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Conserved domains on  [gi|589144305|ref|YP_009003603|]
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cytochrome c oxidase subunit II (mitochondrion) [Praslinia cooperi]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11475905)

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 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-227 1.92e-161

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 445.13  E-value: 1.92e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305   1 MAHPSQLGFQDAASPIMEELLHFHDHTLMVVFLISTLVLYIITIMMTTKLTNTNSMDAQEVEMIWTVLPAIIMIVIALPS 80
Cdd:MTH00117   1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305  81 LRILYLMDEISDPHLTIKSIGHQWYWSYEFTEYDLLSFDSYMTQTHNLEPGQFWLLEVDNRMVVPTESPIWMLITAEDVL 160
Cdd:MTH00117  81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 589144305 161 HSWTVPSMGVKTDAIPGRLNQNTFITTRPGVYYGQCSEICGANHSFMPIVVEATPLMNFEAWSTLML 227
Cdd:MTH00117 161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLLS 227
 
Name Accession Description Interval E-value
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-227 1.92e-161

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 445.13  E-value: 1.92e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305   1 MAHPSQLGFQDAASPIMEELLHFHDHTLMVVFLISTLVLYIITIMMTTKLTNTNSMDAQEVEMIWTVLPAIIMIVIALPS 80
Cdd:MTH00117   1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305  81 LRILYLMDEISDPHLTIKSIGHQWYWSYEFTEYDLLSFDSYMTQTHNLEPGQFWLLEVDNRMVVPTESPIWMLITAEDVL 160
Cdd:MTH00117  81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 589144305 161 HSWTVPSMGVKTDAIPGRLNQNTFITTRPGVYYGQCSEICGANHSFMPIVVEATPLMNFEAWSTLML 227
Cdd:MTH00117 161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLLS 227
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-222 4.28e-86

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: 250.95  E-value: 4.28e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305  93 PHLTIKSIGHQWYWSYEFTEYDLLSFDSYMTQTHNLEPGQFWLLEVDNRMVVPTESPIWMLITAEDVLHSWTVPSMGVKT 172
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 589144305 173 DAIPGRLNQNTFITTRPGVYYGQCSEICGANHSFMPIVVEATPLMNFEAW 222
Cdd:cd13912   81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 9.82e-76

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 224.21  E-value: 9.82e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305   95 LTIKSIGHQWYWSYEFTEYDLLSFDSYMTQTHNLEPGQFWLLEVDNRMVVPTESPIWMLITAEDVLHSWTVPSMGVKTDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 589144305  175 IPGRLNQNTFITTRPGVYYGQCSEICGANHSFMPIVVEAT 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-222 1.51e-56

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 179.25  E-value: 1.51e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305   6 QLGFQDAASPIMEELLHFHdhtlMVVFLISTLVLYIITIMMTTKL-----TNTNSMDAQE-----VEMIWTVLPAIIMIV 75
Cdd:COG1622   18 QLSLPDPAGPIAEEIDDLF----WVSLIIMLVIFVLVFGLLLYFAiryrrRKGDADPAQFhhntkLEIVWTVIPIIIVIV 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305  76 IALPSLRILYLMDEISDPHLTIKSIGHQWYWSYEFTEYDLLsfdsymtqthnlepgqfwlleVDNRMVVPTESPIWMLIT 155
Cdd:COG1622   94 LAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVNELVLPVGRPVRFLLT 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 589144305 156 AEDVLHSWTVPSMGVKTDAIPGRLNQNTFITTRPGVYYGQCSEICGANHSFMPIVVEATPLMNFEAW 222
Cdd:COG1622  153 SADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAW 219
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-222 9.02e-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: 145.99  E-value: 9.02e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305   12 AASPIMEELLHFHDHTLMVVFLISTLVlyiITIMMTTKLTNTNSMDAQE---------VEMIWTVLPAII-MIVIALPSL 81
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLV---AALLAYVVWKFRRKGDEEKpsqihgnrrLEYVWTVIPLIIvVGLFAATAK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305   82 RILYLMDEISDPHLTIKSIGHQWYWSYEFTEYDLLSfdsymtqthnlepgqfwllevDNRMVVPTESPIWMLITAEDVLH 161
Cdd:TIGR02866  78 GLLYLERPIPKDALKVKVTGYQWWWDFEYPESGFTT---------------------VNELVLPAGTPVELQVTSKDVIH 136

