NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|295065514|ref|YP_003587282|]
View 

cytochrome c oxidase subunit II (mitochondrion) [Hylobates pileatus]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11475897)

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
1-227 5.49e-152

cytochrome c oxidase subunit II; Validated


:

Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 421.05  E-value: 5.49e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514   1 MAHATQVGLQDATSPIMEELISFHDHALMIIFLISFLVLYALFLTLTTKLTNTNITDAQEMETVWTILPAIILVLIALPS 80
Cdd:MTH00098   1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514  81 LRILYLTDEINDPSFTIKAIGHQWYWAYEYTDYGGLIFNSYMLPPLFLEPGDLRLLEVDNRVVLPIEAPVRMMITSQDVL 160
Cdd:MTH00098  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 295065514 161 HSWTVPSLGLKTDAIPGRLNQTTFTATRPGVYYGQCSEICGANHSFMPIVLELIPLKIFEMGPVFTL 227
Cdd:MTH00098 161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASML 227
 
Name Accession Description Interval E-value
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
1-227 5.49e-152

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 421.05  E-value: 5.49e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514   1 MAHATQVGLQDATSPIMEELISFHDHALMIIFLISFLVLYALFLTLTTKLTNTNITDAQEMETVWTILPAIILVLIALPS 80
Cdd:MTH00098   1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514  81 LRILYLTDEINDPSFTIKAIGHQWYWAYEYTDYGGLIFNSYMLPPLFLEPGDLRLLEVDNRVVLPIEAPVRMMITSQDVL 160
Cdd:MTH00098  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 295065514 161 HSWTVPSLGLKTDAIPGRLNQTTFTATRPGVYYGQCSEICGANHSFMPIVLELIPLKIFEMGPVFTL 227
Cdd:MTH00098 161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASML 227
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
93-221 1.00e-87

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: 254.80  E-value: 1.00e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514  93 PSFTIKAIGHQWYWAYEYTDYGGLIFNSYMLPPLFLEPGDLRLLEVDNRVVLPIEAPVRMMITSQDVLHSWTVPSLGLKT 172
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 295065514 173 DAIPGRLNQTTFTATRPGVYYGQCSEICGANHSFMPIVLELIPLKIFEM 221
Cdd:cd13912   81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLS 129
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
96-214 8.69e-83

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 242.32  E-value: 8.69e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514   96 TIKAIGHQWYWAYEYTDYGGLIFNSYMLPPLFLEPGDLRLLEVDNRVVLPIEAPVRMMITSQDVLHSWTVPSLGLKTDAI 175
Cdd:pfam00116   2 TIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDAV 81
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 295065514  176 PGRLNQTTFTATRPGVYYGQCSEICGANHSFMPIVLELI 214
Cdd:pfam00116  82 PGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
4-212 6.15e-54

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 172.71  E-value: 6.15e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514   4 ATQVGLQDATSPIMEELISFHDHALMIIFLISFLV----LYALFL--TLTTKLTNTNITDAQEMETVWTILPAIILVLIA 77
Cdd:COG1622   16 SGQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVfgllLYFAIRyrRRKGDADPAQFHHNTKLEIVWTVIPIIIVIVLA 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514  78 LPSLRILYLTDEINDPSFTIKAIGHQWYWAYEYTDYGGLifnsymlpplflepgdlrlleVDNRVVLPIEAPVRMMITSQ 157
Cdd:COG1622   96 VPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVNELVLPVGRPVRFLLTSA 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 295065514 158 DVLHSWTVPSLGLKTDAIPGRLNQTTFTATRPGVYYGQCSEICGANHSFMPIVLE 212
Cdd:COG1622  155 DVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVV 209
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
61-215 4.22e-45

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: 149.07  E-value: 4.22e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514   61 METVWTILPAIILV-LIALPSLRILYLTDEINDPSFTIKAIGHQWYWAYEYTDYGglifnsymlpplflepgdlrlLEVD 139
Cdd:TIGR02866  56 LEYVWTVIPLIIVVgLFAATAKGLLYLERPIPKDALKVKVTGYQWWWDFEYPESG---------------------FTTV 114
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 295065514  140 NRVVLPIEAPVRMMITSQDVLHSWTVPSLGLKTDAIPGRLNQTTFTATRPGVYYGQCSEICGANHSFMPIVLELIP 215
Cdd:TIGR02866 115 NELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVP 190
 
