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Conserved domains on  [gi|115494667|ref|YP_778620|]
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cytochrome c oxidase subunit II (mitochondrion) [Bufo gargarizans]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11475891)

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 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-228 8.79e-169

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 463.87  E-value: 8.79e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667   1 MAHPLQLGFQDAASPIMEELLHFHDHTLMAVFLISTLVLYIISTLMSTKLSNTNTIDAQEIEMVWTIMPAIILIVIALPS 80
Cdd:MTH00076   1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667  81 LRILYLMDEVSNPDVTIKAIGHQWYWSYEYSDFNDLSFDSYMIPSKDLLPGQFRLLEVDNRMTTPVGMTTRTLITAEDVL 160
Cdd:MTH00076  81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115494667 161 HSWAVPSLGVKLDAIPGRLNQTSFIISRPGVYYGQCSEICGANHSFMPIVVESLPIKEFLNWSSASVN 228
Cdd:MTH00076 161 HSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSMLE 228
 
Name Accession Description Interval E-value
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-228 8.79e-169

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 463.87  E-value: 8.79e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667   1 MAHPLQLGFQDAASPIMEELLHFHDHTLMAVFLISTLVLYIISTLMSTKLSNTNTIDAQEIEMVWTIMPAIILIVIALPS 80
Cdd:MTH00076   1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667  81 LRILYLMDEVSNPDVTIKAIGHQWYWSYEYSDFNDLSFDSYMIPSKDLLPGQFRLLEVDNRMTTPVGMTTRTLITAEDVL 160
Cdd:MTH00076  81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115494667 161 HSWAVPSLGVKLDAIPGRLNQTSFIISRPGVYYGQCSEICGANHSFMPIVVESLPIKEFLNWSSASVN 228
Cdd:MTH00076 161 HSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSMLE 228
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-222 4.83e-96

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: 275.99  E-value: 4.83e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667  93 PDVTIKAIGHQWYWSYEYSDFNDLSFDSYMIPSKDLLPGQFRLLEVDNRMTTPVGMTTRTLITAEDVLHSWAVPSLGVKL 172
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 115494667 173 DAIPGRLNQTSFIISRPGVYYGQCSEICGANHSFMPIVVESLPIKEFLNW 222
Cdd:cd13912   81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
96-213 8.30e-83

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 242.32  E-value: 8.30e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667   96 TIKAIGHQWYWSYEYSDFNDLSFDSYMIPSKDLLPGQFRLLEVDNRMTTPVGMTTRTLITAEDVLHSWAVPSLGVKLDAI 175
Cdd:pfam00116   2 TIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDAV 81

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 115494667  176 PGRLNQTSFIISRPGVYYGQCSEICGANHSFMPIVVES 213
Cdd:pfam00116  82 PGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEA 119
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-222 1.15e-60

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 190.04  E-value: 1.15e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667   6 QLGFQDAASPIMEELLHFHDHTL--MAVFLISTLVLYIISTLMSTKlSNTNTIDAQE-----IEMVWTIMPAIILIVIAL 78
Cdd:COG1622   18 QLSLPDPAGPIAEEIDDLFWVSLiiMLVIFVLVFGLLLYFAIRYRR-RKGDADPAQFhhntkLEIVWTVIPIIIVIVLAV 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667  79 PSLRILYLMDEVSNPDVTIKAIGHQWYWSYEYSDFNDLsfdsymipskdllpgqfrlleVDNRMTTPVGMTTRTLITAED 158
Cdd:COG1622   97 PTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVNELVLPVGRPVRFLLTSAD 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115494667 159 VLHSWAVPSLGVKLDAIPGRLNQTSFIISRPGVYYGQCSEICGANHSFMPIVVESLPIKEFLNW 222
Cdd:COG1622  156 VIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAW 219
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-222 1.04e-44

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: 148.30  E-value: 1.04e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667   12 AASPIMEELLHFHDHTLMAVFLISTLVL-YIISTLMSTKLSNTNTIDAQE-----IEMVWTIMPAIILI-VIALPSLRIL 84
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAaLLAYVVWKFRRKGDEEKPSQIhgnrrLEYVWTVIPLIIVVgLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667   85 YLMDEVSNPDVTIKAIGHQWYWSYEYSDFndlsfdsymipskdllpgqfrLLEVDNRMTTPVGMTTRTLITAEDVLHSWA 164
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFW 139

