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Conserved domains on  [gi|1181491983|ref|YP_009353877|]
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cytochrome c oxidase subunit II (mitochondrion) [Tropidomya abbreviata]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11475917)

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 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-294 6.94e-78

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 236.37  E-value: 6.94e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983   1 MSRSGQLLFIDPVSIVMAKLVDFHDATLFLVLMVCLLVLGVIFSALCGSPHFRSISESQVLEVLWTTIPMFFLVFLAVPS 80
Cdd:MTH00140    1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983  81 FMNLYFMEDSEDPFVMIKVTGHQWYWSYgynlswftltkagdvmpdiydrlvsgqELSSVSKMDivplskpgrssgtvay 160
Cdd:MTH00140   81 LRLLYLLDETNNPLLTVKAIGHQWYWSY---------------------------EYSDFSVIE---------------- 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983 161 svtlndyvilpwdgvvekeesiefgFDSYIKSEDELLVGDYRLLEVDSRMVVPVNKVVNLAVSSADVLHCWTVYGTGLKV 240
Cdd:MTH00140  118 -------------------------FDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVPSLGVKV 172

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1181491983 241 DAVPGRVNLMTFVGLRTGIYYGQCSELCGINHSFMPIVMEVVPKDSFMSWLVSV 294
Cdd:MTH00140  173 DAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELM 226
 
Name Accession Description Interval E-value
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-294 6.94e-78

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 236.37  E-value: 6.94e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983   1 MSRSGQLLFIDPVSIVMAKLVDFHDATLFLVLMVCLLVLGVIFSALCGSPHFRSISESQVLEVLWTTIPMFFLVFLAVPS 80
Cdd:MTH00140    1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983  81 FMNLYFMEDSEDPFVMIKVTGHQWYWSYgynlswftltkagdvmpdiydrlvsgqELSSVSKMDivplskpgrssgtvay 160
Cdd:MTH00140   81 LRLLYLLDETNNPLLTVKAIGHQWYWSY---------------------------EYSDFSVIE---------------- 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983 161 svtlndyvilpwdgvvekeesiefgFDSYIKSEDELLVGDYRLLEVDSRMVVPVNKVVNLAVSSADVLHCWTVYGTGLKV 240
Cdd:MTH00140  118 -------------------------FDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVPSLGVKV 172

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1181491983 241 DAVPGRVNLMTFVGLRTGIYYGQCSELCGINHSFMPIVMEVVPKDSFMSWLVSV 294
Cdd:MTH00140  173 DAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELM 226
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-290 1.48e-58

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: 183.54  E-value: 1.48e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983  93 PFVMIKVTGHQWYWSYGYNlswftltkagdvmpdiydrlvsgqelssvskmDIVPLSkpgrssgtvaysvtlndyvilpw 172
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYS--------------------------------DFNDLE----------------------- 25

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983 173 dgvvekeesiefgFDSYIKSEDELLVGDYRLLEVDSRMVVPVNKVVNLAVSSADVLHCWTVYGTGLKVDAVPGRVNLMTF 252
Cdd:cd13912    26 -------------FDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDAVPGRLNQTSF 92

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1181491983 253 VGLRTGIYYGQCSELCGINHSFMPIVMEVVPKDSFMSW 290
Cdd:cd13912    93 FIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
97-282 1.79e-43

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 144.86  E-value: 1.79e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983  97 IKVTGHQWYWSYGYNlswftltkagdvmpdiydrlvsgqelssvskmdivplskpgrssgtvaysvtlnDYVILpwdgvv 176
Cdd:pfam00116   3 IKAIGHQWYWSYEYT------------------------------------------------------DFGDL------ 22

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983 177 ekeesiefGFDSYIKSEDELLVGDYRLLEVDSRMVVPVNKVVNLAVSSADVLHCWTVYGTGLKVDAVPGRVNLMTFVGLR 256
Cdd:pfam00116  23 --------EFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDAVPGRLNQTSFSIDR 94

                         170       180
                  ....*....|....*....|....*.
gi 1181491983 257 TGIYYGQCSELCGINHSFMPIVMEVV 282
Cdd:pfam00116  95 EGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
55-291 1.12e-37

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 133.42  E-value: 1.12e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983  55 ISESQVLEVLWTTIPMFFLVFLAVPSFMNLYFMEDSEDPFVMIKVTGHQWYWSYGYnlswftltkagdvmPDiydrlvsg 134
Cdd:COG1622    73 FHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRY--------------PD-------- 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983 135 qelssvskmdivplskpgrssgtvaysvtlndyvilpwDGVVekeesiefgfdsyiksedellvgdyrlleVDSRMVVPV 214
Cdd:COG1622   131 --------------------------------------QGIA-----------------------------TVNELVLPV 143

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1181491983 215 NKVVNLAVSSADVLHCWTVYGTGLKVDAVPGRVNLMTFVGLRTGIYYGQCSELCGINHSFMPIVMEVVPKDSFMSWL 291
Cdd:COG1622   144 GRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWL 220
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 54-291 2.98e-27

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


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 105.16  E-value: 2.98e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983  54 SISESQVLEVLWTTIPMFFLVFLAVPSFMN-LYFMEDSEDPFVMIKVTGHQWYWSYGYNLSWFTltkagdvmpdiydrlv 132
Cdd:TIGR02866  49 QIHGNRRLEYVWTVIPLIIVVGLFAATAKGlLYLERPIPKDALKVKVTGYQWWWDFEYPESGFT---------------- 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983 133 SGQELssvskmdivplskpgrssgtvaysvtlndyvilpwdgvvekeesiefgfdsyiksedellvgdyrllevdsrmVV 212
Cdd:TIGR02866 113 TVNEL-------------------------------------------------------------------------VL 119

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1181491983 213 PVNKVVNLAVSSADVLHCWTVYGTGLKVDAVPGRVNLMTFVGLRTGIYYGQCSELCGINHSFMPIVMEVVPKDSFMSWL 291
Cdd:TIGR02866 120 PAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYV 198
 
Name Accession Description Interval E-value
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-294 6.94e-78

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 236.37  E-value: 6.94e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983   1 MSRSGQLLFIDPVSIVMAKLVDFHDATLFLVLMVCLLVLGVIFSALCGSPHFRSISESQVLEVLWTTIPMFFLVFLAVPS 80
Cdd:MTH00140    1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983  81 FMNLYFMEDSEDPFVMIKVTGHQWYWSYgynlswftltkagdvmpdiydrlvsgqELSSVSKMDivplskpgrssgtvay 160
Cdd:MTH00140   81 LRLLYLLDETNNPLLTVKAIGHQWYWSY---------------------------EYSDFSVIE---------------- 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983 161 svtlndyvilpwdgvvekeesiefgFDSYIKSEDELLVGDYRLLEVDSRMVVPVNKVVNLAVSSADVLHCWTVYGTGLKV 240
Cdd:MTH00140  118 -------------------------FDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVPSLGVKV 172

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1181491983 241 DAVPGRVNLMTFVGLRTGIYYGQCSELCGINHSFMPIVMEVVPKDSFMSWLVSV 294
Cdd:MTH00140  173 DAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELM 226
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-293 6.23e-76

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 231.41  E-value: 6.23e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983   1 MSRSGQLLFIDPVSIVMAKLVDFHDATLFLVLMVCLLVLGVIFSALCGSPHFRSISESQVLEVLWTTIPMFFLVFLAVPS 80
Cdd:MTH00168    1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983  81 FMNLYFMEDSEDPFVMIKVTGHQWYWSYGYNlswftltkagdvmpdiydrlvsgqelssvskmdivplskpgrssgtvay 160
Cdd:MTH00168   81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYT------------------------------------------------- 111

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983 161 svtlnDYvilpwdgvvekeesIEFGFDSYIKSEDELLVGDYRLLEVDSRMVVPVNKVVNLAVSSADVLHCWTVYGTGLKV 240
Cdd:MTH00168  112 -----DY--------------NDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSWTLPSLGLKM 172