Name Accession Description Interval E-value
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
1-227 5.49e-152

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 421.05  E-value: 5.49e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514   1 MAHATQVGLQDATSPIMEELISFHDHALMIIFLISFLVLYALFLTLTTKLTNTNITDAQEMETVWTILPAIILVLIALPS 80
Cdd:MTH00098   1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514  81 LRILYLTDEINDPSFTIKAIGHQWYWAYEYTDYGGLIFNSYMLPPLFLEPGDLRLLEVDNRVVLPIEAPVRMMITSQDVL 160
Cdd:MTH00098  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 295065514 161 HSWTVPSLGLKTDAIPGRLNQTTFTATRPGVYYGQCSEICGANHSFMPIVLELIPLKIFEMGPVFTL 227
Cdd:MTH00098 161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASML 227
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
1-220 9.03e-139

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 387.73  E-value: 9.03e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514   1 MAHATQVGLQDATSPIMEELISFHDHALMIIFLISFLVLYALFLTLTTKLTNTNITDAQEMETVWTILPAIILVLIALPS 80
Cdd:MTH00117   1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514  81 LRILYLTDEINDPSFTIKAIGHQWYWAYEYTDYGGLIFNSYMLPPLFLEPGDLRLLEVDNRVVLPIEAPVRMMITSQDVL 160
Cdd:MTH00117  81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514 161 HSWTVPSLGLKTDAIPGRLNQTTFTATRPGVYYGQCSEICGANHSFMPIVLELIPLKIFE 220
Cdd:MTH00117 161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFE 220
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
1-220 3.61e-126

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 355.95  E-value: 3.61e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514   1 MAHATQVGLQDATSPIMEELISFHDHALMIIFLISFLVLYALFLTLTTKLTNTNITDAQEMETVWTILPAIILVLIALPS 80
Cdd:MTH00129   1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514  81 LRILYLTDEINDPSFTIKAIGHQWYWAYEYTDYGGLIFNSYMLPPLFLEPGDLRLLEVDNRVVLPIEAPVRMMITSQDVL 160
Cdd:MTH00129  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514 161 HSWTVPSLGLKTDAIPGRLNQTTFTATRPGVYYGQCSEICGANHSFMPIVLELIPLKIFE 220
Cdd:MTH00129 161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFE 220
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
1-220 1.83e-123

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 349.08  E-value: 1.83e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514   1 MAHATQVGLQDATSPIMEELISFHDHALMIIFLISFLVLYALFLTLTTKLTNTNITDAQEMETVWTILPAIILVLIALPS 80
Cdd:MTH00076   1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514  81 LRILYLTDEINDPSFTIKAIGHQWYWAYEYTDYGGLIFNSYMLPPLFLEPGDLRLLEVDNRVVLPIEAPVRMMITSQDVL 160
Cdd:MTH00076  81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVL 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514 161 HSWTVPSLGLKTDAIPGRLNQTTFTATRPGVYYGQCSEICGANHSFMPIVLELIPLKIFE 220
Cdd:MTH00076 161 HSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFL 220
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
1-219 3.49e-123

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 348.36  E-value: 3.49e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514   1 MAHATQVGLQDATSPIMEELISFHDHALMIIFLISFLVLYALFLTLTTKLTNTNITDAQEMETVWTILPAIILVLIALPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514  81 LRILYLTDEINDPSFTIKAIGHQWYWAYEYTDYGGLIFNSYMLPPLFLEPGDLRLLEVDNRVVLPIEAPVRMMITSQDVL 160
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 295065514 161 HSWTVPSLGLKTDAIPGRLNQTTFTATRPGVYYGQCSEICGANHSFMPIVLELIPLKIF 219
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNF 219
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
1-221 7.17e-121