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 115494667  165 VPSLGVKLDAIPGRLNQTSFIISRPGVYYGQCSEICGANHSFMPIVVESLPIKEFLNW 222
Cdd:TIGR02866 140 VPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAY 197
 
Name Accession Description Interval E-value
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-228 8.79e-169

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 463.87  E-value: 8.79e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667   1 MAHPLQLGFQDAASPIMEELLHFHDHTLMAVFLISTLVLYIISTLMSTKLSNTNTIDAQEIEMVWTIMPAIILIVIALPS 80
Cdd:MTH00076   1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667  81 LRILYLMDEVSNPDVTIKAIGHQWYWSYEYSDFNDLSFDSYMIPSKDLLPGQFRLLEVDNRMTTPVGMTTRTLITAEDVL 160
Cdd:MTH00076  81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115494667 161 HSWAVPSLGVKLDAIPGRLNQTSFIISRPGVYYGQCSEICGANHSFMPIVVESLPIKEFLNWSSASVN 228
Cdd:MTH00076 161 HSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSMLE 228
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-224 5.20e-164

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 451.68  E-value: 5.20e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667   1 MAHPLQLGFQDAASPIMEELLHFHDHTLMAVFLISTLVLYIISTLMSTKLSNTNTIDAQEIEMVWTIMPAIILIVIALPS 80
Cdd:MTH00117   1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667  81 LRILYLMDEVSNPDVTIKAIGHQWYWSYEYSDFNDLSFDSYMIPSKDLLPGQFRLLEVDNRMTTPVGMTTRTLITAEDVL 160
Cdd:MTH00117  81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115494667 161 HSWAVPSLGVKLDAIPGRLNQTSFIISRPGVYYGQCSEICGANHSFMPIVVESLPIKEFLNWSS 224
Cdd:MTH00117 161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSS 224
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-224 9.55e-151

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 418.35  E-value: 9.55e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667   1 MAHPLQLGFQDAASPIMEELLHFHDHTLMAVFLISTLVLYIISTLMSTKLSNTNTIDAQEIEMVWTIMPAIILIVIALPS 80
Cdd:MTH00129   1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667  81 LRILYLMDEVSNPDVTIKAIGHQWYWSYEYSDFNDLSFDSYMIPSKDLLPGQFRLLEVDNRMTTPVGMTTRTLITAEDVL 160
Cdd:MTH00129  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115494667 161 HSWAVPSLGVKLDAIPGRLNQTSFIISRPGVYYGQCSEICGANHSFMPIVVESLPIKEFLNWSS 224
Cdd:MTH00129 161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSS 224
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-224 1.45e-150

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 417.58  E-value: 1.45e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667   1 MAHPLQLGFQDAASPIMEELLHFHDHTLMAVFLISTLVLYIISTLMSTKLSNTNTIDAQEIEMVWTIMPAIILIVIALPS 80
Cdd:MTH00098   1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667  81 LRILYLMDEVSNPDVTIKAIGHQWYWSYEYSDFNDLSFDSYMIPSKDLLPGQFRLLEVDNRMTTPVGMTTRTLITAEDVL 160
Cdd:MTH00098  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115494667 161 HSWAVPSLGVKLDAIPGRLNQTSFIISRPGVYYGQCSEICGANHSFMPIVVESLPIKEFLNWSS 224
Cdd:MTH00098 161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSA 224
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-224 3.01e-140

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 391.50  E-value: 3.01e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667   1 MAHPLQLGFQDAASPIMEELLHFHDHTLMAVFLISTLVLYIISTLMSTKLSNTNTIDAQEIEMVWTIMPAIILIVIALPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667  81 LRILYLMDEVSNPDVTIKAIGHQWYWSYEYSDFNDLSFDSYMIPSKDLLPGQFRLLEVDNRMTTPVGMTTRTLITAEDVL 160
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115494667 161 HSWAVPSLGVKLDAIPGRLNQTSFIISRPGVYYGQCSEICGANHSFMPIVVESLPIKEFLNWSS 224
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIK 224
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-224 4.70e-138

