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Conserved domains on  [gi|2252659622|ref|YP_010410318|]
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cytochrome c oxidase subunit II (mitochondrion) [Haplotropis brunneriana]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11475927)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-227 6.35e-162

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 446.20  E-value: 6.35e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622   1 MATWSIFSLQDSASPLMEQLSFFHDHTMTVLTLITIVVGYSLSYMLTIKYSNRYVLHGHLIETIWTTLPAITLIFIALPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622  81 LRLLYMLDDSIDALITIKTIGRQWYWSYEYSDFVDLEFDAYMTPESELEEDGFRLLDVDNRTILPMNTEVRILTSASDVL 160
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2252659622 161 HSWAIPSLGIKIDATPGRLNQGTFTINRPGLFFGQCSEICGANHSFMPIVIESTSVNMFIKWLSKMI 227
Cdd:MTH00154  161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-227 6.35e-162

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 446.20  E-value: 6.35e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622   1 MATWSIFSLQDSASPLMEQLSFFHDHTMTVLTLITIVVGYSLSYMLTIKYSNRYVLHGHLIETIWTTLPAITLIFIALPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622  81 LRLLYMLDDSIDALITIKTIGRQWYWSYEYSDFVDLEFDAYMTPESELEEDGFRLLDVDNRTILPMNTEVRILTSASDVL 160
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2252659622 161 HSWAIPSLGIKIDATPGRLNQGTFTINRPGLFFGQCSEICGANHSFMPIVIESTSVNMFIKWLSKMI 227
Cdd:MTH00154  161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 95-222 4.26e-88

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: 255.96  E-value: 4.26e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622  95 ITIKTIGRQWYWSYEYSDFVDLEFDAYMTPESELEEDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAIPSLGIKIDA 174
Cdd:cd13912     3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2252659622 175 TPGRLNQGTFTINRPGLFFGQCSEICGANHSFMPIVIESTSVNMFIKW 222
Cdd:cd13912    83 VPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 2.67e-78

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 230.76  E-value: 2.67e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622  95 ITIKTIGRQWYWSYEYSDFVDLEFDAYMTPESELEEDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAIPSLGIKIDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2252659622 175 TPGRLNQGTFTINRPGLFFGQCSEICGANHSFMPIVIEST 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
7-226 1.55e-53

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 171.55  E-value: 1.55e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622   7 FSLQDSASPLMEQLSFFHDHTMTVLTLITIVVGYSLSYMLtIKYSNR-------YVLHGHLIETIWTTLPAITLIFIALP 79
Cdd:COG1622    19 LSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFA-IRYRRRkgdadpaQFHHNTKLEIVWTVIPIIIVIVLAVP 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622  80 SLRLLYMLDDSIDALITIKTIGRQWYWSYEYsdfvdlefdaymtpeseLEEDGfrllDVDNRTILPMNTEVRILTSASDV 159
Cdd:COG1622    98 TLRVLHALDDAPEDPLTVEVTGYQWKWLFRY-----------------PDQGI----ATVNELVLPVGRPVRFLLTSADV 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2252659622 160 LHSWAIPSLGIKIDATPGRLNQGTFTINRPGLFFGQCSEICGANHSFMPIVIESTSVNMFIKWLSKM 226
Cdd:COG1622   157 IHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQ 223
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 13-224 1.35e-43

cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions. [Energy metabolism, Electron transport]


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 145.22  E-value: 1.35e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622  13 ASPLMEQLSFFHDHTMTVLTLITIVVGYSLSYMlTIKYSNR-------YVLHGHLIETIWTTLPAITLIFIALPSLRLLY 85
Cdd:TIGR02866   2 GGEIAQQIAFLFLFVLAVSTLISLLVAALLAYV-VWKFRRKgdeekpsQIHGNRRLEYVWTVIPLIIVVGLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622  86 MLDDSID-ALITIKTIGRQWYWSYEYsdfvdlefdaymtpeselEEDGFRlldVDNRTILPMNTEVRILTSASDVLHSWA 164
Cdd:TIGR02866  81 YLERPIPkDALKVKVTGYQWWWDFEY------------------PESGFT---TVNELVLPAGTPVELQVTSKDVIHSFW 139

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622 165 IPSLGIKIDATPGRLNQGTFTINRPGLFFGQCSEICGANHSFMPIVIESTSVNMFIKWLS 224
Cdd:TIGR02866 140 VPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-227 6.35e-162

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 446.20  E-value: 6.35e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622   1 MATWSIFSLQDSASPLMEQLSFFHDHTMTVLTLITIVVGYSLSYMLTIKYSNRYVLHGHLIETIWTTLPAITLIFIALPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622  81 LRLLYMLDDSIDALITIKTIGRQWYWSYEYSDFVDLEFDAYMTPESELEEDGFRLLDVDNRTILPMNTEVRILTSASDVL 160
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2252659622 161 HSWAIPSLGIKIDATPGRLNQGTFTINRPGLFFGQCSEICGANHSFMPIVIESTSVNMFIKWLSKMI 227
Cdd:MTH00154  161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-226 1.46e-122

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 346.93  E-value: 1.46e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622   1 MATWSIFSLQDSASPLMEQLSFFHDHTMTVLTLITIVVGYSLSYMLTIKYSNRYVLHGHLIETIWTTLPAITLIFIALPS 80
Cdd:MTH00140    1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622  81 LRLLYMLDDSIDALITIKTIGRQWYWSYEYSDFVDLEFDAYMTPESELEEDGFRLLDVDNRTILPMNTEVRILTSASDVL 160
Cdd:MTH00140   81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2252659622 161 HSWAIPSLGIKIDATPGRLNQGTFTINRPGLFFGQCSEICGANHSFMPIVIESTSVNMFIKWLSKM 226
Cdd:MTH00140  161 HSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELM 226
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-226 2.61e-122

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 346.13  E-value: 2.61e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622   1 MATWSIFSLQDSASPLMEQLSFFHDHTMTVLTLITIVVGYSLSYMLTIKYSNRYVLHGHLIETIWTTLPAITLIFIALPS 80
Cdd:MTH00117    1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622  81 LRLLYMLDDSIDALITIKTIGRQWYWSYEYSDFVDLEFDAYMTPESELEEDGFRLLDVDNRTILPMNTEVRILTSASDVL 160
Cdd:MTH00117   81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2252659622 161 HSWAIPSLGIKIDATPGRLNQGTFTINRPGLFFGQCSEICGANHSFMPIVIESTSVNMFIKWLSKM 226
Cdd:MTH00117  161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLL 226
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-226 2.54e-120

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 340.93  E-value: 2.54e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622   1 MATWSIFSLQDSASPLMEQLSFFHDHTMTVLTLITIVVGYSLSYMLTIKYSNRYVLHGHLIETIWTTLPAITLIFIALPS 80
Cdd:MTH00139    1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622  81 LRLLYMLDDSIDALITIKTIGRQWYWSYEYSDFVDLEFDAYMTPESELEEDGFRLLDVDNRTILPMNTEVRILTSASDVL 160
Cdd:MTH00139   81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2252659622 161 HSWAIPSLGIKIDATPGRLNQGTFTINRPGLFFGQCSEICGANHSFMPIVIESTSVNMFIKWLSKM 226
Cdd:MTH00139  161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILEK 226
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-227 1.64e-117

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 333.98  E-value: 1.64e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622   1 MATWSIFSLQDSASPLMEQLSFFHDHTMTVLTLITIVVGYSLSYMLTIKYSNRYVLHGHLIETIWTTLPAITLIFIALPS 80
Cdd:MTH00038    1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622  81 LRLLYMLDDSIDALITIKTIGRQWYWSYEYSDFVDLEFDAYMTPESELEEDGFRLLDVDNRTILPMNTEVRILTSASDVL 160
Cdd:MTH00038   81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2252659622 161 HSWAIPSLGIKIDATPGRLNQGTFTINRPGLFFGQCSEICGANHSFMPIVIESTSVNMFIKWLSKMI 227
Cdd:MTH00038  161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFL 227
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-224 4.20e-116

