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Conserved domains on  [gi|378745285|gb|AFC36275|]
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cytochrome oxidase subunit II, partial (mitochondrion) [Chiastocheta setifera]

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
 1-159 3.70e-112

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 317.54  E-value: 3.70e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378745285   1 NLGLQDSSSPLMEQLIFFHDHALLILVMTTVLVGYLMFMLFFNKYVNRYLLHGQTIEIIWTILPAIVLLFIAFPSLRLLY 80
Cdd:MTH00154   6 NLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLY 85

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 378745285  81 LLDEINEPAITLKAIGHQWYWSYEYSDFVNVEFDSYMIPTNELSIDNFRLLDVDNRVVIPMNSQIRILVTAADVIHSWT 159
Cdd:MTH00154  86 LLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWT 164
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-159 3.70e-112

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 317.54  E-value: 3.70e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378745285   1 NLGLQDSSSPLMEQLIFFHDHALLILVMTTVLVGYLMFMLFFNKYVNRYLLHGQTIEIIWTILPAIVLLFIAFPSLRLLY 80
Cdd:MTH00154   6 NLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLY 85

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 378745285  81 LLDEINEPAITLKAIGHQWYWSYEYSDFVNVEFDSYMIPTNELSIDNFRLLDVDNRVVIPMNSQIRILVTAADVIHSWT 159
Cdd:MTH00154  86 LLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWT 164
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 88-159 3.45e-48

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: 151.95  E-value: 3.45e-48
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 378745285  88 PAITLKAIGHQWYWSYEYSDFVNVEFDSYMIPTNELSIDNFRLLDVDNRVVIPMNSQIRILVTAADVIHSWT 159
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWA 72
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
90-159 1.29e-40

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 132.53  E-value: 1.29e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378745285   90 ITLKAIGHQWYWSYEYSDFVNVEFDSYMIPTNELSIDNFRLLDVDNRVVIPMNSQIRILVTAADVIHSWT 159
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWA 70
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-158 1.40e-27

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 102.21  E-value: 1.40e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378745285   1 NLGLQDSSSPLMEQLIFFHDHALLILVMTTVLVGYLM--FMLFF----NKYVNRYLLHGQTIEIIWTILPAIVLLFIAFP 74
Cdd:COG1622   18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLlyFAIRYrrrkGDADPAQFHHNTKLEIVWTVIPIIIVIVLAVP 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378745285  75 SLRLLYLLDEINEPAITLKAIGHQWYWSYEYSDFVNVefdsymiptnelsidnfrlldVDNRVVIPMNSQIRILVTAADV 154
Cdd:COG1622   98 TLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVNELVLPVGRPVRFLLTSADV 156


                 ....
gi 378745285 155 IHSW 158
Cdd:COG1622  157 IHSF 160
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 9-158 3.13e-21

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: 85.12  E-value: 3.13e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378745285    9 SPLMEQLifFHDHALLILVMTTV-LVGYLMFMLFFNKYVNR-------YLLHGQTIEIIWTILPA-IVLLFIAFPSLRLL 79
Cdd:TIGR02866   3 GEIAQQI--AFLFLFVLAVSTLIsLLVAALLAYVVWKFRRKgdeekpsQIHGNRRLEYVWTVIPLiIVVGLFAATAKGLL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 378745285   80 YLLDEINEPAITLKAIGHQWYWSYEYSDFvnvefdsymiptnelsidnfrLLDVDNRVVIPMNSQIRILVTAADVIHSW 158
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSF 138
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-159 3.70e-112

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 317.54  E-value: 3.70e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378745285   1 NLGLQDSSSPLMEQLIFFHDHALLILVMTTVLVGYLMFMLFFNKYVNRYLLHGQTIEIIWTILPAIVLLFIAFPSLRLLY 80
Cdd:MTH00154   6 NLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLY 85