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 386.16  E-value: 4.70e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667   1 MAHPLQLGFQDAASPIMEELLHFHDHTLMAVFLISTLVLYIISTLMSTKLSNTNTIDAQEIEMVWTIMPAIILIVIALPS 80
Cdd:MTH00185   1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667  81 LRILYLMDEVSNPDVTIKAIGHQWYWSYEYSDFNDLSFDSYMIPSKDLLPGQFRLLEVDNRMTTPVGMTTRTLITAEDVL 160
Cdd:MTH00185  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115494667 161 HSWAVPSLGVKLDAIPGRLNQTSFIISRPGVYYGQCSEICGANHSFMPIVVESLPIKEFLNWSS 224
Cdd:MTH00185 161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSS 224
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-225 6.53e-132

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 370.47  E-value: 6.53e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667   1 MAHPLQLGFQDAASPIMEELLHFHDHTLMAVFLISTLVLYIISTLMSTKLSNTNTIDAQEIEMVWTIMPAIILIVIALPS 80
Cdd:MTH00168   1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667  81 LRILYLMDEVSNPDVTIKAIGHQWYWSYEYSDFNDLSFDSYMIPSKDLLPGQFRLLEVDNRMTTPVGMTTRTLITAEDVL 160
Cdd:MTH00168  81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115494667 161 HSWAVPSLGVKLDAIPGRLNQTSFIISRPGVYYGQCSEICGANHSFMPIVVESLPIKEFLNWSSA 225
Cdd:MTH00168 161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVDS 225
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 6-222 1.57e-128

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 361.95  E-value: 1.57e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667   6 QLGFQDAASPIMEELLHFHDHTLMAVFLISTLVLYIISTLMSTKLSNTNTIDAQEIEMVWTIMPAIILIVIALPSLRILY 85
Cdd:MTH00140   6 QLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPSLRLLY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667  86 LMDEVSNPDVTIKAIGHQWYWSYEYSDFNDLSFDSYMIPSKDLLPGQFRLLEVDNRMTTPVGMTTRTLITAEDVLHSWAV 165
Cdd:MTH00140  86 LLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTV 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 115494667 166 PSLGVKLDAIPGRLNQTSFIISRPGVYYGQCSEICGANHSFMPIVVESLPIKEFLNW 222
Cdd:MTH00140 166 PSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKW 222
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-224 2.95e-126

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 356.32  E-value: 2.95e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667   1 MAHPLQLGFQDAASPIMEELLHFHDHTLMAVFLISTLVLYIISTLMSTKLSNTNTIDAQEIEMVWTIMPAIILIVIALPS 80
Cdd:MTH00038   1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667  81 LRILYLMDEVSNPDVTIKAIGHQWYWSYEYSDFNDLSFDSYMIPSKDLLPGQFRLLEVDNRMTTPVGMTTRTLITAEDVL 160
Cdd:MTH00038  81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115494667 161 HSWAVPSLGVKLDAIPGRLNQTSFIISRPGVYYGQCSEICGANHSFMPIVVESLPIKEFLNWSS 224
Cdd:MTH00038 161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVS 224
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-222 7.34e-124

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 350.17  E-value: 7.34e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667   1 MAHPLQLGFQDAASPIMEELLHFHDHTLMAVFLISTLVLYIISTLMSTKLSNTNTIDAQEIEMVWTIMPAIILIVIALPS 80
Cdd:MTH00139   1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667  81 LRILYLMDEVSNPDVTIKAIGHQWYWSYEYSDFNDLSFDSYMIPSKDLLPGQFRLLEVDNRMTTPVGMTTRTLITAEDVL 160
Cdd:MTH00139  81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115494667 161 HSWAVPSLGVKLDAIPGRLNQTSFIISRPGVYYGQCSEICGANHSFMPIVVESLPIKEFLNW 222
Cdd:MTH00139 161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEW 222
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-224 1.37e-118

