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Conserved domains on  [gi|25057132|ref|NP_740234|]
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cytochrome c oxidase subunit II (mitochondrion) [Polyodon spathula]

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 0e+00

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 504.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132    1 MAHPSQLGFQDAASPVMEELLHFHDHTLMIVFLISTLVLYIIVAMVSTKLTNKYVLDSQEIEIVWTVLPAVILILIALPS 80
Cdd:MTH00129   1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYENLGFDSYMIPTQDLTPGQFRLLETDHRMVVPMESPIRVLVSAEDVL 160
Cdd:MTH00129  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132  161 HAWAVPALGIKMDAVPGRLNQTAFITSRPGVYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLMLEES 230
Cdd:MTH00129 161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLMLEDA 230
 
Name Accession Description Interval E-value
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-230 0e+00

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 504.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132    1 MAHPSQLGFQDAASPVMEELLHFHDHTLMIVFLISTLVLYIIVAMVSTKLTNKYVLDSQEIEIVWTVLPAVILILIALPS 80
Cdd:MTH00129   1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYENLGFDSYMIPTQDLTPGQFRLLETDHRMVVPMESPIRVLVSAEDVL 160
Cdd:MTH00129  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132  161 HAWAVPALGIKMDAVPGRLNQTAFITSRPGVYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLMLEES 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 2.47e-97

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: 279.46  E-value: 2.47e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132  93 PHLTIKAMGHQWYWSYEYTDYENLGFDSYMIPTQDLTPGQFRLLETDHRMVVPMESPIRVLVSAEDVLHAWAVPALGIKM 172
Cdd:cd13912   1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 25057132 173 DAVPGRLNQTAFITSRPGVYYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
Cdd:cd13912  81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 1.03e-86

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 252.33  E-value: 1.03e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132    95 LTIKAMGHQWYWSYEYTDYENLGFDSYMIPTQDLTPGQFRLLETDHRMVVPMESPIRVLVSAEDVLHAWAVPALGIKMDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 25057132   175 VPGRLNQTAFITSRPGVYYGQCSEICGANHSFMPIVVEAV 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-222 3.00e-62

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 193.89  E-value: 3.00e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132   6 QLGFQDAASPVMEELLHFHDHTLMIVFLISTLV-LYIIVAMV-----STKLTNKYVLDSQEIEIVWTVLPAVILILIALP 79
Cdd:COG1622  18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVfGLLLYFAIryrrrKGDADPAQFHHNTKLEIVWTVIPIIIVIVLAVP 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132  80 SLRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYENLgfdsymiptqdltpgqfrlleTDHRMVVPMESPIRVLVSAEDV 159
Cdd:COG1622  98 TLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVNELVLPVGRPVRFLLTSADV 156

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25057132 160 LHAWAVPALGIKMDAVPGRLNQTAFITSRPGVYYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
Cdd:COG1622 157 IHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAW 219
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-222 5.07e-48

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: 156.77  E-value: 5.07e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132    12 AASPVMEELLHFHDHTLMIVFLISTLVLYIIVAMV------STKLTNKYVLDSQEIEIVWTVLPAVILI-LIALPSLRIL 84
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVwkfrrkGDEEKPSQIHGNRRLEYVWTVIPLIIVVgLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132    85 YLMDEINDPHLTIKAMGHQWYWSYEYTDYenlgfdsymiptqdltpgqfrLLETDHRMVVPMESPIRVLVSAEDVLHAWA 164
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFW 139

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 25057132   165 VPALGIKMDAVPGRLNQTAFITSRPGVYYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
Cdd:TIGR02866 140 VPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAY 197
 
Name Accession Description Interval E-value
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-230 0e+00

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 504.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132    1 MAHPSQLGFQDAASPVMEELLHFHDHTLMIVFLISTLVLYIIVAMVSTKLTNKYVLDSQEIEIVWTVLPAVILILIALPS 80
Cdd:MTH00129   1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYENLGFDSYMIPTQDLTPGQFRLLETDHRMVVPMESPIRVLVSAEDVL 160
Cdd:MTH00129  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132  161 HAWAVPALGIKMDAVPGRLNQTAFITSRPGVYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLMLEES 230
Cdd:MTH00129 161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLMLEDA 230
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-227 1.15e-171

