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Conserved domains on  [gi|470227334|ref|YP_007624712|]
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cytochrome c oxidase subunit II (mitochondrion) [Tachycineta albiventer]

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 2.93e-164

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 452.06  E-value: 2.93e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334   1 MANHMQLNFQDASSPIMEELMQFHDHALMVALAICSLVLYLLTATLTSKLT-ANTVNAQVMELVWTILPAMVLIALALPS 79
Cdd:MTH00117   1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLThTNTVDAQEVELIWTILPAIVLILLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334  80 LRILYLMDEVNEPDMTLKAIGHQWYWTYEYTDFKDLTFDSYMTPTSDLPMGHFRLLEVDHRVIVPMNSTVRVIVTANDVL 159
Cdd:MTH00117  81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 470227334 160 HSWAVPSLGVKTDAIPGRLNQTSFMAPRPGVYYGQCSEICGANHSFMPIVVESTPLANFENWSSLLS 226
Cdd:MTH00117 161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLLS 227
 
Name Accession Description Interval E-value
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-226 2.93e-164

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 452.06  E-value: 2.93e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334   1 MANHMQLNFQDASSPIMEELMQFHDHALMVALAICSLVLYLLTATLTSKLT-ANTVNAQVMELVWTILPAMVLIALALPS 79
Cdd:MTH00117   1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLThTNTVDAQEVELIWTILPAIVLILLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334  80 LRILYLMDEVNEPDMTLKAIGHQWYWTYEYTDFKDLTFDSYMTPTSDLPMGHFRLLEVDHRVIVPMNSTVRVIVTANDVL 159
Cdd:MTH00117  81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 470227334 160 HSWAVPSLGVKTDAIPGRLNQTSFMAPRPGVYYGQCSEICGANHSFMPIVVESTPLANFENWSSLLS 226
Cdd:MTH00117 161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLLS 227
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 92-221 6.03e-97

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


Pssm-ID: 259979 [Multi-domain]  Cd Length: 130  Bit Score: 278.30  E-value: 6.03e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334  92 PDMTLKAIGHQWYWTYEYTDFKDLTFDSYMTPTSDLPMGHFRLLEVDHRVIVPMNSTVRVIVTANDVLHSWAVPSLGVKT 171
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 470227334 172 DAIPGRLNQTSFMAPRPGVYYGQCSEICGANHSFMPIVVESTPLANFENW 221
Cdd:cd13912   81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
94-213 1.99e-85

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 248.86  E-value: 1.99e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334   94 MTLKAIGHQWYWTYEYTDFKDLTFDSYMTPTSDLPMGHFRLLEVDHRVIVPMNSTVRVIVTANDVLHSWAVPSLGVKTDA 173
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 470227334  174 IPGRLNQTSFMAPRPGVYYGQCSEICGANHSFMPIVVEST 213
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-221 1.35e-60

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 189.65  E-value: 1.35e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334   6 QLNFQDASSPIMEELMQFHDHALMVALAICSLVLYLL-----------TATLTSKLTANTVnaqvMELVWTILPAMVLIA 74
Cdd:COG1622   18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLlyfairyrrrkGDADPAQFHHNTK----LEIVWTVIPIIIVIV 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334  75 LALPSLRILYLMDEVNEPDMTLKAIGHQWYWTYEYTDFKDLTfdsymtptsdlpmghfrllevDHRVIVPMNSTVRVIVT 154
Cdd:COG1622   94 LAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIAT---------------------VNELVLPVGRPVRFLLT 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 470227334 155 ANDVLHSWAVPSLGVKTDAIPGRLNQTSFMAPRPGVYYGQCSEICGANHSFMPIVVESTPLANFENW 221
Cdd:COG1622  153 SADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAW 219
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-221 3.12e-45

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: 149.45  E-value: 3.12e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334   12 ASSPIMEELMQFHDHALMVALAICSLVLYLL-----------TATLTSKLTANTVnaqvMELVWTILPAMVLIAL-ALPS 79
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLayvvwkfrrkgDEEKPSQIHGNRR----LEYVWTVIPLIIVVGLfAATA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334   80 LRILYLMDEVNEPDMTLKAIGHQWYWTYEYtdfKDLTFDSymtptsdlpmghfrllevDHRVIVPMNSTVRVIVTANDVL 159
Cdd:TIGR02866  77 KGLLYLERPIPKDALKVKVTGYQWWWDFEY---PESGFTT------------------VNELVLPAGTPVELQVTSKDVI 135