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 589144305  162 SWTVPSMGVKTDAIPGRLNQNTFITTRPGVYYGQCSEICGANHSFMPIVVEATPLMNFEAW 222
Cdd:TIGR02866 137 SFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAY 197
 
Name Accession Description Interval E-value
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-227 1.92e-161

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 445.13  E-value: 1.92e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305   1 MAHPSQLGFQDAASPIMEELLHFHDHTLMVVFLISTLVLYIITIMMTTKLTNTNSMDAQEVEMIWTVLPAIIMIVIALPS 80
Cdd:MTH00117   1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305  81 LRILYLMDEISDPHLTIKSIGHQWYWSYEFTEYDLLSFDSYMTQTHNLEPGQFWLLEVDNRMVVPTESPIWMLITAEDVL 160
Cdd:MTH00117  81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 589144305 161 HSWTVPSMGVKTDAIPGRLNQNTFITTRPGVYYGQCSEICGANHSFMPIVVEATPLMNFEAWSTLML 227
Cdd:MTH00117 161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLLS 227
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-227 4.96e-153

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 423.81  E-value: 4.96e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305   1 MAHPSQLGFQDAASPIMEELLHFHDHTLMVVFLISTLVLYIITIMMTTKLTNTNSMDAQEVEMIWTVLPAIIMIVIALPS 80
Cdd:MTH00076   1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305  81 LRILYLMDEISDPHLTIKSIGHQWYWSYEFTEYDLLSFDSYMTQTHNLEPGQFWLLEVDNRMVVPTESPIWMLITAEDVL 160
Cdd:MTH00076  81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 589144305 161 HSWTVPSMGVKTDAIPGRLNQNTFITTRPGVYYGQCSEICGANHSFMPIVVEATPLMNFEAWSTLML 227
Cdd:MTH00076 161 HSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSML 227
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-229 3.72e-152

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 421.82  E-value: 3.72e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305   1 MAHPSQLGFQDAASPIMEELLHFHDHTLMVVFLISTLVLYIITIMMTTKLTNTNSMDAQEVEMIWTVLPAIIMIVIALPS 80
Cdd:MTH00129   1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305  81 LRILYLMDEISDPHLTIKSIGHQWYWSYEFTEYDLLSFDSYMTQTHNLEPGQFWLLEVDNRMVVPTESPIWMLITAEDVL 160
Cdd:MTH00129  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 589144305 161 HSWTVPSMGVKTDAIPGRLNQNTFITTRPGVYYGQCSEICGANHSFMPIVVEATPLMNFEAWSTLMLKT 229
Cdd:MTH00129 161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLMLED 229
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-227 1.01e-148

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 412.96  E-value: 1.01e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305   1 MAHPSQLGFQDAASPIMEELLHFHDHTLMVVFLISTLVLYIITIMMTTKLTNTNSMDAQEVEMIWTVLPAIIMIVIALPS 80
Cdd:MTH00098   1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305  81 LRILYLMDEISDPHLTIKSIGHQWYWSYEFTEYDLLSFDSYMTQTHNLEPGQFWLLEVDNRMVVPTESPIWMLITAEDVL 160
Cdd:MTH00098  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 589144305 161 HSWTVPSMGVKTDAIPGRLNQNTFITTRPGVYYGQCSEICGANHSFMPIVVEATPLMNFEAWSTLML 227
Cdd:MTH00098 161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASML 227
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-228 3.07e-143

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 399.26  E-value: 3.07e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305   1 MAHPSQLGFQDAASPIMEELLHFHDHTLMVVFLISTLVLYIITIMMTTKLTNTNSMDAQEVEMIWTVLPAIIMIVIALPS 80
Cdd:MTH00185   1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305  81 LRILYLMDEISDPHLTIKSIGHQWYWSYEFTEYDLLSFDSYMTQTHNLEPGQFWLLEVDNRMVVPTESPIWMLITAEDVL 160
Cdd:MTH00185  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 589144305 161 HSWTVPSMGVKTDAIPGRLNQNTFITTRPGVYYGQCSEICGANHSFMPIVVEATPLMNFEAWSTLMLK 228
Cdd:MTH00185 161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLMLE 228
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-224 1.56e-127