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 336.83  E-value: 1.37e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667   1 MAHPLQLGFQDAASPIMEELLHFHDHTLMAVFLISTLVLYIISTLMSTKLSNTNTIDAQEIEMVWTIMPAIILIVIALPS 80
Cdd:MTH00008   1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667  81 LRILYLMDEVSNPDVTIKAIGHQWYWSYEYSDFNDLSFDSYMIPSKDLLPGQFRLLEVDNRMTTPVGMTTRTLITAEDVL 160
Cdd:MTH00008  81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115494667 161 HSWAVPSLGVKLDAIPGRLNQTSFIISRPGVYYGQCSEICGANHSFMPIVVESLPIKEFLNWSS 224
Cdd:MTH00008 161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVS 224
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 2-228 3.26e-112

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 321.31  E-value: 3.26e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667   2 AHPLQLGFQDAASPIMEELLHFHDHTLMAVFLISTLVLYIISTLMSTKLSNTNTIDAQEIEMVWTIMPAIILIVIALPSL 81
Cdd:MTH00023  11 PEPWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667  82 RILYLMDEVSNPDVTIKAIGHQWYWSYEYSDFND--LSFDSYMIPSKDLLPGQFRLLEVDNRMTTPVGMTTRTLITAEDV 159
Cdd:MTH00023  91 KLLYLMDEVVSPALTIKAIGHQWYWSYEYSDYEGetLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADV 170

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115494667 160 LHSWAVPSLGVKLDAIPGRLNQTSFIISRPGVYYGQCSEICGANHSFMPIVVESLPIKEFLNWSSASVN 228
Cdd:MTH00023 171 LHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLSLSN 239
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 2-225 8.44e-111

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 317.49  E-value: 8.44e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667   2 AHPLQLGFQDAASPIMEELLHFHDHTLMAVFLISTLVLYIISTLMSTKLSNTNTIDAQEIEMVWTIMPAIILIVIALPSL 81
Cdd:MTH00051   4 PEPWQLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667  82 RILYLMDEVSNPDVTIKAIGHQWYWSYEYSDF--NDLSFDSYMIPSKDLLPGQFRLLEVDNRMTTPVGMTTRTLITAEDV 159
Cdd:MTH00051  84 KLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADV 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 115494667 160 LHSWAVPSLGVKLDAIPGRLNQTSFIISRPGVYYGQCSEICGANHSFMPIVVESLPIKEFLNWSSA 225
Cdd:MTH00051 164 LHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVAT 229
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-222 4.83e-96

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: 275.99  E-value: 4.83e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667  93 PDVTIKAIGHQWYWSYEYSDFNDLSFDSYMIPSKDLLPGQFRLLEVDNRMTTPVGMTTRTLITAEDVLHSWAVPSLGVKL 172
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 115494667 173 DAIPGRLNQTSFIISRPGVYYGQCSEICGANHSFMPIVVESLPIKEFLNW 222
Cdd:cd13912   81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 4-222 2.61e-87

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 258.80  E-value: 2.61e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667   4 PLQLGFQDAASPIMEELLHFHDHTLMAVFLISTLVLY-IISTLMSTKLSNT--NTIDAQEIEMVWTIMPAIILIVIALPS 80
Cdd:MTH00027  32 PWQLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWlIIRILLGNNYYSYywNKLDGSLIEVIWTLIPAFILILIAFPS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667  81 LRILYLMDE-VSNPDVTIKAIGHQWYWSYEYSDFND--LSFDSYMIPSKDLLPGQFRLLEVDNRMTTPVGMTTRTLITAE 157
Cdd:MTH00027 112 LRLLYIMDEcGFSANITIKVTGHQWYWSYSYEDYGEknIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAA 191

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115494667 158 DVLHSWAVPSLGVKLDAIPGRLNQTSFIISRPGVYYGQCSEICGANHSFMPIVVESLPIKEFLNW 222
Cdd:MTH00027 192 DVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDW 256
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
96-213 8.30e-83

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 242.32  E-value: 8.30e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667   96 TIKAIGHQWYWSYEYSDFNDLSFDSYMIPSKDLLPGQFRLLEVDNRMTTPVGMTTRTLITAEDVLHSWAVPSLGVKLDAI 175
Cdd:pfam00116   2 TIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDAV 81

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 115494667  176 PGRLNQTSFIISRPGVYYGQCSEICGANHSFMPIVVES 213
Cdd:pfam00116  82 PGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEA 119
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 23-223 2.47e-75

