*....|...
gi 237682780 190 GLFMGQCSEICGTNHSFMPITIE 212
Cdd:MTH00047 166 GVFVGYCSELCGVGHSYMPIVIE 188
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 13-224 4.03e-40

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: 136.36  E-value: 4.03e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780   13 ASPMMEQLLFFHDHTMTMLIMITVIVSYSIIYMM-----KINYTNQNFLHEHM-IEMIWTTLPA-ITLIFIAMPSLRLLY 85
Cdd:TIGR02866   2 GGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVwkfrrKGDEEKPSQIHGNRrLEYVWTVIPLiIVVGLFAATAKGLLY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780   86 LFDDSMNTMMTIKTIGRQWYWSYEYsdfnniefdtymmpekelKNGGFRlleVDNRTILPMNLEIRVMVTASDVIHSWTI 165
Cdd:TIGR02866  82 LERPIPKDALKVKVTGYQWWWDFEY------------------PESGFT---TVNELVLPAGTPVELQVTSKDVIHSFWV 140

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 237682780  166 PSLGIKIDAMPGRLNQSTFSINRPGLFMGQCSEICGTNHSFMPITIESTSVNLFIKWLS 224
Cdd:TIGR02866 141 PELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 118-215 7.76e-39

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 131.87  E-value: 7.76e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780 118 FDTYMMPEKELKNGGFRLLEVDNRTILPMNLEIRVMVTASDVIHSWTIPSLGIKIDAMPGRLNQSTFSINRPGLFMGQCS 197
Cdd:PTZ00047  51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                         90
                 ....*....|....*...
gi 237682780 198 EICGTNHSFMPITIESTS 215
Cdd:PTZ00047 131 EMCGTLHGFMPIVVEAVS 148
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-212 6.93e-28

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: 101.60  E-value: 6.93e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780  95 MTIKTIGRQWYWSYEYSDfnniefdtymmpekelknggfrlLEVDNRTILPMNLEIRVMVTASDVIHSWTIPSLGIKIDA 174
Cdd:cd13842    1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 237682780 175 MPGRLNQSTFSINRPGLFMGQCSEICGTNHSFMPITIE 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 6.82e-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: 6.82e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780  95 MTIKTIGRQWYWSYEYSDfnniefdtymMPEKELKNGgfrllevdNRTILPMNLEIRVMVTASDVIHSWTIPSLGIKIDA 174
Cdd:cd04213    2 LTIEVTGHQWWWEFRYPD----------EPGRGIVTA--------NELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDM 63

                         90       100       110
                 ....*....|....*....|....*....|...
gi 237682780 175 MPGRLNQSTFSINRPGLFMGQCSEICGTNHSFM 207
Cdd:cd04213   64 IPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-207 9.44e-23

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: 88.47  E-value: 9.44e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780  95 MTIKTIGRQWYWSYEYsdfnniefdtymmPEKELKNGGFRLLEVdNRTILPMNLEIRVMVTASDVIHSWTIPSLGIKIDA 174
Cdd:cd13919    2 LVVEVTAQQWAWTFRY-------------PGGDGKLGTDDDVTS-PELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                         90       100       110
                 ....*....|....*....|....*....|...
gi 237682780 175 MPGRLNQSTFSINRPGLFMGQCSEICGTNHSFM 207
Cdd:cd13919   68 VPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-207 5.58e-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: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 86.53  E-value: 5.58e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780  95 MTIKTIGRQWYWSYEYsdfnniefdtymmpekelKNGgfrlLEVDNRTILPMNLEIRVMVTASDVIHSWTIPSLGIKIDA 174
Cdd:cd13915    2 LEIQVTGRQWMWEFTY------------------PNG----KREINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDV 59

                         90       100       110
                 ....*....|....*....|....*....|...
gi 237682780 175 MPGRLNQSTFSINRPGLFMGQCSEICGTNHSFM 207
Cdd:cd13915   60 VPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-83 2.18e-20

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: 81.99  E-value: 2.18e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780    1 MSTWSNFSLQDSASPMMEQLLFFHDHTMTMLIMITVIVSYsIIYMMKINY-------TNQNFLHEHMIEMIWTTLPAITL 73
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLY-ILVTCLIRFnrrknpiTARYTTHGQTIEIIWTIIPAVIL 79

                          90
                  ....*....|
gi 237682780   74 IFIAMPSLRL 83
Cdd:pfam02790  80 ILIALPSFKL 89
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 96-223 8.34e-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: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 80.92  E-value: 8.34e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780  96 TIKTIGRQWYWSYEYSDFNNIEFdtymmpekelknggfrllevdNRTILPMNLEIRVMVTASDVIHSWTIPSLGIKIDAM 175
Cdd:cd13914    2 EIEVEAYQWGWEFSYPEANVTTS---------------------EQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAF 60

