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Conserved domains on  [gi|2301263212|ref|YP_010466484|]
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cytochrome c oxidase subunit II (mitochondrion) [Opsarius pulchellus]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11475911)

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 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-230 5.04e-162

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 446.85  E-value: 5.04e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212   1 MAYPTQLGFQDAASPVMEELLCFHDHALMIVFLISTLVLYIIVAMVSTKLTNKFILDSQEIEIVWTILPAIILILIALPS 80
Cdd:MTH00129    1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212  81 LRILYLMDEINDPHVTVKAMGHQWYWSYEYTDYEDLGFDSYMVPTQDLTTGSFRLLEVDHRMVIPKESPIRVLVSAEDVL 160
Cdd:MTH00129   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212 161 HSWAVPSLGVKMDAVPGRLNQTTLIVTRPGVFYGQCSEICGANHSFMPIVVEAVPLESFEIWSALVLENA 230
Cdd:MTH00129  161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLMLEDA 230
 
Name Accession Description Interval E-value
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-230 5.04e-162

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 446.85  E-value: 5.04e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212   1 MAYPTQLGFQDAASPVMEELLCFHDHALMIVFLISTLVLYIIVAMVSTKLTNKFILDSQEIEIVWTILPAIILILIALPS 80
Cdd:MTH00129    1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212  81 LRILYLMDEINDPHVTVKAMGHQWYWSYEYTDYEDLGFDSYMVPTQDLTTGSFRLLEVDHRMVIPKESPIRVLVSAEDVL 160
Cdd:MTH00129   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212 161 HSWAVPSLGVKMDAVPGRLNQTTLIVTRPGVFYGQCSEICGANHSFMPIVVEAVPLESFEIWSALVLENA 230
Cdd:MTH00129  161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLMLEDA 230
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-222 2.04e-94

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: 272.14  E-value: 2.04e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212  93 PHVTVKAMGHQWYWSYEYTDYEDLGFDSYMVPTQDLTTGSFRLLEVDHRMVIPKESPIRVLVSAEDVLHSWAVPSLGVKM 172
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2301263212 173 DAVPGRLNQTTLIVTRPGVFYGQCSEICGANHSFMPIVVEAVPLESFEIW 222
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
96-214 3.41e-84

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 245.78  E-value: 3.41e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212  96 TVKAMGHQWYWSYEYTDYEDLGFDSYMVPTQDLTTGSFRLLEVDHRMVIPKESPIRVLVSAEDVLHSWAVPSLGVKMDAV 175
Cdd:pfam00116   2 TIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDAV 81

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2301263212 176 PGRLNQTTLIVTRPGVFYGQCSEICGANHSFMPIVVEAV 214
Cdd:pfam00116  82 PGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-222 2.20e-48

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 158.45  E-value: 2.20e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212   6 QLGFQDAASPVMEELlcfhDHALMIVFLISTLV-----LYIIVAMV-----STKLTNKFILDSQEIEIVWTILPAIILIL 75
Cdd:COG1622    18 QLSLPDPAGPIAEEI----DDLFWVSLIIMLVIfvlvfGLLLYFAIryrrrKGDADPAQFHHNTKLEIVWTVIPIIIVIV 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212  76 IALPSLRILYLMDEINDPHVTVKAMGHQWYWSYEYTDYEDLgfdsymvptqdlttgsfrlleVDHRMVIPKESPIRVLVS 155
Cdd:COG1622    94 LAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVNELVLPVGRPVRFLLT 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2301263212 156 AEDVLHSWAVPSLGVKMDAVPGRLNQTTLIVTRPGVFYGQCSEICGANHSFMPIVVEAVPLESFEIW 222
Cdd:COG1622   153 SADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAW 219
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-222 2.50e-38

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


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 131.73  E-value: 2.50e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212  12 AASPVMEELLCFHDHALMIVFLISTLVLYIIVAMV------STKLTNKFILDSQEIEIVWTIL-PAIILILIALPSLRIL 84
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVwkfrrkGDEEKPSQIHGNRRLEYVWTVIpLIIVVGLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212  85 YLMDEINDPHVTVKAMGHQWYWSYEYTDYedlgfdsymvptqdlttgsfrLLEVDHRMVIPKESPIRVLVSAEDVLHSWA 164
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFW 139