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 470227334  160 HSWAVPSLGVKTDAIPGRLNQTSFMAPRPGVYYGQCSEICGANHSFMPIVVESTPLANFENW 221
Cdd:TIGR02866 136 HSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAY 197
 
Name Accession Description Interval E-value
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-226 2.93e-164

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 452.06  E-value: 2.93e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334   1 MANHMQLNFQDASSPIMEELMQFHDHALMVALAICSLVLYLLTATLTSKLT-ANTVNAQVMELVWTILPAMVLIALALPS 79
Cdd:MTH00117   1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLThTNTVDAQEVELIWTILPAIVLILLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334  80 LRILYLMDEVNEPDMTLKAIGHQWYWTYEYTDFKDLTFDSYMTPTSDLPMGHFRLLEVDHRVIVPMNSTVRVIVTANDVL 159
Cdd:MTH00117  81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 470227334 160 HSWAVPSLGVKTDAIPGRLNQTSFMAPRPGVYYGQCSEICGANHSFMPIVVESTPLANFENWSSLLS 226
Cdd:MTH00117 161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLLS 227
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-225 2.70e-136

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 381.37  E-value: 2.70e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334   1 MANHMQLNFQDASSPIMEELMQFHDHALMVALAICSLVLYLLTATLTSKLT-ANTVNAQVMELVWTILPAMVLIALALPS 79
Cdd:MTH00098   1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLThTSTMDAQEVETIWTILPAIILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334  80 LRILYLMDEVNEPDMTLKAIGHQWYWTYEYTDFKDLTFDSYMTPTSDLPMGHFRLLEVDHRVIVPMNSTVRVIVTANDVL 159
Cdd:MTH00098  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 470227334 160 HSWAVPSLGVKTDAIPGRLNQTSFMAPRPGVYYGQCSEICGANHSFMPIVVESTPLANFENWSSLL 225
Cdd:MTH00098 161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASM 226
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-226 7.04e-135

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 378.02  E-value: 7.04e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334   1 MANHMQLNFQDASSPIMEELMQFHDHALMVALAICSLVLYLLTATLTSKLTANTVN-AQVMELVWTILPAMVLIALALPS 79
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLeGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334  80 LRILYLMDEVNEPDMTLKAIGHQWYWTYEYTDFKDLTFDSYMTPTSDLPMGHFRLLEVDHRVIVPMNSTVRVIVTANDVL 159
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 470227334 160 HSWAVPSLGVKTDAIPGRLNQTSFMAPRPGVYYGQCSEICGANHSFMPIVVESTPLANFENWSSLLS 226
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-224 1.60e-133

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 374.50  E-value: 1.60e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334   1 MANHMQLNFQDASSPIMEELMQFHDHALMVALAICSLVLYLLTATLTSKLT-ANTVNAQVMELVWTILPAMVLIALALPS 79
Cdd:MTH00076   1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTnTNTMDAQEIEMVWTIMPAIILIVIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334  80 LRILYLMDEVNEPDMTLKAIGHQWYWTYEYTDFKDLTFDSYMTPTSDLPMGHFRLLEVDHRVIVPMNSTVRVIVTANDVL 159
Cdd:MTH00076  81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 470227334 160 HSWAVPSLGVKTDAIPGRLNQTSFMAPRPGVYYGQCSEICGANHSFMPIVVESTPLANFENWSSL 224
Cdd:MTH00076 161 HSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSS 225
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-225 7.01e-133

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 372.89  E-value: 7.01e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334   1 MANHMQLNFQDASSPIMEELMQFHDHALMVALAICSLVLYLLTATLTSKLT-ANTVNAQVMELVWTILPAMVLIALALPS 79
Cdd:MTH00129   1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTnKYILDSQEIEIIWTVLPAVILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334  80 LRILYLMDEVNEPDMTLKAIGHQWYWTYEYTDFKDLTFDSYMTPTSDLPMGHFRLLEVDHRVIVPMNSTVRVIVTANDVL 159
Cdd:MTH00129  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 470227334 160 HSWAVPSLGVKTDAIPGRLNQTSFMAPRPGVYYGQCSEICGANHSFMPIVVESTPLANFENWSSLL 225
Cdd:MTH00129 161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLM 226
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-223 2.11e-124

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 351.70  E-value: 2.11e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334   1 MANHMQLNFQDASSPIMEELMQFHDHALMVALAICSLVLYLLTATLTSKLTANT-VNAQVMELVWTILPAMVLIALALPS 79
Cdd:MTH00038   1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFfLEGQELETIWTIVPAFILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334  80 LRILYLMDEVNEPDMTLKAIGHQWYWTYEYTDFKDLTFDSYMTPTSDLPMGHFRLLEVDHRVIVPMNSTVRVIVTANDVL 159
Cdd:MTH00038  81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 470227334 160 HSWAVPSLGVKTDAIPGRLNQTSFMAPRPGVYYGQCSEICGANHSFMPIVVESTPLANFENWSS 223
Cdd:MTH00038 161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVS 224
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-223 2.21e-124

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 351.21  E-value: 2.21e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334   1 MANHMQLNFQDASSPIMEELMQFHDHALMVALAICSLVLYLLTATLTSKLTANTVN-AQVMELVWTILPAMVLIALALPS 79
Cdd:MTH00168   1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLdSQMIEFVWTIIPAFILISLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334  80 LRILYLMDEVNEPDMTLKAIGHQWYWTYEYTDFKDLTFDSYMTPTSDLPMGHFRLLEVDHRVIVPMNSTVRVIVTANDVL 159
Cdd:MTH00168  81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 470227334 160 HSWAVPSLGVKTDAIPGRLNQTSFMAPRPGVYYGQCSEICGANHSFMPIVVESTPLANFENWSS 223
Cdd:MTH00168 161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVD 224
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 6-227 2.73e-124

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 351.16  E-value: 2.73e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334   6 QLNFQDASSPIMEELMQFHDHALMVALAICSLVLYLLTATLTSKLTANTV-NAQVMELVWTILPAMVLIALALPSLRILY 84
Cdd:MTH00140   6 QLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTIlEAQKLETIWTIVPALILVFLALPSLRLLY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334  85 LMDEVNEPDMTLKAIGHQWYWTYEYTDFKDLTFDSYMTPTSDLPMGHFRLLEVDHRVIVPMNSTVRVIVTANDVLHSWAV 164
Cdd:MTH00140  86 LLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTV 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 470227334 165 PSLGVKTDAIPGRLNQTSFMAPRPGVYYGQCSEICGANHSFMPIVVESTPLANFENWSSLLSS 227
Cdd:MTH00140 166 PSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELMSE 228
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-225 1.34e-123

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 349.57  E-value: 1.34e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334   1 MANHMQLNFQDASSPIMEELMQFHDHALMVALAICSLVLYLLTATLTSKLTAN-TVNAQVMELVWTILPAMVLIALALPS 79
Cdd:MTH00185   1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKyILDSQEIEIVWTILPAIILIMIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334  80 LRILYLMDEVNEPDMTLKAIGHQWYWTYEYTDFKDLTFDSYMTPTSDLPMGHFRLLEVDHRVIVPMNSTVRVIVTANDVL 159
Cdd:MTH00185  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 470227334 160 HSWAVPSLGVKTDAIPGRLNQTSFMAPRPGVYYGQCSEICGANHSFMPIVVESTPLANFENWSSLL 225
Cdd:MTH00185 161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLM 226
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-221 7.92e-118

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 334.76  E-value: 7.92e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334   1 MANHMQLNFQDASSPIMEELMQFHDHALMVALAICSLVLYLLTATLTSKLTANT-VNAQVMELVWTILPAMVLIALALPS 79
Cdd:MTH00139   1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSlLESQEVETIWTVLPAFILLFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334  80 LRILYLMDEVNEPDMTLKAIGHQWYWTYEYTDFKDLTFDSYMTPTSDLPMGHFRLLEVDHRVIVPMNSTVRVIVTANDVL 159
Cdd:MTH00139  81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 470227334 160 HSWAVPSLGVKTDAIPGRLNQTSFMAPRPGVYYGQCSEICGANHSFMPIVVESTPLANFENW 221
Cdd:MTH00139 161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEW 222
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-227 1.30e-111

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 319.11  E-value: 1.30e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334   1 MANHMQLNFQDASSPIMEELMQFHDHALMVALAICSLVLYLLTATLTSKLTANTV-NAQVMELVWTILPAMVLIALALPS 79
Cdd:MTH00008   1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYIlEAQQIETIWTILPALILLFLAFPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334  80 LRILYLMDEVNEPDMTLKAIGHQWYWTYEYTDFKDLTFDSYMTPTSDLPMGHFRLLEVDHRVIVPMNSTVRVIVTANDVL 159
Cdd:MTH00008  81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 470227334 160 HSWAVPSLGVKTDAIPGRLNQTSFMAPRPGVYYGQCSEICGANHSFMPIVVESTPLANFENWSSLLSS 227
Cdd:MTH00008 161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSSFAE 228
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 6-227 3.40e-106

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 305.91  E-value: 3.40e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334   6 QLNFQDASSPIMEELMQFHDHALMVALAICSLVLYLLTATLTSK-LTANTVNAQVMELVWTILPAMVLIALALPSLRILY 84
Cdd:MTH00023  15 QLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKfYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLY 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334  85 LMDEVNEPDMTLKAIGHQWYWTYEYTDFKD--LTFDSYMTPTSDLPMGHFRLLEVDHRVIVPMNSTVRVIVTANDVLHSW 162
Cdd:MTH00023  95 LMDEVVSPALTIKAIGHQWYWSYEYSDYEGetLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSF 174

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 470227334 163 AVPSLGVKTDAIPGRLNQTSFMAPRPGVYYGQCSEICGANHSFMPIVVESTPLANFENWSSLLSS 227
Cdd:MTH00023 175 AVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLSLSN 239
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 6-226 1.40e-102

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 296.69  E-value: 1.40e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334   6 QLNFQDASSPIMEELMQFHDHALMVALAICSLVLYLLTATLTSKLTANTV-NAQVMELVWTILPAMVLIALALPSLRILY 84
Cdd:MTH00051   8 QLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLfEGTLIEIIWTLIPAAILIFIAFPSLKLLY 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334  85 LMDEVNEPDMTLKAIGHQWYWTYEYTDF--KDLTFDSYMTPTSDLPMGHFRLLEVDHRVIVPMNSTVRVIVTANDVLHSW 162
Cdd:MTH00051  88 LMDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSF 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 470227334 163 AVPSLGVKTDAIPGRLNQTSFMAPRPGVYYGQCSEICGANHSFMPIVVESTPLANFENWSSLLS 226
Cdd:MTH00051 168 AVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQS 231
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 92-221 6.03e-97

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


Pssm-ID: 259979 [Multi-domain]  Cd Length: 130  Bit Score: 278.30  E-value: 6.03e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334  92 PDMTLKAIGHQWYWTYEYTDFKDLTFDSYMTPTSDLPMGHFRLLEVDHRVIVPMNSTVRVIVTANDVLHSWAVPSLGVKT 171
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 470227334 172 DAIPGRLNQTSFMAPRPGVYYGQCSEICGANHSFMPIVVESTPLANFENW 221
Cdd:cd13912   81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
94-213 1.99e-85

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 248.86  E-value: 1.99e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334   94 MTLKAIGHQWYWTYEYTDFKDLTFDSYMTPTSDLPMGHFRLLEVDHRVIVPMNSTVRVIVTANDVLHSWAVPSLGVKTDA 173
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 470227334  174 IPGRLNQTSFMAPRPGVYYGQCSEICGANHSFMPIVVEST 213
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 6-221 2.27e-85

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 253.79  E-value: 2.27e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334   6 QLNFQDASSPIMEELMQFHDHALMVALAICSLVLYLLTATLTSK----LTANTVNAQVMELVWTILPAMVLIALALPSLR 81
Cdd:MTH00027  34 QLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLGNnyysYYWNKLDGSLIEVIWTLIPAFILILIAFPSLR 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334  82 ILYLMDE-VNEPDMTLKAIGHQWYWTYEYTDF--KDLTFDSYMTPTSDLPMGHFRLLEVDHRVIVPMNSTVRVIVTANDV 158
Cdd:MTH00027 114 LLYIMDEcGFSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADV 193

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 470227334 159 LHSWAVPSLGVKTDAIPGRLNQTSFMAPRPGVYYGQCSEICGANHSFMPIVVESTPLANFENW 221
Cdd:MTH00027 194 LHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDW 256
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 7-225 5.57e-79

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 236.44  E-value: 5.57e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334   7 LNFQDASSPI-MEELMQFHDHALMVALAICSLV-LYLLTATLTSKLTANTVNAQVMELVWTILPAMVLIALALPSLRILY 84
Cdd:MTH00080   8 LNFSNSLFSSyMDWFHNFNCSLLFGEFVLAFVVfLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLY 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334  85 LMDEVN-EPDMTLKAIGHQWYWTYEYTDFKDLTFDSYMTPTSDLPMGHFRLLEVDHRVIVPMNSTVRVIVTANDVLHSWA 163
Cdd:MTH00080  88 YYGLMNlDSNLTVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWA 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 470227334 164 VPSLGVKTDAIPGRLNQTSFMAPRPGVYYGQCSEICGANHSFMPIVVESTPLANFENWSSLL 225
Cdd:MTH00080 168 LPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWCKLL 229
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-221 1.35e-60

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 189.65  E-value: 1.35e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334   6 QLNFQDASSPIMEELMQFHDHALMVALAICSLVLYLL-----------TATLTSKLTANTVnaqvMELVWTILPAMVLIA 74
Cdd:COG1622   18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLlyfairyrrrkGDADPAQFHHNTK----LEIVWTVIPIIIVIV 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334  75 LALPSLRILYLMDEVNEPDMTLKAIGHQWYWTYEYTDFKDLTfdsymtptsdlpmghfrllevDHRVIVPMNSTVRVIVT 154
Cdd:COG1622   94 LAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIAT---------------------VNELVLPVGRPVRFLLT 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 470227334 155 ANDVLHSWAVPSLGVKTDAIPGRLNQTSFMAPRPGVYYGQCSEICGANHSFMPIVVESTPLANFENW 221
Cdd:COG1622  153 SADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAW 219
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 57-211 1.44e-46

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 152.80  E-value: 1.44e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334  57 AQVMELVWTILPAMVLIALALPSLRILYlMDEVNEPDMTLKAIGHQWYWTYEYTDfkDLTFDSYMTptsDLPMGhfrlle 136
Cdd:MTH00047  46 NQVLELLWTVVPTLLVLVLCFLNLNFIT-SDLDCFSSETIKVIGHQWYWSYEYSF--GGSYDSFMT---DDIFG------ 113

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 470227334 137 VDHRVIVPMNSTVRVIVTANDVLHSWAVPSLGVKTDAIPGRLNQTSFMAPRPGVYYGQCSEICGANHSFMPIVVE 211
Cdd:MTH00047 114 VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIE 188
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-221 3.12e-45

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: 149.45  E-value: 3.12e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334   12 ASSPIMEELMQFHDHALMVALAICSLVLYLL-----------TATLTSKLTANTVnaqvMELVWTILPAMVLIAL-ALPS 79
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLayvvwkfrrkgDEEKPSQIHGNRR----LEYVWTVIPLIIVVGLfAATA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334   80 LRILYLMDEVNEPDMTLKAIGHQWYWTYEYtdfKDLTFDSymtptsdlpmghfrllevDHRVIVPMNSTVRVIVTANDVL 159
Cdd:TIGR02866  77 KGLLYLERPIPKDALKVKVTGYQWWWDFEY---PESGFTT------------------VNELVLPAGTPVELQVTSKDVI 135

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 470227334  160 HSWAVPSLGVKTDAIPGRLNQTSFMAPRPGVYYGQCSEICGANHSFMPIVVESTPLANFENW 221
Cdd:TIGR02866 136 HSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAY 197
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 116-212 2.36e-38

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 130.71  E-value: 2.36e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334 116 TFDSYMTPTSDLPMGHFRLLEVDHRVIVPMNSTVRVIVTANDVLHSWAVPSLGVKTDAIPGRLNQTSFMAPRPGVYYGQC 195
Cdd:PTZ00047  50 SFQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQC 129

                         90
                 ....*....|....*..
gi 470227334 196 SEICGANHSFMPIVVES 212
Cdd:PTZ00047 130 SEMCGTLHGFMPIVVEA 146
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 94-211 1.71e-33