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 342.35  E-value: 7.17e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514   1 MAHATQVGLQDATSPIMEELISFHDHALMIIFLISFLVLYALFLTLTTKLTNTNITDAQEMETVWTILPAIILVLIALPS 80
Cdd:MTH00168   1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514  81 LRILYLTDEINDPSFTIKAIGHQWYWAYEYTDYGGLIFNSYMLPPLFLEPGDLRLLEVDNRVVLPIEAPVRMMITSQDVL 160
Cdd:MTH00168  81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 295065514 161 HSWTVPSLGLKTDAIPGRLNQTTFTATRPGVYYGQCSEICGANHSFMPIVLELIPLKIFEM 221
Cdd:MTH00168 161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFEN 221
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
1-220 5.47e-119

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 338.01  E-value: 5.47e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514   1 MAHATQVGLQDATSPIMEELISFHDHALMIIFLISFLVLYALFLTLTTKLTNTNITDAQEMETVWTILPAIILVLIALPS 80
Cdd:MTH00185   1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514  81 LRILYLTDEINDPSFTIKAIGHQWYWAYEYTDYGGLIFNSYMLPPLFLEPGDLRLLEVDNRVVLPIEAPVRMMITSQDVL 160
Cdd:MTH00185  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514 161 HSWTVPSLGLKTDAIPGRLNQTTFTATRPGVYYGQCSEICGANHSFMPIVLELIPLKIFE 220
Cdd:MTH00185 161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFE 220
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
1-221 1.71e-115

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 328.82  E-value: 1.71e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514   1 MAHATQVGLQDATSPIMEELISFHDHALMIIFLISFLVLYALFLTLTTKLTNTNITDAQEMETVWTILPAIILVLIALPS 80
Cdd:MTH00140   1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514  81 LRILYLTDEINDPSFTIKAIGHQWYWAYEYTDYGGLIFNSYMLPPLFLEPGDLRLLEVDNRVVLPIEAPVRMMITSQDVL 160
Cdd:MTH00140  81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVI 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 295065514 161 HSWTVPSLGLKTDAIPGRLNQTTFTATRPGVYYGQCSEICGANHSFMPIVLELIPLKIFEM 221
Cdd:MTH00140 161 HSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVK 221
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
1-220 5.16e-115

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 327.81  E-value: 5.16e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514   1 MAHATQVGLQDATSPIMEELISFHDHALMIIFLISFLVLYALFLTLTTKLTNTNITDAQEMETVWTILPAIILVLIALPS 80
Cdd:MTH00038   1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514  81 LRILYLTDEINDPSFTIKAIGHQWYWAYEYTDYGGLIFNSYMLPPLFLEPGDLRLLEVDNRVVLPIEAPVRMMITSQDVL 160
Cdd:MTH00038  81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514 161 HSWTVPSLGLKTDAIPGRLNQTTFTATRPGVYYGQCSEICGANHSFMPIVLELIPLKIFE 220
Cdd:MTH00038 161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFE 220
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
1-219 1.71e-109

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 313.58  E-value: 1.71e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514   1 MAHATQVGLQDATSPIMEELISFHDHALMIIFLISFLVLYALFLTLTTKLTNTNITDAQEMETVWTILPAIILVLIALPS 80
Cdd:MTH00139   1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514  81 LRILYLTDEINDPSFTIKAIGHQWYWAYEYTDYGGLIFNSYMLPPLFLEPGDLRLLEVDNRVVLPIEAPVRMMITSQDVL 160
Cdd:MTH00139  81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 295065514 161 HSWTVPSLGLKTDAIPGRLNQTTFTATRPGVYYGQCSEICGANHSFMPIVLELIPLKIF 219
Cdd:MTH00139 161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFF 219
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
1-219 4.60e-109

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 312.56  E-value: 4.60e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514   1 MAHATQVGLQDATSPIMEELISFHDHALMIIFLISFLVLYALFLTLTTKLTNTNITDAQEMETVWTILPAIILVLIALPS 80
Cdd:MTH00008   1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514  81 LRILYLTDEINDPSFTIKAIGHQWYWAYEYTDYGGLIFNSYMLPPLFLEPGDLRLLEVDNRVVLPIEAPVRMMITSQDVL 160
Cdd:MTH00008  81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 295065514 161 HSWTVPSLGLKTDAIPGRLNQTTFTATRPGVYYGQCSEICGANHSFMPIVLELIPLKIF 219
Cdd:MTH00008 161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSF 219
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
2-216 2.44e-95