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 330.40  E-value: 4.20e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622   1 MATWSIFSLQDSASPLMEQLSFFHDHTMTVLTLITIVVGYSLSYMLTIKYSNRYVLHGHLIETIWTTLPAITLIFIALPS 80
Cdd:MTH00168    1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622  81 LRLLYMLDDSIDALITIKTIGRQWYWSYEYSDFVDLEFDAYMTPESELEEDGFRLLDVDNRTILPMNTEVRILTSASDVL 160
Cdd:MTH00168   81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2252659622 161 HSWAIPSLGIKIDATPGRLNQGTFTINRPGLFFGQCSEICGANHSFMPIVIESTSVNMFIKWLS 224
Cdd:MTH00168  161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVD 224
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-225 1.47e-113

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 324.12  E-value: 1.47e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622   1 MATWSIFSLQDSASPLMEQLSFFHDHTMTVLTLITIVVGYSLSYMLTIKYSNRYVLHGHLIETIWTTLPAITLIFIALPS 80
Cdd:MTH00008    1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622  81 LRLLYMLDDSIDALITIKTIGRQWYWSYEYSDFVDLEFDAYMTPESELEEDGFRLLDVDNRTILPMNTEVRILTSASDVL 160
Cdd:MTH00008   81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2252659622 161 HSWAIPSLGIKIDATPGRLNQGTFTINRPGLFFGQCSEICGANHSFMPIVIESTSVNMFIKWLSK 225
Cdd:MTH00008  161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSS 225
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-227 1.41e-107

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 308.96  E-value: 1.41e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622   1 MATWSIFSLQDSASPLMEQLSFFHDHTMTVLTLITIVVGYSLSYMLTIKYSNRYVLHGHLIETIWTTLPAITLIFIALPS 80
Cdd:MTH00098    1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622  81 LRLLYMLDDSIDALITIKTIGRQWYWSYEYSDFVDLEFDAYMTPESELEEDGFRLLDVDNRTILPMNTEVRILTSASDVL 160
Cdd:MTH00098   81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2252659622 161 HSWAIPSLGIKIDATPGRLNQGTFTINRPGLFFGQCSEICGANHSFMPIVIESTSVNMFIKWLSKMI 227
Cdd:MTH00098  161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASML 227
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 8-227 1.48e-104

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 301.67  E-value: 1.48e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622   8 SLQDSASPLMEQLSFFHDHTMTVLTLITIVVGYSLSYMLTIKYSNRYVLHGHLIETIWTTLPAITLIFIALPSLRLLYML 87
Cdd:MTH00023   17 GFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYLM 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622  88 DDSIDALITIKTIGRQWYWSYEYSDFVD--LEFDAYMTPESELEEDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAI 165
Cdd:MTH00023   97 DEVVSPALTIKAIGHQWYWSYEYSDYEGetLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAV 176

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2252659622 166 PSLGIKIDATPGRLNQGTFTINRPGLFFGQCSEICGANHSFMPIVIESTSVNMFIKWLSKMI 227
Cdd:MTH00023  177 PSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLSLS 238
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-227 1.51e-103

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 298.94  E-value: 1.51e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622   1 MATWSIFSLQDSASPLMEQLSFFHDHTMTVLTLITIVVGYSLSYMLTIKYSNRYVLHGHLIETIWTTLPAITLIFIALPS 80
Cdd:MTH00129    1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622  81 LRLLYMLDDSIDALITIKTIGRQWYWSYEYSDFVDLEFDAYMTPESELEEDGFRLLDVDNRTILPMNTEVRILTSASDVL 160
Cdd:MTH00129   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2252659622 161 HSWAIPSLGIKIDATPGRLNQGTFTINRPGLFFGQCSEICGANHSFMPIVIESTSVNMFIKWLSKMI 227
Cdd:MTH00129  161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLML 227
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-227 2.98e-103

