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Conserved domains on  [gi|226463962|ref|YP_002734919|]
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cytochrome c oxidase subunit II (mitochondrion) [Chamaeleo zeylanicus]

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
 1-226 8.76e-156

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 430.87  E-value: 8.76e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962   1 MVEPIQLSLHDAASPVMEELLFFHDYSMLMMLMIGTSVIIALVIASTTKTYHTALTDANHLEFLWTLLPVMILLFLATPS 80
Cdd:MTH00117   1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962  81 MRTLFLLENQENPNTTIKAIGHQWYWSYEYSDYENILFDSYMIQNQDLEKGSPRLLETDNRMVFPMQTPVRLLISAEDVL 160
Cdd:MTH00117  81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 226463962 161 HSWTLPALGVKIDAIPGRLNQLIFSTMRPGIFYGQCSEICGANHSFMPISTESVPTKYFEKWLDKM 226
Cdd:MTH00117 161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLL 226
 
Name Accession Description Interval E-value
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-226 8.76e-156

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 430.87  E-value: 8.76e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962   1 MVEPIQLSLHDAASPVMEELLFFHDYSMLMMLMIGTSVIIALVIASTTKTYHTALTDANHLEFLWTLLPVMILLFLATPS 80
Cdd:MTH00117   1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962  81 MRTLFLLENQENPNTTIKAIGHQWYWSYEYSDYENILFDSYMIQNQDLEKGSPRLLETDNRMVFPMQTPVRLLISAEDVL 160
Cdd:MTH00117  81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 226463962 161 HSWTLPALGVKIDAIPGRLNQLIFSTMRPGIFYGQCSEICGANHSFMPISTESVPTKYFEKWLDKM 226
Cdd:MTH00117 161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLL 226
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-222 4.29e-90

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: 260.97  E-value: 4.29e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962  93 PNTTIKAIGHQWYWSYEYSDYENILFDSYMIQNQDLEKGSPRLLETDNRMVFPMQTPVRLLISAEDVLHSWTLPALGVKI 172
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 226463962 173 DAIPGRLNQLIFSTMRPGIFYGQCSEICGANHSFMPISTESVPTKYFEKW 222
Cdd:cd13912   81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
96-214 1.11e-78

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 231.91  E-value: 1.11e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962   96 TIKAIGHQWYWSYEYSDYENILFDSYMIQNQDLEKGSPRLLETDNRMVFPMQTPVRLLISAEDVLHSWTLPALGVKIDAI 175
Cdd:pfam00116   2 TIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDAV 81

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 226463962  176 PGRLNQLIFSTMRPGIFYGQCSEICGANHSFMPISTESV 214
Cdd:pfam00116  82 PGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-227 1.70e-62

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 194.66  E-value: 1.70e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962   6 QLSLHDAASPVMEELLFFHDYSMLMMLMIGTSVIIALVIAS-----TTKTYHTALTDANH-LEFLWTLLPVMILLFLATP 79
Cdd:COG1622   18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAiryrrRKGDADPAQFHHNTkLEIVWTVIPIIIVIVLAVP 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962  80 SMRTLFLLENQENPNTTIKAIGHQWYWSYEYSDyENILfdsymiqnqdlekgsprlleTDNRMVFPMQTPVRLLISAEDV 159
Cdd:COG1622   98 TLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPD-QGIA--------------------TVNELVLPVGRPVRFLLTSADV 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 226463962 160 LHSWTLPALGVKIDAIPGRLNQLIFSTMRPGIFYGQCSEICGANHSFMPISTESVPTKYFEKWLDKMA 227
Cdd:COG1622  157 IHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQK 224
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-223 9.96e-47

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: 153.31  E-value: 9.96e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962   12 AASPVMEELLFFHDYSMLMMLMIGTSV--IIALVI---------ASTTKTYHTALtdanhLEFLWTLLPVMILLFLATPS 80
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVaaLLAYVVwkfrrkgdeEKPSQIHGNRR-----LEYVWTVIPLIIVVGLFAAT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962   81 -MRTLFLLENQENPNTTIKAIGHQWYWSYEYSDYenilfdsymiqnqdlekgsprLLETDNRMVFPMQTPVRLLISAEDV 159
Cdd:TIGR02866  76 aKGLLYLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDV 134