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 278.56  E-value: 2.44e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514   2 AHATQVGLQDATSPIMEELISFHDHALMIIFLISFLVLYALFLTLTTKLTNTNITDAQEMETVWTILPAIILVLIALPSL 81
Cdd:MTH00023  11 PEPWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514  82 RILYLTDEINDPSFTIKAIGHQWYWAYEYTDYGG--LIFNSYMLPPLFLEPGDLRLLEVDNRVVLPIEAPVRMMITSQDV 159
Cdd:MTH00023  91 KLLYLMDEVVSPALTIKAIGHQWYWSYEYSDYEGetLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADV 170
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 295065514 160 LHSWTVPSLGLKTDAIPGRLNQTTFTATRPGVYYGQCSEICGANHSFMPIVLELIPL 216
Cdd:MTH00023 171 LHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSL 227
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
6-217 7.65e-95

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 277.05  E-value: 7.65e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514   6 QVGLQDATSPIMEELISFHDHALMIIFLISFLVLYALFLTLTTKLTNTNITDAQEMETVWTILPAIILVLIALPSLRILY 85
Cdd:MTH00051   8 QLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLY 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514  86 LTDEINDPSFTIKAIGHQWYWAYEYTDYGG--LIFNSYMLPPLFLEPGDLRLLEVDNRVVLPIEAPVRMMITSQDVLHSW 163
Cdd:MTH00051  88 LMDEVIDPALTIKAIGHQWYWSYEYSDYGTdtIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSF 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 295065514 164 TVPSLGLKTDAIPGRLNQTTFTATRPGVYYGQCSEICGANHSFMPIVLELIPLK 217
Cdd:MTH00051 168 AVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLD 221
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
93-221 1.00e-87

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: 254.80  E-value: 1.00e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514  93 PSFTIKAIGHQWYWAYEYTDYGGLIFNSYMLPPLFLEPGDLRLLEVDNRVVLPIEAPVRMMITSQDVLHSWTVPSLGLKT 172
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 295065514 173 DAIPGRLNQTTFTATRPGVYYGQCSEICGANHSFMPIVLELIPLKIFEM 221
Cdd:cd13912   81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLS 129
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
96-214 8.69e-83

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 242.32  E-value: 8.69e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514   96 TIKAIGHQWYWAYEYTDYGGLIFNSYMLPPLFLEPGDLRLLEVDNRVVLPIEAPVRMMITSQDVLHSWTVPSLGLKTDAI 175
Cdd:pfam00116   2 TIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDAV 81
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 295065514  176 PGRLNQTTFTATRPGVYYGQCSEICGANHSFMPIVLELI 214
Cdd:pfam00116  82 PGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
6-216 3.99e-76

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 230.30  E-value: 3.99e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514   6 QVGLQDATSPIMEELISFHDHALMIIFLISFLVLYALFLTLTTKLTNTNI---TDAQEMETVWTILPAIILVLIALPSLR 82
Cdd:MTH00027  34 QLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLGNNYYSYYwnkLDGSLIEVIWTLIPAFILILIAFPSLR 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514  83 ILYLTDE-INDPSFTIKAIGHQWYWAYEYTDYG--GLIFNSYMLPPLFLEPGDLRLLEVDNRVVLPIEAPVRMMITSQDV 159
Cdd:MTH00027 114 LLYIMDEcGFSANITIKVTGHQWYWSYSYEDYGekNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADV 193
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 295065514 160 LHSWTVPSLGLKTDAIPGRLNQTTFTATRPGVYYGQCSEICGANHSFMPIVLELIPL 216
Cdd:MTH00027 194 LHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSL 250
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
17-219 1.01e-68

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 210.64  E-value: 1.01e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514  17 MEELISFHDHALMIIFLISFLVLYALFLTLTTKLTNTNITDAQEMETVWTILPAIILVLIALPSLRILYLTDEIN-DPSF 95
Cdd:MTH00080  19 MDWFHNFNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMNlDSNL 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514  96 TIKAIGHQWYWAYEYTDYGGLIFNSYMLPPLFLEPGDLRLLEVDNRVVLPIEAPVRMMITSQDVLHSWTVPSLGLKTDAI 175
Cdd:MTH00080  99 TVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAM 178
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 295065514 176 PGRLNQTTFTATRPGVYYGQCSEICGANHSFMPIVLELIPLKIF 219
Cdd:MTH00080 179 SGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNF 222
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
4-212 6.15e-54

