NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|223951274|gb|ACN29567|]
View 

cytochrome c oxidase subunit II (mitochondrion) [Gobiobotia brevibarba]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11475911)

cytochrome c oxidase subunit II, part of the functional core of the enzyme, transfers the electrons from cytochrome c via its binuclear copper A center to the bimetallic center of the catalytic subunit I

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-230 0e+00

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 501.55  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274   1 MAHPTQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIIAMVSTKLTNKYILDSQEIEIVWTVLPAVILVLIALPS 80
Cdd:MTH00129   1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMTPTHDLTPGQFRLLETDHRMVVPMESPIRVLVSAEDVL 160
Cdd:MTH00129  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274 161 HSWAVPSLGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFESWSSLMLEDA 230
Cdd:MTH00129 161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLMLEDA 230
 
Name Accession Description Interval E-value
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-230 0e+00

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 501.55  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274   1 MAHPTQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIIAMVSTKLTNKYILDSQEIEIVWTVLPAVILVLIALPS 80
Cdd:MTH00129   1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMTPTHDLTPGQFRLLETDHRMVVPMESPIRVLVSAEDVL 160
Cdd:MTH00129  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274 161 HSWAVPSLGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFESWSSLMLEDA 230
Cdd:MTH00129 161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLMLEDA 230
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-222 6.62e-97

C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the binuclear center (active site) in subunit I.


Pssm-ID: 259979 [Multi-domain]  Cd Length: 130  Bit Score: 278.30  E-value: 6.62e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274  93 PHLTIKAMGHQWYWSYEYTDYEDLGFDSYMTPTHDLTPGQFRLLETDHRMVVPMESPIRVLVSAEDVLHSWAVPSLGVKM 172
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 223951274 173 DAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFESW 222
Cdd:cd13912   81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 1.02e-86

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 252.33  E-value: 1.02e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274   95 LTIKAMGHQWYWSYEYTDYEDLGFDSYMTPTHDLTPGQFRLLETDHRMVVPMESPIRVLVSAEDVLHSWAVPSLGVKMDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 223951274  175 VPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAV 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-222 9.42e-63

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 195.43  E-value: 9.42e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274   6 QLGFQDAASPVMEELLHFHDHALMIVFLISTLV-LYIIIAMV-----STKLTNKYILDSQEIEIVWTVLPAVILVLIALP 79
Cdd:COG1622   18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVfGLLLYFAIryrrrKGDADPAQFHHNTKLEIVWTVIPIIIVIVLAVP 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274  80 SLRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLgfdsymtpthdltpgqfrlleTDHRMVVPMESPIRVLVSAEDV 159
Cdd:COG1622   98 TLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVNELVLPVGRPVRFLLTSADV 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 223951274 160 LHSWAVPSLGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFESW 222
Cdd:COG1622  157 IHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAW 219
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-222 8.47e-49

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: 158.70  E-value: 8.47e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274   12 AASPVMEELLHFHDHALMIVFLISTLVLYIIIAMV------STKLTNKYILDSQEIEIVWTVLPAVILV-LIALPSLRIL 84
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVwkfrrkGDEEKPSQIHGNRRLEYVWTVIPLIIVVgLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274   85 YLMDEINDPHLTIKAMGHQWYWSYEYTDYedlgfdsymtpthdltpgqfrLLETDHRMVVPMESPIRVLVSAEDVLHSWA 164
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFW 139

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 223951274  165 VPSLGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFESW 222
Cdd:TIGR02866 140 VPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAY 197
 
Name Accession Description Interval E-value
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-230 0e+00

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 501.55  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274   1 MAHPTQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIIAMVSTKLTNKYILDSQEIEIVWTVLPAVILVLIALPS 80
Cdd:MTH00129   1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMTPTHDLTPGQFRLLETDHRMVVPMESPIRVLVSAEDVL 160
Cdd:MTH00129  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274 161 HSWAVPSLGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFESWSSLMLEDA 230
Cdd:MTH00129 161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLMLEDA 230
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-227 4.91e-171