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 470.94  E-value: 1.15e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132    1 MAHPSQLGFQDAASPVMEELLHFHDHTLMIVFLISTLVLYIIVAMVSTKLTNKYVLDSQEIEIVWTVLPAVILILIALPS 80
Cdd:MTH00117   1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYENLGFDSYMIPTQDLTPGQFRLLETDHRMVVPMESPIRVLVSAEDVL 160
Cdd:MTH00117  81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25057132  161 HAWAVPALGIKMDAVPGRLNQTAFITSRPGVYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLML 227
Cdd:MTH00117 161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLLS 227
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-230 6.21e-167

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 459.35  E-value: 6.21e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132    1 MAHPSQLGFQDAASPVMEELLHFHDHTLMIVFLISTLVLYIIVAMVSTKLTNKYVLDSQEIEIVWTVLPAVILILIALPS 80
Cdd:MTH00185   1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYENLGFDSYMIPTQDLTPGQFRLLETDHRMVVPMESPIRVLVSAEDVL 160
Cdd:MTH00185  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132  161 HAWAVPALGIKMDAVPGRLNQTAFITSRPGVYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLMLEES 230
Cdd:MTH00185 161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLMLEEA 230
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-227 3.35e-157

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 434.53  E-value: 3.35e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132    1 MAHPSQLGFQDAASPVMEELLHFHDHTLMIVFLISTLVLYIIVAMVSTKLTNKYVLDSQEIEIVWTVLPAVILILIALPS 80
Cdd:MTH00098   1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYENLGFDSYMIPTQDLTPGQFRLLETDHRMVVPMESPIRVLVSAEDVL 160
Cdd:MTH00098  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25057132  161 HAWAVPALGIKMDAVPGRLNQTAFITSRPGVYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLML 227
Cdd:MTH00098 161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASML 227
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-228 5.46e-156

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 431.51  E-value: 5.46e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132    1 MAHPSQLGFQDAASPVMEELLHFHDHTLMIVFLISTLVLYIIVAMVSTKLTNKYVLDSQEIEIVWTVLPAVILILIALPS 80
Cdd:MTH00076   1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYENLGFDSYMIPTQDLTPGQFRLLETDHRMVVPMESPIRVLVSAEDVL 160
Cdd:MTH00076  81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25057132  161 HAWAVPALGIKMDAVPGRLNQTAFITSRPGVYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLMLE 228
Cdd:MTH00076 161 HSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSMLE 228
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-224 1.70e-143

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 399.74  E-value: 1.70e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132    1 MAHPSQLGFQDAASPVMEELLHFHDHTLMIVFLISTLVLYIIVAMVSTKLTNKYVLDSQEIEIVWTVLPAVILILIALPS 80
Cdd:MTH00168   1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYENLGFDSYMIPTQDLTPGQFRLLETDHRMVVPMESPIRVLVSAEDVL 160
Cdd:MTH00168  81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25057132  161 HAWAVPALGIKMDAVPGRLNQTAFITSRPGVYYGQCSEICGANHSFMPIVVEAVPLEHFENWSS 224
Cdd:MTH00168 161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVD 224
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-227 1.72e-143

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 399.97  E-value: 1.72e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132    1 MAHPSQLGFQDAASPVMEELLHFHDHTLMIVFLISTLVLYIIVAMVSTKLTNKYVLDSQEIEIVWTVLPAVILILIALPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYENLGFDSYMIPTQDLTPGQFRLLETDHRMVVPMESPIRVLVSAEDVL 160
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25057132  161 HAWAVPALGIKMDAVPGRLNQTAFITSRPGVYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLML 227
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-229 8.53e-137

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 383.28  E-value: 8.53e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132    1 MAHPSQLGFQDAASPVMEELLHFHDHTLMIVFLISTLVLYIIVAMVSTKLTNKYVLDSQEIEIVWTVLPAVILILIALPS 80
Cdd:MTH00038   1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYENLGFDSYMIPTQDLTPGQFRLLETDHRMVVPMESPIRVLVSAEDVL 160
Cdd:MTH00038  81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25057132  161 HAWAVPALGIKMDAVPGRLNQTAFITSRPGVYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLMLEE 229
Cdd:MTH00038 161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFLEE 229
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-226 1.01e-128

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 362.72  E-value: 1.01e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132    1 MAHPSQLGFQDAASPVMEELLHFHDHTLMIVFLISTLVLYIIVAMVSTKLTNKYVLDSQEIEIVWTVLPAVILILIALPS 80
Cdd:MTH00140   1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYENLGFDSYMIPTQDLTPGQFRLLETDHRMVVPMESPIRVLVSAEDVL 160
Cdd:MTH00140  81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25057132  161 HAWAVPALGIKMDAVPGRLNQTAFITSRPGVYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLM 226
Cdd:MTH00140 161 HSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELM 226
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-222 6.82e-127

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 357.88  E-value: 6.82e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132    1 MAHPSQLGFQDAASPVMEELLHFHDHTLMIVFLISTLVLYIIVAMVSTKLTNKYVLDSQEIEIVWTVLPAVILILIALPS 80
Cdd:MTH00139   1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYENLGFDSYMIPTQDLTPGQFRLLETDHRMVVPMESPIRVLVSAEDVL 160
Cdd:MTH00139  81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25057132  161 HAWAVPALGIKMDAVPGRLNQTAFITSRPGVYYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
Cdd:MTH00139 161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEW 222
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-224 8.26e-120

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 340.29  E-value: 8.26e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132    1 MAHPSQLGFQDAASPVMEELLHFHDHTLMIVFLISTLVLYIIVAMVSTKLTNKYVLDSQEIEIVWTVLPAVILILIALPS 80
Cdd:MTH00008   1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYENLGFDSYMIPTQDLTPGQFRLLETDHRMVVPMESPIRVLVSAEDVL 160
Cdd:MTH00008  81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25057132  161 HAWAVPALGIKMDAVPGRLNQTAFITSRPGVYYGQCSEICGANHSFMPIVVEAVPLEHFENWSS 224
Cdd:MTH00008 161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVS 224
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 2-224 2.01e-119

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 339.42  E-value: 2.01e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132    2 AHPSQLGFQDAASPVMEELLHFHDHTLMIVFLISTLVLYIIVAMVSTKLTNKYVLDSQEIEIVWTVLPAVILILIALPSL 81
Cdd:MTH00023  11 PEPWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132   82 RILYLMDEINDPHLTIKAMGHQWYWSYEYTDY--ENLGFDSYMIPTQDLTPGQFRLLETDHRMVVPMESPIRVLVSAEDV 159
Cdd:MTH00023  91 KLLYLMDEVVSPALTIKAIGHQWYWSYEYSDYegETLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADV 170

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25057132  160 LHAWAVPALGIKMDAVPGRLNQTAFITSRPGVYYGQCSEICGANHSFMPIVVEAVPLEHFENWSS 224
Cdd:MTH00023 171 LHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLL 235
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 2-229 8.22e-114

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 325.20  E-value: 8.22e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132    2 AHPSQLGFQDAASPVMEELLHFHDHTLMIVFLISTLVLYIIVAMVSTKLTNKYVLDSQEIEIVWTVLPAVILILIALPSL 81
Cdd:MTH00051   4 PEPWQLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132   82 RILYLMDEINDPHLTIKAMGHQWYWSYEYTDY--ENLGFDSYMIPTQDLTPGQFRLLETDHRMVVPMESPIRVLVSAEDV 159
Cdd:MTH00051  84 KLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADV 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132  160 LHAWAVPALGIKMDAVPGRLNQTAFITSRPGVYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLMLEE 229
Cdd:MTH00051 164 LHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQSEE 233
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-222 2.47e-97

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: 279.46  E-value: 2.47e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132  93 PHLTIKAMGHQWYWSYEYTDYENLGFDSYMIPTQDLTPGQFRLLETDHRMVVPMESPIRVLVSAEDVLHAWAVPALGIKM 172
Cdd:cd13912   1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 25057132 173 DAVPGRLNQTAFITSRPGVYYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
Cdd:cd13912  81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 4-222 7.80e-89

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 263.04  E-value: 7.80e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132    4 PSQLGFQDAASPVMEELLHFHDHTLMIVFLISTLVLYIIVAMVstkLTNKYV------LDSQEIEIVWTVLPAVILILIA 77
Cdd:MTH00027  32 PWQLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRIL---LGNNYYsyywnkLDGSLIEVIWTLIPAFILILIA 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132   78 LPSLRILYLMDE-INDPHLTIKAMGHQWYWSYEYTDY--ENLGFDSYMIPTQDLTPGQFRLLETDHRMVVPMESPIRVLV 154
Cdd:MTH00027 109 FPSLRLLYIMDEcGFSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLI 188

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25057132  155 SAEDVLHAWAVPALGIKMDAVPGRLNQTAFITSRPGVYYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
Cdd:MTH00027 189 TAADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDW 256
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 1.03e-86

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 252.33  E-value: 1.03e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132    95 LTIKAMGHQWYWSYEYTDYENLGFDSYMIPTQDLTPGQFRLLETDHRMVVPMESPIRVLVSAEDVLHAWAVPALGIKMDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 25057132   175 VPGRLNQTAFITSRPGVYYGQCSEICGANHSFMPIVVEAV 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 23-228 1.12e-76

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 231.05  E-value: 1.12e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132   23 FHDHTLMIVFLISTLVLYIIVAMVSTKLTNKYVLDSQEIEIVWTVLPAVILILIALPSLRILYLMDEIN-DPHLTIKAMG 101
Cdd:MTH00080  25 FNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMNlDSNLTVKVTG 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132  102 HQWYWSYEYTDYENLGFDSYMIPTQDLTPGQFRLLETDHRMVVPMESPIRVLVSAEDVLHAWAVPALGIKMDAVPGRLNQ 181
Cdd:MTH00080 105 HQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILST 184

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 25057132  182 TAFITSRPGVYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLMLE 228
Cdd:MTH00080 185 LCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWCKLLLD 231
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-222 3.00e-62

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 193.89  E-value: 3.00e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132   6 QLGFQDAASPVMEELLHFHDHTLMIVFLISTLV-LYIIVAMV-----STKLTNKYVLDSQEIEIVWTVLPAVILILIALP 79
Cdd:COG1622  18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVfGLLLYFAIryrrrKGDADPAQFHHNTKLEIVWTVIPIIIVIVLAVP 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132  80 SLRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYENLgfdsymiptqdltpgqfrlleTDHRMVVPMESPIRVLVSAEDV 159
Cdd:COG1622  98 TLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVNELVLPVGRPVRFLLTSADV 156

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25057132 160 LHAWAVPALGIKMDAVPGRLNQTAFITSRPGVYYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
Cdd:COG1622 157 IHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAW 219
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-222 5.07e-48

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: 156.77  E-value: 5.07e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132    12 AASPVMEELLHFHDHTLMIVFLISTLVLYIIVAMV------STKLTNKYVLDSQEIEIVWTVLPAVILI-LIALPSLRIL 84
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVwkfrrkGDEEKPSQIHGNRRLEYVWTVIPLIIVVgLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132    85 YLMDEINDPHLTIKAMGHQWYWSYEYTDYenlgfdsymiptqdltpgqfrLLETDHRMVVPMESPIRVLVSAEDVLHAWA 164
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFW 139

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 25057132   165 VPALGIKMDAVPGRLNQTAFITSRPGVYYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
Cdd:TIGR02866 140 VPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAY 197
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 17-214 5.19e-45

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 148.95  E-value: 5.19e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132   17 MEELLHFHDHTLMIVFLISTLVLYIIVAM----VSTKLTNKYVLDSQEIEIVWTVLPAVI-LILIALPSLRILYLMDEIn 91
Cdd:MTH00047   1 MNLSLLYYDIVCYILALCVFIPCWVYIMLcwqvVSGNGSVNFGSENQVLELLWTVVPTLLvLVLCFLNLNFITSDLDCF- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132   92 dPHLTIKAMGHQWYWSYEYTDyeNLGFDSYMIptqDLTPGqfrlleTDHRMVVPMESPIRVLVSAEDVLHAWAVPALGIK 171
Cdd:MTH00047  80 -SSETIKVIGHQWYWSYEYSF--GGSYDSFMT---DDIFG------VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLK 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 25057132  172 MDAVPGRLNQTAFITSRPGVYYGQCSEICGANHSFMPIVVEAV 214
Cdd:MTH00047 148 MDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVV 190
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 118-219 2.58e-41