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 172.71  E-value: 6.15e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514   4 ATQVGLQDATSPIMEELISFHDHALMIIFLISFLV----LYALFL--TLTTKLTNTNITDAQEMETVWTILPAIILVLIA 77
Cdd:COG1622   16 SGQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVfgllLYFAIRyrRRKGDADPAQFHHNTKLEIVWTVIPIIIVIVLA 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514  78 LPSLRILYLTDEINDPSFTIKAIGHQWYWAYEYTDYGGLifnsymlpplflepgdlrlleVDNRVVLPIEAPVRMMITSQ 157
Cdd:COG1622   96 VPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVNELVLPVGRPVRFLLTSA 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 295065514 158 DVLHSWTVPSLGLKTDAIPGRLNQTTFTATRPGVYYGQCSEICGANHSFMPIVLE 212
Cdd:COG1622  155 DVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVV 209
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
57-214 1.34e-45

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 150.10  E-value: 1.34e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514  57 DAQEMETVWTILPAIIlVLIaLPSLRILYLTDEIND-PSFTIKAIGHQWYWAYEYTDygGLIFNSYMLPPLFLepgdlrl 135
Cdd:MTH00047  45 ENQVLELLWTVVPTLL-VLV-LCFLNLNFITSDLDCfSSETIKVIGHQWYWSYEYSF--GGSYDSFMTDDIFG------- 113
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 295065514 136 leVDNRVVLPIEAPVRMMITSQDVLHSWTVPSLGLKTDAIPGRLNQTTFTATRPGVYYGQCSEICGANHSFMPIVLELI 214
Cdd:MTH00047 114 --VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVV 190
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
61-215 4.22e-45

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: 149.07  E-value: 4.22e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514   61 METVWTILPAIILV-LIALPSLRILYLTDEINDPSFTIKAIGHQWYWAYEYTDYGglifnsymlpplflepgdlrlLEVD 139
Cdd:TIGR02866  56 LEYVWTVIPLIIVVgLFAATAKGLLYLERPIPKDALKVKVTGYQWWWDFEYPESG---------------------FTTV 114
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 295065514  140 NRVVLPIEAPVRMMITSQDVLHSWTVPSLGLKTDAIPGRLNQTTFTATRPGVYYGQCSEICGANHSFMPIVLELIP 215
Cdd:TIGR02866 115 NELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVP 190
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
118-212 1.72e-37

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 128.40  E-value: 1.72e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514 118 FNSYMLPPLFLEPGDLRLLEVDNRVVLPIEAPVRMMITSQDVLHSWTVPSLGLKTDAIPGRLNQTTFTATRPGVYYGQCS 197
Cdd:PTZ00047  51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130
                         90
                 ....*....|....*
gi 295065514 198 EICGANHSFMPIVLE 212
Cdd:PTZ00047 131 EMCGTLHGFMPIVVE 145
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
96-207 5.30e-34

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: 117.34  E-value: 5.30e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514  96 TIKAIGHQWYWAYEYTDYGGlifnsymlpplflepgdlRLLEVDNRVVLPIEAPVRMMITSQDVLHSWTVPSLGLKTDAI 175
Cdd:cd04213    3 TIEVTGHQWWWEFRYPDEPG------------------RGIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDMI 64
                         90       100       110
                 ....*....|....*....|....*....|..
gi 295065514 176 PGRLNQTTFTATRPGVYYGQCSEICGANHSFM 207
Cdd:cd04213   65 PGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
96-212 3.61e-33

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: 115.09  E-value: 3.61e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514  96 TIKAIGHQWYWAYEYTDygglifnsymlpplflepgdlrlLEVDNRVVLPIEAPVRMMITSQDVLHSWTVPSLGLKTDAI 175
Cdd:cd13842    2 TVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDAV 58
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 295065514 176 PGRLNQTTFTATRPGVYYGQCSEICGANHSFMPIVLE 212
Cdd:cd13842   59 PGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
96-207 1.15e-27