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 469.39  E-value: 4.91e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274   1 MAHPTQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIIAMVSTKLTNKYILDSQEIEIVWTVLPAVILVLIALPS 80
Cdd:MTH00117   1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMTPTHDLTPGQFRLLETDHRMVVPMESPIRVLVSAEDVL 160
Cdd:MTH00117  81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 223951274 161 HSWAVPSLGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFESWSSLML 227
Cdd:MTH00117 161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLLS 227
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-230 2.72e-164

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 452.42  E-value: 2.72e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274   1 MAHPTQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIIAMVSTKLTNKYILDSQEIEIVWTVLPAVILVLIALPS 80
Cdd:MTH00185   1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMTPTHDLTPGQFRLLETDHRMVVPMESPIRVLVSAEDVL 160
Cdd:MTH00185  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274 161 HSWAVPSLGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFESWSSLMLEDA 230
Cdd:MTH00185 161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLMLEEA 230
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-227 2.37e-157

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 434.92  E-value: 2.37e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274   1 MAHPTQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIIAMVSTKLTNKYILDSQEIEIVWTVLPAVILVLIALPS 80
Cdd:MTH00098   1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMTPTHDLTPGQFRLLETDHRMVVPMESPIRVLVSAEDVL 160
Cdd:MTH00098  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 223951274 161 HSWAVPSLGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFESWSSLML 227
Cdd:MTH00098 161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASML 227
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-228 2.50e-155

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 429.97  E-value: 2.50e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274   1 MAHPTQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIIAMVSTKLTNKYILDSQEIEIVWTVLPAVILVLIALPS 80
Cdd:MTH00076   1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMTPTHDLTPGQFRLLETDHRMVVPMESPIRVLVSAEDVL 160
Cdd:MTH00076  81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 223951274 161 HSWAVPSLGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFESWSSLMLE 228
Cdd:MTH00076 161 HSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSMLE 228
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-224 2.65e-143

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 399.35  E-value: 2.65e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274   1 MAHPTQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIIAMVSTKLTNKYILDSQEIEIVWTVLPAVILVLIALPS 80
Cdd:MTH00168   1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMTPTHDLTPGQFRLLETDHRMVVPMESPIRVLVSAEDVL 160
Cdd:MTH00168  81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223951274 161 HSWAVPSLGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFESWSS 224
Cdd:MTH00168 161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVD 224
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-227 1.60e-142

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 397.28  E-value: 1.60e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274   1 MAHPTQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIIAMVSTKLTNKYILDSQEIEIVWTVLPAVILVLIALPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMTPTHDLTPGQFRLLETDHRMVVPMESPIRVLVSAEDVL 160
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 223951274 161 HSWAVPSLGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFESWSSLML 227
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-229 1.89e-138

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 387.13  E-value: 1.89e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274   1 MAHPTQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIIAMVSTKLTNKYILDSQEIEIVWTVLPAVILVLIALPS 80
Cdd:MTH00038   1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMTPTHDLTPGQFRLLETDHRMVVPMESPIRVLVSAEDVL 160
Cdd:MTH00038  81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 223951274 161 HSWAVPSLGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFESWSSLMLED 229
Cdd:MTH00038 161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFLEE 229
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-226 3.76e-129

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 363.49  E-value: 3.76e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274   1 MAHPTQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIIAMVSTKLTNKYILDSQEIEIVWTVLPAVILVLIALPS 80
Cdd:MTH00140   1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMTPTHDLTPGQFRLLETDHRMVVPMESPIRVLVSAEDVL 160
Cdd:MTH00140  81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 223951274 161 HSWAVPSLGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFESWSSLM 226
Cdd:MTH00140 161 HSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELM 226
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-222 2.53e-126