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 138.41  E-value: 2.58e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132  118 FDSYMIPTQDLTPGQFRLLETDHRMVVPMESPIRVLVSAEDVLHAWAVPALGIKMDAVPGRLNQTAFITSRPGVYYGQCS 197
Cdd:PTZ00047  51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                         90       100
                 ....*....|....*....|..
gi 25057132  198 EICGANHSFMPIVVEAVPLEHF 219
Cdd:PTZ00047 131 EMCGTLHGFMPIVVEAVSPEAY 152
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-212 4.18e-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: 110.08  E-value: 4.18e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132  95 LTIKAMGHQWYWSYEYTDyenlgfdsymiptqdltpgqfrlLETDHRMVVPMESPIRVLVSAEDVLHAWAVPALGIKMDA 174
Cdd:cd13842   1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 25057132 175 VPGRLNQTAFITSRPGVYYGQCSEICGANHSFMPIVVE 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 1.69e-29

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: 106.16  E-value: 1.69e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132  94 HLTIKAMGHQWYWSYEYTDYENLGFdsymiptqdltpgqfrllETDHRMVVPMESPIRVLVSAEDVLHAWAVPALGIKMD 173
Cdd:cd04213   1 ALTIEVTGHQWWWEFRYPDEPGRGI------------------VTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMD 62

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 25057132 174 AVPGRLNQTAFITSRPGVYYGQCSEICGANHSFMPIVVEAV 214
Cdd:cd04213  63 MIPGRTNRLWLQADEPGVYRGQCAEFCGASHALMRFKVIAL 103
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-83 1.77e-29

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: 105.49  E-value: 1.77e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132     1 MAHPSQLGFQDAASPVMEELLHFHDHTLMIVFLISTLVLYIIVAMV------STKLTNKYVLDSQEIEIVWTVLPAVILI 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLirfnrrKNPITARYTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 25057132    75 LIALPSLRI 83
Cdd:pfam02790  81 LIALPSFKL 89
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 68-222 1.57e-26

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: 99.45  E-value: 1.57e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132  68 LPAVILI-LIALPSLRILYLMD---EINDPHLTIKAMGHQWYWSYEYtdyENLGfdsymiptqdltpgqfrllETDHRMV 143
Cdd:cd13918   2 LSAIIVIsLIVWTYGMLLYVEDppdEADEDALEVEVEGFQFGWQFEY---PNGV-------------------TTGNTLR 59

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25057132 144 VPMESPIRVLVSAEDVLHAWAVPALGIKMDAVPGRLNQTAFITSRPGVYYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
Cdd:cd13918  60 VPADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAW 138
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-212 3.50e-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: 92.32  E-value: 3.50e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132  95 LTIKAMGHQWYWSYEYTDYenlgfDSYMIPTQDLTPGQfrlletdhrMVVPMESPIRVLVSAEDVLHAWAVPALGIKMDA 174
Cdd:cd13919   2 LVVEVTAQQWAWTFRYPGG-----DGKLGTDDDVTSPE---------LHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 25057132 175 VPGRLNQTAFITSRPGVYYGQCSEICGANHSFM--PIVVE 212
Cdd:cd13919  68 VPGRTTRLWFTPTREGEYEVRCAELCGLGHYRMraTVKVV 107
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-213 7.76e-23

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


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 88.84  E-value: 7.76e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132  95 LTIKAMGHQWYWSYEYtdyenlgfdsymiptqdltPGQFRlleTDHRMVVPMESPIRVLVSAEDVLHAWAVPALGIKMDA 174
Cdd:cd13915   2 LEIQVTGRQWMWEFTY-------------------PNGKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDV 59

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 25057132 175 VPGRLNQTAFITSRPGVYYGQCSEICGANHSFMPIVVEA 213
Cdd:cd13915  60 VPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGMIGKVRV 98
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 96-222 7.05e-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: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 86.69  E-value: 7.05e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132  96 TIKAMGHQWYWSYEYTDYENlgfdsymiptqdltpgqfrllETDHRMVVPMESPIRVLVSAEDVLHAWAVPALGIKMDAV 175
Cdd:cd13914   2 EIEVEAYQWGWEFSYPEANV---------------------TTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAF 60

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 25057132 176 PGRLNQTAFITSRPGVYYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
Cdd:cd13914  61 PGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQW 107
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 142-212 6.00e-08