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 359.29  E-value: 1.56e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305   1 MAHPSQLGFQDAASPIMEELLHFHDHTLMVVFLISTLVLYIITIMMTTKLTNTNSMDAQEVEMIWTVLPAIIMIVIALPS 80
Cdd:MTH00168   1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305  81 LRILYLMDEISDPHLTIKSIGHQWYWSYEFTEYDLLSFDSYMTQTHNLEPGQFWLLEVDNRMVVPTESPIWMLITAEDVL 160
Cdd:MTH00168  81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 589144305 161 HSWTVPSMGVKTDAIPGRLNQNTFITTRPGVYYGQCSEICGANHSFMPIVVEATPLMNFEAWST 224
Cdd:MTH00168 161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVD 224
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-227 4.29e-127

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 358.37  E-value: 4.29e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305   1 MAHPSQLGFQDAASPIMEELLHFHDHTLMVVFLISTLVLYIITIMMTTKLTNTNSMDAQEVEMIWTVLPAIIMIVIALPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305  81 LRILYLMDEISDPHLTIKSIGHQWYWSYEFTEYDLLSFDSYMTQTHNLEPGQFWLLEVDNRMVVPTESPIWMLITAEDVL 160
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 589144305 161 HSWTVPSMGVKTDAIPGRLNQNTFITTRPGVYYGQCSEICGANHSFMPIVVEATPLMNFEAWSTLML 227
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-226 3.31e-116

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 330.75  E-value: 3.31e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305   1 MAHPSQLGFQDAASPIMEELLHFHDHTLMVVFLISTLVLYIITIMMTTKLTNTNSMDAQEVEMIWTVLPAIIMIVIALPS 80
Cdd:MTH00140   1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305  81 LRILYLMDEISDPHLTIKSIGHQWYWSYEFTEYDLLSFDSYMTQTHNLEPGQFWLLEVDNRMVVPTESPIWMLITAEDVL 160
Cdd:MTH00140  81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 589144305 161 HSWTVPSMGVKTDAIPGRLNQNTFITTRPGVYYGQCSEICGANHSFMPIVVEATPLMNFEAWSTLM 226
Cdd:MTH00140 161 HSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELM 226
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-227 4.35e-116

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 330.51  E-value: 4.35e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305   1 MAHPSQLGFQDAASPIMEELLHFHDHTLMVVFLISTLVLYIITIMMTTKLTNTNSMDAQEVEMIWTVLPAIIMIVIALPS 80
Cdd:MTH00038   1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305  81 LRILYLMDEISDPHLTIKSIGHQWYWSYEFTEYDLLSFDSYMTQTHNLEPGQFWLLEVDNRMVVPTESPIWMLITAEDVL 160
Cdd:MTH00038  81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 589144305 161 HSWTVPSMGVKTDAIPGRLNQNTFITTRPGVYYGQCSEICGANHSFMPIVVEATPLMNFEAWSTLML 227
Cdd:MTH00038 161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFL 227
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-222 1.38e-111

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 318.97  E-value: 1.38e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305   1 MAHPSQLGFQDAASPIMEELLHFHDHTLMVVFLISTLVLYIITIMMTTKLTNTNSMDAQEVEMIWTVLPAIIMIVIALPS 80
Cdd:MTH00139   1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305  81 LRILYLMDEISDPHLTIKSIGHQWYWSYEFTEYDLLSFDSYMTQTHNLEPGQFWLLEVDNRMVVPTESPIWMLITAEDVL 160
Cdd:MTH00139  81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 589144305 161 HSWTVPSMGVKTDAIPGRLNQNTFITTRPGVYYGQCSEICGANHSFMPIVVEATPLMNFEAW 222
Cdd:MTH00139 161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEW 222
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-224 7.19e-108