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1181491983 241 DAVPGRVNLMTFVGLRTGIYYGQCSELCGINHSFMPIVMEVVPKDSFMSWLVS 293
Cdd:MTH00168  173 DAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVDS 225
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-293 1.08e-74

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 228.17  E-value: 1.08e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983   1 MSRSGQLLFIDPVSIVMAKLVDFHDATLFLVLMVCLLVLGVIFSALCGSPHFRSISESQVLEVLWTTIPMFFLVFLAVPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983  81 FMNLYFMEDSEDPFVMIKVTGHQWYWSYGYNlswftltkagdvmpdiydrlvsgqelssvskmdivplskpgrssgtvay 160
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYS------------------------------------------------- 111

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983 161 svtlndyvilpwdgvvekeESIEFGFDSYIKSEDELLVGDYRLLEVDSRMVVPVNKVVNLAVSSADVLHCWTVYGTGLKV 240
Cdd:MTH00154  112 -------------------DFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKV 172

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1181491983 241 DAVPGRVNLMTFVGLRTGIYYGQCSELCGINHSFMPIVMEVVPKDSFMSWLVS 293
Cdd:MTH00154  173 DAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKN 225
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-291 3.36e-72

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 221.90  E-value: 3.36e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983   1 MSRSGQLLFIDPVSIVMAKLVDFHDATLFLVLMVCLLVLGVIFSALCGSPHFRSISESQVLEVLWTTIPMFFLVFLAVPS 80
Cdd:MTH00139    1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983  81 FMNLYFMEDSEDPFVMIKVTGHQWYWSYgynlswftltkagdvmpdiydrlvsgqELSSVSKMdivplskpgrssgtvay 160
Cdd:MTH00139   81 LRLLYLMDEVSDPYLTFKAVGHQWYWSY---------------------------EYSDFKNL----------------- 116

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983 161 svtlndyvilpwdgvvekeesiefGFDSYIKSEDELLVGDYRLLEVDSRMVVPVNKVVNLAVSSADVLHCWTVYGTGLKV 240
Cdd:MTH00139  117 ------------------------SFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSWTVPSLGVKI 172

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1181491983 241 DAVPGRVNLMTFVGLRTGIYYGQCSELCGINHSFMPIVMEVVPKDSFMSWL 291
Cdd:MTH00139  173 DAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWI 223
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-290 1.97e-70

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 217.65  E-value: 1.97e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983   1 MSRSGQLLFIDPVSIVMAKLVDFHDATLFLVLMVCLLVLGVIFSALCGSPHFRSISESQVLEVLWTTIPMFFLVFLAVPS 80
Cdd:MTH00038    1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983  81 FMNLYFMEDSEDPFVMIKVTGHQWYWSYGYnlswftltkagdvmpdiydrlvsgqelssvskmdivplskpgrssgtvay 160
Cdd:MTH00038   81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEY-------------------------------------------------- 110

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983 161 svtlndyvilpWDgvvekEESIEFgfDSYIKSEDELLVGDYRLLEVDSRMVVPVNKVVNLAVSSADVLHCWTVYGTGLKV 240
Cdd:MTH00038  111 -----------TD-----YNDLEF--DSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLHSWAVPSLGVKM 172

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1181491983 241 DAVPGRVNLMTFVGLRTGIYYGQCSELCGINHSFMPIVMEVVPKDSFMSW 290
Cdd:MTH00038  173 DAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENW 222
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-293 7.50e-68

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 210.93  E-value: 7.50e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983   1 MSRSGQLLFIDPVSIVMAKLVDFHDATLFLVLMVCLLVLGVIFSALCGSPHFRSISESQVLEVLWTTIPMFFLVFLAVPS 80
Cdd:MTH00117    1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983  81 FMNLYFMEDSEDPFVMIKVTGHQWYWSYGYNlswftltkagdvmpdiydrlvsgqelssvskmDIVPLSkpgrssgtvay 160
Cdd:MTH00117   81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYT--------------------------------DYKDLS----------- 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983 161 svtlndyvilpwdgvvekeesiefgFDSYIKSEDELLVGDYRLLEVDSRMVVPVNKVVNLAVSSADVLHCWTVYGTGLKV 240
Cdd:MTH00117  118 -------------------------FDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVPSLGVKT 172