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 356.33  E-value: 2.53e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274   1 MAHPTQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIIAMVSTKLTNKYILDSQEIEIVWTVLPAVILVLIALPS 80
Cdd:MTH00139   1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMTPTHDLTPGQFRLLETDHRMVVPMESPIRVLVSAEDVL 160
Cdd:MTH00139  81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 223951274 161 HSWAVPSLGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFESW 222
Cdd:MTH00139 161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEW 222
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-224 1.07e-121

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 344.92  E-value: 1.07e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274   1 MAHPTQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIIAMVSTKLTNKYILDSQEIEIVWTVLPAVILVLIALPS 80
Cdd:MTH00008   1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMTPTHDLTPGQFRLLETDHRMVVPMESPIRVLVSAEDVL 160
Cdd:MTH00008  81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223951274 161 HSWAVPSLGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFESWSS 224
Cdd:MTH00008 161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVS 224
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 2-229 1.28e-119

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 340.19  E-value: 1.28e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274   2 AHPTQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIIAMVSTKLTNKYILDSQEIEIVWTVLPAVILVLIALPSL 81
Cdd:MTH00023  11 PEPWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274  82 RILYLMDEINDPHLTIKAMGHQWYWSYEYTDYED--LGFDSYMTPTHDLTPGQFRLLETDHRMVVPMESPIRVLVSAEDV 159
Cdd:MTH00023  91 KLLYLMDEVVSPALTIKAIGHQWYWSYEYSDYEGetLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADV 170

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274 160 LHSWAVPSLGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFESWSSLMLED 229
Cdd:MTH00023 171 LHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLSLSND 240
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 2-230 6.17e-114

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 325.58  E-value: 6.17e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274   2 AHPTQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIIAMVSTKLTNKYILDSQEIEIVWTVLPAVILVLIALPSL 81
Cdd:MTH00051   4 PEPWQLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274  82 RILYLMDEINDPHLTIKAMGHQWYWSYEYTDY--EDLGFDSYMTPTHDLTPGQFRLLETDHRMVVPMESPIRVLVSAEDV 159
Cdd:MTH00051  84 KLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADV 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 223951274 160 LHSWAVPSLGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFESWSSLMLEDA 230
Cdd:MTH00051 164 LHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQSEEI 234
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-222 6.62e-97

C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the binuclear center (active site) in subunit I.


Pssm-ID: 259979 [Multi-domain]  Cd Length: 130  Bit Score: 278.30  E-value: 6.62e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274  93 PHLTIKAMGHQWYWSYEYTDYEDLGFDSYMTPTHDLTPGQFRLLETDHRMVVPMESPIRVLVSAEDVLHSWAVPSLGVKM 172
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 223951274 173 DAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFESW 222
Cdd:cd13912   81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 4-222 8.34e-89

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 262.65  E-value: 8.34e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274   4 PTQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIIAMVstkLTNKYI------LDSQEIEIVWTVLPAVILVLIA 77
Cdd:MTH00027  32 PWQLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRIL---LGNNYYsyywnkLDGSLIEVIWTLIPAFILILIA 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274  78 LPSLRILYLMDE-INDPHLTIKAMGHQWYWSYEYTDY--EDLGFDSYMTPTHDLTPGQFRLLETDHRMVVPMESPIRVLV 154
Cdd:MTH00027 109 FPSLRLLYIMDEcGFSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLI 188

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 223951274 155 SAEDVLHSWAVPSLGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFESW 222
Cdd:MTH00027 189 TAADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDW 256
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 1.02e-86

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 252.33  E-value: 1.02e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274   95 LTIKAMGHQWYWSYEYTDYEDLGFDSYMTPTHDLTPGQFRLLETDHRMVVPMESPIRVLVSAEDVLHSWAVPSLGVKMDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 223951274  175 VPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAV 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 23-228 2.26e-78