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 309.86  E-value: 7.19e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305   1 MAHPSQLGFQDAASPIMEELLHFHDHTLMVVFLISTLVLYIITIMMTTKLTNTNSMDAQEVEMIWTVLPAIIMIVIALPS 80
Cdd:MTH00008   1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305  81 LRILYLMDEISDPHLTIKSIGHQWYWSYEFTEYDLLSFDSYMTQTHNLEPGQFWLLEVDNRMVVPTESPIWMLITAEDVL 160
Cdd:MTH00008  81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 589144305 161 HSWTVPSMGVKTDAIPGRLNQNTFITTRPGVYYGQCSEICGANHSFMPIVVEATPLMNFEAWST 224
Cdd:MTH00008 161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVS 224
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 2-223 1.23e-99

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 289.34  E-value: 1.23e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305   2 AHPSQLGFQDAASPIMEELLHFHDHTLMVVFLISTLVLYIITIMMTTKLTNTNSMDAQEVEMIWTVLPAIIMIVIALPSL 81
Cdd:MTH00023  11 PEPWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305  82 RILYLMDEISDPHLTIKSIGHQWYWSYEFTEY--DLLSFDSYMTQTHNLEPGQFWLLEVDNRMVVPTESPIWMLITAEDV 159
Cdd:MTH00023  91 KLLYLMDEVVSPALTIKAIGHQWYWSYEYSDYegETLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADV 170

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 589144305 160 LHSWTVPSMGVKTDAIPGRLNQNTFITTRPGVYYGQCSEICGANHSFMPIVVEATPLMNFEAWS 223
Cdd:MTH00023 171 LHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWL 234
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 2-222 3.37e-99

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 288.22  E-value: 3.37e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305   2 AHPSQLGFQDAASPIMEELLHFHDHTLMVVFLISTLVLYIITIMMTTKLTNTNSMDAQEVEMIWTVLPAIIMIVIALPSL 81
Cdd:MTH00051   4 PEPWQLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305  82 RILYLMDEISDPHLTIKSIGHQWYWSYEFTEY--DLLSFDSYMTQTHNLEPGQFWLLEVDNRMVVPTESPIWMLITAEDV 159
Cdd:MTH00051  84 KLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADV 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 589144305 160 LHSWTVPSMGVKTDAIPGRLNQNTFITTRPGVYYGQCSEICGANHSFMPIVVEATPLMNFEAW 222
Cdd:MTH00051 164 LHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINW 226
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-222 4.28e-86

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: 250.95  E-value: 4.28e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305  93 PHLTIKSIGHQWYWSYEFTEYDLLSFDSYMTQTHNLEPGQFWLLEVDNRMVVPTESPIWMLITAEDVLHSWTVPSMGVKT 172
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 589144305 173 DAIPGRLNQNTFITTRPGVYYGQCSEICGANHSFMPIVVEATPLMNFEAW 222
Cdd:cd13912   81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 4-222 5.45e-79

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 238.00  E-value: 5.45e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305   4 PSQLGFQDAASPIMEELLHFHDHTLMVVFLISTLVLY-IITIMMTTKLTNT--NSMDAQEVEMIWTVLPAIIMIVIALPS 80
Cdd:MTH00027  32 PWQLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWlIIRILLGNNYYSYywNKLDGSLIEVIWTLIPAFILILIAFPS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305  81 LRILYLMDE-ISDPHLTIKSIGHQWYWSYEFTEY--DLLSFDSYMTQTHNLEPGQFWLLEVDNRMVVPTESPIWMLITAE 157
Cdd:MTH00027 112 LRLLYIMDEcGFSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAA 191

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 589144305 158 DVLHSWTVPSMGVKTDAIPGRLNQNTFITTRPGVYYGQCSEICGANHSFMPIVVEATPLMNFEAW 222
Cdd:MTH00027 192 DVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDW 256
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 9.82e-76

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 224.21  E-value: 9.82e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305   95 LTIKSIGHQWYWSYEFTEYDLLSFDSYMTQTHNLEPGQFWLLEVDNRMVVPTESPIWMLITAEDVLHSWTVPSMGVKTDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 589144305  175 IPGRLNQNTFITTRPGVYYGQCSEICGANHSFMPIVVEAT 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 23-227 3.44e-71

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 216.80  E-value: 3.44e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305  23 FHDHTLMVVFLISTLVLYIITIMMTTKLTNTNSMDAQEVEMIWTVLPAIIMIVIALPSLRILYLMDEIS-DPHLTIKSIG 101
Cdd:MTH00080  25 FNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMNlDSNLTVKVTG 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305 102 HQWYWSYEFTEYDLLSFDSYMTQTHNLEPGQFWLLEVDNRMVVPTESPIWMLITAEDVLHSWTVPSMGVKTDAIPGRLNQ 181
Cdd:MTH00080 105 HQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILST 184

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 589144305 182 NTFITTRPGVYYGQCSEICGANHSFMPIVVEATPLMNFEAWSTLML 227
Cdd:MTH00080 185 LCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWCKLLL 230
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-222 1.51e-56

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 179.25  E-value: 1.51e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305   6 QLGFQDAASPIMEELLHFHdhtlMVVFLISTLVLYIITIMMTTKL-----TNTNSMDAQE-----VEMIWTVLPAIIMIV 75
Cdd:COG1622   18 QLSLPDPAGPIAEEIDDLF----WVSLIIMLVIFVLVFGLLLYFAiryrrRKGDADPAQFhhntkLEIVWTVIPIIIVIV 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305  76 IALPSLRILYLMDEISDPHLTIKSIGHQWYWSYEFTEYDLLsfdsymtqthnlepgqfwlleVDNRMVVPTESPIWMLIT 155
Cdd:COG1622   94 LAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVNELVLPVGRPVRFLLT 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 589144305 156 AEDVLHSWTVPSMGVKTDAIPGRLNQNTFITTRPGVYYGQCSEICGANHSFMPIVVEATPLMNFEAW 222
Cdd:COG1622  153 SADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAW 219
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 17-214 5.49e-44

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 146.25  E-value: 5.49e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305  17 MEELLHFHDHTLMVVFLISTLVLYIITIM---MTTKLTNTNSM-DAQEVEMIWTVLPAiiMIVIALPSLRILYLMDEISD 92
Cdd:MTH00047   1 MNLSLLYYDIVCYILALCVFIPCWVYIMLcwqVVSGNGSVNFGsENQVLELLWTVVPT--LLVLVLCFLNLNFITSDLDC 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305  93 -PHLTIKSIGHQWYWSYEFTEYDllSFDSYMTQTHNLepgqfwlleVDNRMVVPTESPIWMLITAEDVLHSWTVPSMGVK 171
Cdd:MTH00047  79 fSSETIKVIGHQWYWSYEYSFGG--SYDSFMTDDIFG---------VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLK 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 589144305 172 TDAIPGRLNQNTFITTRPGVYYGQCSEICGANHSFMPIVVEAT 214
Cdd:MTH00047 148 MDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVV 190
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-222 9.02e-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: 145.99  E-value: 9.02e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305   12 AASPIMEELLHFHDHTLMVVFLISTLVlyiITIMMTTKLTNTNSMDAQE---------VEMIWTVLPAII-MIVIALPSL 81
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLV---AALLAYVVWKFRRKGDEEKpsqihgnrrLEYVWTVIPLIIvVGLFAATAK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305   82 RILYLMDEISDPHLTIKSIGHQWYWSYEFTEYDLLSfdsymtqthnlepgqfwllevDNRMVVPTESPIWMLITAEDVLH 161
Cdd:TIGR02866  78 GLLYLERPIPKDALKVKVTGYQWWWDFEYPESGFTT---------------------VNELVLPAGTPVELQVTSKDVIH 136

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 589144305  162 SWTVPSMGVKTDAIPGRLNQNTFITTRPGVYYGQCSEICGANHSFMPIVVEATPLMNFEAW 222
Cdd:TIGR02866 137 SFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAY 197
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 117-213 3.69e-41

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 138.03  E-value: 3.69e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305 117 SFDSYMTQTHNLEPGQFWLLEVDNRMVVPTESPIWMLITAEDVLHSWTVPSMGVKTDAIPGRLNQ-NTFITtRPGVYYGQ 195
Cdd:PTZ00047  50 SFQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKiNTFIL-REGVFYGQ 128

                         90
                 ....*....|....*...
gi 589144305 196 CSEICGANHSFMPIVVEA 213
Cdd:PTZ00047 129 CSEMCGTLHGFMPIVVEA 146
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-212 1.66e-28

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: 103.14  E-value: 1.66e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305  95 LTIKSIGHQWYWSYEFTEydllsfdsymtqthnlepgqfwlLEVDNRMVVPTESPIWMLITAEDVLHSWTVPSMGVKTDA 174
Cdd:cd13842    1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 589144305 175 IPGRLNQNTFITTRPGVYYGQCSEICGANHSFMPIVVE 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), ...
 94-213 3.26e-27

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: 100.00  E-value: 3.26e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305  94 HLTIKSIGHQWYWSYEFTEYDLLSFdsymtqthnlepgqfwllEVDNRMVVPTESPIWMLITAEDVLHSWTVPSMGVKTD 173
Cdd:cd04213    1 ALTIEVTGHQWWWEFRYPDEPGRGI------------------VTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMD 62

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 589144305 174 AIPGRLNQNTFITTRPGVYYGQCSEICGANHSFMPIVVEA 213
Cdd:cd04213   63 MIPGRTNRLWLQADEPGVYRGQCAEFCGASHALMRFKVIA 102
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-83 1.17e-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: 98.17  E-value: 1.17e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305    1 MAHPSQLGFQDAASPIMEELLHFHDHTLMVVFLISTLVLYIITIMMTT------KLTNTNSMDAQEVEMIWTVLPAIIMI 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRfnrrknPITARYTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 589144305   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; ...
 95-212 3.41e-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: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 87.31  E-value: 3.41e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305  95 LTIKSIGHQWYWSYEFTEYDllsfdSYMTQTHNLEPGQfwllevdnrMVVPTESPIWMLITAEDVLHSWTVPSMGVKTDA 174
Cdd:cd13919    2 LVVEVTAQQWAWTFRYPGGD-----GKLGTDDDVTSPE---------LHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 589144305 175 IPGRLNQNTFITTRPGVYYGQCSEICGANHSFM--PIVVE 212
Cdd:cd13919   68 VPGRTTRLWFTPTREGEYEVRCAELCGLGHYRMraTVKVV 107
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 68-222 2.32e-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: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 85.97  E-value: 2.32e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305  68 LPAIIMI-VIALPSLRILYLMD---EISDPHLTIKSIGHQWYWSYEfteydllsfdsYMTQTHNLepgqfwllevdNRMV 143
Cdd:cd13918    2 LSAIIVIsLIVWTYGMLLYVEDppdEADEDALEVEVEGFQFGWQFE-----------YPNGVTTG-----------NTLR 59

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 589144305 144 VPTESPIWMLITAEDVLHSWTVPSMGVKTDAIPGRLNQNTFITTRPGVYYGQCSEICGANHSFMPIVVEATPLMNFEAW 222
Cdd:cd13918   60 VPADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAW 138
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 96-222 1.77e-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: 82.84  E-value: 1.77e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305  96 TIKSIGHQWYWSYEFTEYDLLSFdsymtqthnlepgqfwllevdNRMVVPTESPIWMLITAEDVLHSWTVPSMGVKTDAI 175
Cdd:cd13914    2 EIEVEAYQWGWEFSYPEANVTTS---------------------EQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAF 60

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 589144305 176 PGRlnQNTFIT--TRPGVYYGQCSEICGANHSFMPIVVEATPLMNFEAW 222
Cdd:cd13914   61 PGQ--YNTIKTeaTEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQW 107
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-213 7.79e-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: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 80.75  E-value: 7.79e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305  95 LTIKSIGHQWYWSYEFteydllsfdsymtqthnlePGQfwlLEVDNRMVVPTESPIWMLITAEDVLHSWTVPSMGVKTDA 174
Cdd:cd13915    2 LEIQVTGRQWMWEFTY-------------------PNG---KREINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDV 59

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 589144305 175 IPGRLNQNTFITTRPGVYYGQCSEICGANHSFMPIVVEA 213
Cdd:cd13915   60 VPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGMIGKVRV 98
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 140-212 1.80e-09

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: 53.34  E-value: 1.80e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 589144305 140 NRMVVPTESPIWMLITAEDVLHSWTVPSMGVKTDAIPGRLNQNTFITTRPGVYYGQCSEICGANHSFM--PIVVE 212
Cdd:cd13913   25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNMygKIIVE 99
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 140-214 1.34e-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: 42.54  E-value: 1.34e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 589144305 140 NRMVVPTESPIWMLITAEDVLHSWTVPSMGVKTDAIPGRLNQNTFITTRPGVYYGQCSEICGANHSFMPIVVEAT 214
Cdd:cd04212   25 NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDMKFKVLAV 99
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 131-207 5.87e-05

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


Pssm-ID: 259983 [Multi-domain]  Cd Length: 93  Bit Score: 40.83  E-value: 5.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305 131 GQFWLLEVDnRMVVPTESPIWMLITAEDVLHSWTV--PSMGV--KTDAIPGRLNQNTFITTRPGVYYGQCSEICGANHSF 206
Cdd:cd13916    7 GHQWYWELS-RTEIPAGKPVEFRVTSADVNHGFGIydPDMRLlaQTQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHV 85


                 .
gi 589144305 207 M 207
Cdd:cd13916   86 M 86
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 156-207 6.45e-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: 40.68  E-value: 6.45e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 589144305 156 AEDVLHSWTVPSMGVKTDAIPGRLNQNTFITTRPGVYYGQCSEICGANHSFM 207
Cdd:cd04223   36 DEDITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALHLEM 87
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 121-212 1.57e-03

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: 37.21  E-value: 1.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305 121 YMTQTHNLEPGQFWLLEVDNRMVVPT-ESPIWMLITAEDVLHSWTVPSMGVKTDAI---------------PGRLNQNTF 184
Cdd:cd00920    4 TASDWGWSFTYNGVLLFGPPVLVVPVgDTVRVQFVNKLGENHSVTIAGFGVPVVAMagganpglvntlvigPGESAEVTF 83

                         90       100
                 ....*....|....*....|....*...
gi 589144305 185 ITTRPGVYYGQCSEICGaNHSFMPIVVE 212
Cdd:cd00920   84 TTDQAGVYWFYCTIPGH-NHAGMVGTIN 110
PRK10525 PRK10525
cytochrome o ubiquinol oxidase subunit II; Provisional
 63-222 1.68e-03

cytochrome o ubiquinol oxidase subunit II; Provisional


Pssm-ID: 182518 [Multi-domain]  Cd Length: 315  Bit Score: 38.63  E-value: 1.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305  63 MIWTVlPAIIMIVIALPSLRILYLMDE----ISDPH-LTIKSIGHQWYWSYEFTEYDLLSFdsymtqthnlepgqfwlle 137
Cdd:PRK10525  91 VVWTV-PILIIIFLAVLTWKTTHALEPskplAHDEKpITIEVVSMDWKWFFIYPEQGIATV------------------- 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589144305 138 vdNRMVVPTESPIWMLITAEDVLHSWTVPSMGVKTDAIPGRLNQNTFITTRPGVYYGQCSEICGANHSFMPIVVEATP-L 216
Cdd:PRK10525 151 --NEIAFPANVPVYFKVTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIANEPGTYDGISASYSGPGFSGMKFKAIATPdR 228


                 ....*.
gi 589144305 217 MNFEAW 222
Cdd:PRK10525 229 AEFDQW 234
PRK02888 PRK02888
nitrous-oxide reductase; Validated
 157-213 1.70e-03

nitrous-oxide reductase; Validated


Pssm-ID: 235082 [Multi-domain]  Cd Length: 635  Bit Score: 39.19  E-value: 1.70e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 589144305 157 EDVLHSWTVPSMGVKTDAIPGRLNQNTFITTRPGVYYGQCSEICGANHSFMP--IVVEA 213
Cdd:PRK02888 576 EDLTHGFAIPNYGVNMEVAPQATASVTFTADKPGVYWYYCTWFCHALHMEMRgrMLVEP 634
 
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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