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1181491983 241 DAVPGRVNLMTFVGLRTGIYYGQCSELCGINHSFMPIVMEVVPKDSFMSWLVS 293
Cdd:MTH00117  173 DAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSL 225
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-293 1.14e-64

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 202.78  E-value: 1.14e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983   1 MSRSGQLLFIDPVSIVMAKLVDFHDATLFLVLMVCLLVLGVIFSALCGSPHFRSISESQVLEVLWTTIPMFFLVFLAVPS 80
Cdd:MTH00008    1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983  81 FMNLYFMEDSEDPFVMIKVTGHQWYWSYGYnlswftltkagdvmpdiydrlvsgqelSSVSKMDivplskpgrssgtvay 160
Cdd:MTH00008   81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEY---------------------------SDFSNLE---------------- 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983 161 svtlndyvilpwdgvvekeesiefgFDSYIKSEDELLVGDYRLLEVDSRMVVPVNKVVNLAVSSADVLHCWTVYGTGLKV 240
Cdd:MTH00008  118 -------------------------FDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKV 172

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1181491983 241 DAVPGRVNLMTFVGLRTGIYYGQCSELCGINHSFMPIVMEVVPKDSFMSWLVS 293
Cdd:MTH00008  173 DAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSS 225
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 6-296 8.43e-62

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 195.74  E-value: 8.43e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983   6 QLLFIDPVSIVMAKLVDFHDATLFLVLMVCLLVLGVIFSALCGSPHFRSISESQVLEVLWTTIPMFFLVFLAVPSFMNLY 85
Cdd:MTH00023   15 QLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLY 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983  86 FMEDSEDPFVMIKVTGHQWYWSYGYNlswftltkagdvmpdiydrlvsgqelssvskmdivplskpgrssgtvaysvtln 165
Cdd:MTH00023   95 LMDEVVSPALTIKAIGHQWYWSYEYS------------------------------------------------------ 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983 166 DYvilpwdgvveKEESIEFgfDSYIKSEDELLVGDYRLLEVDSRMVVPVNKVVNLAVSSADVLHCWTVYGTGLKVDAVPG 245
Cdd:MTH00023  121 DY----------EGETLEF--DSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVPSLGLKIDAVPG 188

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1181491983 246 RVNLMTFVGLRTGIYYGQCSELCGINHSFMPIVMEVVPKDSFMSWLVSVYN 296
Cdd:MTH00023  189 RLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLSLSN 239
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-290 3.89e-59

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 188.77  E-value: 3.89e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983   1 MSRSGQLLFIDPVSIVMAKLVDFHDATLFLVLMVCLLVLGVIFSALCGSPHFRSISESQVLEVLWTTIPMFFLVFLAVPS 80
Cdd:MTH00129    1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983  81 FMNLYFMEDSEDPFVMIKVTGHQWYWSYGYNlswftltkagdvmpdiydrlvsgqelssvskmdivplskpgrssgtvay 160
Cdd:MTH00129   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYT------------------------------------------------- 111

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983 161 svtlnDYVilpwdgvvekeesiEFGFDSYIKSEDELLVGDYRLLEVDSRMVVPVNKVVNLAVSSADVLHCWTVYGTGLKV 240
Cdd:MTH00129  112 -----DYE--------------DLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVPALGVKM 172

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1181491983 241 DAVPGRVNLMTFVGLRTGIYYGQCSELCGINHSFMPIVMEVVPKDSFMSW 290
Cdd:MTH00129  173 DAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-295 4.16e-59