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: 101.18  E-value: 1.15e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514  96 TIKAIGHQWYWAYEYTDYGGlifnsYMLPPLFLEPGDLrllevdnrvVLPIEAPVRMMITSQDVLHSWTVPSLGLKTDAI 175
Cdd:cd13919    3 VVEVTAQQWAWTFRYPGGDG-----KLGTDDDVTSPEL---------HLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDAV 68
                         90       100       110
                 ....*....|....*....|....*....|..
gi 295065514 176 PGRLNQTTFTATRPGVYYGQCSEICGANHSFM 207
Cdd:cd13919   69 PGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
94-207 1.07e-26

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


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 98.47  E-value: 1.07e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514  94 SFTIKAIGHQWYWAYEYtdygglifnsymlpplflePGDLRlleVDNRVVLPIEAPVRMMITSQDVLHSWTVPSLGLKTD 173
Cdd:cd13915    1 ALEIQVTGRQWMWEFTY-------------------PNGKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQD 58
                         90       100       110
                 ....*....|....*....|....*....|....
gi 295065514 174 AIPGRLNQTTFTATRPGVYYGQCSEICGANHSFM 207
Cdd:cd13915   59 VVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
67-220 1.29e-24

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


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 94.44  E-value: 1.29e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514  67 ILPAIILV-LIALPSLRILYLTD---EINDPSFTIKAIGHQWYWAYEYTDYGGLIfnsymlpplflepgdlrllevdNRV 142
Cdd:cd13918    1 GLSAIIVIsLIVWTYGMLLYVEDppdEADEDALEVEVEGFQFGWQFEYPNGVTTG----------------------NTL 58
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 295065514 143 VLPIEAPVRMMITSQDVLHSWTVPSLGLKTDAIPGRLNQTTFTATRPGVYYGQCSEICGANHSFMPIVLELIPLKIFE 220
Cdd:cd13918   59 RVPADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFE 136
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
96-207 5.07e-22

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


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 86.69  E-value: 5.07e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514  96 TIKAIGHQWYWAYEYTDYGglIFNSymlpplflepgdlrllevdNRVVLPIEAPVRMMITSQDVLHSWTVPSLGLKTDAI 175
Cdd:cd13914    2 EIEVEAYQWGWEFSYPEAN--VTTS-------------------EQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAF 60
                         90       100       110
                 ....*....|....*....|....*....|..
gi 295065514 176 PGRLNQTTFTATRPGVYYGQCSEICGANHSFM 207
Cdd:cd13914   61 PGQYNTIKTEATEEGEYQLYCAEYCGAGHSQM 92
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
1-83 2.76e-19

Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C oxidase contains two transmembrane alpha-helices.


Pssm-ID: 397083 [Multi-domain]  Cd Length: 89  Bit Score: 78.91  E-value: 2.76e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514    1 MAHATQVGLQDATSPIMEELISFHDHALMIIFLISFLVLYALFLTLTTKLTNT------NITDAQEMETVWTILPAIILV 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRFNRRKnpitarYTTHGQTIEIIWTIIPAVILI 80

                  ....*....
gi 295065514   75 LIALPSLRI 83
Cdd:pfam02790  81 LIALPSFKL 89
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
140-207 4.90e-12

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: 60.28  E-value: 4.90e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 295065514 140 NRVVLPIEAPVRMMITSQDVLHSWTVPSLGLKTDAIPGRLNQTTFTATRPGVYYGQCSEICGANHSFM 207
Cdd:cd13913   25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
96-207 3.50e-09

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: 52.55  E-value: 3.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514  96 TIKAIGHQWYWAYEYTDYGglifnsymlpplflepgdlrlLEVDNRVVLPIEAPVRMMITSQDVLHSWTVPSLGLKTDAI 175
Cdd:cd04212    2 EIQVVSLDWKWLFIYPEQG---------------------IATVNELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAM 60
                         90       100       110
                 ....*....|....*....|....*....|..
gi 295065514 176 PGRLNQTTFTATRPGVYYGQCSEICGANHSFM 207
Cdd:cd04212   61 AGMQTQLHLIADKPGTYQGLSANYSGEGFSDM 92
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
96-207 1.32e-08