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 297.95  E-value: 2.98e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622   1 MATWSIFSLQDSASPLMEQLSFFHDHTMTVLTLITIVVGYSLSYMLTIKYSNRYVLHGHLIETIWTTLPAITLIFIALPS 80
Cdd:MTH00185    1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622  81 LRLLYMLDDSIDALITIKTIGRQWYWSYEYSDFVDLEFDAYMTPESELEEDGFRLLDVDNRTILPMNTEVRILTSASDVL 160
Cdd:MTH00185   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2252659622 161 HSWAIPSLGIKIDATPGRLNQGTFTINRPGLFFGQCSEICGANHSFMPIVIESTSVNMFIKWLSKMI 227
Cdd:MTH00185  161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLML 227
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-226 1.03e-102

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 296.69  E-value: 1.03e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622   1 MATWSIFSLQDSASPLMEQLSFFHDHTMTVLTLITIVVGYSLSYMLTIKYSNRYVLHGHLIETIWTTLPAITLIFIALPS 80
Cdd:MTH00076    1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622  81 LRLLYMLDDSIDALITIKTIGRQWYWSYEYSDFVDLEFDAYMTPESELEEDGFRLLDVDNRTILPMNTEVRILTSASDVL 160
Cdd:MTH00076   81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2252659622 161 HSWAIPSLGIKIDATPGRLNQGTFTINRPGLFFGQCSEICGANHSFMPIVIESTSVNMFIKWLSKM 226
Cdd:MTH00076  161 HSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSM 226
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 10-224 2.66e-102

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 295.92  E-value: 2.66e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622  10 QDSASPLMEQLSFFHDHTMTVLTLITIVVGYSLSYMLTIKYSNRYVLHGHLIETIWTTLPAITLIFIALPSLRLLYMLDD 89
Cdd:MTH00051   12 QDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYLMDE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622  90 SIDALITIKTIGRQWYWSYEYSDF--VDLEFDAYMTPESELEEDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAIPS 167
Cdd:MTH00051   92 VIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPS 171

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2252659622 168 LGIKIDATPGRLNQGTFTINRPGLFFGQCSEICGANHSFMPIVIESTSVNMFIKWLS 224
Cdd:MTH00051  172 LSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVA 228
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 95-222 4.26e-88

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: 255.96  E-value: 4.26e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622  95 ITIKTIGRQWYWSYEYSDFVDLEFDAYMTPESELEEDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAIPSLGIKIDA 174
Cdd:cd13912     3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2252659622 175 TPGRLNQGTFTINRPGLFFGQCSEICGANHSFMPIVIESTSVNMFIKW 222
Cdd:cd13912    83 VPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 2.67e-78

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 230.76  E-value: 2.67e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622  95 ITIKTIGRQWYWSYEYSDFVDLEFDAYMTPESELEEDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAIPSLGIKIDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2252659622 175 TPGRLNQGTFTINRPGLFFGQCSEICGANHSFMPIVIEST 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 9-225 1.41e-77

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 234.15  E-value: 1.41e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622   9 LQDSASPLMEQLSFFHDHtmtVLTLITIVVGYSLSYMLTIKYSNRYV------LHGHLIETIWTTLPAITLIFIALPSLR 82
Cdd:MTH00027   37 FQDAGSPVMEEIIMLHDQ---ILFILTIIVGVVLWLIIRILLGNNYYsyywnkLDGSLIEVIWTLIPAFILILIAFPSLR 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622  83 LLYMLDDSI-DALITIKTIGRQWYWSYEYSDF--VDLEFDAYMTPESELEEDGFRLLDVDNRTILPMNTEVRILTSASDV 159
Cdd:MTH00027  114 LLYIMDECGfSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADV 193

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2252659622 160 LHSWAIPSLGIKIDATPGRLNQGTFTINRPGLFFGQCSEICGANHSFMPIVIESTSVNMFIKWLSK 225
Cdd:MTH00027  194 LHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWIGR 259
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 23-223 2.25e-70