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2301263212 165 VPSLGVKMDAVPGRLNQTTLIVTRPGVFYGQCSEICGANHSFMPIVVEAVPLESFEIW 222
Cdd:TIGR02866 140 VPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAY 197
 
Name Accession Description Interval E-value
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-230 5.04e-162

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 446.85  E-value: 5.04e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212   1 MAYPTQLGFQDAASPVMEELLCFHDHALMIVFLISTLVLYIIVAMVSTKLTNKFILDSQEIEIVWTILPAIILILIALPS 80
Cdd:MTH00129    1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212  81 LRILYLMDEINDPHVTVKAMGHQWYWSYEYTDYEDLGFDSYMVPTQDLTTGSFRLLEVDHRMVIPKESPIRVLVSAEDVL 160
Cdd:MTH00129   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212 161 HSWAVPSLGVKMDAVPGRLNQTTLIVTRPGVFYGQCSEICGANHSFMPIVVEAVPLESFEIWSALVLENA 230
Cdd:MTH00129  161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLMLEDA 230
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-227 1.93e-153

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 425.10  E-value: 1.93e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212   1 MAYPTQLGFQDAASPVMEELLCFHDHALMIVFLISTLVLYIIVAMVSTKLTNKFILDSQEIEIVWTILPAIILILIALPS 80
Cdd:MTH00117    1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212  81 LRILYLMDEINDPHVTVKAMGHQWYWSYEYTDYEDLGFDSYMVPTQDLTTGSFRLLEVDHRMVIPKESPIRVLVSAEDVL 160
Cdd:MTH00117   81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2301263212 161 HSWAVPSLGVKMDAVPGRLNQTTLIVTRPGVFYGQCSEICGANHSFMPIVVEAVPLESFEIWSALVL 227
Cdd:MTH00117  161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLLS 227
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-230 5.65e-145

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 403.88  E-value: 5.65e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212   1 MAYPTQLGFQDAASPVMEELLCFHDHALMIVFLISTLVLYIIVAMVSTKLTNKFILDSQEIEIVWTILPAIILILIALPS 80
Cdd:MTH00185    1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212  81 LRILYLMDEINDPHVTVKAMGHQWYWSYEYTDYEDLGFDSYMVPTQDLTTGSFRLLEVDHRMVIPKESPIRVLVSAEDVL 160
Cdd:MTH00185   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212 161 HSWAVPSLGVKMDAVPGRLNQTTLIVTRPGVFYGQCSEICGANHSFMPIVVEAVPLESFEIWSALVLENA 230
Cdd:MTH00185  161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLMLEEA 230
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-227 7.25e-141

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 393.31  E-value: 7.25e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212   1 MAYPTQLGFQDAASPVMEELLCFHDHALMIVFLISTLVLYIIVAMVSTKLTNKFILDSQEIEIVWTILPAIILILIALPS 80
Cdd:MTH00098    1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212  81 LRILYLMDEINDPHVTVKAMGHQWYWSYEYTDYEDLGFDSYMVPTQDLTTGSFRLLEVDHRMVIPKESPIRVLVSAEDVL 160
Cdd:MTH00098   81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2301263212 161 HSWAVPSLGVKMDAVPGRLNQTTLIVTRPGVFYGQCSEICGANHSFMPIVVEAVPLESFEIWSALVL 227
Cdd:MTH00098  161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASML 227
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-228 1.29e-138

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 387.60  E-value: 1.29e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212   1 MAYPTQLGFQDAASPVMEELLCFHDHALMIVFLISTLVLYIIVAMVSTKLTNKFILDSQEIEIVWTILPAIILILIALPS 80
Cdd:MTH00076    1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212  81 LRILYLMDEINDPHVTVKAMGHQWYWSYEYTDYEDLGFDSYMVPTQDLTTGSFRLLEVDHRMVIPKESPIRVLVSAEDVL 160
Cdd:MTH00076   81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2301263212 161 HSWAVPSLGVKMDAVPGRLNQTTLIVTRPGVFYGQCSEICGANHSFMPIVVEAVPLESFEIWSALVLE 228
Cdd:MTH00076  161 HSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSMLE 228
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-224 1.25e-128