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 378745285  81 LLDEINEPAITLKAIGHQWYWSYEYSDFVNVEFDSYMIPTNELSIDNFRLLDVDNRVVIPMNSQIRILVTAADVIHSWT 159
Cdd:MTH00154  86 LLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWT 164
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 2-159 1.95e-89

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 259.87  E-value: 1.95e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378745285   2 LGLQDSSSPLMEQLIFFHDHALLILVMTTVLVGYLMFMLFFNKYVNRYLLHGQTIEIIWTILPAIVLLFIAFPSLRLLYL 81
Cdd:MTH00140   7 LGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPSLRLLYL 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 378745285  82 LDEINEPAITLKAIGHQWYWSYEYSDFVNVEFDSYMIPTNELSIDNFRLLDVDNRVVIPMNSQIRILVTAADVIHSWT 159
Cdd:MTH00140  87 LDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWT 164
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 2-159 3.73e-86

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 251.56  E-value: 3.73e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378745285   2 LGLQDSSSPLMEQLIFFHDHALLILVMTTVLVGYLMFMLFFNKYVNRYLLHGQTIEIIWTILPAIVLLFIAFPSLRLLYL 81
Cdd:MTH00139   7 LGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPSLRLLYL 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 378745285  82 LDEINEPAITLKAIGHQWYWSYEYSDFVNVEFDSYMIPTNELSIDNFRLLDVDNRVVIPMNSQIRILVTAADVIHSWT 159
Cdd:MTH00139  87 MDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSWT 164
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 2-159 3.83e-86

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 251.70  E-value: 3.83e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378745285   2 LGLQDSSSPLMEQLIFFHDHALLILVMTTVLVGYLMFMLFFNKYVNRYLLHGQTIEIIWTILPAIVLLFIAFPSLRLLYL 81
Cdd:MTH00008   7 LMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSLRLLYL 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 378745285  82 LDEINEPAITLKAIGHQWYWSYEYSDFVNVEFDSYMIPTNELSIDNFRLLDVDNRVVIPMNSQIRILVTAADVIHSWT 159
Cdd:MTH00008  87 MDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWT 164
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 2-159 5.06e-83

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 243.67  E-value: 5.06e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378745285   2 LGLQDSSSPLMEQLIFFHDHALLILVMTTVLVGYLMFMLFFNKYVNRYLLHGQTIEIIWTILPAIVLLFIAFPSLRLLYL 81
Cdd:MTH00117   7 LGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPSLRILYL 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 378745285  82 LDEINEPAITLKAIGHQWYWSYEYSDFVNVEFDSYMIPTNELSIDNFRLLDVDNRVVIPMNSQIRILVTAADVIHSWT 159
Cdd:MTH00117  87 MDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWA 164
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 2-159 4.65e-82

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 241.42  E-value: 4.65e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378745285   2 LGLQDSSSPLMEQLIFFHDHALLILVMTTVLVGYLMFMLFFNKYVNRYLLHGQTIEIIWTILPAIVLLFIAFPSLRLLYL 81
Cdd:MTH00168   7 LGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPSLRLLYL 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 378745285  82 LDEINEPAITLKAIGHQWYWSYEYSDFVNVEFDSYMIPTNELSIDNFRLLDVDNRVVIPMNSQIRILVTAADVIHSWT 159
Cdd:MTH00168  87 MDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSWT 164
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 2-159 1.09e-78

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 233.05  E-value: 1.09e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378745285   2 LGLQDSSSPLMEQLIFFHDHALLILVMTTVLVGYLMFMLFFNKYVNRYLLHGQTIEIIWTILPAIVLLFIAFPSLRLLYL 81
Cdd:MTH00038   7 LGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPSLQLLYL 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 378745285  82 LDEINEPAITLKAIGHQWYWSYEYSDFVNVEFDSYMIPTNELSIDNFRLLDVDNRVVIPMNSQIRILVTAADVIHSWT 159
Cdd:MTH00038  87 MDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLHSWA 164
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 2-159 7.29e-76