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 188.39  E-value: 4.16e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983   1 MSRSGQLLFIDPVSIVMAKLVDFHDATLFLVLMVCLLVLGVIFSALCGSPHFRSISESQVLEVLWTTIPMFFLVFLAVPS 80
Cdd:MTH00098    1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983  81 FMNLYFMEDSEDPFVMIKVTGHQWYWSYGYnlswftlTKAGDVMpdiydrlvsgqelssvskmdivplskpgrssgtvay 160
Cdd:MTH00098   81 LRILYMMDEINNPSLTVKTMGHQWYWSYEY-------TDYEDLS------------------------------------ 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983 161 svtlndyvilpwdgvvekeesiefgFDSYIKSEDELLVGDYRLLEVDSRMVVPVNKVVNLAVSSADVLHCWTVYGTGLKV 240
Cdd:MTH00098  118 -------------------------FDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKT 172

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1181491983 241 DAVPGRVNLMTFVGLRTGIYYGQCSELCGINHSFMPIVMEVVPKDSFMSWLVSVY 295
Cdd:MTH00098  173 DAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASML 227
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-290 1.48e-58

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: 183.54  E-value: 1.48e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983  93 PFVMIKVTGHQWYWSYGYNlswftltkagdvmpdiydrlvsgqelssvskmDIVPLSkpgrssgtvaysvtlndyvilpw 172
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYS--------------------------------DFNDLE----------------------- 25

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983 173 dgvvekeesiefgFDSYIKSEDELLVGDYRLLEVDSRMVVPVNKVVNLAVSSADVLHCWTVYGTGLKVDAVPGRVNLMTF 252
Cdd:cd13912    26 -------------FDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDAVPGRLNQTSF 92

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1181491983 253 VGLRTGIYYGQCSELCGINHSFMPIVMEVVPKDSFMSW 290
Cdd:cd13912    93 FIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-294 2.29e-58

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 186.63  E-value: 2.29e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983   1 MSRSGQLLFIDPVSIVMAKLVDFHDATLFLVLMVCLLVLGVIFSALCGSPHFRSISESQVLEVLWTTIPMFFLVFLAVPS 80
Cdd:MTH00185    1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983  81 FMNLYFMEDSEDPFVMIKVTGHQWYWSYGYNlswftltkagdvmpdiydrlvsgqelssvskmdivplskpgrssgtvay 160
Cdd:MTH00185   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYT------------------------------------------------- 111

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983 161 svtlnDYVilpwdgvvekeesiEFGFDSYIKSEDELLVGDYRLLEVDSRMVVPVNKVVNLAVSSADVLHCWTVYGTGLKV 240
Cdd:MTH00185  112 -----DYE--------------QLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVPALGVKM 172

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1181491983 241 DAVPGRVNLMTFVGLRTGIYYGQCSELCGINHSFMPIVMEVVPKDSFMSWLVSV 294
Cdd:MTH00185  173 DAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLM 226
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-293 2.82e-56

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 181.52  E-value: 2.82e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983   1 MSRSGQLLFIDPVSIVMAKLVDFHDATLFLVLMVCLLVLGVIFSALCGSPHFRSISESQVLEVLWTTIPMFFLVFLAVPS 80
Cdd:MTH00076    1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983  81 FMNLYFMEDSEDPFVMIKVTGHQWYWSYGYNlswftltkagdvmpdiydrlvsgqelssvskmdivplskpgrssgtvay 160
Cdd:MTH00076   81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYT------------------------------------------------- 111

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983 161 svtlnDYVILpwdgvvekeesiefGFDSYIKSEDELLVGDYRLLEVDSRMVVPVNKVVNLAVSSADVLHCWTVYGTGLKV 240
Cdd:MTH00076  112 -----DYEDL--------------SFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSLGIKT 172

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1181491983 241 DAVPGRVNLMTFVGLRTGIYYGQCSELCGINHSFMPIVMEVVPKDSFMSWLVS 293
Cdd:MTH00076  173 DAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSS 225
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 6-293 6.38e-56

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 180.75  E-value: 6.38e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983   6 QLLFIDPVSIVMAKLVDFHDATLFLVLMVCLLVLGVIFSALCGSPHFRSISESQVLEVLWTTIPMFFLVFLAVPSFMNLY 85
Cdd:MTH00051    8 QLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLY 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983  86 FMEDSEDPFVMIKVTGHQWYWSYGYNlswftltkagdvmpdiydrlvsgqelssvskmdivplskpgrssgtvaysvtln 165
Cdd:MTH00051   88 LMDEVIDPALTIKAIGHQWYWSYEYS------------------------------------------------------ 113

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983 166 DYvilpwdgvveKEESIEFgfDSYIKSEDELLVGDYRLLEVDSRMVVPVNKVVNLAVSSADVLHCWTVYGTGLKVDAVPG 245
Cdd:MTH00051  114 DY----------GTDTIEF--DSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPSLSVKIDAVPG 181

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1181491983 246 RVNLMTFVGLRTGIYYGQCSELCGINHSFMPIVMEVVPKDSFMSWLVS 293
Cdd:MTH00051  182 RLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVAT 229
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 56-293 1.61e-45

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 153.63  E-value: 1.61e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983  56 SESQVLEVLWTTIPMFFLVFLAVPSFMNLYFME----DSEdpfVMIKVTGHQWYWSYGYnlswftltkagdvmPDIydrl 131
Cdd:MTH00080   58 IEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGlmnlDSN---LTVKVTGHQWYWSYEF--------------SDI---- 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983 132 vsgqelssvskmdivplskPGRSsgtvaysvtlndyvilpwdgvvekeesiefgFDSYIKSEDELLVGDYRLLEVDSRMV 211
Cdd:MTH00080  117 -------------------PGLE-------------------------------FDSYMKSLDQLRLGEPRLLEVDNRCV 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983 212 VPVNKVVNLAVSSADVLHCWTVYGTGLKVDAVPGRVNLMTFVGLRTGIYYGQCSELCGINHSFMPIVMEVVPKDSFMSWL 291
Cdd:MTH00080  147 LPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWC 226


                  ..
gi 1181491983 292 VS 293
Cdd:MTH00080  227 KL 228
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 6-291 1.73e-44

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 152.10  E-value: 1.73e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983   6 QLLFIDPVSIVMAKLVDFHDATLFLVLMVCLLVLGVIFSALCGSPHFR---SISESQVLEVLWTTIPMFFLVFLAVPSFM 82
Cdd:MTH00027   34 QLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLGNNYYSyywNKLDGSLIEVIWTLIPAFILILIAFPSLR 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983  83 NLYFMEDSE-DPFVMIKVTGHQWYWSYGYNlswftltkagdvmpdiydrlvsgqelssvskmdivplskpgrssgtvays 161
Cdd:MTH00027  114 LLYIMDECGfSANITIKVTGHQWYWSYSYE-------------------------------------------------- 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983 162 vtlnDYvilpwdgvveKEESIEFgfDSYIKSEDELLVGDYRLLEVDSRMVVPVNKVVNLAVSSADVLHCWTVYGTGLKVD 241
Cdd:MTH00027  144 ----DY----------GEKNIEF--DSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVLHSWTVPSLAVKMD 207

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1181491983 242 AVPGRVNLMTFVGLRTGIYYGQCSELCGINHSFMPIVMEVVPKDSFMSWL 291
Cdd:MTH00027  208 AVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWI 257
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
97-282 1.79e-43

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 144.86  E-value: 1.79e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983  97 IKVTGHQWYWSYGYNlswftltkagdvmpdiydrlvsgqelssvskmdivplskpgrssgtvaysvtlnDYVILpwdgvv 176
Cdd:pfam00116   3 IKAIGHQWYWSYEYT------------------------------------------------------DFGDL------ 22

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983 177 ekeesiefGFDSYIKSEDELLVGDYRLLEVDSRMVVPVNKVVNLAVSSADVLHCWTVYGTGLKVDAVPGRVNLMTFVGLR 256
Cdd:pfam00116  23 --------EFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDAVPGRLNQTSFSIDR 94

                         170       180
                  ....*....|....*....|....*.
gi 1181491983 257 TGIYYGQCSELCGINHSFMPIVMEVV 282
Cdd:pfam00116  95 EGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
55-291 1.12e-37

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 133.42  E-value: 1.12e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983  55 ISESQVLEVLWTTIPMFFLVFLAVPSFMNLYFMEDSEDPFVMIKVTGHQWYWSYGYnlswftltkagdvmPDiydrlvsg 134
Cdd:COG1622    73 FHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRY--------------PD-------- 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983 135 qelssvskmdivplskpgrssgtvaysvtlndyvilpwDGVVekeesiefgfdsyiksedellvgdyrlleVDSRMVVPV 214
Cdd:COG1622   131 --------------------------------------QGIA-----------------------------TVNELVLPV 143

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1181491983 215 NKVVNLAVSSADVLHCWTVYGTGLKVDAVPGRVNLMTFVGLRTGIYYGQCSELCGINHSFMPIVMEVVPKDSFMSWL 291
Cdd:COG1622   144 GRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWL 220
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 184-287 8.44e-30

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 110.68  E-value: 8.44e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983 184 FGFDSYIKSEDELLVGDYRLLEVDSRMVVPVNKVVNLAVSSADVLHCWTVYGTGLKVDAVPGR-VNLMTFVgLRTGIYYG 262
Cdd:PTZ00047   49 YSFQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRlHKINTFI-LREGVFYG 127

                          90       100
                  ....*....|....*....|....*
gi 1181491983 263 QCSELCGINHSFMPIVMEVVPKDSF 287
Cdd:PTZ00047  128 QCSEMCGTLHGFMPIVVEAVSPEAY 152
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 54-291 2.98e-27

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


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 105.16  E-value: 2.98e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983  54 SISESQVLEVLWTTIPMFFLVFLAVPSFMN-LYFMEDSEDPFVMIKVTGHQWYWSYGYNLSWFTltkagdvmpdiydrlv 132
Cdd:TIGR02866  49 QIHGNRRLEYVWTVIPLIIVVGLFAATAKGlLYLERPIPKDALKVKVTGYQWWWDFEYPESGFT---------------- 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983 133 SGQELssvskmdivplskpgrssgtvaysvtlndyvilpwdgvvekeesiefgfdsyiksedellvgdyrllevdsrmVV 212
Cdd:TIGR02866 113 TVNEL-------------------------------------------------------------------------VL 119

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1181491983 213 PVNKVVNLAVSSADVLHCWTVYGTGLKVDAVPGRVNLMTFVGLRTGIYYGQCSELCGINHSFMPIVMEVVPKDSFMSWL 291
Cdd:TIGR02866 120 PAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYV 198
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 56-286 1.27e-26

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 103.11  E-value: 1.27e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983  56 SESQVLEVLWTTIPMFFLVFLAvpsFMNLYFM-EDSED-PFVMIKVTGHQWYWSYGYnlswftltkagdvmpdiydrlvs 133
Cdd:MTH00047   44 SENQVLELLWTVVPTLLVLVLC---FLNLNFItSDLDCfSSETIKVIGHQWYWSYEY----------------------- 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983 134 gqelssvskmdivplskpgrssgtvaysvtlndyvilpwdgvvekeeSIEFGFDSYiksedelLVGDYRLleVDSRMVVP 213
Cdd:MTH00047   98 -----------------------------------------------SFGGSYDSF-------MTDDIFG--VDKPLRLV 121

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1181491983 214 VNKVVNLAVSSADVLHCWTVYGTGLKVDAVPGRVNLMTFVGLRTGIYYGQCSELCGINHSFMPIVMEVVPKDS 286
Cdd:MTH00047  122 YGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVVDVDS 194
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 200-280 1.26e-21

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: 86.97  E-value: 1.26e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983 200 DYRLLEVDSRMVVPVNKVVNLAVSSADVLHCWTVYGTGLKVDAVPGRVNLMTFVGLRTGIYYGQCSELCGINHSFMPIVM 279
Cdd:cd13842    15 IYPNVRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDAVPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKV 94