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226463962  160 LHSWTLPALGVKIDAIPGRLNQLIFSTMRPGIFYGQCSEICGANHSFMPISTESVPTKYFEKWL 223
Cdd:TIGR02866 135 IHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYV 198
 
Name Accession Description Interval E-value
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-226 8.76e-156

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 430.87  E-value: 8.76e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962   1 MVEPIQLSLHDAASPVMEELLFFHDYSMLMMLMIGTSVIIALVIASTTKTYHTALTDANHLEFLWTLLPVMILLFLATPS 80
Cdd:MTH00117   1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962  81 MRTLFLLENQENPNTTIKAIGHQWYWSYEYSDYENILFDSYMIQNQDLEKGSPRLLETDNRMVFPMQTPVRLLISAEDVL 160
Cdd:MTH00117  81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 226463962 161 HSWTLPALGVKIDAIPGRLNQLIFSTMRPGIFYGQCSEICGANHSFMPISTESVPTKYFEKWLDKM 226
Cdd:MTH00117 161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLL 226
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 6-226 1.30e-121

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 344.50  E-value: 1.30e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962   6 QLSLHDAASPVMEELLFFHDYSMLMMLMIGTSVIIALVIASTTKTYHTALTDANHLEFLWTLLPVMILLFLATPSMRTLF 85
Cdd:MTH00154   6 NLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962  86 LLENQENPNTTIKAIGHQWYWSYEYSDYENILFDSYMIQNQDLEKGSPRLLETDNRMVFPMQTPVRLLISAEDVLHSWTL 165
Cdd:MTH00154  86 LLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTV 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226463962 166 PALGVKIDAIPGRLNQLIFSTMRPGIFYGQCSEICGANHSFMPISTESVPTKYFEKWLDKM 226
Cdd:MTH00154 166 PSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNM 226
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-224 2.87e-117

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 333.49  E-value: 2.87e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962   1 MVEPIQLSLHDAASPVMEELLFFHDYSMLMMLMIGTSVIIALVIASTTKTYHTALTDANHLEFLWTLLPVMILLFLATPS 80
Cdd:MTH00168   1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962  81 MRTLFLLENQENPNTTIKAIGHQWYWSYEYSDYENILFDSYMIQNQDLEKGSPRLLETDNRMVFPMQTPVRLLISAEDVL 160
Cdd:MTH00168  81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226463962 161 HSWTLPALGVKIDAIPGRLNQLIFSTMRPGIFYGQCSEICGANHSFMPISTESVPTKYFEKWLD 224
Cdd:MTH00168 161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVD 224
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-226 8.01e-113

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 322.05  E-value: 8.01e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962   1 MVEPIQLSLHDAASPVMEELLFFHDYSMLMMLMIGTSVIIALVIASTTKTYHTALTDANHLEFLWTLLPVMILLFLATPS 80
Cdd:MTH00098   1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962  81 MRTLFLLENQENPNTTIKAIGHQWYWSYEYSDYENILFDSYMIQNQDLEKGSPRLLETDNRMVFPMQTPVRLLISAEDVL 160
Cdd:MTH00098  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 226463962 161 HSWTLPALGVKIDAIPGRLNQLIFSTMRPGIFYGQCSEICGANHSFMPISTESVPTKYFEKWLDKM 226
Cdd:MTH00098 161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASM 226
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 6-227 3.64e-111

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 318.04  E-value: 3.64e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962   6 QLSLHDAASPVMEELLFFHDYSMLMMLMIGTSVIIALVIASTTK-TYHTALTDANhLEFLWTLLPVMILLFLATPSMRTL 84
Cdd:MTH00140   6 QLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKfSCRTILEAQK-LETIWTIVPALILVFLALPSLRLL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962  85 FLLENQENPNTTIKAIGHQWYWSYEYSDYENILFDSYMIQNQDLEKGSPRLLETDNRMVFPMQTPVRLLISAEDVLHSWT 164
Cdd:MTH00140  85 YLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWT 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 226463962 165 LPALGVKIDAIPGRLNQLIFSTMRPGIFYGQCSEICGANHSFMPISTESVPTKYFEKWLDKMA 227
Cdd:MTH00140 165 VPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELMS 227
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-226 7.44e-111