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 235.29  E-value: 2.26e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274  23 FHDHALMIVFLISTLVLYIIIAMVSTKLTNKYILDSQEIEIVWTVLPAVILVLIALPSLRILYLMDEIN-DPHLTIKAMG 101
Cdd:MTH00080  25 FNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMNlDSNLTVKVTG 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274 102 HQWYWSYEYTDYEDLGFDSYMTPTHDLTPGQFRLLETDHRMVVPMESPIRVLVSAEDVLHSWAVPSLGVKMDAVPGRLNQ 181
Cdd:MTH00080 105 HQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILST 184

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 223951274 182 TAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFESWSSLMLE 228
Cdd:MTH00080 185 LCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWCKLLLD 231
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-222 9.42e-63

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 195.43  E-value: 9.42e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274   6 QLGFQDAASPVMEELLHFHDHALMIVFLISTLV-LYIIIAMV-----STKLTNKYILDSQEIEIVWTVLPAVILVLIALP 79
Cdd:COG1622   18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVfGLLLYFAIryrrrKGDADPAQFHHNTKLEIVWTVIPIIIVIVLAVP 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274  80 SLRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLgfdsymtpthdltpgqfrlleTDHRMVVPMESPIRVLVSAEDV 159
Cdd:COG1622   98 TLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVNELVLPVGRPVRFLLTSADV 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 223951274 160 LHSWAVPSLGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFESW 222
Cdd:COG1622  157 IHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAW 219
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-222 8.47e-49

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: 158.70  E-value: 8.47e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274   12 AASPVMEELLHFHDHALMIVFLISTLVLYIIIAMV------STKLTNKYILDSQEIEIVWTVLPAVILV-LIALPSLRIL 84
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVwkfrrkGDEEKPSQIHGNRRLEYVWTVIPLIIVVgLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274   85 YLMDEINDPHLTIKAMGHQWYWSYEYTDYedlgfdsymtpthdltpgqfrLLETDHRMVVPMESPIRVLVSAEDVLHSWA 164
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFW 139

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 223951274  165 VPSLGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFESW 222
Cdd:TIGR02866 140 VPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAY 197
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 17-214 5.76e-48

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 156.27  E-value: 5.76e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274  17 MEELLHFHDHALMIVFLISTLVLYIIIAM----VSTKLTNKYILDSQEIEIVWTVLPAVI-LVLIALPSLRILYLMDEIn 91
Cdd:MTH00047   1 MNLSLLYYDIVCYILALCVFIPCWVYIMLcwqvVSGNGSVNFGSENQVLELLWTVVPTLLvLVLCFLNLNFITSDLDCF- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274  92 dPHLTIKAMGHQWYWSYEYTDyeDLGFDSYMTpthDLTPGqfrlleTDHRMVVPMESPIRVLVSAEDVLHSWAVPSLGVK 171
Cdd:MTH00047  80 -SSETIKVIGHQWYWSYEYSF--GGSYDSFMT---DDIFG------VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLK 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 223951274 172 MDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAV 214
Cdd:MTH00047 148 MDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVV 190
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 118-219 3.21e-41

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 138.03  E-value: 3.21e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274 118 FDSYMTPTHDLTPGQFRLLETDHRMVVPMESPIRVLVSAEDVLHSWAVPSLGVKMDAVPGRLNQ-TAFIAsRPGVFYGQC 196
Cdd:PTZ00047  51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKiNTFIL-REGVFYGQC 129

                         90       100
                 ....*....|....*....|...
gi 223951274 197 SEICGANHSFMPIVVEAVPLEHF 219
Cdd:PTZ00047 130 SEMCGTLHGFMPIVVEAVSPEAY 152
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-212 2.05e-31

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


Pssm-ID: 259911 [Multi-domain]  Cd Length: 95  Bit Score: 110.85  E-value: 2.05e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274  95 LTIKAMGHQWYWSYEYTDyedlgfdsymtpthdltpgqfrlLETDHRMVVPMESPIRVLVSAEDVLHSWAVPSLGVKMDA 174
Cdd:cd13842    1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 223951274 175 VPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVE 212
Cdd:cd13842   58 VPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 94-214 2.44e-31