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 227.20  E-value: 2.47e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667  23 FHDHTLMAVFLISTLVLYIISTLMSTKLSNTNTIDAQEIEMVWTIMPAIILIVIALPSLRILY---LMDEVSNpdVTIKA 99
Cdd:MTH00080  25 FNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYyygLMNLDSN--LTVKV 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667 100 IGHQWYWSYEYSDFNDLSFDSYMIPSKDLLPGQFRLLEVDNRMTTPVGMTTRTLITAEDVLHSWAVPSLGVKLDAIPGRL 179
Cdd:MTH00080 103 TGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGIL 182

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 115494667 180 NQTSFIISRPGVYYGQCSEICGANHSFMPIVVESLPIKEFLNWS 223
Cdd:MTH00080 183 STLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWC 226
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-222 1.15e-60

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 190.04  E-value: 1.15e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667   6 QLGFQDAASPIMEELLHFHDHTL--MAVFLISTLVLYIISTLMSTKlSNTNTIDAQE-----IEMVWTIMPAIILIVIAL 78
Cdd:COG1622   18 QLSLPDPAGPIAEEIDDLFWVSLiiMLVIFVLVFGLLLYFAIRYRR-RKGDADPAQFhhntkLEIVWTVIPIIIVIVLAV 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667  79 PSLRILYLMDEVSNPDVTIKAIGHQWYWSYEYSDFNDLsfdsymipskdllpgqfrlleVDNRMTTPVGMTTRTLITAED 158
Cdd:COG1622   97 PTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVNELVLPVGRPVRFLLTSAD 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115494667 159 VLHSWAVPSLGVKLDAIPGRLNQTSFIISRPGVYYGQCSEICGANHSFMPIVVESLPIKEFLNW 222
Cdd:COG1622  156 VIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAW 219
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 57-212 3.87e-49

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 159.35  E-value: 3.87e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667  57 DAQEIEMVWTIMPAIILIVIALPSLR-ILYLMDEVSNpdVTIKAIGHQWYWSYEYSDfnDLSFDSYMIpskDLLPGqfrl 135
Cdd:MTH00047  45 ENQVLELLWTVVPTLLVLVLCFLNLNfITSDLDCFSS--ETIKVIGHQWYWSYEYSF--GGSYDSFMT---DDIFG---- 113

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 115494667 136 leVDNRMTTPVGMTTRTLITAEDVLHSWAVPSLGVKLDAIPGRLNQTSFIISRPGVYYGQCSEICGANHSFMPIVVE 212
Cdd:MTH00047 114 --VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIE 188
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-222 1.04e-44

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: 148.30  E-value: 1.04e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667   12 AASPIMEELLHFHDHTLMAVFLISTLVL-YIISTLMSTKLSNTNTIDAQE-----IEMVWTIMPAIILI-VIALPSLRIL 84
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAaLLAYVVWKFRRKGDEEKPSQIhgnrrLEYVWTVIPLIIVVgLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667   85 YLMDEVSNPDVTIKAIGHQWYWSYEYSDFndlsfdsymipskdllpgqfrLLEVDNRMTTPVGMTTRTLITAEDVLHSWA 164
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFW 139

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 115494667  165 VPSLGVKLDAIPGRLNQTSFIISRPGVYYGQCSEICGANHSFMPIVVESLPIKEFLNW 222
Cdd:TIGR02866 140 VPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAY 197
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 117-214 1.43e-43

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 144.19  E-value: 1.43e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667 117 SFDSYMIPSKDLLPGQFRLLEVDNRMTTPVGMTTRTLITAEDVLHSWAVPSLGVKLDAIPGRLNQTSFIISRPGVYYGQC 196
Cdd:PTZ00047  50 SFQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQC 129

                         90
                 ....*....|....*...
gi 115494667 197 SEICGANHSFMPIVVESL 214
Cdd:PTZ00047 130 SEMCGTLHGFMPIVVEAV 147
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-212 1.45e-30