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 317.43  E-value: 7.44e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962   1 MVEPIQLSLHDAASPVMEELLFFHDYSMLMMLMIGTSVIIALVIASTTKTYHTALTDANHLEFLWTLLPVMILLFLATPS 80
Cdd:MTH00129   1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962  81 MRTLFLLENQENPNTTIKAIGHQWYWSYEYSDYENILFDSYMIQNQDLEKGSPRLLETDNRMVFPMQTPVRLLISAEDVL 160
Cdd:MTH00129  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 226463962 161 HSWTLPALGVKIDAIPGRLNQLIFSTMRPGIFYGQCSEICGANHSFMPISTESVPTKYFEKWLDKM 226
Cdd:MTH00129 161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLM 226
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-226 2.20e-106

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 306.04  E-value: 2.20e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962   1 MVEPIQLSLHDAASPVMEELLFFHDYSMLMMLMIGTSVIIALVIASTTKTYHTALTDANHLEFLWTLLPVMILLFLATPS 80
Cdd:MTH00185   1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962  81 MRTLFLLENQENPNTTIKAIGHQWYWSYEYSDYENILFDSYMIQNQDLEKGSPRLLETDNRMVFPMQTPVRLLISAEDVL 160
Cdd:MTH00185  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 226463962 161 HSWTLPALGVKIDAIPGRLNQLIFSTMRPGIFYGQCSEICGANHSFMPISTESVPTKYFEKWLDKM 226
Cdd:MTH00185 161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLM 226
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-222 2.41e-106

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 305.86  E-value: 2.41e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962   1 MVEPIQLSLHDAASPVMEELLFFHDYSMLMMLMIGTSVIIALVIASTTKTYHTALTDANHLEFLWTLLPVMILLFLATPS 80
Cdd:MTH00038   1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962  81 MRTLFLLENQENPNTTIKAIGHQWYWSYEYSDYENILFDSYMIQNQDLEKGSPRLLETDNRMVFPMQTPVRLLISAEDVL 160
Cdd:MTH00038  81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226463962 161 HSWTLPALGVKIDAIPGRLNQLIFSTMRPGIFYGQCSEICGANHSFMPISTESVPTKYFEKW 222
Cdd:MTH00038 161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENW 222
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-226 6.59e-106

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 304.78  E-value: 6.59e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962   1 MVEPIQLSLHDAASPVMEELLFFHDYSMLMMLMIGTSVIIALVIASTTKTYHTALTDANHLEFLWTLLPVMILLFLATPS 80
Cdd:MTH00076   1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962  81 MRTLFLLENQENPNTTIKAIGHQWYWSYEYSDYENILFDSYMIQNQDLEKGSPRLLETDNRMVFPMQTPVRLLISAEDVL 160
Cdd:MTH00076  81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 226463962 161 HSWTLPALGVKIDAIPGRLNQLIFSTMRPGIFYGQCSEICGANHSFMPISTESVPTKYFEKWLDKM 226
Cdd:MTH00076 161 HSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSM 226
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 6-223 1.01e-103

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 298.94  E-value: 1.01e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962   6 QLSLHDAASPVMEELLFFHDYSMLMMLMIGTSVIIALVIASTTKTYHTALTDANHLEFLWTLLPVMILLFLATPSMRTLF 85
Cdd:MTH00139   6 QLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPSLRLLY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962  86 LLENQENPNTTIKAIGHQWYWSYEYSDYENILFDSYMIQNQDLEKGSPRLLETDNRMVFPMQTPVRLLISAEDVLHSWTL 165
Cdd:MTH00139  86 LMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSWTV 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 226463962 166 PALGVKIDAIPGRLNQLIFSTMRPGIFYGQCSEICGANHSFMPISTESVPTKYFEKWL 223
Cdd:MTH00139 166 PSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWI 223
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 3-223 1.84e-99

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 288.96  E-value: 1.84e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962   3 EPIQLSLHDAASPVMEELLFFHDYSMLMMLMIGTSVIIALVIASTTKTYHTALTDANHLEFLWTLLPVMILLFLATPSMR 82
Cdd:MTH00023  12 EPWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLK 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962  83 TLFLLENQENPNTTIKAIGHQWYWSYEYSDY--ENILFDSYMIQNQDLEKGSPRLLETDNRMVFPMQTPVRLLISAEDVL 160
Cdd:MTH00023  92 LLYLMDEVVSPALTIKAIGHQWYWSYEYSDYegETLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVL 171

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 226463962 161 HSWTLPALGVKIDAIPGRLNQLIFSTMRPGIFYGQCSEICGANHSFMPISTESVPTKYFEKWL 223
Cdd:MTH00023 172 HSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWL 234
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 3-223 2.38e-99

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 288.22  E-value: 2.38e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962   3 EPIQLSLHDAASPVMEELLFFHDYSMLMMLMIGTSVIIALVIASTTKTYHTALTDANHLEFLWTLLPVMILLFLATPSMR 82
Cdd:MTH00051   5 EPWQLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLK 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962  83 TLFLLENQENPNTTIKAIGHQWYWSYEYSDY--ENILFDSYMIQNQDLEKGSPRLLETDNRMVFPMQTPVRLLISAEDVL 160
Cdd:MTH00051  85 LLYLMDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVL 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 226463962 161 HSWTLPALGVKIDAIPGRLNQLIFSTMRPGIFYGQCSEICGANHSFMPISTESVPTKYFEKWL 223
Cdd:MTH00051 165 HSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWV 227
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 6-227 8.56e-98

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 284.06  E-value: 8.56e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962   6 QLSLHDAASPVMEELLFFHDYSMLMMLMIGTSVIIALVIASTTKTYHTALTDANHLEFLWTLLPVMILLFLATPSMRTLF 85
Cdd:MTH00008   6 QLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSLRLLY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962  86 LLENQENPNTTIKAIGHQWYWSYEYSDYENILFDSYMIQNQDLEKGSPRLLETDNRMVFPMQTPVRLLISAEDVLHSWTL 165
Cdd:MTH00008  86 LMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTV 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226463962 166 PALGVKIDAIPGRLNQLIFSTMRPGIFYGQCSEICGANHSFMPISTESVPTKYFEKWLDKMA 227
Cdd:MTH00008 166 PSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSSFA 227
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-222 4.29e-90

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: 260.97  E-value: 4.29e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962  93 PNTTIKAIGHQWYWSYEYSDYENILFDSYMIQNQDLEKGSPRLLETDNRMVFPMQTPVRLLISAEDVLHSWTLPALGVKI 172
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 226463962 173 DAIPGRLNQLIFSTMRPGIFYGQCSEICGANHSFMPISTESVPTKYFEKW 222
Cdd:cd13912   81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
96-214 1.11e-78

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 231.91  E-value: 1.11e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962   96 TIKAIGHQWYWSYEYSDYENILFDSYMIQNQDLEKGSPRLLETDNRMVFPMQTPVRLLISAEDVLHSWTLPALGVKIDAI 175
Cdd:pfam00116   2 TIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDAV 81

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 226463962  176 PGRLNQLIFSTMRPGIFYGQCSEICGANHSFMPISTESV 214
Cdd:pfam00116  82 PGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 3-225 1.20e-76

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 231.84  E-value: 1.20e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962   3 EPIQLSLHDAASPVMEELLFFHDYSMLMMLMIGTSV---IIALVIASTTKTYHTALTDANHLEFLWTLLPVMILLFLATP 79
Cdd:MTH00027  31 EPWQLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVlwlIIRILLGNNYYSYYWNKLDGSLIEVIWTLIPAFILILIAFP 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962  80 SMRTLFLL-ENQENPNTTIKAIGHQWYWSYEYSDY--ENILFDSYMIQNQDLEKGSPRLLETDNRMVFPMQTPVRLLISA 156
Cdd:MTH00027 111 SLRLLYIMdECGFSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITA 190

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 226463962 157 EDVLHSWTLPALGVKIDAIPGRLNQLIFSTMRPGIFYGQCSEICGANHSFMPISTESVPTKYFEKWLDK 225
Cdd:MTH00027 191 ADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWIGR 259
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 20-223 2.17e-69

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 212.18  E-value: 2.17e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962  20 LLFFHDYSMLMML---MIGTSVIIALVIASTTKTYHTALTDANHLEFLWTLLPVMILLFLATPSMRTLFLLE--NQENpN 94
Cdd:MTH00080  19 MDWFHNFNCSLLFgefVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGlmNLDS-N 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962  95 TTIKAIGHQWYWSYEYSDYENILFDSYMIQNQDLEKGSPRLLETDNRMVFPMQTPVRLLISAEDVLHSWTLPALGVKIDA 174
Cdd:MTH00080  98 LTVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDA 177

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 226463962 175 IPGRLNQLIFSTMRPGIFYGQCSEICGANHSFMPISTESVPTKYFEKWL 223
Cdd:MTH00080 178 MSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWC 226
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-227 1.70e-62

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 194.66  E-value: 1.70e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962   6 QLSLHDAASPVMEELLFFHDYSMLMMLMIGTSVIIALVIAS-----TTKTYHTALTDANH-LEFLWTLLPVMILLFLATP 79
Cdd:COG1622   18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAiryrrRKGDADPAQFHHNTkLEIVWTVIPIIIVIVLAVP 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962  80 SMRTLFLLENQENPNTTIKAIGHQWYWSYEYSDyENILfdsymiqnqdlekgsprlleTDNRMVFPMQTPVRLLISAEDV 159
Cdd:COG1622   98 TLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPD-QGIA--------------------TVNELVLPVGRPVRFLLTSADV 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 226463962 160 LHSWTLPALGVKIDAIPGRLNQLIFSTMRPGIFYGQCSEICGANHSFMPISTESVPTKYFEKWLDKMA 227
Cdd:COG1622  157 IHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQK 224
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 57-214 4.46e-47

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 153.96  E-value: 4.46e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962  57 DANHLEFLWTLLPVMILLFLAtpSMRTLFLLENQE-NPNTTIKAIGHQWYWSYEYSDyeNILFDSYMIQNQDLekgsprl 135
Cdd:MTH00047  45 ENQVLELLWTVVPTLLVLVLC--FLNLNFITSDLDcFSSETIKVIGHQWYWSYEYSF--GGSYDSFMTDDIFG------- 113

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 226463962 136 leTDNRMVFPMQTPVRLLISAEDVLHSWTLPALGVKIDAIPGRLNQLIFSTMRPGIFYGQCSEICGANHSFMPISTESV 214
Cdd:MTH00047 114 --VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVV 190
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-223 9.96e-47

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: 153.31  E-value: 9.96e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962   12 AASPVMEELLFFHDYSMLMMLMIGTSV--IIALVI---------ASTTKTYHTALtdanhLEFLWTLLPVMILLFLATPS 80
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVaaLLAYVVwkfrrkgdeEKPSQIHGNRR-----LEYVWTVIPLIIVVGLFAAT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962   81 -MRTLFLLENQENPNTTIKAIGHQWYWSYEYSDYenilfdsymiqnqdlekgsprLLETDNRMVFPMQTPVRLLISAEDV 159
Cdd:TIGR02866  76 aKGLLYLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDV 134

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226463962  160 LHSWTLPALGVKIDAIPGRLNQLIFSTMRPGIFYGQCSEICGANHSFMPISTESVPTKYFEKWL 223
Cdd:TIGR02866 135 IHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYV 198
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 118-218 2.03e-37

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 128.40  E-value: 2.03e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962 118 FDSYMIQNQDLEKGSPRLLETDNRMVFPMQTPVRLLISAEDVLHSWTLPALGVKIDAIPGRLNQLIFSTMRPGIFYGQCS 197
Cdd:PTZ00047  51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                         90       100
                 ....*....|....*....|..
gi 226463962 198 EICGANHSFMPISTESV-PTKY 218
Cdd:PTZ00047 131 EMCGTLHGFMPIVVEAVsPEAY 152
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 96-207 1.78e-30

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: 108.48  E-value: 1.78e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962  96 TIKAIGHQWYWSYEYSDYEnilfdsymiqnqdlekgsPRLLETDNRMVFPMQTPVRLLISAEDVLHSWTLPALGVKIDAI 175
Cdd:cd04213    3 TIEVTGHQWWWEFRYPDEP------------------GRGIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDMI 64

                         90       100       110
                 ....*....|....*....|....*....|..
gi 226463962 176 PGRLNQLIFSTMRPGIFYGQCSEICGANHSFM 207
Cdd:cd04213   65 PGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 96-208 5.18e-29

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: 104.30  E-value: 5.18e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962  96 TIKAIGHQWYWSYEYSDyenilfdsymiqnqdlekgsprlLETDNRMVFPMQTPVRLLISAEDVLHSWTLPALGVKIDAI 175
Cdd:cd13842    2 TVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDAV 58

                         90       100       110
                 ....*....|....*....|....*....|...
gi 226463962 176 PGRLNQLIFSTMRPGIFYGQCSEICGANHSFMP 208
Cdd:cd13842   59 PGYTSELWFVADKPGTYTIICAEYCGLGHSYML 91
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 96-207 3.01e-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: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 90.01  E-value: 3.01e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962  96 TIKAIGHQWYWSYEYSDYEnilfdsymiqnqdlEKGSPRLLETDNRMVFPMQTPVRLLISAEDVLHSWTLPALGVKIDAI 175
Cdd:cd13919    3 VVEVTAQQWAWTFRYPGGD--------------GKLGTDDDVTSPELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDAV 68

                         90       100       110
                 ....*....|....*....|....*....|..
gi 226463962 176 PGRLNQLIFSTMRPGIFYGQCSEICGANHSFM 207
Cdd:cd13919   69 PGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 96-207 4.64e-23

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


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 89.23  E-value: 4.64e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962  96 TIKAIGHQWYWSYEYsdyenilfdsymiqnqdlekgsPRLLETDNRMVFPMQTPVRLLISAEDVLHSWTLPALGVKIDAI 175
Cdd:cd13915    3 EIQVTGRQWMWEFTY----------------------PNGKREINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDVV 60

                         90       100       110
                 ....*....|....*....|....*....|..
gi 226463962 176 PGRLNQLIFSTMRPGIFYGQCSEICGANHSFM 207
Cdd:cd13915   61 PGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 70-223 1.06e-22

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


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 89.44  E-value: 1.06e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962  70 VMILLFLATPSMrTLFL----LENQENPnTTIKAIGHQWYWSYEYsdyenilfdsymiqnqdlekgsPRLLETDNRMVFP 145
Cdd:cd13918    6 IVISLIVWTYGM-LLYVedppDEADEDA-LEVEVEGFQFGWQFEY----------------------PNGVTTGNTLRVP 61

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 226463962 146 MQTPVRLLISAEDVLHSWTLPALGVKIDAIPGRLNQLIFSTMRPGIFYGQCSEICGANHSFMPISTESVPTKYFEKWL 223
Cdd:cd13918   62 ADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAWY 139
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-223 1.69e-22

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


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 88.23  E-value: 1.69e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962  95 TTIKAIGHQWYWSYEYSDyENIlfdsymiqnqdlekgsprllETDNRMVFPMQTPVRLLISAEDVLHSWTLPALGVKIDA 174
Cdd:cd13914    1 VEIEVEAYQWGWEFSYPE-ANV--------------------TTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDA 59

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 226463962 175 IPGRLNQLIFSTMRPGIFYGQCSEICGANHSFMPISTESVPTKYFEKWL 223
Cdd:cd13914   60 FPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-82 8.06e-15

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: 67.36  E-value: 8.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962    1 MVEPIQLSLHDAASPVMEELLFFHDYSMLMMLMIGTSVIIALVIASTTKTY------HTALTDANHLEFLWTLLPVMILL 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRFNRrknpitARYTTHGQTIEIIWTIIPAVILI 80


                  ....*...
gi 226463962   75 FLATPSMR 82
Cdd:pfam02790  81 LIALPSFK 88
PRK10525 PRK10525
cytochrome o ubiquinol oxidase subunit II; Provisional
 29-225 1.10e-09

cytochrome o ubiquinol oxidase subunit II; Provisional


Pssm-ID: 182518 [Multi-domain]  Cd Length: 315  Bit Score: 57.12  E-value: 1.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962  29 LMMLMIGTSVIIALVIA------STTKTYHTALTDANHLE-FLWTLlPVMILLFLATPSMRTLFLLE------NQENPnT 95
Cdd:PRK10525  50 LMLIVVIPAILMAVGFAwkyrasNKDAKYSPNWSHSNKVEaVVWTV-PILIIIFLAVLTWKTTHALEpskplaHDEKP-I 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962  96 TIKAIGHQWYWSYEYSdyenilfdsymiqnqdlEKGsprlLETDNRMVFPMQTPVRLLISAEDVLHSWTLPALGVKIDAI 175
Cdd:PRK10525 128 TIEVVSMDWKWFFIYP-----------------EQG----IATVNEIAFPANVPVYFKVTSNSVMNSFFIPRLGSQIYAM 186

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 226463962 176 PGRLNQLIFSTMRPGIFYGQCSEICGANHSFMPISTESVPTKY-FEKWLDK 225
Cdd:PRK10525 187 AGMQTRLHLIANEPGTYDGISASYSGPGFSGMKFKAIATPDRAeFDQWVAK 237
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 96-214 2.17e-07

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: 47.54  E-value: 2.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962  96 TIKAIGHQWYWSYEYSDYeNIlfdsymiqnqdlekgsprllETDNRMVFPMQTPVRLLISAEDVLHSWTLPALGVKIDAI 175
Cdd:cd04212    2 EIQVVSLDWKWLFIYPEQ-GI--------------------ATVNELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAM 60

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 226463962 176 PGRLNQLIFSTMRPGIFYGQCSEICGANHSFMPISTESV 214
Cdd:cd04212   61 AGMQTQLHLIADKPGTYQGLSANYSGEGFSDMKFKVLAV 99
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 138-207 1.60e-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: 1.60e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962 138 TDNRMVFPMQTPVRLLISAEDVLHSWTLPALGVKIDAIPGRLNQLIFSTMRPGIFYGQCSEICGANHSFM 207
Cdd:cd13913   23 NPNEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-207 1.07e-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: 42.75  E-value: 1.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962  95 TTIKAIGHQWYWSYeysdyenilfdsymiqnqdlekgsprlletdNRMVFPMQTPVRLLISAEDVLHSWTL--PALGV-- 170
Cdd:cd13916    1 QVVAVTGHQWYWEL-------------------------------SRTEIPAGKPVEFRVTSADVNHGFGIydPDMRLla 49

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 226463962 171 KIDAIPGRLNQLIFSTMRPGIFYGQCSEICGANHSFM 207
Cdd:cd13916   50 QTQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 97-209 1.59e-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: 1.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463962  97 IKAIGHQWYWSYEYSDYenilfdsymiqnqdlekgsprLLETDNRMVFPMQTPVRL-LISAEDVLHSWTLPALGVKIDAI 175
Cdd:cd00920    1 ITVTASDWGWSFTYNGV---------------------LLFGPPVLVVPVGDTVRVqFVNKLGENHSVTIAGFGVPVVAM 59

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 226463962 176 ---------------PGRLNQLIFSTMRPGIFYGQCSEICGaNHSFMPI 209
Cdd:cd00920   60 agganpglvntlvigPGESAEVTFTTDQAGVYWFYCTIPGH-NHAGMVG 107
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 151-207 2.92e-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: 35.81  E-value: 2.92e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 226463962 151 RLLISAEDVLHSWTLPALGVKIDAIPGRLNQLIFSTMRPGIFYGQCSEICGANHSFM 207
Cdd:cd13917   25 RLHLSSLDVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIICNEYCGIGHHTM 81
 
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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