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: 49.11  E-value: 6.00e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25057132 142 MVVPMESPIRVLVSAEDVLHAWAVPALGIKMDAVPGRLNQTAFITSRPGVYYGQCSEICGANHSFM--PIVVE 212
Cdd:cd13913  27 IEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNMygKIIVE 99
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 96-207 1.72e-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: 42.37  E-value: 1.72e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132  96 TIKAMGHQWYWSyeytdyenlgfdsymiptqdLTPGQFrlletdhrmvvPMESPIRVLVSAEDVLHAWAV--PALGI--K 171
Cdd:cd13916   2 VVAVTGHQWYWE--------------------LSRTEI-----------PAGKPVEFRVTSADVNHGFGIydPDMRLlaQ 50

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 25057132 172 MDAVPGRLNQTAFITSRPGVYYGQCSEICGANHSFM 207
Cdd:cd13916  51 TQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 156-207 3.67e-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: 41.45  E-value: 3.67e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 25057132 156 AEDVLHAWAVPALGIKMDAVPGRLNQTAFITSRPGVYYGQCSEICGANHSFM 207
Cdd:cd04223  36 DEDITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALHLEM 87
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 95-214 6.09e-05

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


Pssm-ID: 259874 [Multi-domain]  Cd Length: 99  Bit Score: 40.61  E-value: 6.09e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132  95 LTIKAMGHQWYWSYEYtdyenlgfdsymiPTQDLtpgqfrllETDHRMVVPMESPIRVLVSAEDVLHAWAVPALGIKMDA 174
Cdd:cd04212   1 LEIQVVSLDWKWLFIY-------------PEQGI--------ATVNELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYA 59

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 25057132 175 VPGRLNQTAFITSRPGVYYGQCSEICGANHSFMPIVVEAV 214
Cdd:cd04212  60 MAGMQTQLHLIADKPGTYQGLSANYSGEGFSDMKFKVLAV 99
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 97-212 6.70e-05

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: 41.06  E-value: 6.70e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132  97 IKAMGHQWYWSYEYTDYENLGFDSYMIPTQDLTpgQFRLLETDHR--MVVPMESPIRVlVSAEDVLHAWAVPALGIKmda 174
Cdd:cd00920   1 ITVTASDWGWSFTYNGVLLFGPPVLVVPVGDTV--RVQFVNKLGEnhSVTIAGFGVPV-VAMAGGANPGLVNTLVIG--- 74

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 25057132 175 vPGRLNQTAFITSRPGVYYGQCSEICGaNHSFMPIVVE 212
Cdd:cd00920  75 -PGESAEVTFTTDQAGVYWFYCTIPGH-NHAGMVGTIN 110
PRK02888 PRK02888
nitrous-oxide reductase; Validated
 157-213 1.20e-04

nitrous-oxide reductase; Validated


Pssm-ID: 235082 [Multi-domain]  Cd Length: 635  Bit Score: 42.66  E-value: 1.20e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25057132  157 EDVLHAWAVPALGIKMDAVPgrlNQTA---FITSRPGVYYGQCSEICGANHSFMP--IVVEA 213
Cdd:PRK02888 576 EDLTHGFAIPNYGVNMEVAP---QATAsvtFTADKPGVYWYYCTWFCHALHMEMRgrMLVEP 634
PRK10525 PRK10525
cytochrome o ubiquinol oxidase subunit II; Provisional
 58-222 6.54e-03

cytochrome o ubiquinol oxidase subunit II; Provisional


Pssm-ID: 182518 [Multi-domain]  Cd Length: 315  Bit Score: 37.09  E-value: 6.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132   58 SQEIE-IVWTVlPAVILILIALPSLRILYLMDEI-----NDPHLTIKAMGHQWYWSYEYtdyenlgfdsymiPTQDLTpg 131
Cdd:PRK10525  85 SNKVEaVVWTV-PILIIIFLAVLTWKTTHALEPSkplahDEKPITIEVVSMDWKWFFIY-------------PEQGIA-- 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25057132  132 qfrlleTDHRMVVPMESPIRVLVSAEDVLHAWAVPALGIKMDAVPGRLNQTAFITSRPGVYYGQCSEICGANHSFMPIVV 211
Cdd:PRK10525 149 ------TVNEIAFPANVPVYFKVTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIANEPGTYDGISASYSGPGFSGMKFKA 222

                        170
                 ....*....|..
gi 25057132  212 EAVP-LEHFENW 222
Cdd:PRK10525 223 IATPdRAEFDQW 234
 
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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