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 214.49  E-value: 2.25e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622  23 FHDHTMTVLTLITIVVGYSLSYMLTIKYSNRYVLHGHLIETIWTTLPAITLIFIALPSLRLLYMLD-DSIDALITIKTIG 101
Cdd:MTH00080   25 FNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGlMNLDSNLTVKVTG 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622 102 RQWYWSYEYSDFVDLEFDAYMTPESELEEDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAIPSLGIKIDATPGRLNQ 181
Cdd:MTH00080  105 HQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILST 184

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2252659622 182 GTFTINRPGLFFGQCSEICGANHSFMPIVIESTSVNMFIKWL 223
Cdd:MTH00080  185 LCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWC 226
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
7-226 1.55e-53

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 171.55  E-value: 1.55e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622   7 FSLQDSASPLMEQLSFFHDHTMTVLTLITIVVGYSLSYMLtIKYSNR-------YVLHGHLIETIWTTLPAITLIFIALP 79
Cdd:COG1622    19 LSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFA-IRYRRRkgdadpaQFHHNTKLEIVWTVIPIIIVIVLAVP 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622  80 SLRLLYMLDDSIDALITIKTIGRQWYWSYEYsdfvdlefdaymtpeseLEEDGfrllDVDNRTILPMNTEVRILTSASDV 159
Cdd:COG1622    98 TLRVLHALDDAPEDPLTVEVTGYQWKWLFRY-----------------PDQGI----ATVNELVLPVGRPVRFLLTSADV 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2252659622 160 LHSWAIPSLGIKIDATPGRLNQGTFTINRPGLFFGQCSEICGANHSFMPIVIESTSVNMFIKWLSKM 226
Cdd:COG1622   157 IHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQ 223
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 13-224 1.35e-43

cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions. [Energy metabolism, Electron transport]


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 145.22  E-value: 1.35e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622  13 ASPLMEQLSFFHDHTMTVLTLITIVVGYSLSYMlTIKYSNR-------YVLHGHLIETIWTTLPAITLIFIALPSLRLLY 85
Cdd:TIGR02866   2 GGEIAQQIAFLFLFVLAVSTLISLLVAALLAYV-VWKFRRKgdeekpsQIHGNRRLEYVWTVIPLIIVVGLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622  86 MLDDSID-ALITIKTIGRQWYWSYEYsdfvdlefdaymtpeselEEDGFRlldVDNRTILPMNTEVRILTSASDVLHSWA 164
Cdd:TIGR02866  81 YLERPIPkDALKVKVTGYQWWWDFEY------------------PESGFT---TVNELVLPAGTPVELQVTSKDVIHSFW 139

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622 165 IPSLGIKIDATPGRLNQGTFTINRPGLFFGQCSEICGANHSFMPIVIESTSVNMFIKWLS 224
Cdd:TIGR02866 140 VPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 60-212 7.70e-43

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 143.17  E-value: 7.70e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622  60 LIETIWTTLPaiTLIFIALPSLRLLYMLDDSID-ALITIKTIGRQWYWSYEYSDfvDLEFDAYMTpeseleEDGFrllDV 138
Cdd:MTH00047   48 VLELLWTVVP--TLLVLVLCFLNLNFITSDLDCfSSETIKVIGHQWYWSYEYSF--GGSYDSFMT------DDIF---GV 114

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2252659622 139 DNRTILPMNTEVRILTSASDVLHSWAIPSLGIKIDATPGRLNQGTFTINRPGLFFGQCSEICGANHSFMPIVIE 212
Cdd:MTH00047  115 DKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIE 188
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 118-215 2.54e-36

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 125.32  E-value: 2.54e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622 118 FDAYMTPESELEEDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAIPSLGIKIDATPGRLNQGTFTINRPGLFFGQCS 197
Cdd:PTZ00047   51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                          90
                  ....*....|....*...
gi 2252659622 198 EICGANHSFMPIVIESTS 215
Cdd:PTZ00047  131 EMCGTLHGFMPIVVEAVS 148
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-212 1.79e-27

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: 100.45  E-value: 1.79e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622  95 ITIKTIGRQWYWSYEYSDfvdlefdaymtpeseleedgfrlLDVDNRTILPMNTEVRILTSASDVLHSWAIPSLGIKIDA 174
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2252659622 175 TPGRLNQGTFTINRPGLFFGQCSEICGANHSFMPIVIE 212
Cdd:cd13842    58 VPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-83 5.23e-25

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: 93.94  E-value: 5.23e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622   1 MATWSIFSLQDSASPLMEQLSFFHDHTMTVLTLITIVVGYSLSYMLT------IKYSNRYVLHGHLIETIWTTLPAITLI 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIrfnrrkNPITARYTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 2252659622  75 FIALPSLRL 83
Cdd:pfam02790  81 LIALPSFKL 89
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 95-207 1.09e-24

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: 93.45  E-value: 1.09e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622  95 ITIKTIGRQWYWSYEYSDfvdlefdaymtpeseleEDGFRLLDVdNRTILPMNTEVRILTSASDVLHSWAIPSLGIKIDA 174
Cdd:cd04213     2 LTIEVTGHQWWWEFRYPD-----------------EPGRGIVTA-NELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDM 63

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2252659622 175 TPGRLNQGTFTINRPGLFFGQCSEICGANHSFM 207
Cdd:cd04213    64 IPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-207 2.41e-22

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


Pssm-ID: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 87.70  E-value: 2.41e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622  95 ITIKTIGRQWYWSYEYSDFVDLEFDAYMTPESELEedgfrlldvdnrtiLPMNTEVRILTSASDVLHSWAIPSLGIKIDA 174
Cdd:cd13919     2 LVVEVTAQQWAWTFRYPGGDGKLGTDDDVTSPELH--------------LPVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2252659622 175 TPGRLNQGTFTINRPGLFFGQCSEICGANHSFM 207
Cdd:cd13919    68 VPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-207 8.43e-21

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


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 83.45  E-value: 8.43e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622  95 ITIKTIGRQWYWSYEYSDfvdlefdaymtpeseleedGFRlldVDNRTILPMNTEVRILTSASDVLHSWAIPSLGIKIDA 174
Cdd:cd13915     2 LEIQVTGRQWMWEFTYPN-------------------GKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDV 59

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2252659622 175 TPGRLNQGTFTINRPGLFFGQCSEICGANHSFM 207
Cdd:cd13915    60 VPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-223 1.65e-17

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: 75.14  E-value: 1.65e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622  95 ITIKTIGRQWYWSYEYsdfvdlefdaymtPESELEEDgfrlldvdNRTILPMNTEVRILTSASDVLHSWAIPSLGIKIDA 174
Cdd:cd13914     1 VEIEVEAYQWGWEFSY-------------PEANVTTS--------EQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDA 59

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2252659622 175 TPGRLNQGTFTINRPGLFFGQCSEICGANHSFMPIVIESTSVNMFIKWL 223
Cdd:cd13914    60 FPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 83-207 1.08e-15

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: 70.95  E-value: 1.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622  83 LLYM----LDDSIDALiTIKTIGRQWYWSYEYSDFVdlefdaymTPESELeedgfrlldvdnrtILPMNTEVRILTSASD 158
Cdd:cd13918    18 LLYVedppDEADEDAL-EVEVEGFQFGWQFEYPNGV--------TTGNTL--------------RVPADTPIALRVTSTD 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2252659622 159 VLHSWAIPSLGIKIDATPGRLNQGTFTINRPGLFFGQCSEICGANHSFM 207
Cdd:cd13918    75 VFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLM 123
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 144-207 2.59e-08

C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and some archaea, which catalyze the reduction of O2 and simultaneously pump protons across the membrane. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. The ba3 family contains oxidases that lack the conserved residues that form the D- and K-pathways in CcO and ubiquinol oxidase. Instead, they contain a potential alternative K-pathway. Additional proton channels have been proposed for this family of oxidases but none have been identified definitively.


Pssm-ID: 259980 [Multi-domain]  Cd Length: 99  Bit Score: 50.26  E-value: 2.59e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2252659622 144 LPMNTEVRILTSASDVLHSWAIPSLGIKIDATPGRLNQGTFTINRPGLFFGQCSEICGANHSFM 207
Cdd:cd13913    29 VPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-207 2.52e-05

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


Pssm-ID: 259983 [Multi-domain]  Cd Length: 93  Bit Score: 41.60  E-value: 2.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622  95 ITIKTIGRQWYWSYeysdfvdlefdaymtpeseleedgfrlldvdNRTILPMNTEVRILTSASDVLHSWAI--PSLGI-- 170
Cdd:cd13916     1 QVVAVTGHQWYWEL-------------------------------SRTEIPAGKPVEFRVTSADVNHGFGIydPDMRLla 49

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2252659622 171 KIDATPGRLNQGTFTINRPGLFFGQCSEICGANHSFM 207
Cdd:cd13916    50 QTQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
PRK02888 PRK02888
nitrous-oxide reductase; Validated
 112-207 7.03e-05

nitrous-oxide reductase; Validated


Pssm-ID: 235082 [Multi-domain]  Cd Length: 635  Bit Score: 43.43  E-value: 7.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622 112 DFVDLEFDA-----------YMT---PESELEEdgFRLLDVDNRTILPMNtevriLTSASDVLHSWAIPSLGIKIDATPG 177
Cdd:PRK02888  524 DGVDLEEDSkvirdgnkvrvYMTsqaPAFGLRE--FTVKQGDEVTVIVTN-----LDKVEDLTHGFAIPNYGVNMEVAPQ 596

                          90       100       110
                  ....*....|....*....|....*....|
gi 2252659622 178 RLNQGTFTINRPGLFFGQCSEICGANHSFM 207
Cdd:PRK02888  597 ATASVTFTADKPGVYWYYCTWFCHALHMEM 626
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 132-212 1.53e-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: 39.91  E-value: 1.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252659622 132 GFRLLDVDNRTILPMNTEVR-ILTSASDVLHSWAIPSLGIKIDA---------------TPGRLNQGTFTINRPGLFFGQ 195
Cdd:cd00920    15 NGVLLFGPPVLVVPVGDTVRvQFVNKLGENHSVTIAGFGVPVVAmagganpglvntlviGPGESAEVTFTTDQAGVYWFY 94

                          90
                  ....*....|....*..
gi 2252659622 196 CSEICGaNHSFMPIVIE 212
Cdd:cd00920    95 CTIPGH-NHAGMVGTIN 110
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 147-207 1.72e-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: 259984 [Multi-domain]  Cd Length: 88  Bit Score: 39.28  E-value: 1.72e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2252659622 147 NTEVRILTSASDVLHSWAIPSLGIKIDATPGRLNQGTFTINRPGLFFGQCSEICGANHSFM 207
Cdd:cd13917    21 GKTYRLHLSSLDVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIICNEYCGIGHHTM 81
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 156-207 2.56e-04

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: 38.76  E-value: 2.56e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2252659622 156 ASDVLHSWAIPSLGIKIDATPGRLNQGTFTINRPGLFFGQCSEICGANHSFM 207
Cdd:cd04223    36 DEDITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALHLEM 87
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 140-207 2.82e-04

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


Pssm-ID: 259874 [Multi-domain]  Cd Length: 99  Bit Score: 39.07  E-value: 2.82e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2252659622 140 NRTILPMNTEVRI-LTSASdVLHSWAIPSLGIKIDATPGRLNQGTFTINRPGLFFGQCSEICGANHSFM 207
Cdd:cd04212    25 NELVIPVGRPVNFrLTSDS-VMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDM 92
NosZ COG4263
Nitrous oxide reductase [Inorganic ion transport and metabolism];
158-207 3.07e-03

Nitrous oxide reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443405 [Multi-domain]  Cd Length: 621  Bit Score: 38.35  E-value: 3.07e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2252659622 158 DVLHSWAIPSLGIKIDATPGRLNQGTFTINRPGLFFGQCSEICGANHSFM 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.
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