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: 108.54  E-value: 1.45e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667  95 VTIKAIGHQWYWSYEYSDfndlsfdsymipskdllpgqfrlLEVDNRMTTPVGMTTRTLITAEDVLHSWAVPSLGVKLDA 174
Cdd:cd13842    1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 115494667 175 IPGRLNQTSFIISRPGVYYGQCSEICGANHSFMPIVVE 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), ...
 94-207 7.02e-28

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: 101.93  E-value: 7.02e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667  94 DVTIKAIGHQWYWSYEYSDfndlsfdsymipskdllpGQFRLLEVDNRMTTPVGMTTRTLITAEDVLHSWAVPSLGVKLD 173
Cdd:cd04213    1 ALTIEVTGHQWWWEFRYPD------------------EPGRGIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMD 62

                         90       100       110
                 ....*....|....*....|....*....|....
gi 115494667 174 AIPGRLNQTSFIISRPGVYYGQCSEICGANHSFM 207
Cdd:cd04213   63 MIPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-83 1.98e-26

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: 97.79  E-value: 1.98e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667    1 MAHPLQLGFQDAASPIMEELLHFHDHTLMAVFLISTLVLYIISTLM------STKLSNTNTIDAQEIEMVWTIMPAIILI 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLirfnrrKNPITARYTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 115494667   75 VIALPSLRI 83
Cdd:pfam02790  81 LIALPSFKL 89
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 94-212 3.22e-25

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: 95.01  E-value: 3.22e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667  94 DVTIKAIGHQWYWSYEYsdfndlsfdsymiPSKDLLPGQFRLLEVdNRMTTPVGMTTRTLITAEDVLHSWAVPSLGVKLD 173
Cdd:cd13919    1 ALVVEVTAQQWAWTFRY-------------PGGDGKLGTDDDVTS-PELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQD 66

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 115494667 174 AIPGRLNQTSFIISRPGVYYGQCSEICGANHSFM--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; ...
 67-222 2.81e-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: 88.67  E-value: 2.81e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667  67 IMPAIILI-VIALPSLRILYLMDEVSNPD---VTIKAIGHQWYWSYEYSdfNDLSFDSYMIPSKDllpgqfrllevdnrm 142
Cdd:cd13918    1 GLSAIIVIsLIVWTYGMLLYVEDPPDEADedaLEVEVEGFQFGWQFEYP--NGVTTGNTLRVPAD--------------- 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667 143 tTPVgmttRTLITAEDVLHSWAVPSLGVKLDAIPGRLNQTSFIISRPGVYYGQCSEICGANHSFMPIVVESLPIKEFLNW 222
Cdd:cd13918   64 -TPI----ALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAW 138
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 96-211 2.74e-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: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 84.60  E-value: 2.74e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667  96 TIKAIGHQWYWSYEYsdfndlsfdsymipskdllPGQFRlleVDNRMTTPVGMTTRTLITAEDVLHSWAVPSLGVKLDAI 175
Cdd:cd13915    3 EIQVTGRQWMWEFTY-------------------PNGKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDVV 60

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 115494667 176 PGRLNQTSFIISRPGVYYGQCSEICGANHSFMPIVV 211
Cdd:cd13915   61 PGRYTYLWFEATKPGEYDLFCTEYCGTGHSGMIGKV 96
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-222 8.26e-20

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


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 80.92  E-value: 8.26e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667  95 VTIKAIGHQWYWSYEYSDFNDLSFDSYMIPSKdllpgqfrllevdnrmtTPVGMTtrtlITAEDVLHSWAVPSLGVKLDA 174
Cdd:cd13914    1 VEIEVEAYQWGWEFSYPEANVTTSEQLVIPAD-----------------RPVYFR----ITSRDVIHAFHVPELGLKQDA 59

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 115494667 175 IPGRLNQTSFIISRPGVYYGQCSEICGANHSFMPIVVESLPIKEFLNW 222
Cdd:cd13914   60 FPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQW 107
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 140-212 2.49e-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: 55.65  E-value: 2.49e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115494667 140 NRMTTPVGMTTRTLITAEDVLHSWAVPSLGVKLDAIPGRLNQTSFIISRPGVYYGQCSEICGANHSFM--PIVVE 212
Cdd:cd13913   25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNMygKIIVE 99
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-207 3.07e-06

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


Pssm-ID: 259983 [Multi-domain]  Cd Length: 93  Bit Score: 44.29  E-value: 3.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667  95 VTIKAIGHQWYWSyeysdfndlsfdsymipskdLLPGQFrllevdnrmttPVGMTTRTLITAEDVLHSWAVPSLGVKL-- 172
Cdd:cd13916    1 QVVAVTGHQWYWE--------------------LSRTEI-----------PAGKPVEFRVTSADVNHGFGIYDPDMRLla 49

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 115494667 173 --DAIPGRLNQTSFIISRPGVYYGQCSEICGANHSFM 207
Cdd:cd13916   50 qtQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 97-212 1.24e-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: 42.99  E-value: 1.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667  97 IKAIGHQWYWSYEYSDFndlsfdsymipskdllpgqfrLLEVDNRMTTPVGMTTR-TLITAEDVLHSWAVPSLGVKLDAI 175
Cdd:cd00920    1 ITVTASDWGWSFTYNGV---------------------LLFGPPVLVVPVGDTVRvQFVNKLGENHSVTIAGFGVPVVAM 59

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 115494667 176 ---------------PGRLNQTSFIISRPGVYYGQCSEICGaNHSFMPIVVE 212
Cdd:cd00920   60 agganpglvntlvigPGESAEVTFTTDQAGVYWFYCTIPGH-NHAGMVGTIN 110
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 156-207 4.17e-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: 4.17e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 115494667 156 AEDVLHSWAVPSLGVKLDAIPGRLNQTSFIISRPGVYYGQCSEICGANHSFM 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 3.63e-04

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: 38.68  E-value: 3.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667  95 VTIKAIGHQWYWSYEYSDFNDLSFDSYMIPSKdllpgqfrllevdnrmtTPVGMTtrtlITAEDVLHSWAVPSLGVKLDA 174
Cdd:cd04212    1 LEIQVVSLDWKWLFIYPEQGIATVNELVIPVG-----------------RPVNFR----LTSDSVMNSFFIPQLGGQIYA 59

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 115494667 175 IPGRLNQTSFIISRPGVYYGQCSEICGANHSFMPIVVESL 214
Cdd:cd04212   60 MAGMQTQLHLIADKPGTYQGLSANYSGEGFSDMKFKVLAV 99
PRK02888 PRK02888
nitrous-oxide reductase; Validated
 146-207 9.78e-04

nitrous-oxide reductase; Validated


Pssm-ID: 235082 [Multi-domain]  Cd Length: 635  Bit Score: 39.96  E-value: 9.78e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115494667 146 VGMTTRTLITAEDVLHSWAVPSLGVKLDAIPGRLNQTSFIISRPGVYYGQCSEICGANHSFM 207
Cdd:PRK02888 565 VTVIVTNLDKVEDLTHGFAIPNYGVNMEVAPQATASVTFTADKPGVYWYYCTWFCHALHMEM 626
PRK10525 PRK10525
cytochrome o ubiquinol oxidase subunit II; Provisional
 51-222 1.47e-03

cytochrome o ubiquinol oxidase subunit II; Provisional


Pssm-ID: 182518 [Multi-domain]  Cd Length: 315  Bit Score: 39.01  E-value: 1.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667  51 SNTNTIDAqeieMVWTImPAIILIVIALPSLRILYLMDE----VSNPD-VTIKAIGHQWYWSYEYSD-----FNDLSFds 120
Cdd:PRK10525  83 SHSNKVEA----VVWTV-PILIIIFLAVLTWKTTHALEPskplAHDEKpITIEVVSMDWKWFFIYPEqgiatVNEIAF-- 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494667 121 ymiPSKdlLPGQFRllevdnrmttpvgmttrtlITAEDVLHSWAVPSLGVKLDAIPGRLNQTSFIISRPGVYYGQCSEIC 200
Cdd:PRK10525 156 ---PAN--VPVYFK-------------------VTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIANEPGTYDGISASYS 211

                        170       180
                 ....*....|....*....|...
gi 115494667 201 GANHSFMPIVVESLPIKE-FLNW 222
Cdd:PRK10525 212 GPGFSGMKFKAIATPDRAeFDQW 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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