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: 50.84  E-value: 1.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514  96 TIKAIGHQWYWayeytdygglifnsymlpplflepgdlrllEVDnRVVLPIEAPVRMMITSQDVLHSWTV--PSLGL--K 171
Cdd:cd13916    2 VVAVTGHQWYW------------------------------ELS-RTEIPAGKPVEFRVTSADVNHGFGIydPDMRLlaQ 50
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 295065514 172 TDAIPGRLNQTTFTATRPGVYYGQCSEICGANHSFM 207
Cdd:cd13916   51 TQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
130-212 2.67e-07

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: 47.61  E-value: 2.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514 130 PGDLRLLEVDNRVVLPIEAPVRMMITS-QDVLHSWTVPSLGLKTDAI---------------PGRLNQTTFTATRPGVYY 193
Cdd:cd00920   13 TYNGVLLFGPPVLVVPVGDTVRVQFVNkLGENHSVTIAGFGVPVVAMagganpglvntlvigPGESAEVTFTTDQAGVYW 92
                         90
                 ....*....|....*....
gi 295065514 194 GQCSEICGaNHSFMPIVLE 212
Cdd:cd00920   93 FYCTIPGH-NHAGMVGTIN 110
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
150-207 1.99e-06

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: 44.92  E-value: 1.99e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 295065514 150 VRMMIT----SQDVLHSWTVPSLGLKTDAIPGRLNQTTFTATRPGVYYGQCSEICGANHSFM 207
Cdd:cd04223   26 VTVHLTnleqDEDITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALHLEM 87
PRK10525 PRK10525
cytochrome o ubiquinol oxidase subunit II; Provisional
64-207 2.94e-05

cytochrome o ubiquinol oxidase subunit II; Provisional


Pssm-ID: 182518 [Multi-domain]  Cd Length: 315  Bit Score: 44.02  E-value: 2.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295065514  64 VWTIlPAIILVLIALpslrILYLTDEINDPS---------FTIKAIGHQWYWAYEYTDYGglifnsymlpplflepgdlr 134
Cdd:PRK10525  92 VWTV-PILIIIFLAV----LTWKTTHALEPSkplahdekpITIEVVSMDWKWFFIYPEQG-------------------- 146
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 295065514 135 lLEVDNRVVLPIEAPVRMMITSQDVLHSWTVPSLGLKTDAIPGRLNQTTFTATRPGVYYGQCSEICGANHSFM 207
Cdd:PRK10525 147 -IATVNEIAFPANVPVYFKVTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIANEPGTYDGISASYSGPGFSGM 218
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
151-207 1.10e-03

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


Pssm-ID: 259984 [Multi-domain]  Cd Length: 88  Bit Score: 36.97  E-value: 1.10e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 295065514 151 RMMITSQDVLHSWTVPSLGLKTDAIPGRLNQTTFTATRPGVYYGQCSEICGANHSFM 207
Cdd:cd13917   25 RLHLSSLDVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIICNEYCGIGHHTM 81
PRK02888 PRK02888
nitrous-oxide reductase; Validated
157-207 1.44e-03

nitrous-oxide reductase; Validated


Pssm-ID: 235082 [Multi-domain]  Cd Length: 635  Bit Score: 39.19  E-value: 1.44e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 295065514 157 QDVLHSWTVPSLGLKTDAIPGRLNQTTFTATRPGVYYGQCSEICGANHSFM 207
Cdd:PRK02888 576 EDLTHGFAIPNYGVNMEVAPQATASVTFTADKPGVYWYYCTWFCHALHMEM 626
NosZ COG4263
Nitrous oxide reductase [Inorganic ion transport and metabolism];
158-207 3.13e-03

Nitrous oxide reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443405 [Multi-domain]  Cd Length: 621  Bit Score: 38.35  E-value: 3.13e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 295065514 158 DVLHSWTVPSLGLKTDAIPGRLNQTTFTATRPGVYYGQCSEICGANHSFM 207
Cdd:COG4263  564 DLTHGFAIPGYNINMEIMPQETASVTFVADKPGVYWYYCTWFCHALHMEM 613
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH