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Conserved domains on  [gi|511768950|ref|YP_008083602|]
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cytochrome c oxidase subunit II (mitochondrion) [Python bivittatus]

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 2.72e-160

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 442.05  E-value: 2.72e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950   1 MPYATQLSLQEATGPAMEEVVFLHDHVLLLTFLMSLVILLFATTAITATVTHNDpTEEVEQLEAAWTAAPIMILILTALP 80
Cdd:MTH00117   1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTN-TVDAQEVELIWTILPAIVLILLALP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950  81 SVRSLYLMEEVFDPYVTIKATGHQWYWNYEYTDGTNVSFDSYMIQTQDLPNSAPRLLEVDHRMVMPANLQTRIVVTAEDV 160
Cdd:MTH00117  80 SLRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 511768950 161 LHSWAIPSLGIKVDAVPGRLNQLPLATSRTGVFFGQCSEICGANHSFMPIVVEAVPLNYFEQWLTTEQ 228
Cdd:MTH00117 160 LHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLLS 227
 
Name Accession Description Interval E-value
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-228 2.72e-160

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 442.05  E-value: 2.72e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950   1 MPYATQLSLQEATGPAMEEVVFLHDHVLLLTFLMSLVILLFATTAITATVTHNDpTEEVEQLEAAWTAAPIMILILTALP 80
Cdd:MTH00117   1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTN-TVDAQEVELIWTILPAIVLILLALP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950  81 SVRSLYLMEEVFDPYVTIKATGHQWYWNYEYTDGTNVSFDSYMIQTQDLPNSAPRLLEVDHRMVMPANLQTRIVVTAEDV 160
Cdd:MTH00117  80 SLRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 511768950 161 LHSWAIPSLGIKVDAVPGRLNQLPLATSRTGVFFGQCSEICGANHSFMPIVVEAVPLNYFEQWLTTEQ 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 1.23e-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: 257.11  E-value: 1.23e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950  94 PYVTIKATGHQWYWNYEYTDGTNVSFDSYMIQTQDLPNSAPRLLEVDHRMVMPANLQTRIVVTAEDVLHSWAIPSLGIKV 173
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 511768950 174 DAVPGRLNQLPLATSRTGVFFGQCSEICGANHSFMPIVVEAVPLNYFEQW 223
Cdd:cd13912   81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
97-215 6.67e-74

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 219.59  E-value: 6.67e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950   97 TIKATGHQWYWNYEYTDGTNVSFDSYMIQTQDLPNSAPRLLEVDHRMVMPANLQTRIVVTAEDVLHSWAIPSLGIKVDAV 176
Cdd:pfam00116   2 TIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDAV 81

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 511768950  177 PGRLNQLPLATSRTGVFFGQCSEICGANHSFMPIVVEAV 215
Cdd:pfam00116  82 PGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
4-228 1.21e-51

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 166.93  E-value: 1.21e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950   4 ATQLSLQEATGPAMEEVVFLHDHVLLLTFLMSLVILLF-----------ATTAITATVTHNDPteeveqLEAAWTAAPIM 72
Cdd:COG1622   16 SGQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLllyfairyrrrKGDADPAQFHHNTK------LEIVWTVIPII 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950  73 ILILTALPSVRSLYLMEEVFDPYVTIKATGHQWYWNYEYTDGTNVsfdsymiqtqdlpnsaprlleVDHRMVMPANLQTR 152
Cdd:COG1622   90 IVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVNELVLPVGRPVR 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 511768950 153 IVVTAEDVLHSWAIPSLGIKVDAVPGRLNQLPLATSRTGVFFGQCSEICGANHSFMPIVVEAVPLNYFEQWLTTEQ 228
Cdd:COG1622  149 FLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQK 224
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-224 4.51e-41

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: 138.67  E-value: 4.51e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950   12 ATGPAMEEVVFLHDHVLLLTFLMSLVILLFATTAITATVTHNDPTEEVE-----QLEAAWTAAPIMILI-LTALPSVRSL 85
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVWKFRRKGDEEKPSQihgnrRLEYVWTVIPLIIVVgLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950   86 YLMEEVFDPYVTIKATGHQWYWNYEYTDGTnvsfdsymiqtqdlpnsaprlLEVDHRMVMPANLQTRIVVTAEDVLHSWA 165
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPESG---------------------FTTVNELVLPAGTPVELQVTSKDVIHSFW 139

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 511768950  166 IPSLGIKVDAVPGRLNQLPLATSRTGVFFGQCSEICGANHSFMPIVVEAVPLNYFEQWL 224
Cdd:TIGR02866 140 VPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYV 198
 
Name Accession Description Interval E-value
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-228 2.72e-160

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 442.05  E-value: 2.72e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950   1 MPYATQLSLQEATGPAMEEVVFLHDHVLLLTFLMSLVILLFATTAITATVTHNDpTEEVEQLEAAWTAAPIMILILTALP 80
Cdd:MTH00117   1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTN-TVDAQEVELIWTILPAIVLILLALP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950  81 SVRSLYLMEEVFDPYVTIKATGHQWYWNYEYTDGTNVSFDSYMIQTQDLPNSAPRLLEVDHRMVMPANLQTRIVVTAEDV 160
Cdd:MTH00117  80 SLRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 511768950 161 LHSWAIPSLGIKVDAVPGRLNQLPLATSRTGVFFGQCSEICGANHSFMPIVVEAVPLNYFEQWLTTEQ 228
Cdd:MTH00117 160 LHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLLS 227
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-224 1.98e-110

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 316.00  E-value: 1.98e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950   1 MPYATQLSLQEATGPAMEEVVFLHDHVLLLtFLMSLVILLFATTAITATVTHNDPTEEVEQLEAAWTAAPIMILILTALP 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMI-LIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950  81 SVRSLYLMEEVFDPYVTIKATGHQWYWNYEYTDGTNVSFDSYMIQTQDLPNSAPRLLEVDHRMVMPANLQTRIVVTAEDV 160
Cdd:MTH00154  80 SLRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 511768950 161 LHSWAIPSLGIKVDAVPGRLNQLPLATSRTGVFFGQCSEICGANHSFMPIVVEAVPLNYFEQWL 224
Cdd:MTH00154 160 IHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWI 223
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-226 7.54e-106

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 304.72  E-value: 7.54e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950   1 MPYATQLSLQEATGPAMEEVVFLHDHVLLLTFLMSLVILLFATTAITATVTHNDpTEEVEQLEAAWTAAPIMILILTALP 80
Cdd:MTH00098   1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTS-TMDAQEVETIWTILPAIILILIALP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950  81 SVRSLYLMEEVFDPYVTIKATGHQWYWNYEYTDGTNVSFDSYMIQTQDLPNSAPRLLEVDHRMVMPANLQTRIVVTAEDV 160
Cdd:MTH00098  80 SLRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 511768950 161 LHSWAIPSLGIKVDAVPGRLNQLPLATSRTGVFFGQCSEICGANHSFMPIVVEAVPLNYFEQWLTT 226
Cdd:MTH00098 160 LHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSAS 225
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-224 6.27e-105

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 302.24  E-value: 6.27e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950   1 MPYATQLSLQEATGPAMEEVVFLHDHVL-LLTFLMSLVILLFATTAITATVTHNdpTEEVEQLEAAWTAAPIMILILTAL 79
Cdd:MTH00140   1 MSYWGQLGFQDPASPLMEELIFFHDHAMvVLVLIFSFVMYMLVLLLFNKFSCRT--ILEAQKLETIWTIVPALILVFLAL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950  80 PSVRSLYLMEEVFDPYVTIKATGHQWYWNYEYTDGTNVSFDSYMIQTQDLPNSAPRLLEVDHRMVMPANLQTRIVVTAED 159
Cdd:MTH00140  79 PSLRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSAD 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 511768950 160 VLHSWAIPSLGIKVDAVPGRLNQLPLATSRTGVFFGQCSEICGANHSFMPIVVEAVPLNYFEQWL 224
Cdd:MTH00140 159 VIHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWL 223
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-226 6.90e-104

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 299.71  E-value: 6.90e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950   1 MPYATQLSLQEATGPAMEEVVFLHDHVLLLTFLMSlVILLFATTAITATVTHNDPTEEVEQLEAAWTAAPIMILILTALP 80
Cdd:MTH00129   1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLIS-TLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950  81 SVRSLYLMEEVFDPYVTIKATGHQWYWNYEYTDGTNVSFDSYMIQTQDLPNSAPRLLEVDHRMVMPANLQTRIVVTAEDV 160
Cdd:MTH00129  80 SLRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 511768950 161 LHSWAIPSLGIKVDAVPGRLNQLPLATSRTGVFFGQCSEICGANHSFMPIVVEAVPLNYFEQWLTT 226
Cdd:MTH00129 160 LHSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSL 225
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 6-226 1.64e-103

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 298.43  E-value: 1.64e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950   6 QLSLQEATGPAMEEVVFLHDHVLLLTFLMSLVILLFATTAITATVThNDPTEEVEQLEAAWTAAPIMILILTALPSVRSL 85
Cdd:MTH00168   6 QLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYT-NRFLLDSQMIEFVWTIIPAFILISLALPSLRLL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950  86 YLMEEVFDPYVTIKATGHQWYWNYEYTDGTNVSFDSYMIQTQDLPNSAPRLLEVDHRMVMPANLQTRIVVTAEDVLHSWA 165
Cdd:MTH00168  85 YLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSWT 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 511768950 166 IPSLGIKVDAVPGRLNQLPLATSRTGVFFGQCSEICGANHSFMPIVVEAVPLNYFEQWLTT 226
Cdd:MTH00168 165 LPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVDS 225
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-225 1.68e-100

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 290.85  E-value: 1.68e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950   1 MPYATQLSLQEATGPAMEEVVFLHDHVLLLtFLMSLVILLFATTAITATVTHNDPTEEVEQLEAAWTAAPIMILILTALP 80
Cdd:MTH00139   1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVI-LIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950  81 SVRSLYLMEEVFDPYVTIKATGHQWYWNYEYTDGTNVSFDSYMIQTQDLPNSAPRLLEVDHRMVMPANLQTRIVVTAEDV 160
Cdd:MTH00139  80 SLRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 511768950 161 LHSWAIPSLGIKVDAVPGRLNQLPLATSRTGVFFGQCSEICGANHSFMPIVVEAVPLNYFEQWLT 225
Cdd:MTH00139 160 LHSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWIL 224
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-226 4.13e-100

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 290.06  E-value: 4.13e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950   1 MPYATQLSLQEATGPAMEEVVFLHDHVLL-LTFLMSLVI-----LLFattaitatvthNDPTE----EVEQLEAAWTAAP 70
Cdd:MTH00038   1 MATWLQLGLQDASSPLMEELIYFHDYALIiLTLITILVFyglasLLF-----------SSPTNrfflEGQELETIWTIVP 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950  71 IMILILTALPSVRSLYLMEEVFDPYVTIKATGHQWYWNYEYTDGTNVSFDSYMIQTQDLPNSAPRLLEVDHRMVMPANLQ 150
Cdd:MTH00038  70 AFILIFIALPSLQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTP 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 511768950 151 TRIVVTAEDVLHSWAIPSLGIKVDAVPGRLNQLPLATSRTGVFFGQCSEICGANHSFMPIVVEAVPLNYFEQWLTT 226
Cdd:MTH00038 150 IRVLVSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSN 225
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-228 2.48e-99

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 288.22  E-value: 2.48e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950   1 MPYATQLSLQEATGPAMEEVVFLHDHVLLLTFLMSLVILlFATTAITATVTHNDPTEEVEQLEAAWTAAPIMILILTALP 80
Cdd:MTH00076   1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVL-YIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950  81 SVRSLYLMEEVFDPYVTIKATGHQWYWNYEYTDGTNVSFDSYMIQTQDLPNSAPRLLEVDHRMVMPANLQTRIVVTAEDV 160
Cdd:MTH00076  80 SLRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 511768950 161 LHSWAIPSLGIKVDAVPGRLNQLPLATSRTGVFFGQCSEICGANHSFMPIVVEAVPLNYFEQWLTTEQ 228
Cdd:MTH00076 160 LHSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSML 227
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-225 1.17e-97

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 284.09  E-value: 1.17e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950   1 MPYATQLSLQEATGPAMEEVVFLHDHVLLLTFLMSlVILLFATTAITATVTHNDPTEEVEQLEAAWTAAPIMILILTALP 80
Cdd:MTH00185   1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLIS-TLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950  81 SVRSLYLMEEVFDPYVTIKATGHQWYWNYEYTDGTNVSFDSYMIQTQDLPNSAPRLLEVDHRMVMPANLQTRIVVTAEDV 160
Cdd:MTH00185  80 SLRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 511768950 161 LHSWAIPSLGIKVDAVPGRLNQLPLATSRTGVFFGQCSEICGANHSFMPIVVEAVPLNYFEQWLT 225
Cdd:MTH00185 160 LHSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSS 224
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-226 5.78e-90

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 264.41  E-value: 5.78e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950   1 MPYATQLSLQEATGPAMEEVVFLHDHVLLLTFLMsLVILLFATTAITATVTHNDPTEEVEQLEAAWTAAPIMILILTALP 80
Cdd:MTH00008   1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLV-LTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950  81 SVRSLYLMEEVFDPYVTIKATGHQWYWNYEYTDGTNVSFDSYMIQTQDLPNSAPRLLEVDHRMVMPANLQTRIVVTAEDV 160
Cdd:MTH00008  80 SLRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 511768950 161 LHSWAIPSLGIKVDAVPGRLNQLPLATSRTGVFFGQCSEICGANHSFMPIVVEAVPLNYFEQWLTT 226
Cdd:MTH00008 160 IHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSS 225
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 94-223 1.23e-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: 257.11  E-value: 1.23e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950  94 PYVTIKATGHQWYWNYEYTDGTNVSFDSYMIQTQDLPNSAPRLLEVDHRMVMPANLQTRIVVTAEDVLHSWAIPSLGIKV 173
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 511768950 174 DAVPGRLNQLPLATSRTGVFFGQCSEICGANHSFMPIVVEAVPLNYFEQW 223
Cdd:cd13912   81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 2-224 1.42e-88

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 261.22  E-value: 1.42e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950   2 PYATQLSLQEATGPAMEEVVFLHDHVLLLTFLMSLVILLFATTAITATVTHNDPTEEVeQLEAAWTAAPIMILILTALPS 81
Cdd:MTH00023  11 PEPWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGT-FLEIVWTIIPAVILVFIALPS 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950  82 VRSLYLMEEVFDPYVTIKATGHQWYWNYEYTD--GTNVSFDSYMIQTQDLPNSAPRLLEVDHRMVMPANLQTRIVVTAED 159
Cdd:MTH00023  90 LKLLYLMDEVVSPALTIKAIGHQWYWSYEYSDyeGETLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGAD 169

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 511768950 160 VLHSWAIPSLGIKVDAVPGRLNQLPLATSRTGVFFGQCSEICGANHSFMPIVVEAVPLNYFEQWL 224
Cdd:MTH00023 170 VLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWL 234
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 6-226 3.00e-87

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 257.79  E-value: 3.00e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950   6 QLSLQEATGPAMEEVVFLHDHVLLLTFLMSLVILLFATTAITATVTHNDPTEEVeQLEAAWTAAPIMILILTALPSVRSL 85
Cdd:MTH00051   8 QLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGT-LIEIIWTLIPAAILIFIAFPSLKLL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950  86 YLMEEVFDPYVTIKATGHQWYWNYEYTD--GTNVSFDSYMIQTQDLPNSAPRLLEVDHRMVMPANLQTRIVVTAEDVLHS 163
Cdd:MTH00051  87 YLMDEVIDPALTIKAIGHQWYWSYEYSDygTDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHS 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 511768950 164 WAIPSLGIKVDAVPGRLNQLPLATSRTGVFFGQCSEICGANHSFMPIVVEAVPLNYFEQWLTT 226
Cdd:MTH00051 167 FAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVAT 229
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
97-215 6.67e-74

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 219.59  E-value: 6.67e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950   97 TIKATGHQWYWNYEYTDGTNVSFDSYMIQTQDLPNSAPRLLEVDHRMVMPANLQTRIVVTAEDVLHSWAIPSLGIKVDAV 176
Cdd:pfam00116   2 TIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDAV 81

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 511768950  177 PGRLNQLPLATSRTGVFFGQCSEICGANHSFMPIVVEAV 215
Cdd:pfam00116  82 PGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 6-227 2.19e-70

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 216.04  E-value: 2.19e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950   6 QLSLQEATGPAMEEVVFLHDHVLLLTFLMSLVILLFATTAITATVTHNDPTEEVEQ--LEAAWTAAPIMILILTALPSVR 83
Cdd:MTH00027  34 QLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLGNNYYSYYWNKLDGslIEVIWTLIPAFILILIAFPSLR 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950  84 SLYLMEE-VFDPYVTIKATGHQWYWNYEYTD--GTNVSFDSYMIQTQDLPNSAPRLLEVDHRMVMPANLQTRIVVTAEDV 160
Cdd:MTH00027 114 LLYIMDEcGFSANITIKVTGHQWYWSYSYEDygEKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADV 193

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 511768950 161 LHSWAIPSLGIKVDAVPGRLNQLPLATSRTGVFFGQCSEICGANHSFMPIVVEAVPLNYFEQWLTTE 227
Cdd:MTH00027 194 LHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWIGRE 260
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 25-224 5.92e-66

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 203.32  E-value: 5.92e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950  25 DHVLLLTFLMSLVILLFATTAITATVTHNDPTEEvEQLEAAWTAAPIMILILTALPSVRSLYLMEEV-FDPYVTIKATGH 103
Cdd:MTH00080  27 CSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEY-QFGELLCSVFPVLILLMQMVPSLSLLYYYGLMnLDSNLTVKVTGH 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950 104 QWYWNYEYTDGTNVSFDSYMIQTQDLPNSAPRLLEVDHRMVMPANLQTRIVVTAEDVLHSWAIPSLGIKVDAVPGRLNQL 183
Cdd:MTH00080 106 QWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILSTL 185

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 511768950 184 PLATSRTGVFFGQCSEICGANHSFMPIVVEAVPLNYFEQWL 224
Cdd:MTH00080 186 CYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWC 226
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
4-228 1.21e-51

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 166.93  E-value: 1.21e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950   4 ATQLSLQEATGPAMEEVVFLHDHVLLLTFLMSLVILLF-----------ATTAITATVTHNDPteeveqLEAAWTAAPIM 72
Cdd:COG1622   16 SGQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLllyfairyrrrKGDADPAQFHHNTK------LEIVWTVIPII 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950  73 ILILTALPSVRSLYLMEEVFDPYVTIKATGHQWYWNYEYTDGTNVsfdsymiqtqdlpnsaprlleVDHRMVMPANLQTR 152
Cdd:COG1622   90 IVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVNELVLPVGRPVR 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 511768950 153 IVVTAEDVLHSWAIPSLGIKVDAVPGRLNQLPLATSRTGVFFGQCSEICGANHSFMPIVVEAVPLNYFEQWLTTEQ 228
Cdd:COG1622  149 FLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQK 224
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 62-215 7.80e-46

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 150.88  E-value: 7.80e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950  62 LEAAWTAAP-IMILILTALPSVRSLYLMEEVFDpyVTIKATGHQWYWNYEYTDGTnvSFDSYMIQTQDLpnsaprlleVD 140
Cdd:MTH00047  49 LELLWTVVPtLLVLVLCFLNLNFITSDLDCFSS--ETIKVIGHQWYWSYEYSFGG--SYDSFMTDDIFG---------VD 115

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 511768950 141 HRMVMPANLQTRIVVTAEDVLHSWAIPSLGIKVDAVPGRLNQLPLATSRTGVFFGQCSEICGANHSFMPIVVEAV 215
Cdd:MTH00047 116 KPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVV 190
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-224 4.51e-41

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: 138.67  E-value: 4.51e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950   12 ATGPAMEEVVFLHDHVLLLTFLMSLVILLFATTAITATVTHNDPTEEVE-----QLEAAWTAAPIMILI-LTALPSVRSL 85
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVWKFRRKGDEEKPSQihgnrRLEYVWTVIPLIIVVgLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950   86 YLMEEVFDPYVTIKATGHQWYWNYEYTDGTnvsfdsymiqtqdlpnsaprlLEVDHRMVMPANLQTRIVVTAEDVLHSWA 165
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPESG---------------------FTTVNELVLPAGTPVELQVTSKDVIHSFW 139

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 511768950  166 IPSLGIKVDAVPGRLNQLPLATSRTGVFFGQCSEICGANHSFMPIVVEAVPLNYFEQWL 224
Cdd:TIGR02866 140 VPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYV 198
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 118-215 4.18e-39

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 132.64  E-value: 4.18e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950 118 SFDSYMIQTQDLPNSAPRLLEVDHRMVMPANLQTRIVVTAEDVLHSWAIPSLGIKVDAVPGRLNQLPLATSRTGVFFGQC 197
Cdd:PTZ00047  50 SFQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQC 129

                         90
                 ....*....|....*...
gi 511768950 198 SEICGANHSFMPIVVEAV 215
Cdd:PTZ00047 130 SEMCGTLHGFMPIVVEAV 147
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 96-215 1.38e-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: 103.47  E-value: 1.38e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950  96 VTIKATGHQWYWNYEYtdgtnvsfdsymiqtqdlPNSAPRLLEVDHRMVMPANLQTRIVVTAEDVLHSWAIPSLGIKVDA 175
Cdd:cd04213    2 LTIEVTGHQWWWEFRY------------------PDEPGRGIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDM 63

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 511768950 176 VPGRLNQLPLATSRTGVFFGQCSEICGANHSFMPIVVEAV 215
Cdd:cd04213   64 IPGRTNRLWLQADEPGVYRGQCAEFCGASHALMRFKVIAL 103
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 96-213 1.27e-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: 95.83  E-value: 1.27e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950  96 VTIKATGHQWYWNYEYTDgtnvsfdsymiqtqdlpnsaprlLEVDHRMVMPANLQTRIVVTAEDVLHSWAIPSLGIKVDA 175
Cdd:cd13842    1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 511768950 176 VPGRLNQLPLATSRTGVFFGQCSEICGANHSFMPIVVE 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 5.41e-23

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


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 89.39  E-value: 5.41e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950  96 VTIKATGHQWYWNYEYTDGTNVSFDsymiqtqdlpnsaprllevdhRMVMPANLQTRIVVTAEDVLHSWAIPSLGIKVDA 175
Cdd:cd13914    1 VEIEVEAYQWGWEFSYPEANVTTSE---------------------QLVIPADRPVYFRITSRDVIHAFHVPELGLKQDA 59

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 511768950 176 VPGRLNQLPLATSRTGVFFGQCSEICGANHSFMPIVVEAVPLNYFEQWL 224
Cdd:cd13914   60 FPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 96-213 7.07e-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: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 83.84  E-value: 7.07e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950  96 VTIKATGHQWYWNYEYTDGTNVSFDSYMIQTQDLpnsaprllevdhrmVMPANLQTRIVVTAEDVLHSWAIPSLGIKVDA 175
Cdd:cd13919    2 LVVEVTAQQWAWTFRYPGGDGKLGTDDDVTSPEL--------------HLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 511768950 176 VPGRLNQLPLATSRTGVFFGQCSEICGANHSFM--PIVVE 213
Cdd:cd13919   68 VPGRTTRLWFTPTREGEYEVRCAELCGLGHYRMraTVKVV 107
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 97-214 2.42e-20

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


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 82.29  E-value: 2.42e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950  97 TIKATGHQWYWNYEYTDGTnvsfdsymiqtqdlpnsaprllEVDHRMVMPANLQTRIVVTAEDVLHSWAIPSLGIKVDAV 176
Cdd:cd13915    3 EIQVTGRQWMWEFTYPNGK----------------------REINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDVV 60

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 511768950 177 PGRLNQLPLATSRTGVFFGQCSEICGANHSFMPIVVEA 214
Cdd:cd13915   61 PGRYTYLWFEATKPGEYDLFCTEYCGTGHSGMIGKVRV 98
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 96-224 2.94e-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: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 83.27  E-value: 2.94e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950  96 VTIKATGHQWYWNYEYTDGtnVSFDSYmiqtqdlpnsaprllevdhrMVMPANLQTRIVVTAEDVLHSWAIPSLGIKVDA 175
Cdd:cd13918   33 LEVEVEGFQFGWQFEYPNG--VTTGNT--------------------LRVPADTPIALRVTSTDVFHTFGIPELRVKADA 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 511768950 176 VPGRLNQLPLATSRTGVFFGQCSEICGANHSFMPIVVEAVPLNYFEQWL 224
Cdd:cd13918   91 IPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAWY 139
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-83 8.99e-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: 53.87  E-value: 8.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950    1 MPYATQLSLQEATGPAMEEVVFLHDHVLL-LTFLMSLVILLFATTAITATVTHND----PTEEVEQLEAAWTAAPIMILI 75
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFiLTLILILVLYILVTCLIRFNRRKNPitarYTTHGQTIEIIWTIIPAVILI 80


                  ....*...
gi 511768950   76 LTALPSVR 83
Cdd:pfam02790  81 LIALPSFK 88
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 143-213 1.40e-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: 45.25  E-value: 1.40e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 511768950 143 MVMPANLQTRIVVTAEDVLHSWAIPSLGIKVDAVPGRLNQLPLATSRTGVFFGQCSEICGANHSFM--PIVVE 213
Cdd:cd13913   27 IEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNMygKIIVE 99
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 96-208 3.77e-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: 41.21  E-value: 3.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950  96 VTIKATGHQWYWnyeytdgtnvsfdsymiqtqdlpnsaprllEVDhRMVMPANLQTRIVVTAEDVLHSWAI--PSLGI-- 171
Cdd:cd13916    1 QVVAVTGHQWYW------------------------------ELS-RTEIPAGKPVEFRVTSADVNHGFGIydPDMRLla 49

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 511768950 172 KVDAVPGRLNQLPLATSRTGVFFGQCSEICGANHSFM 208
Cdd:cd13916   50 QTQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 143-215 1.46e-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: 39.84  E-value: 1.46e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 511768950 143 MVMPANLQTRIVVTAEDVLHSWAIPSLGIKVDAVPGRLNQLPLATSRTGVFFGQCSEICGANHSFMPIVVEAV 215
Cdd:cd04212   27 LVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDMKFKVLAV 99
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 152-213 3.11e-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: 38.51  E-value: 3.11e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 511768950 152 RIVVTAEDVLHSWAIPSLGIKVDAVPGRLNQLPLATSRTGVFFGQCSEICGANHSFM--PIVVE 213
Cdd:cd13917   25 RLHLSSLDVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIICNEYCGIGHHTMhgRIIVE 88
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 98-213 1.13e-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: 37.60  E-value: 1.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950  98 IKATGHQWYWNYEYTDGTNVSFDSYmiqtqdlpnSAPRLLEVDHRMVMPANLQTRIVVTAEDVLHSWAI----PSLGIKV 173
Cdd:cd00920    1 ITVTASDWGWSFTYNGVLLFGPPVL---------VVPVGDTVRVQFVNKLGENHSVTIAGFGVPVVAMAgganPGLVNTL 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 511768950 174 DAVPGRLNQLPLATSRTGVFFGQCSEICGaNHSFMPIVVE 213
Cdd:cd00920   72 VIGPGESAEVTFTTDQAGVYWFYCTIPGH-NHAGMVGTIN 110
PRK10525 PRK10525
cytochrome o ubiquinol oxidase subunit II; Provisional
 66-224 6.60e-03

cytochrome o ubiquinol oxidase subunit II; Provisional


Pssm-ID: 182518 [Multi-domain]  Cd Length: 315  Bit Score: 37.09  E-value: 6.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950  66 WTAAPIMILILTAL--PSVRSLylmeevfDPY---------VTIKATGHQWYWNYEYTDGTnvsfdsymIQTQDlpnsap 134
Cdd:PRK10525  93 WTVPILIIIFLAVLtwKTTHAL-------EPSkplahdekpITIEVVSMDWKWFFIYPEQG--------IATVN------ 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511768950 135 rllevdhRMVMPANLQTRIVVTAEDVLHSWAIPSLGIKVDAVPGRLNQLPLATSRTGVFFGQCSEICGANHSFMPIVVEA 214
Cdd:PRK10525 152 -------EIAFPANVPVYFKVTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIANEPGTYDGISASYSGPGFSGMKFKAIA 224

                        170
                 ....*....|.
gi 511768950 215 VPLNY-FEQWL 224
Cdd:PRK10525 225 TPDRAeFDQWV 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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