                  .
gi 1181491983 280 E 280
Cdd:cd13842    95 E 95
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 207-291 9.41e-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: 77.06  E-value: 9.41e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983 207 DSRMVVPVNKVVNLAVSSADVLHCWTVYGTGLKVDAVPGRVNLMTFVGLRTGIYYGQCSELCGINHSFMPIVMEVVPKDS 286
Cdd:cd13914    24 SEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAFPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDE 103


                  ....*
gi 1181491983 287 FMSWL 291
Cdd:cd13914   104 YQQWL 108
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 210-275 1.87e-17

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: 76.12  E-value: 1.87e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1181491983 210 MVVPVNKVVNLAVSSADVLHCWTVYGTGLKVDAVPGRVNLMTFVGLRTGIYYGQCSELCGINHSFM 275
Cdd:cd04213    31 LHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDMIPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 160-291 5.05e-16

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


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 73.26  E-value: 5.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983 160 YSVTLndYVILPWDGVVEKEESIE---FGFDSYIKSEDELLVGDYrllevdsrMVVPVNKVVNLAVSSADVLHCWTVYGT 236
Cdd:cd13918    15 YGMLL--YVEDPPDEADEDALEVEvegFQFGWQFEYPNGVTTGNT--------LRVPADTPIALRVTSTDVFHTFGIPEL 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1181491983 237 GLKVDAVPGRVNLMTFVGLRTGIYYGQCSELCGINHSFMPIVMEVVPKDSFMSWL 291
Cdd:cd13918    85 RVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAWY 139
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 207-281 3.66e-15

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


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 69.58  E-value: 3.66e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1181491983 207 DSRMVVPVNKVVNLAVSSADVLHCWTVYGTGLKVDAVPGRVNLMTFVGLRTGIYYGQCSELCGINHSFMPIVMEV 281
Cdd:cd13915    24 INELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDVVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGMIGKVRV 98
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 210-282 7.15e-15

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


Pssm-ID: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 69.21  E-value: 7.15e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1181491983 210 MVVPVNKVVNLAVSSADVLHCWTVYGTGLKVDAVPGRVNLMTFVGLRTGIYYGQCSELCGINHSFMPIVMEVV 282
Cdd:cd13919    35 LHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDAVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRMRATVKVV 107
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 208-282 4.03e-11

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: 58.74  E-value: 4.03e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1181491983 208 SRMVVPVNKVVNLAVSSADVLHCWTVYGTGLKVDAVPGRVNLMTFVGLRTGIYYGQCSELCGINHSFMPIVMEVV 282
Cdd:cd13913    25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNMYGKIIVE 99
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 208-282 1.29e-08

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: 51.61  E-value: 1.29e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1181491983 208 SRMVVPVNKVVNLAVSSADVLHCWTVYGTGLK----VDAVPGRVNLMTFVGLRTGIYYGQCSELCGINHSFMPIVMEVV 282
Cdd:cd13916    15 SRTEIPAGKPVEFRVTSADVNHGFGIYDPDMRllaqTQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVMMAEFTVV 93
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-81 1.92e-05

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: 42.32  E-value: 1.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491983   1 MSRSGQLLFIDPVSIVMAKLVDFHDATLFLVLMVCLLVLGVIFSALCGSPH------FRSISESQVLEVLWTTIPMFFLV 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRFNRrknpitARYTTHGQTIEIIWTIIPAVILI 80


                  ....*..
gi 1181491983  75 FLAVPSF 81
Cdd:pfam02790  81 LIALPSF 87
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 202-275 2.26e-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: 259984 [Multi-domain]  Cd Length: 88  Bit Score: 39.28  E-value: 2.26e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1181491983 202 RLLEVDSRMVVPVNKVVNLAVSSADVLHCWTVYGTGLKVDAVPGRVNLMTFVGLRTGIYYGQCSELCGINHSFM 275
Cdd:cd13917     8 RAWQWRPVLVLKKGKTYRLHLSSLDVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIICNEYCGIGHHTM 81
 
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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