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 362.38  E-value: 1.25e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212   1 MAYPTQLGFQDAASPVMEELLCFHDHALMIVFLISTLVLYIIVAMVSTKLTNKFILDSQEIEIVWTILPAIILILIALPS 80
Cdd:MTH00168    1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212  81 LRILYLMDEINDPHVTVKAMGHQWYWSYEYTDYEDLGFDSYMVPTQDLTTGSFRLLEVDHRMVIPKESPIRVLVSAEDVL 160
Cdd:MTH00168   81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2301263212 161 HSWAVPSLGVKMDAVPGRLNQTTLIVTRPGVFYGQCSEICGANHSFMPIVVEAVPLESFEIWSA 224
Cdd:MTH00168  161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVD 224
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-222 7.21e-125

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 352.59  E-value: 7.21e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212   1 MAYPTQLGFQDAASPVMEELLCFHDHALMIVFLISTLVLYIIVAMVSTKLTNKFILDSQEIEIVWTILPAIILILIALPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212  81 LRILYLMDEINDPHVTVKAMGHQWYWSYEYTDYEDLGFDSYMVPTQDLTTGSFRLLEVDHRMVIPKESPIRVLVSAEDVL 160
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2301263212 161 HSWAVPSLGVKMDAVPGRLNQTTLIVTRPGVFYGQCSEICGANHSFMPIVVEAVPLESFEIW 222
Cdd:MTH00154  161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINW 222
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-229 2.00e-124

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 351.70  E-value: 2.00e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212   1 MAYPTQLGFQDAASPVMEELLCFHDHALMIVFLISTLVLYIIVAMVSTKLTNKFILDSQEIEIVWTILPAIILILIALPS 80
Cdd:MTH00038    1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212  81 LRILYLMDEINDPHVTVKAMGHQWYWSYEYTDYEDLGFDSYMVPTQDLTTGSFRLLEVDHRMVIPKESPIRVLVSAEDVL 160
Cdd:MTH00038   81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2301263212 161 HSWAVPSLGVKMDAVPGRLNQTTLIVTRPGVFYGQCSEICGANHSFMPIVVEAVPLESFEIWSALVLEN 229
Cdd:MTH00038  161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFLEE 229
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-222 1.58e-116

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 331.52  E-value: 1.58e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212   1 MAYPTQLGFQDAASPVMEELLCFHDHALMIVFLISTLVLYIIVAMVSTKLTNKFILDSQEIEIVWTILPAIILILIALPS 80
Cdd:MTH00140    1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212  81 LRILYLMDEINDPHVTVKAMGHQWYWSYEYTDYEDLGFDSYMVPTQDLTTGSFRLLEVDHRMVIPKESPIRVLVSAEDVL 160
Cdd:MTH00140   81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2301263212 161 HSWAVPSLGVKMDAVPGRLNQTTLIVTRPGVFYGQCSEICGANHSFMPIVVEAVPLESFEIW 222
Cdd:MTH00140  161 HSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKW 222
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-222 1.75e-116

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 331.68  E-value: 1.75e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212   1 MAYPTQLGFQDAASPVMEELLCFHDHALMIVFLISTLVLYIIVAMVSTKLTNKFILDSQEIEIVWTILPAIILILIALPS 80
Cdd:MTH00139    1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212  81 LRILYLMDEINDPHVTVKAMGHQWYWSYEYTDYEDLGFDSYMVPTQDLTTGSFRLLEVDHRMVIPKESPIRVLVSAEDVL 160
Cdd:MTH00139   81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2301263212 161 HSWAVPSLGVKMDAVPGRLNQTTLIVTRPGVFYGQCSEICGANHSFMPIVVEAVPLESFEIW 222
Cdd:MTH00139  161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEW 222
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-222 2.79e-108

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 311.02  E-value: 2.79e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212   1 MAYPTQLGFQDAASPVMEELLCFHDHALMIVFLISTLVLYIIVAMVSTKLTNKFILDSQEIEIVWTILPAIILILIALPS 80
Cdd:MTH00008    1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212  81 LRILYLMDEINDPHVTVKAMGHQWYWSYEYTDYEDLGFDSYMVPTQDLTTGSFRLLEVDHRMVIPKESPIRVLVSAEDVL 160
Cdd:MTH00008   81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2301263212 161 HSWAVPSLGVKMDAVPGRLNQTTLIVTRPGVFYGQCSEICGANHSFMPIVVEAVPLESFEIW 222
Cdd:MTH00008  161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKW 222
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 4-223 2.51e-105