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: 110.79  E-value: 2.44e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274  94 HLTIKAMGHQWYWSYEYTDYEDLGFdsymtpthdltpgqfrllETDHRMVVPMESPIRVLVSAEDVLHSWAVPSLGVKMD 173
Cdd:cd04213    1 ALTIEVTGHQWWWEFRYPDEPGRGI------------------VTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMD 62

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 223951274 174 AVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAV 214
Cdd:cd04213   63 MIPGRTNRLWLQADEPGVYRGQCAEFCGASHALMRFKVIAL 103
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-83 4.10e-29

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


Pssm-ID: 397083 [Multi-domain]  Cd Length: 89  Bit Score: 104.72  E-value: 4.10e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274    1 MAHPTQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIIAMV------STKLTNKYILDSQEIEIVWTVLPAVILV 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLirfnrrKNPITARYTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 223951274   75 LIALPSLRI 83
Cdd:pfam02790  81 LIALPSFKL 89
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 68-222 3.71e-25

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


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 95.99  E-value: 3.71e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274  68 LPAVILV-LIALPSLRILYLMD---EINDPHLTIKAMGHQWYWSYEYtdyedlgfdsymtpthdltPGQFRLLETdhrMV 143
Cdd:cd13918    2 LSAIIVIsLIVWTYGMLLYVEDppdEADEDALEVEVEGFQFGWQFEY-------------------PNGVTTGNT---LR 59

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 223951274 144 VPMESPIRVLVSAEDVLHSWAVPSLGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFESW 222
Cdd:cd13918   60 VPADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAW 138
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-212 4.96e-25

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


Pssm-ID: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 94.63  E-value: 4.96e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274  95 LTIKAMGHQWYWSYEYTDYedlgfDSYMTPTHDLTPGQfrlletdhrMVVPMESPIRVLVSAEDVLHSWAVPSLGVKMDA 174
Cdd:cd13919    2 LVVEVTAQQWAWTFRYPGG-----DGKLGTDDDVTSPE---------LHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 223951274 175 VPGRLNQTAFIASRPGVFYGQCSEICGANHSFM--PIVVE 212
Cdd:cd13919   68 VPGRTTRLWFTPTREGEYEVRCAELCGLGHYRMraTVKVV 107
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-213 4.43e-23

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


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 89.23  E-value: 4.43e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274  95 LTIKAMGHQWYWSYEYtdyedlgfdsymtpthdltPGQFRlleTDHRMVVPMESPIRVLVSAEDVLHSWAVPSLGVKMDA 174
Cdd:cd13915    2 LEIQVTGRQWMWEFTY-------------------PNGKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDV 59

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 223951274 175 VPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEA 213
Cdd:cd13915   60 VPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGMIGKVRV 98
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 96-222 1.73e-21

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


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 85.54  E-value: 1.73e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274  96 TIKAMGHQWYWSYEYTDYEdlgfdsymtpthdltpgqfrlLETDHRMVVPMESPIRVLVSAEDVLHSWAVPSLGVKMDAV 175
Cdd:cd13914    2 EIEVEAYQWGWEFSYPEAN---------------------VTTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAF 60

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 223951274 176 PGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFESW 222
Cdd:cd13914   61 PGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQW 107
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 142-212 1.25e-07

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: 48.33  E-value: 1.25e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 223951274 142 MVVPMESPIRVLVSAEDVLHSWAVPSLGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFM--PIVVE 212
Cdd:cd13913   27 IEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNMygKIIVE 99
PRK02888 PRK02888
nitrous-oxide reductase; Validated
 121-213 1.80e-06

nitrous-oxide reductase; Validated


Pssm-ID: 235082 [Multi-domain]  Cd Length: 635  Bit Score: 48.05  E-value: 1.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274 121 YMT---PTHDLTpgQFRLLETDHRMVVpmespIRVLVSAEDVLHSWAVPSLGVKMDAVPgrlNQTA---FIASRPGVFYG 194
Cdd:PRK02888 544 YMTsqaPAFGLR--EFTVKQGDEVTVI-----VTNLDKVEDLTHGFAIPNYGVNMEVAP---QATAsvtFTADKPGVYWY 613