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 225.75  E-value: 7.29e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378745285   2 LGLQDSSSPLMEQLIFFHDHALLILVMTTVLVGYLMFMLFFNKYVNRYLLHGQTIEIIWTILPAIVLLFIAFPSLRLLYL 81
Cdd:MTH00129   7 LGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRILYL 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 378745285  82 LDEINEPAITLKAIGHQWYWSYEYSDFVNVEFDSYMIPTNELSIDNFRLLDVDNRVVIPMNSQIRILVTAADVIHSWT 159
Cdd:MTH00129  87 MDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWA 164
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 2-159 4.12e-74

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 221.30  E-value: 4.12e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378745285   2 LGLQDSSSPLMEQLIFFHDHALLILVMTTVLVGYLMFMLFFNKYVNRYLLHGQTIEIIWTILPAIVLLFIAFPSLRLLYL 81
Cdd:MTH00185   7 LGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLRILYL 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 378745285  82 LDEINEPAITLKAIGHQWYWSYEYSDFVNVEFDSYMIPTNELSIDNFRLLDVDNRVVIPMNSQIRILVTAADVIHSWT 159
Cdd:MTH00185  87 MDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWT 164
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 2-159 8.86e-73

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 218.47  E-value: 8.86e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378745285   2 LGLQDSSSPLMEQLIFFHDHALLILVMTTVLVGYLMFMLFFNKYVNRYLLHGQTIEIIWTILPAIVLLFIAFPSLRLLYL 81
Cdd:MTH00023  16 LGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378745285  82 LDEINEPAITLKAIGHQWYWSYEYSDFV--NVEFDSYMIPTNELSIDNFRLLDVDNRVVIPMNSQIRILVTAADVIHSWT 159
Cdd:MTH00023  96 MDEVVSPALTIKAIGHQWYWSYEYSDYEgeTLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFA 175
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 2-159 3.97e-72

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 216.12  E-value: 3.97e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378745285   2 LGLQDSSSPLMEQLIFFHDHALLILVMTTVLVGYLMFMLFFNKYVNRYLLHGQTIEIIWTILPAIVLLFIAFPSLRLLYL 81
Cdd:MTH00098   7 LGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRILYM 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 378745285  82 LDEINEPAITLKAIGHQWYWSYEYSDFVNVEFDSYMIPTNELSIDNFRLLDVDNRVVIPMNSQIRILVTAADVIHSWT 159
Cdd:MTH00098  87 MDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWA 164
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 2-159 2.49e-71

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 214.26  E-value: 2.49e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378745285   2 LGLQDSSSPLMEQLIFFHDHALLILVMTTVLVGYLMFMLFFNKYVNRYLLHGQTIEIIWTILPAIVLLFIAFPSLRLLYL 81
Cdd:MTH00076   7 LGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRILYL 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 378745285  82 LDEINEPAITLKAIGHQWYWSYEYSDFVNVEFDSYMIPTNELSIDNFRLLDVDNRVVIPMNSQIRILVTAADVIHSWT 159
Cdd:MTH00076  87 MDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWA 164
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 2-158 3.09e-68

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 206.56  E-value: 3.09e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378745285   2 LGLQDSSSPLMEQLIFFHDHALLILVMTTVLVGYLMFMLFFNKYVNRYLLHGQTIEIIWTILPAIVLLFIAFPSLRLLYL 81
Cdd:MTH00051   9 LGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYL 88

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 378745285  82 LDEINEPAITLKAIGHQWYWSYEYSDF--VNVEFDSYMIPTNELSIDNFRLLDVDNRVVIPMNSQIRILVTAADVIHSW 158
Cdd:MTH00051  89 MDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSF 167
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 2-159 1.65e-50

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 162.50  E-value: 1.65e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378745285   2 LGLQDSSSPLMEQLIFFHDHALLILVMTTVLVGYLMF-MLFFNKYVNRYL--LHGQTIEIIWTILPAIVLLFIAFPSLRL 78
Cdd:MTH00027  35 LGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIrILLGNNYYSYYWnkLDGSLIEVIWTLIPAFILILIAFPSLRL 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378745285  79 LYLLDEINEPA-ITLKAIGHQWYWSYEYSDF--VNVEFDSYMIPTNELSIDNFRLLDVDNRVVIPMNSQIRILVTAADVI 155
Cdd:MTH00027 115 LYIMDECGFSAnITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVL 194


                 ....
gi 378745285 156 HSWT 159
Cdd:MTH00027 195 HSWT 198
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 88-159 3.45e-48

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: 151.95  E-value: 3.45e-48
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 378745285  88 PAITLKAIGHQWYWSYEYSDFVNVEFDSYMIPTNELSIDNFRLLDVDNRVVIPMNSQIRILVTAADVIHSWT 159
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWA 72
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 1-159 6.29e-44

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 144.38  E-value: 6.29e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378745285   1 NLGLQDSS-SPLMEQLIFFHDHALLILVMTTVLVGYLMFMLFFNKYVNRYLLHGQTIEIIWTILPAIVLLFIAFPSLRLL 79
Cdd:MTH00080   7 NLNFSNSLfSSYMDWFHNFNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378745285  80 YLLDEIN-EPAITLKAIGHQWYWSYEYSDFVNVEFDSYMIPTNELSIDNFRLLDVDNRVVIPMNSQIRILVTAADVIHSW 158
Cdd:MTH00080  87 YYYGLMNlDSNLTVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSW 166


                 .
gi 378745285 159 T 159
Cdd:MTH00080 167 A 167
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
90-159 1.29e-40

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 132.53  E-value: 1.29e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378745285   90 ITLKAIGHQWYWSYEYSDFVNVEFDSYMIPTNELSIDNFRLLDVDNRVVIPMNSQIRILVTAADVIHSWT 159
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWA 70
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-158 1.40e-27

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 102.21  E-value: 1.40e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378745285   1 NLGLQDSSSPLMEQLIFFHDHALLILVMTTVLVGYLM--FMLFF----NKYVNRYLLHGQTIEIIWTILPAIVLLFIAFP 74
Cdd:COG1622   18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLlyFAIRYrrrkGDADPAQFHHNTKLEIVWTVIPIIIVIVLAVP 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378745285  75 SLRLLYLLDEINEPAITLKAIGHQWYWSYEYSDFVNVefdsymiptnelsidnfrlldVDNRVVIPMNSQIRILVTAADV 154
Cdd:COG1622   98 TLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVNELVLPVGRPVRFLLTSADV 156


                 ....
gi 378745285 155 IHSW 158
Cdd:COG1622  157 IHSF 160
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-78 1.67e-24

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: 90.47  E-value: 1.67e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378745285    1 NLGLQDSSSPLMEQLIFFHDHALLILVMTTVLVGYLMFMLFF------NKYVNRYLLHGQTIEIIWTILPAIVLLFIAFP 74
Cdd:pfam02790   6 GLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIrfnrrkNPITARYTTHGQTIEIIWTIIPAVILILIALP 85


                  ....
gi 378745285   75 SLRL 78
Cdd:pfam02790  86 SFKL 89
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 9-158 3.13e-21

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: 85.12  E-value: 3.13e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378745285    9 SPLMEQLifFHDHALLILVMTTV-LVGYLMFMLFFNKYVNR-------YLLHGQTIEIIWTILPA-IVLLFIAFPSLRLL 79
Cdd:TIGR02866   3 GEIAQQI--AFLFLFVLAVSTLIsLLVAALLAYVVWKFRRKgdeekpsQIHGNRRLEYVWTVIPLiIVVGLFAATAKGLL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 378745285   80 YLLDEINEPAITLKAIGHQWYWSYEYSDFvnvefdsymiptnelsidnfrLLDVDNRVVIPMNSQIRILVTAADVIHSW 158
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSF 138
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 12-157 2.48e-17

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 74.99  E-value: 2.48e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378745285  12 MEQLIFFHDHALLILVMTTVLVGYLMFMLFFNKYV-NRYLLHG---QTIEIIWTILPAIVLLFIAFpsLRLLYLLDEIN- 86
Cdd:MTH00047   1 MNLSLLYYDIVCYILALCVFIPCWVYIMLCWQVVSgNGSVNFGsenQVLELLWTVVPTLLVLVLCF--LNLNFITSDLDc 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 378745285  87 EPAITLKAIGHQWYWSYEYSDfvNVEFDSYMiptnelSIDNFrllDVDNRVVIPMNSQIRILVTAADVIHS 157
Cdd:MTH00047  79 FSSETIKVIGHQWYWSYEYSF--GGSYDSFM------TDDIF---GVDKPLRLVYGVPYHLLVTSSDVIHS 138
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 113-159 1.49e-08

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 50.97  E-value: 1.49e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 378745285 113 FDSYMIPTNELSIDNFRLLDVDNRVVIPMNSQIRILVTAADVIHSWT 159
Cdd:PTZ00047  51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWS 97
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 89-158 2.08e-07

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: 46.46  E-value: 2.08e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 378745285  89 AITLKAIGHQWYWSYEYSDFVNVEFDSymipTNELsidnfrlldvdnrvVIPMNSQIRILVTAADVIHS-W 158
Cdd:cd04213    1 ALTIEVTGHQWWWEFRYPDEPGRGIVT----ANEL--------------HIPVGRPVRLRLTSADVIHSfW 53
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 90-159 4.17e-06

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: 43.05  E-value: 4.17e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378745285  90 ITLKAIGHQWYWSYEYSDfvnvefdsymiptnelsidnfrlLDVDNRVVIPMNSQIRILVTAADVIHSWT 159
Cdd:cd13842    1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFY 47
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 89-157 5.77e-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: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 43.01  E-value: 5.77e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 378745285  89 AITLKAIGHQWYWSYEYSDFVNVEFDSYMIPTNELsidnfrlldvdnrvVIPMNSQIRILVTAADVIHS 157
Cdd:cd13919    1 ALVVEVTAQQWAWTFRYPGGDGKLGTDDDVTSPEL--------------HLPVGRPVLFNLRSKDVIHS 55
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 89-157 8.09e-05

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: 39.53  E-value: 8.09e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 378745285  89 AITLKAIGHQWYWSYEYSdfvnvefdsymiptNELSIDNfrlldvdnRVVIPMNSQIRILVTAADVIHS 157
Cdd:cd13915    1 ALEIQVTGRQWMWEFTYP--------------NGKREIN--------ELHVPVGKPVRLILTSKDVIHS 47
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 66-157 1.20e-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: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 39.75  E-value: 1.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378745285  66 IVLLFIAFPSLRLLYLLD---EINEPAITLKAIGHQWYWSYEYSdfVNVEFDSYMiptnelsidnfrlldvdnrvVIPMN 142
Cdd:cd13918    6 IVISLIVWTYGMLLYVEDppdEADEDALEVEVEGFQFGWQFEYP--NGVTTGNTL--------------------RVPAD 63

                         90
                 ....*....|....*
gi 378745285 143 SQIRILVTAADVIHS 157
Cdd:cd13918   64 TPIALRVTSTDVFHT 78
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 90-157 1.10e-03

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


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 36.62  E-value: 1.10e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 378745285  90 ITLKAIGHQWYWSYEYsdfvnvefdsymiptNELSIDNFrlldvdNRVVIPMNSQIRILVTAADVIHS 157
Cdd:cd13914    1 VEIEVEAYQWGWEFSY---------------PEANVTTS------EQLVIPADRPVYFRITSRDVIHA 47
 
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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