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 303.98  E-value: 2.51e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212   4 PTQLGFQDAASPVMEELLCFHDHALMIVFLISTLVLYIIVAMVSTKLTNKFILDSQEIEIVWTILPAIILILIALPSLRI 83
Cdd:MTH00023   13 PWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212  84 LYLMDEINDPHVTVKAMGHQWYWSYEYTDYED--LGFDSYMVPTQDLTTGSFRLLEVDHRMVIPKESPIRVLVSAEDVLH 161
Cdd:MTH00023   93 LYLMDEVVSPALTIKAIGHQWYWSYEYSDYEGetLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLH 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2301263212 162 SWAVPSLGVKMDAVPGRLNQTTLIVTRPGVFYGQCSEICGANHSFMPIVVEAVPLESFEIWS 223
Cdd:MTH00023  173 SFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWL 234
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 4-224 1.42e-100

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 291.68  E-value: 1.42e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212   4 PTQLGFQDAASPVMEELLCFHDHALMIVFLISTLVLYIIVAMVSTKLTNKFILDSQEIEIVWTILPAIILILIALPSLRI 83
Cdd:MTH00051    6 PWQLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212  84 LYLMDEINDPHVTVKAMGHQWYWSYEYTDY--EDLGFDSYMVPTQDLTTGSFRLLEVDHRMVIPKESPIRVLVSAEDVLH 161
Cdd:MTH00051   86 LYLMDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLH 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2301263212 162 SWAVPSLGVKMDAVPGRLNQTTLIVTRPGVFYGQCSEICGANHSFMPIVVEAVPLESFEIWSA 224
Cdd:MTH00051  166 SFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVA 228
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-222 2.04e-94

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: 272.14  E-value: 2.04e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212  93 PHVTVKAMGHQWYWSYEYTDYEDLGFDSYMVPTQDLTTGSFRLLEVDHRMVIPKESPIRVLVSAEDVLHSWAVPSLGVKM 172
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2301263212 173 DAVPGRLNQTTLIVTRPGVFYGQCSEICGANHSFMPIVVEAVPLESFEIW 222
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
96-214 3.41e-84

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 245.78  E-value: 3.41e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212  96 TVKAMGHQWYWSYEYTDYEDLGFDSYMVPTQDLTTGSFRLLEVDHRMVIPKESPIRVLVSAEDVLHSWAVPSLGVKMDAV 175
Cdd:pfam00116   2 TIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDAV 81

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2301263212 176 PGRLNQTTLIVTRPGVFYGQCSEICGANHSFMPIVVEAV 214
Cdd:pfam00116  82 PGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 4-222 9.04e-79

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 237.23  E-value: 9.04e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212   4 PTQLGFQDAASPVMEELLCFHDHALMIVFLISTLVLYIIVAMVstkLTNKFI------LDSQEIEIVWTILPAIILILIA 77
Cdd:MTH00027   32 PWQLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRIL---LGNNYYsyywnkLDGSLIEVIWTLIPAFILILIA 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212  78 LPSLRILYLMDE-INDPHVTVKAMGHQWYWSYEYTDY--EDLGFDSYMVPTQDLTTGSFRLLEVDHRMVIPKESPIRVLV 154
Cdd:MTH00027  109 FPSLRLLYIMDEcGFSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLI 188

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2301263212 155 SAEDVLHSWAVPSLGVKMDAVPGRLNQTTLIVTRPGVFYGQCSEICGANHSFMPIVVEAVPLESFEIW 222
Cdd:MTH00027  189 TAADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDW 256
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 23-228 1.45e-67

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 207.55  E-value: 1.45e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212  23 FHDHALMIVFLISTLVLYIIVAMVSTKLTNKFILDSQEIEIVWTILPAIILILIALPSLRILYLMDEIN-DPHVTVKAMG 101
Cdd:MTH00080   25 FNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMNlDSNLTVKVTG 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212 102 HQWYWSYEYTDYEDLGFDSYMVPTQDLTTGSFRLLEVDHRMVIPKESPIRVLVSAEDVLHSWAVPSLGVKMDAVPGRLNQ 181
Cdd:MTH00080  105 HQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILST 184

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2301263212 182 TTLIVTRPGVFYGQCSEICGANHSFMPIVVEAVPLESFEIWSALVLE 228
Cdd:MTH00080  185 LCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWCKLLLD 231
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-222 2.20e-48

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 158.45  E-value: 2.20e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212   6 QLGFQDAASPVMEELlcfhDHALMIVFLISTLV-----LYIIVAMV-----STKLTNKFILDSQEIEIVWTILPAIILIL 75
Cdd:COG1622    18 QLSLPDPAGPIAEEI----DDLFWVSLIIMLVIfvlvfGLLLYFAIryrrrKGDADPAQFHHNTKLEIVWTVIPIIIVIV 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212  76 IALPSLRILYLMDEINDPHVTVKAMGHQWYWSYEYTDYEDLgfdsymvptqdlttgsfrlleVDHRMVIPKESPIRVLVS 155
Cdd:COG1622    94 LAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVNELVLPVGRPVRFLLT 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2301263212 156 AEDVLHSWAVPSLGVKMDAVPGRLNQTTLIVTRPGVFYGQCSEICGANHSFMPIVVEAVPLESFEIW 222
Cdd:COG1622   153 SADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAW 219
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 118-219 8.94e-44

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 144.58  E-value: 8.94e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212 118 FDSYMVPTQDLTTGSFRLLEVDHRMVIPKESPIRVLVSAEDVLHSWAVPSLGVKMDAVPGRLNQTTLIVTRPGVFYGQCS 197
Cdd:PTZ00047   51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                          90       100
                  ....*....|....*....|..
gi 2301263212 198 EICGANHSFMPIVVEAVPLESF 219
Cdd:PTZ00047  131 EMCGTLHGFMPIVVEAVSPEAY 152
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 17-214 5.47e-40

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 135.85  E-value: 5.47e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212  17 MEELLCFHDHALMIVFLISTLVLYIIVAM----VSTKLTNKFILDSQEIEIVWTILPAIILILIALPslRILYLMDEIND 92
Cdd:MTH00047    1 MNLSLLYYDIVCYILALCVFIPCWVYIMLcwqvVSGNGSVNFGSENQVLELLWTVVPTLLVLVLCFL--NLNFITSDLDC 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212  93 -PHVTVKAMGHQWYWSYEYTDyeDLGFDSYMVptqDLTTGsfrlleVDHRMVIPKESPIRVLVSAEDVLHSWAVPSLGVK 171
Cdd:MTH00047   79 fSSETIKVIGHQWYWSYEYSF--GGSYDSFMT---DDIFG------VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLK 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2301263212 172 MDAVPGRLNQTTLIVTRPGVFYGQCSEICGANHSFMPIVVEAV 214
Cdd:MTH00047  148 MDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVV 190
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-222 2.50e-38

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


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 131.73  E-value: 2.50e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212  12 AASPVMEELLCFHDHALMIVFLISTLVLYIIVAMV------STKLTNKFILDSQEIEIVWTIL-PAIILILIALPSLRIL 84
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVwkfrrkGDEEKPSQIHGNRRLEYVWTVIpLIIVVGLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212  85 YLMDEINDPHVTVKAMGHQWYWSYEYTDYedlgfdsymvptqdlttgsfrLLEVDHRMVIPKESPIRVLVSAEDVLHSWA 164
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFW 139

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2301263212 165 VPSLGVKMDAVPGRLNQTTLIVTRPGVFYGQCSEICGANHSFMPIVVEAVPLESFEIW 222
Cdd:TIGR02866 140 VPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAY 197
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-212 7.88e-31

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: 109.31  E-value: 7.88e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212  95 VTVKAMGHQWYWSYEYTDyedlgfdsymvptqdlttgsfrlLEVDHRMVIPKESPIRVLVSAEDVLHSWAVPSLGVKMDA 174
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2301263212 175 VPGRLNQTTLIVTRPGVFYGQCSEICGANHSFMPIVVE 212
Cdd:cd13842    58 VPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 94-214 1.48e-30

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: 108.86  E-value: 1.48e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212  94 HVTVKAMGHQWYWSYEYTDYEDLGFdsymvptqdlTTGSfrllevdhRMVIPKESPIRVLVSAEDVLHSWAVPSLGVKMD 173
Cdd:cd04213     1 ALTIEVTGHQWWWEFRYPDEPGRGI----------VTAN--------ELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMD 62

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2301263212 174 AVPGRLNQTTLIVTRPGVFYGQCSEICGANHSFMPIVVEAV 214
Cdd:cd04213    63 MIPGRTNRLWLQADEPGVYRGQCAEFCGASHALMRFKVIAL 103
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-212 2.52e-24

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: 92.70  E-value: 2.52e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212  95 VTVKAMGHQWYWSYEYTDY-EDLGFDSYMVPTQdlttgsfrllevdhrMVIPKESPIRVLVSAEDVLHSWAVPSLGVKMD 173
Cdd:cd13919     2 LVVEVTAQQWAWTFRYPGGdGKLGTDDDVTSPE---------------LHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQD 66

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2301263212 174 AVPGRLNQTTLIVTRPGVFYGQCSEICGANHSFM--PIVVE 212
Cdd:cd13919    67 AVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRMraTVKVV 107
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 83-222 6.05e-22

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


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 87.51  E-value: 6.05e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212  83 ILYLMD---EINDPHVTVKAMGHQWYWSYEYTDyedlgfdsymvptqDLTTGSFrllevdhrMVIPKESPIRVLVSAEDV 159
Cdd:cd13918    18 LLYVEDppdEADEDALEVEVEGFQFGWQFEYPN--------------GVTTGNT--------LRVPADTPIALRVTSTDV 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2301263212 160 LHSWAVPSLGVKMDAVPGRLNQTTLIVTRPGVFYGQCSEICGANHSFMPIVVEAVPLESFEIW 222
Cdd:cd13918    76 FHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAW 138
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-222 1.01e-21

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: 85.92  E-value: 1.01e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212  95 VTVKAMGHQWYWSYEYtdyedlgfdsymvPTQDLTTGSfrllevdhRMVIPKESPIRVLVSAEDVLHSWAVPSLGVKMDA 174
Cdd:cd13914     1 VEIEVEAYQWGWEFSY-------------PEANVTTSE--------QLVIPADRPVYFRITSRDVIHAFHVPELGLKQDA 59

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2301263212 175 VPGRLNQTTLIVTRPGVFYGQCSEICGANHSFMPIVVEAVPLESFEIW 222
Cdd:cd13914    60 FPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQW 107
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 96-213 1.96e-19

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


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 79.98  E-value: 1.96e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212  96 TVKAMGHQWYWSYEYTDyedlgfdsymvptqdlttGsfrlLEVDHRMVIPKESPIRVLVSAEDVLHSWAVPSLGVKMDAV 175
Cdd:cd13915     3 EIQVTGRQWMWEFTYPN------------------G----KREINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDVV 60

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2301263212 176 PGRLNQTTLIVTRPGVFYGQCSEICGANHSFMPIVVEA 213
Cdd:cd13915    61 PGRYTYLWFEATKPGEYDLFCTEYCGTGHSGMIGKVRV 98
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-66 5.39e-19

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: 78.53  E-value: 5.39e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2301263212   1 MAYPTQLGFQDAASPVMEELLCFHDHALMIVFLISTLVLYIIVAMV------STKLTNKFILDSQEIEIVWT 66
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLirfnrrKNPITARYTTHGQTIEIIWT 72
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 142-212 9.12e-10

C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and some archaea, which catalyze the reduction of O2 and simultaneously pump protons across the membrane. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. The ba3 family contains oxidases that lack the conserved residues that form the D- and K-pathways in CcO and ubiquinol oxidase. Instead, they contain a potential alternative K-pathway. Additional proton channels have been proposed for this family of oxidases but none have been identified definitively.


Pssm-ID: 259980 [Multi-domain]  Cd Length: 99  Bit Score: 54.11  E-value: 9.12e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2301263212 142 MVIPKESPIRVLVSAEDVLHSWAVPSLGVKMDAVPGRLNQTTLIVTRPGVFYGQCSEICGANHSFM--PIVVE 212
Cdd:cd13913    27 IEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNMygKIIVE 99
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 142-214 1.86e-06

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


Pssm-ID: 259874 [Multi-domain]  Cd Length: 99  Bit Score: 44.85  E-value: 1.86e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2301263212 142 MVIPKESPIRVLVSAEDVLHSWAVPSLGVKMDAVPGRLNQTTLIVTRPGVFYGQCSEICGANHSFMPIVVEAV 214
Cdd:cd04212    27 LVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDMKFKVLAV 99
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 156-207 4.08e-05

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


Pssm-ID: 259885 [Multi-domain]  Cd Length: 95  Bit Score: 41.07  E-value: 4.08e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2301263212 156 AEDVLHSWAVPSLGVKMDAVPGRLNQTTLIVTRPGVFYGQCSEICGANHSFM 207
Cdd:cd04223    36 DEDITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALHLEM 87
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-207 9.22e-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: 259983 [Multi-domain]  Cd Length: 93  Bit Score: 40.06  E-value: 9.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212  95 VTVKAMGHQWYWSyeytdyedlgfdsyMVPTQdlttgsfrllevdhrmvIPKESPIRVLVSAEDVLHSWAVPS----LGV 170
Cdd:cd13916     1 QVVAVTGHQWYWE--------------LSRTE-----------------IPAGKPVEFRVTSADVNHGFGIYDpdmrLLA 49

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2301263212 171 KMDAVPGRLNQTTLIVTRPGVFYGQCSEICGANHSFM 207
Cdd:cd13916    50 QTQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 97-212 1.31e-04

Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in inter-molecular electron transfer reactions. Cupredoxins are blue copper proteins, having an intense blue color due to the presence of a mononuclear type 1 (T1) copper site. Structurally, the cupredoxin-like fold consists of a beta-sandwich with 7 strands in 2 beta-sheets, which is arranged in a Greek-key beta-barrel. Some of these proteins have lost the ability to bind copper. The majority of family members contain multiple cupredoxin domain repeats: ceruloplasmin and the coagulation factors V/VIII have six repeats; laccase, ascorbate oxidase, spore coat protein A, and multicopper oxidase CueO contain three repeats; and nitrite reductase has two repeats. Others are mono-domain cupredoxins, such as plastocyanin, pseudoazurin, plantacyanin, azurin, rusticyanin, stellacyanin, quinol oxidase, and the periplasmic domain of cytochrome c oxidase subunit II.


Pssm-ID: 259860 [Multi-domain]  Cd Length: 110  Bit Score: 40.29  E-value: 1.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301263212  97 VKAMGHQWYWSYEYTDYEDLGFDSYMVPTQDLTTgsFRL---LEVDHRMVIPKESPirVLVSAEDVLHSWAVPSLGVKmd 173
Cdd:cd00920     1 ITVTASDWGWSFTYNGVLLFGPPVLVVPVGDTVR--VQFvnkLGENHSVTIAGFGV--PVVAMAGGANPGLVNTLVIG-- 74

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2301263212 174 avPGRLNQTTLIVTRPGVFYGQCSEICGaNHSFMPIVVE 212
Cdd:cd00920    75 --PGESAEVTFTTDQAGVYWFYCTIPGH-NHAGMVGTIN 110
PRK02888 PRK02888
nitrous-oxide reductase; Validated
 157-213 6.06e-04

nitrous-oxide reductase; Validated


Pssm-ID: 235082 [Multi-domain]  Cd Length: 635  Bit Score: 40.35  E-value: 6.06e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2301263212 157 EDVLHSWAVPSLGVKMDAVPGRLNQTTLIVTRPGVFYGQCSEICGANHSFMP--IVVEA 213
Cdd:PRK02888  576 EDLTHGFAIPNYGVNMEVAPQATASVTFTADKPGVYWYYCTWFCHALHMEMRgrMLVEP 634
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 142-212 3.52e-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: 259984 [Multi-domain]  Cd Length: 88  Bit Score: 35.42  E-value: 3.52e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2301263212 142 MVIPKESPIRVLVSAEDVLHSWAVPSLGVKMDAVPGRLNQTTLIVTRPGVFYGQCSEICGANHSFM--PIVVE 212
Cdd:cd13917    16 LVLKKGKTYRLHLSSLDVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIICNEYCGIGHHTMhgRIIVE 88
 
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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