                         90       100
                 ....*....|....*....|.
gi 223951274 195 QCSEICGANHSFMP--IVVEA 213
Cdd:PRK02888 614 YCTWFCHALHMEMRgrMLVEP 634
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 95-214 3.93e-06

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


Pssm-ID: 259874 [Multi-domain]  Cd Length: 99  Bit Score: 44.08  E-value: 3.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274  95 LTIKAMGHQWYWSYEYTDYEdlgfdsymtpthdltpgqfrlLETDHRMVVPMESPIRVLVSAEDVLHSWAVPSLGVKMDA 174
Cdd:cd04212    1 LEIQVVSLDWKWLFIYPEQG---------------------IATVNELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYA 59

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 223951274 175 VPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAV 214
Cdd:cd04212   60 MAGMQTQLHLIADKPGTYQGLSANYSGEGFSDMKFKVLAV 99
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 156-207 5.44e-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: 43.76  E-value: 5.44e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 223951274 156 AEDVLHSWAVPSLGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFM 207
Cdd:cd04223   36 DEDITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALHLEM 87
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 96-207 3.20e-04

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: 38.52  E-value: 3.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274  96 TIKAMGHQWYWSyeytdyedlgfdsyMTPThdltpgqfrlletdhrmVVPMESPIRVLVSAEDVLHSWAVPS----LGVK 171
Cdd:cd13916    2 VVAVTGHQWYWE--------------LSRT-----------------EIPAGKPVEFRVTSADVNHGFGIYDpdmrLLAQ 50

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 223951274 172 MDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFM 207
Cdd:cd13916   51 TQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 121-212 5.76e-04

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


Pssm-ID: 259860 [Multi-domain]  Cd Length: 110  Bit Score: 38.37  E-value: 5.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274 121 YMTPTHDLTPGQFRLLETDHRMVVPMESPIRV-LVSAEDVLHSWAVPSLGVKMDA---------------VPGRLNQTAF 184
Cdd:cd00920    4 TASDWGWSFTYNGVLLFGPPVLVVPVGDTVRVqFVNKLGENHSVTIAGFGVPVVAmagganpglvntlviGPGESAEVTF 83

                         90       100
                 ....*....|....*....|....*...
gi 223951274 185 IASRPGVFYGQCSEICGaNHSFMPIVVE 212
Cdd:cd00920   84 TTDQAGVYWFYCTIPGH-NHAGMVGTIN 110
PRK10525 PRK10525
cytochrome o ubiquinol oxidase subunit II; Provisional
 58-222 1.88e-03

cytochrome o ubiquinol oxidase subunit II; Provisional


Pssm-ID: 182518 [Multi-domain]  Cd Length: 315  Bit Score: 38.63  E-value: 1.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274  58 SQEIE-IVWTVlPAVILVLIALPSLRILYLMDEI-----NDPHLTIKAMGHQWYWSYEYTDyedLGfdsymtpthdltpg 131
Cdd:PRK10525  85 SNKVEaVVWTV-PILIIIFLAVLTWKTTHALEPSkplahDEKPITIEVVSMDWKWFFIYPE---QG-------------- 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223951274 132 qfrlLETDHRMVVPMESPIRVLVSAEDVLHSWAVPSLGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVV 211
Cdd:PRK10525 147 ----IATVNEIAFPANVPVYFKVTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIANEPGTYDGISASYSGPGFSGMKFKA 222

                        170
                 ....*....|..
gi 223951274 212 EAVP-LEHFESW 222
Cdd:PRK10525 223 IATPdRAEFDQW 234
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH