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Conserved domains on  [gi|74310590|ref|YP_313723|]
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cytochrome c oxidase subunit II (mitochondrion) [Cylindrophis ruffus]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11475905)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-228 9.12e-165

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 453.60  E-value: 9.12e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590    1 MPYATQLSLQEATGPTMEEVVFLHDHVLMLTCLMTLVILLFAMTATMATVTHNDpTEEVEQLEAAWTAAPIMILILTALP 80
Cdd:MTH00117   1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTN-TVDAQEVELIWTILPAIVLILLALP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590   81 SVRSLYLMEEVFDPYVTIKATGHQWYWNYEYTDGVNISFDSYMIQTEDLPNGSPRLLEVDHRMIMPANLQTRIVVTAEDV 160
Cdd:MTH00117  80 SLRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74310590  161 LHSWAVPSLGVKIDAVPGRLNQLPLSTSRTGVFYGQCSEICGANHSFMPIVAEAVPLKYFEHWLSSEN 228
Cdd:MTH00117 160 LHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLLS 227
 
Name Accession Description Interval E-value
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-228 9.12e-165

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 453.60  E-value: 9.12e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590    1 MPYATQLSLQEATGPTMEEVVFLHDHVLMLTCLMTLVILLFAMTATMATVTHNDpTEEVEQLEAAWTAAPIMILILTALP 80
Cdd:MTH00117   1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTN-TVDAQEVELIWTILPAIVLILLALP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590   81 SVRSLYLMEEVFDPYVTIKATGHQWYWNYEYTDGVNISFDSYMIQTEDLPNGSPRLLEVDHRMIMPANLQTRIVVTAEDV 160
Cdd:MTH00117  80 SLRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74310590  161 LHSWAVPSLGVKIDAVPGRLNQLPLSTSRTGVFYGQCSEICGANHSFMPIVAEAVPLKYFEHWLSSEN 228
Cdd:MTH00117 160 LHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLLS 227
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 94-223 1.87e-89

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: 259.42  E-value: 1.87e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590  94 PYVTIKATGHQWYWNYEYTDGVNISFDSYMIQTEDLPNGSPRLLEVDHRMIMPANLQTRIVVTAEDVLHSWAVPSLGVKI 173
Cdd:cd13912   1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 74310590 174 DAVPGRLNQLPLSTSRTGVFYGQCSEICGANHSFMPIVAEAVPLKYFEHW 223
Cdd:cd13912  81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
97-215 2.10e-75

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 223.44  E-value: 2.10e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590    97 TIKATGHQWYWNYEYTDGVNISFDSYMIQTEDLPNGSPRLLEVDHRMIMPANLQTRIVVTAEDVLHSWAVPSLGVKIDAV 176
Cdd:pfam00116   2 TIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDAV 81

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 74310590   177 PGRLNQLPLSTSRTGVFYGQCSEICGANHSFMPIVAEAV 215
Cdd:pfam00116  82 PGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
4-226 3.65e-53

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 170.78  E-value: 3.65e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590   4 ATQLSLQEATGPTMEEVVFLHdhvLMLTCLMTLVILL-FAMT-------------ATMATVTHNDPteeveqLEAAWTAA 69
Cdd:COG1622  16 SGQLSLPDPAGPIAEEIDDLF---WVSLIIMLVIFVLvFGLLlyfairyrrrkgdADPAQFHHNTK------LEIVWTVI 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590  70 PIMILILTALPSVRSLYLMEEVFDPYVTIKATGHQWYWNYEYTDGvNIsfdsymiqtedlpngsprllEVDHRMIMPANL 149
Cdd:COG1622  87 PIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQ-GI--------------------ATVNELVLPVGR 145

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74310590 150 QTRIVVTAEDVLHSWAVPSLGVKIDAVPGRLNQLPLSTSRTGVFYGQCSEICGANHSFMPIVAEAVPLKYFEHWLSS 226
Cdd:COG1622 146 PVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAE 222
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-225 1.63e-40

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: 137.51  E-value: 1.63e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590    12 ATGPTMEEVVFLHDHVLML-TCLMTLVILLFAMTA----TMATVTHNDPTEEVEQLEAAWTAAPIMILILTALPSV-RSL 85
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVsTLISLLVAALLAYVVwkfrRKGDEEKPSQIHGNRRLEYVWTVIPLIIVVGLFAATAkGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590    86 YLMEEVFDPYVTIKATGHQWYWNYEYTDGvnisfdsymiqtedlpngsprLLEVDHRMIMPANLQTRIVVTAEDVLHSWA 165
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFW 139

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590   166 VPSLGVKIDAVPGRLNQLPLSTSRTGVFYGQCSEICGANHSFMPIVAEAVPLKYFEHWLS 225
Cdd:TIGR02866 140 VPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
 
Name Accession Description Interval E-value
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-228 9.12e-165

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 453.60  E-value: 9.12e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590    1 MPYATQLSLQEATGPTMEEVVFLHDHVLMLTCLMTLVILLFAMTATMATVTHNDpTEEVEQLEAAWTAAPIMILILTALP 80
Cdd:MTH00117   1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTN-TVDAQEVELIWTILPAIVLILLALP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590   81 SVRSLYLMEEVFDPYVTIKATGHQWYWNYEYTDGVNISFDSYMIQTEDLPNGSPRLLEVDHRMIMPANLQTRIVVTAEDV 160
Cdd:MTH00117  80 SLRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74310590  161 LHSWAVPSLGVKIDAVPGRLNQLPLSTSRTGVFYGQCSEICGANHSFMPIVAEAVPLKYFEHWLSSEN 228
Cdd:MTH00117 160 LHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLLS 227
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-226 5.11e-113

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 322.55  E-value: 5.11e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590    1 MPYATQLSLQEATGPTMEEVVFLHDHVLMLTcLMTLVILLFAMTATMATVTHNDPTEEVEQLEAAWTAAPIMILILTALP 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMIL-IMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590   81 SVRSLYLMEEVFDPYVTIKATGHQWYWNYEYTDGVNISFDSYMIQTEDLPNGSPRLLEVDHRMIMPANLQTRIVVTAEDV 160
Cdd:MTH00154  80 SLRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74310590  161 LHSWAVPSLGVKIDAVPGRLNQLPLSTSRTGVFYGQCSEICGANHSFMPIVAEAVPLKYFEHWLSS 226
Cdd:MTH00154 160 IHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKN 225
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-228 1.08e-108

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 311.87  E-value: 1.08e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590    1 MPYATQLSLQEATGPTMEEVVFLHDHVLMLTCLMTLVILLFAMTATMATVTHNDPTEEvEQLEAAWTAAPIMILILTALP 80
Cdd:MTH00140   1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEA-QKLETIWTIVPALILVFLALP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590   81 SVRSLYLMEEVFDPYVTIKATGHQWYWNYEYTDGVNISFDSYMIQTEDLPNGSPRLLEVDHRMIMPANLQTRIVVTAEDV 160
Cdd:MTH00140  80 SLRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74310590  161 LHSWAVPSLGVKIDAVPGRLNQLPLSTSRTGVFYGQCSEICGANHSFMPIVAEAVPLKYFEHWLSSEN 228
Cdd:MTH00140 160 IHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELMS 227
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-226 1.99e-107

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 308.57  E-value: 1.99e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590    1 MPYATQLSLQEATGPTMEEVVFLHDHVLMLTCLMTLVILlFAMTATMATVTHNDPTEEVEQLEAAWTAAPIMILILTALP 80
Cdd:MTH00098   1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVL-YIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590   81 SVRSLYLMEEVFDPYVTIKATGHQWYWNYEYTDGVNISFDSYMIQTEDLPNGSPRLLEVDHRMIMPANLQTRIVVTAEDV 160
Cdd:MTH00098  80 SLRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74310590  161 LHSWAVPSLGVKIDAVPGRLNQLPLSTSRTGVFYGQCSEICGANHSFMPIVAEAVPLKYFEHWLSS 226
Cdd:MTH00098 160 LHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSAS 225
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-226 3.33e-105

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 303.17  E-value: 3.33e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590    1 MPYATQLSLQEATGPTMEEVVFLHDHVLMLTCLM-TLVilLFAMTATMATVTHNDPTEEVEQLEAAWTAAPIMILILTAL 79
Cdd:MTH00129   1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLIsTLV--LYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIAL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590   80 PSVRSLYLMEEVFDPYVTIKATGHQWYWNYEYTDGVNISFDSYMIQTEDLPNGSPRLLEVDHRMIMPANLQTRIVVTAED 159
Cdd:MTH00129  79 PSLRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAED 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74310590  160 VLHSWAVPSLGVKIDAVPGRLNQLPLSTSRTGVFYGQCSEICGANHSFMPIVAEAVPLKYFEHWLSS 226
Cdd:MTH00129 159 VLHSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSL 225
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-226 5.35e-105

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 302.41  E-value: 5.35e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590    1 MPYATQLSLQEATGPTMEEVVFLHDHVLMLTcLMTLVILLFAMTATMATVTHNDPTEEVEQLEAAWTAAPIMILILTALP 80
Cdd:MTH00139   1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVIL-IMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590   81 SVRSLYLMEEVFDPYVTIKATGHQWYWNYEYTDGVNISFDSYMIQTEDLPNGSPRLLEVDHRMIMPANLQTRIVVTAEDV 160
Cdd:MTH00139  80 SLRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74310590  161 LHSWAVPSLGVKIDAVPGRLNQLPLSTSRTGVFYGQCSEICGANHSFMPIVAEAVPLKYFEHWLSS 226
Cdd:MTH00139 160 LHSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILE 225
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 6-226 8.52e-105

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 301.90  E-value: 8.52e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590    6 QLSLQEATGPTMEEVVFLHDHVLMLTCLMTLVILlFAMTATMATVTHNDPTEEVEQLEAAWTAAPIMILILTALPSVRSL 85
Cdd:MTH00168   6 QLGLQDAASPVMEELILFHDHALLILVLILTLVL-YSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPSLRLL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590   86 YLMEEVFDPYVTIKATGHQWYWNYEYTDGVNISFDSYMIQTEDLPNGSPRLLEVDHRMIMPANLQTRIVVTAEDVLHSWA 165
Cdd:MTH00168  85 YLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSWT 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74310590  166 VPSLGVKIDAVPGRLNQLPLSTSRTGVFYGQCSEICGANHSFMPIVAEAVPLKYFEHWLSS 226
Cdd:MTH00168 165 LPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVDS 225
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-226 1.33e-104

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 301.62  E-value: 1.33e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590    1 MPYATQLSLQEATGPTMEEVVFLHDHVLMLTCLMTLVILLFAMTATMATVTHNDPTEEvEQLEAAWTAAPIMILILTALP 80
Cdd:MTH00038   1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEG-QELETIWTIVPAFILIFIALP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590   81 SVRSLYLMEEVFDPYVTIKATGHQWYWNYEYTDGVNISFDSYMIQTEDLPNGSPRLLEVDHRMIMPANLQTRIVVTAEDV 160
Cdd:MTH00038  80 SLQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74310590  161 LHSWAVPSLGVKIDAVPGRLNQLPLSTSRTGVFYGQCSEICGANHSFMPIVAEAVPLKYFEHWLSS 226
Cdd:MTH00038 160 LHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSN 225
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-228 3.37e-101

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 292.84  E-value: 3.37e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590    1 MPYATQLSLQEATGPTMEEVVFLHDHVLMLTCLMTLVILlFAMTATMATVTHNDPTEEVEQLEAAWTAAPIMILILTALP 80
Cdd:MTH00076   1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVL-YIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590   81 SVRSLYLMEEVFDPYVTIKATGHQWYWNYEYTDGVNISFDSYMIQTEDLPNGSPRLLEVDHRMIMPANLQTRIVVTAEDV 160
Cdd:MTH00076  80 SLRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74310590  161 LHSWAVPSLGVKIDAVPGRLNQLPLSTSRTGVFYGQCSEICGANHSFMPIVAEAVPLKYFEHWLSSEN 228
Cdd:MTH00076 160 LHSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSML 227
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-226 7.70e-99

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 286.78  E-value: 7.70e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590    1 MPYATQLSLQEATGPTMEEVVFLHDHVLMLTCLMTlVILLFAMTATMATVTHNDPTEEVEQLEAAWTAAPIMILILTALP 80
Cdd:MTH00185   1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLIS-TLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590   81 SVRSLYLMEEVFDPYVTIKATGHQWYWNYEYTDGVNISFDSYMIQTEDLPNGSPRLLEVDHRMIMPANLQTRIVVTAEDV 160
Cdd:MTH00185  80 SLRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74310590  161 LHSWAVPSLGVKIDAVPGRLNQLPLSTSRTGVFYGQCSEICGANHSFMPIVAEAVPLKYFEHWLSS 226
Cdd:MTH00185 160 LHSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSL 225
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-228 5.47e-95

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 277.12  E-value: 5.47e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590    1 MPYATQLSLQEATGPTMEEVVFLHDHVLMLTCLMTLVILlFAMTATMATVTHNDPTEEVEQLEAAWTAAPIMILILTALP 80
Cdd:MTH00008   1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVG-YAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590   81 SVRSLYLMEEVFDPYVTIKATGHQWYWNYEYTDGVNISFDSYMIQTEDLPNGSPRLLEVDHRMIMPANLQTRIVVTAEDV 160
Cdd:MTH00008  80 SLRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74310590  161 LHSWAVPSLGVKIDAVPGRLNQLPLSTSRTGVFYGQCSEICGANHSFMPIVAEAVPLKYFEHWLSSEN 228
Cdd:MTH00008 160 IHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSSFA 227
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 6-226 2.56e-92

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 270.50  E-value: 2.56e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590    6 QLSLQEATGPTMEEVVFLHDHVLMLTCLMTLVILLFAMTATMATVTHNDPTEEVeQLEAAWTAAPIMILILTALPSVRSL 85
Cdd:MTH00051   8 QLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGT-LIEIIWTLIPAAILIFIAFPSLKLL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590   86 YLMEEVFDPYVTIKATGHQWYWNYEYTD--GVNISFDSYMIQTEDLPNGSPRLLEVDHRMIMPANLQTRIVVTAEDVLHS 163
Cdd:MTH00051  87 YLMDEVIDPALTIKAIGHQWYWSYEYSDygTDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHS 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74310590  164 WAVPSLGVKIDAVPGRLNQLPLSTSRTGVFYGQCSEICGANHSFMPIVAEAVPLKYFEHWLSS 226
Cdd:MTH00051 167 FAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVAT 229
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 2-226 4.58e-92

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 270.08  E-value: 4.58e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590    2 PYATQLSLQEATGPTMEEVVFLHDHVLMLTCLMTLVILLFAMTATMATVTHNDPTEEVeQLEAAWTAAPIMILILTALPS 81
Cdd:MTH00023  11 PEPWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGT-FLEIVWTIIPAVILVFIALPS 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590   82 VRSLYLMEEVFDPYVTIKATGHQWYWNYEYTD--GVNISFDSYMIQTEDLPNGSPRLLEVDHRMIMPANLQTRIVVTAED 159
Cdd:MTH00023  90 LKLLYLMDEVVSPALTIKAIGHQWYWSYEYSDyeGETLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGAD 169

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74310590  160 VLHSWAVPSLGVKIDAVPGRLNQLPLSTSRTGVFYGQCSEICGANHSFMPIVAEAVPLKYFEHWLSS 226
Cdd:MTH00023 170 VLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLS 236
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 94-223 1.87e-89

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: 259.42  E-value: 1.87e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590  94 PYVTIKATGHQWYWNYEYTDGVNISFDSYMIQTEDLPNGSPRLLEVDHRMIMPANLQTRIVVTAEDVLHSWAVPSLGVKI 173
Cdd:cd13912   1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 74310590 174 DAVPGRLNQLPLSTSRTGVFYGQCSEICGANHSFMPIVAEAVPLKYFEHW 223
Cdd:cd13912  81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
97-215 2.10e-75

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 223.44  E-value: 2.10e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590    97 TIKATGHQWYWNYEYTDGVNISFDSYMIQTEDLPNGSPRLLEVDHRMIMPANLQTRIVVTAEDVLHSWAVPSLGVKIDAV 176
Cdd:pfam00116   2 TIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDAV 81

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 74310590   177 PGRLNQLPLSTSRTGVFYGQCSEICGANHSFMPIVAEAV 215
Cdd:pfam00116  82 PGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 6-228 1.05e-73

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 224.52  E-value: 1.05e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590    6 QLSLQEATGPTMEEVVFLHDHVLMLTCLMTLVILLFAMTATMATVTHNDPTEEVEQ--LEAAWTAAPIMILILTALPSVR 83
Cdd:MTH00027  34 QLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLGNNYYSYYWNKLDGslIEVIWTLIPAFILILIAFPSLR 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590   84 SLYLMEE-VFDPYVTIKATGHQWYWNYEYTD--GVNISFDSYMIQTEDLPNGSPRLLEVDHRMIMPANLQTRIVVTAEDV 160
Cdd:MTH00027 114 LLYIMDEcGFSANITIKVTGHQWYWSYSYEDygEKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADV 193

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74310590  161 LHSWAVPSLGVKIDAVPGRLNQLPLSTSRTGVFYGQCSEICGANHSFMPIVAEAVPLKYFEHWLSSEN 228
Cdd:MTH00027 194 LHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWIGRED 261
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 25-224 6.79e-67

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 206.01  E-value: 6.79e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590   25 DHVLMLTCLMTLVILLFAMTaTMATVTHNDPTEEVEQLEAAWTAAPIMILILTALPSVRSLYLMEEV-FDPYVTIKATGH 103
Cdd:MTH00080  27 CSLLFGEFVLAFVVFLFLYL-ISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMnLDSNLTVKVTGH 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590  104 QWYWNYEYTDGVNISFDSYMIQTEDLPNGSPRLLEVDHRMIMPANLQTRIVVTAEDVLHSWAVPSLGVKIDAVPGRLNQL 183
Cdd:MTH00080 106 QWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILSTL 185

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 74310590  184 PLSTSRTGVFYGQCSEICGANHSFMPIVAEAVPLKYFEHWL 224
Cdd:MTH00080 186 CYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWC 226
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
4-226 3.65e-53

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 170.78  E-value: 3.65e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590   4 ATQLSLQEATGPTMEEVVFLHdhvLMLTCLMTLVILL-FAMT-------------ATMATVTHNDPteeveqLEAAWTAA 69
Cdd:COG1622  16 SGQLSLPDPAGPIAEEIDDLF---WVSLIIMLVIFVLvFGLLlyfairyrrrkgdADPAQFHHNTK------LEIVWTVI 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590  70 PIMILILTALPSVRSLYLMEEVFDPYVTIKATGHQWYWNYEYTDGvNIsfdsymiqtedlpngsprllEVDHRMIMPANL 149
Cdd:COG1622  87 PIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQ-GI--------------------ATVNELVLPVGR 145

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74310590 150 QTRIVVTAEDVLHSWAVPSLGVKIDAVPGRLNQLPLSTSRTGVFYGQCSEICGANHSFMPIVAEAVPLKYFEHWLSS 226
Cdd:COG1622 146 PVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAE 222
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 32-215 3.44e-45

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 149.33  E-value: 3.44e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590   32 CLMTLVILLFAMTATMATVTHNdptEEVEQLEAAWTAAP-IMILILTALPSVRSLYLMEEVFDpyVTIKATGHQWYWNYE 110
Cdd:MTH00047  22 PCWVYIMLCWQVVSGNGSVNFG---SENQVLELLWTVVPtLLVLVLCFLNLNFITSDLDCFSS--ETIKVIGHQWYWSYE 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590  111 YTDGvnISFDSYMIqteDLPNGsprlleVDHRMIMPANLQTRIVVTAEDVLHSWAVPSLGVKIDAVPGRLNQLPLSTSRT 190
Cdd:MTH00047  97 YSFG--GSYDSFMT---DDIFG------VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRH 165

                        170       180
                 ....*....|....*....|....*
gi 74310590  191 GVFYGQCSEICGANHSFMPIVAEAV 215
Cdd:MTH00047 166 GVFVGYCSELCGVGHSYMPIVIEVV 190
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 118-222 1.41e-41

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 138.80  E-value: 1.41e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590  118 SFDSYMIQTEDLPNGSPRLLEVDHRMIMPANLQTRIVVTAEDVLHSWAVPSLGVKIDAVPGRLNQLPLSTSRTGVFYGQC 197
Cdd:PTZ00047  50 SFQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQC 129

                         90       100
                 ....*....|....*....|....*.
gi 74310590  198 SEICGANHSFMPIVAEAV-PLKYFEH 222
Cdd:PTZ00047 130 SEMCGTLHGFMPIVVEAVsPEAYAAH 155
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-225 1.63e-40

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: 137.51  E-value: 1.63e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590    12 ATGPTMEEVVFLHDHVLML-TCLMTLVILLFAMTA----TMATVTHNDPTEEVEQLEAAWTAAPIMILILTALPSV-RSL 85
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVsTLISLLVAALLAYVVwkfrRKGDEEKPSQIHGNRRLEYVWTVIPLIIVVGLFAATAkGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590    86 YLMEEVFDPYVTIKATGHQWYWNYEYTDGvnisfdsymiqtedlpngsprLLEVDHRMIMPANLQTRIVVTAEDVLHSWA 165
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFW 139

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590   166 VPSLGVKIDAVPGRLNQLPLSTSRTGVFYGQCSEICGANHSFMPIVAEAVPLKYFEHWLS 225
Cdd:TIGR02866 140 VPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 96-208 1.05e-28

The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of most bacteria, is a multi-chain transmembrane protein located in the inner membrane the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. Caa3 type of CcO Subunit II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the cytochromes a, a3 and CuB active site in subunit I.


Pssm-ID: 259875 [Multi-domain]  Cd Length: 103  Bit Score: 103.85  E-value: 1.05e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590  96 VTIKATGHQWYWNYEYtdgvnisfdsymiqtedlPNGSPRLLEVDHRMIMPANLQTRIVVTAEDVLHSWAVPSLGVKIDA 175
Cdd:cd04213   2 LTIEVTGHQWWWEFRY------------------PDEPGRGIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDM 63

                        90       100       110
                ....*....|....*....|....*....|...
gi 74310590 176 VPGRLNQLPLSTSRTGVFYGQCSEICGANHSFM 208
Cdd:cd04213  64 IPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 96-213 8.77e-25

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: 93.51  E-value: 8.77e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590  96 VTIKATGHQWYWNYEYTDgvnisfdsymiqtedlpngsprlLEVDHRMIMPANLQTRIVVTAEDVLHSWAVPSLGVKIDA 175
Cdd:cd13842   1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 74310590 176 VPGRLNQLPLSTSRTGVFYGQCSEICGANHSFMPIVAE 213
Cdd:cd13842  58 VPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 96-224 6.39e-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: 84.00  E-value: 6.39e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590  96 VTIKATGHQWYWNYEYTDGvnisfdsyMIQTEDlpngsprllevdhRMIMPANLQTRIVVTAEDVLHSWAVPSLGVKIDA 175
Cdd:cd13914   1 VEIEVEAYQWGWEFSYPEA--------NVTTSE-------------QLVIPADRPVYFRITSRDVIHAFHVPELGLKQDA 59

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 74310590 176 VPGRLNQLPLSTSRTGVFYGQCSEICGANHSFMPIVAEAVPLKYFEHWL 224
Cdd:cd13914  60 FPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 96-208 3.00e-20

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


Pssm-ID: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 82.30  E-value: 3.00e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590  96 VTIKATGHQWYWNYEYTDGVNISfdsymiqTEDLPNGSPRLlevdHrmiMPANLQTRIVVTAEDVLHSWAVPSLGVKIDA 175
Cdd:cd13919   2 LVVEVTAQQWAWTFRYPGGDGKL-------GTDDDVTSPEL----H---LPVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                        90       100       110
                ....*....|....*....|....*....|...
gi 74310590 176 VPGRLNQLPLSTSRTGVFYGQCSEICGANHSFM 208
Cdd:cd13919  68 VPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 96-224 2.23e-19

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: 80.96  E-value: 2.23e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590  96 VTIKATGHQWYWNYEYTDGVnisfdsymiqtedlpngsprllEVDHRMIMPANLQTRIVVTAEDVLHSWAVPSLGVKIDA 175
Cdd:cd13918  33 LEVEVEGFQFGWQFEYPNGV----------------------TTGNTLRVPADTPIALRVTSTDVFHTFGIPELRVKADA 90

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 74310590 176 VPGRLNQLPLSTSRTGVFYGQCSEICGANHSFMPIVAEAVPLKYFEHWL 224
Cdd:cd13918  91 IPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAWY 139
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 97-208 5.25e-19

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: 78.44  E-value: 5.25e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590  97 TIKATGHQWYWNYEYtdgvnisfdsymiqtedlPNGsprlLEVDHRMIMPANLQTRIVVTAEDVLHSWAVPSLGVKIDAV 176
Cdd:cd13915   3 EIQVTGRQWMWEFTY------------------PNG----KREINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDVV 60

                        90       100       110
                ....*....|....*....|....*....|..
gi 74310590 177 PGRLNQLPLSTSRTGVFYGQCSEICGANHSFM 208
Cdd:cd13915  61 PGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-83 5.73e-10

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: 54.26  E-value: 5.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590     1 MPYATQLSLQEATGPTMEEVVFLHDHVLMLTCLMT------LVILLFAMTATMATVTHNDPTEEVEqLEAAWTAAPIMIL 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILilvlyiLVTCLIRFNRRKNPITARYTTHGQT-IEIIWTIIPAVIL 79


                  ....*....
gi 74310590    75 ILTALPSVR 83
Cdd:pfam02790  80 ILIALPSFK 88
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 146-208 6.08e-06

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: 43.71  E-value: 6.08e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74310590 146 PANLQTRIVVTAEDVLHSWAVPSLGVKIDAVPGRLNQLPLSTSRTGVFYGQCSEICGANHSFM 208
Cdd:cd13913  30 PAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 96-208 1.76e-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: 39.29  E-value: 1.76e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590  96 VTIKATGHQWYWNyeytdgvnisfdsymIQTEDLPNGSPrlleVDHRmimpanlqtrivVTAEDVLHSWAVPS----LGV 171
Cdd:cd13916   1 QVVAVTGHQWYWE---------------LSRTEIPAGKP----VEFR------------VTSADVNHGFGIYDpdmrLLA 49

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 74310590 172 KIDAVPGRLNQLPLSTSRTGVFYGQCSEICGANHSFM 208
Cdd:cd13916  50 QTQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 146-215 6.96e-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: 37.91  E-value: 6.96e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590 146 PANLQTRIVVTAEDVLHSWAVPSLGVKIDAVPGRLNQLPLSTSRTGVFYGQCSEICGANHSFMPIVAEAV 215
Cdd:cd04212  30 PVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDMKFKVLAV 99
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 152-208 1.24e-03

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


Pssm-ID: 259984 [Multi-domain]  Cd Length: 88  Bit Score: 36.97  E-value: 1.24e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 74310590 152 RIVVTAEDVLHSWAVPSLGVKIDAVPGRLNQLPLSTSRTGVFYGQCSEICGANHSFM 208
Cdd:cd13917  25 RLHLSSLDVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIICNEYCGIGHHTM 81
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 98-211 1.45e-03

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


Pssm-ID: 259860 [Multi-domain]  Cd Length: 110  Bit Score: 37.21  E-value: 1.45e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590  98 IKATGHQWYWNYEYTDGVNISFDSYMIQTEDLpngsprlleVDHRMIMPANLQTRIVVTAEDVLHSW----AVPSLGVKI 173
Cdd:cd00920   1 ITVTASDWGWSFTYNGVLLFGPPVLVVPVGDT---------VRVQFVNKLGENHSVTIAGFGVPVVAmaggANPGLVNTL 71

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 74310590 174 DAVPGRLNQLPLSTSRTGVFYGQCSEICGaNHSFMPIV 211
Cdd:cd00920  72 VIGPGESAEVTFTTDQAGVYWFYCTIPGH-NHAGMVGT 108
PRK10525 PRK10525
cytochrome o ubiquinol oxidase subunit II; Provisional
 28-224 6.43e-03

cytochrome o ubiquinol oxidase subunit II; Provisional


Pssm-ID: 182518 [Multi-domain]  Cd Length: 315  Bit Score: 37.09  E-value: 6.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590   28 LMLTCLMTLVILLFAM------TATMATVT----HNDPTEEVeqleaAWTAAPIMILILTAL--PSVRSLylmeevfDPY 95
Cdd:PRK10525  50 LMLIVVIPAILMAVGFawkyraSNKDAKYSpnwsHSNKVEAV-----VWTVPILIIIFLAVLtwKTTHAL-------EPS 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74310590   96 ---------VTIKATGHQWYWNYEYTD----GVN-ISFdsymiqtedlpngsprllevdhrmimPANLQTRIVVTAEDVL 161
Cdd:PRK10525 118 kplahdekpITIEVVSMDWKWFFIYPEqgiaTVNeIAF--------------------------PANVPVYFKVTSNSVM 171

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74310590  162 HSWAVPSLGVKIDAVPGRLNQLPLSTSRTGVFYGQCSEICGANHSFMPIVAEAVPLKY-FEHWL 224
Cdd:PRK10525 172 NSFFIPRLGSQIYAMAGMQTRLHLIANEPGTYDGISASYSGPGFSGMKFKAIATPDRAeFDQWV 235
 
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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