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 237682780 176 PGRLNQSTFSINRPGLFMGQCSEICGTNHSFMPITIESTSVNLFIKWL 223
Cdd:cd13914   61 PGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 83-223 1.38e-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: 75.95  E-value: 1.38e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780  83 LLYLFD---DSMNTMMTIKTIGRQWYWSYEYSdfnniefdtymmpekelkNGGFRLlevdNRTILPMNLEIRVMVTASDV 159
Cdd:cd13918   18 LLYVEDppdEADEDALEVEVEGFQFGWQFEYP------------------NGVTTG----NTLRVPADTPIALRVTSTDV 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 237682780 160 IHSWTIPSLGIKIDAMPGRLNQSTFSINRPGLFMGQCSEICGTNHSFMPITIESTSVNLFIKWL 223
Cdd:cd13918   76 FHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAWY 139
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 144-212 4.44e-09

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: 52.19  E-value: 4.44e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 237682780 144 LPMNLEIRVMVTASDVIHSWTIPSLGIKIDAMPGRLNQSTFSINRPGLFMGQCSEICGTNHSFMPITIE 212
Cdd:cd13913   29 VPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNMYGKII 97
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 96-212 2.68e-06

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


Pssm-ID: 259983 [Multi-domain]  Cd Length: 93  Bit Score: 44.29  E-value: 2.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780  96 TIKTIGRQWYWsyeysdfnniefdtymmpekELKnggfrllevdnRTILPMNLEIRVMVTASDVIHSWTI--PSLGI--K 171
Cdd:cd13916    2 VVAVTGHQWYW--------------------ELS-----------RTEIPAGKPVEFRVTSADVNHGFGIydPDMRLlaQ 50

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 237682780 172 IDAMPGRLNQSTFSINRPGLFMGQCSEICGTNHSFMPITIE 212
Cdd:cd13916   51 TQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVMMAEFT 91
PRK10525 PRK10525
cytochrome o ubiquinol oxidase subunit II; Provisional
 30-225 2.73e-05

cytochrome o ubiquinol oxidase subunit II; Provisional


Pssm-ID: 182518 [Multi-domain]  Cd Length: 315  Bit Score: 44.02  E-value: 2.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780  30 MLIMITVIVSYSIIYMMKINYTNQ------NFLHEHMIEMIWTTLPAITLIFIAMPSLRLLYLFD-----DSMNTMMTIK 98
Cdd:PRK10525  51 MLIVVIPAILMAVGFAWKYRASNKdakyspNWSHSNKVEAVVWTVPILIIIFLAVLTWKTTHALEpskplAHDEKPITIE 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780  99 TIGRQWYWSYEYsdfnniefdtymmPEKELKnggfrlleVDNRTILPMNLEIRVMVTASDVIHSWTIPSLGIKIDAMPGR 178
Cdd:PRK10525 131 VVSMDWKWFFIY-------------PEQGIA--------TVNEIAFPANVPVYFKVTSNSVMNSFFIPRLGSQIYAMAGM 189

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 237682780 179 LNQSTFSINRPGLFMGQCSEICGTNHSFMPIT-IESTSVNLFIKWLSK 225
Cdd:PRK10525 190 QTRLHLIANEPGTYDGISASYSGPGFSGMKFKaIATPDRAEFDQWVAK 237
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 140-207 5.02e-05

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


Pssm-ID: 259874 [Multi-domain]  Cd Length: 99  Bit Score: 40.99  E-value: 5.02e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 237682780 140 NRTILPMNLEIRVMVTASDVIHSWTIPSLGIKIDAMPGRLNQSTFSINRPGLFMGQCSEICGTNHSFM 207
Cdd:cd04212   25 NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDM 92
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 129-212 6.23e-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: 35.28  E-value: 6.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780 129 KNGGFRLLEVDNRTILPMNLEIRVMVT-ASDVIHSWTIPSLGIKIDAM---------------PGRLNQSTFSINRPGLF 192
Cdd:cd00920   12 FTYNGVLLFGPPVLVVPVGDTVRVQFVnKLGENHSVTIAGFGVPVVAMagganpglvntlvigPGESAEVTFTTDQAGVY 91

                         90       100
                 ....*....|....*....|
gi 237682780 193 MGQCSEICGtNHSFMPITIE 212
Cdd:cd00920   92 WFYCTIPGH-NHAGMVGTIN 110
PRK02888 PRK02888
nitrous-oxide reductase; Validated
 120-207 7.39e-03

nitrous-oxide reductase; Validated


Pssm-ID: 235082 [Multi-domain]  Cd Length: 635  Bit Score: 36.88  E-value: 7.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237682780 120 TYMMPEKELKNGgfrllevDNRTILPMNLEirvmvTASDVIHSWTIPSLGIKIDAMPGRLNQSTFSINRPGLFMGQCSEI 199
Cdd:PRK02888 551 AFGLREFTVKQG-------DEVTVIVTNLD-----KVEDLTHGFAIPNYGVNMEVAPQATASVTFTADKPGVYWYYCTWF 618


                 ....*...
gi 237682780 200 CGTNHSFM 207
Cdd:PRK02888 619 CHALHMEM 626
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 149-207 8.06e-03

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: 34.52  E-value: 8.06e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 237682780 149 EIRVMVT----ASDVIHSWTIPSLGIKIDAMPGRLNQSTFSINRPGLFMGQCSEICGTNHSFM 207
Cdd:cd04223   25 EVTVHLTnleqDEDITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALHLEM 87
 
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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