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: 115.86  E-value: 1.71e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334  94 MTLKAIGHQWYWTYEYTDfkdltfdsymtptsdlpmghfrlLEVDHRVIVPMNSTVRVIVTANDVLHSWAVPSLGVKTDA 173
Cdd:cd13842    1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 470227334 174 IPGRLNQTSFMAPRPGVYYGQCSEICGANHSFMPIVVE 211
Cdd:cd13842   58 VPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 93-206 8.16e-29

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: 104.24  E-value: 8.16e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334  93 DMTLKAIGHQWYWTYEYtdfkdltfdsymtptsdlPMGHFRLLEVDHRVIVPMNSTVRVIVTANDVLHSWAVPSLGVKTD 172
Cdd:cd04213    1 ALTIEVTGHQWWWEFRY------------------PDEPGRGIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMD 62

                         90       100       110
                 ....*....|....*....|....*....|....
gi 470227334 173 AIPGRLNQTSFMAPRPGVYYGQCSEICGANHSFM 206
Cdd:cd04213   63 MIPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 82-221 9.94e-26

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: 97.53  E-value: 9.94e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334  82 ILYLMD---EVNEPDMTLKAIGHQWYWTYEYTDfkDLTFDSYMtptsdlpmghfrllevdhrvIVPMNSTVRVIVTANDV 158
Cdd:cd13918   18 LLYVEDppdEADEDALEVEVEGFQFGWQFEYPN--GVTTGNTL--------------------RVPADTPIALRVTSTDV 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 470227334 159 LHSWAVPSLGVKTDAIPGRLNQTSFMAPRPGVYYGQCSEICGANHSFMPIVVESTPLANFENW 221
Cdd:cd13918   76 FHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAW 138
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-82 2.08e-24

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: 92.39  E-value: 2.08e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334    1 MANHMQLNFQDASSPIMEELMQFHDHALMVALAICSLVLYLLTATLT------SKLTA-NTVNAQVMELVWTILPAMVLI 73
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIrfnrrkNPITArYTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 470227334   74 ALALPSLRI 82
Cdd:pfam02790  81 LIALPSFKL 89
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 93-211 3.95e-24

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: 92.32  E-value: 3.95e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334  93 DMTLKAIGHQWYWTYEYtdfkdltfdsymtPTSDLPMGHFRLLEVDHRVIvPMNSTVRVIVTANDVLHSWAVPSLGVKTD 172
Cdd:cd13919    1 ALVVEVTAQQWAWTFRY-------------PGGDGKLGTDDDVTSPELHL-PVGRPVLFNLRSKDVIHSFWVPEFRVKQD 66

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 470227334 173 AIPGRLNQTSFMAPRPGVYYGQCSEICGANHSFM--PIVVE 211
Cdd:cd13919   67 AVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRMraTVKVV 107
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 93-210 6.19e-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: 88.84  E-value: 6.19e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334  93 DMTLKAIGHQWYWTYEYTDFKdltfdsymTPTSDLpmghfrllevdhrvIVPMNSTVRVIVTANDVLHSWAVPSLGVKTD 172
Cdd:cd13915    1 ALEIQVTGRQWMWEFTYPNGK--------REINEL--------------HVPVGKPVRLILTSKDVIHSFYVPAFRIKQD 58

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 470227334 173 AIPGRLNQTSFMAPRPGVYYGQCSEICGANHSFMPIVV 210
Cdd:cd13915   59 VVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGMIGKV 96
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-221 9.88e-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: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 80.92  E-value: 9.88e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334  95 TLKAIGHQWYWTYEYTDFKDLTFDsymtptsdlpmghfrllevdhRVIVPMNSTVRVIVTANDVLHSWAVPSLGVKTDAI 174
Cdd:cd13914    2 EIEVEAYQWGWEFSYPEANVTTSE---------------------QLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAF 60

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 470227334 175 PGRLNQTSFMAPRPGVYYGQCSEICGANHSFMPIVVESTPLANFENW 221
Cdd:cd13914   61 PGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQW 107
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 143-211 5.11e-12

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: 60.28  E-value: 5.11e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 470227334 143 VPMNSTVRVIVTANDVLHSWAVPSLGVKTDAIPGRLNQTSFMAPRPGVYYGQCSEICGANHSFM--PIVVE 211
Cdd:cd13913   29 VPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNMygKIIVE 99
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-206 4.42e-07

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: 46.61  E-value: 4.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334  95 TLKAIGHQWYWTyeytdfkdltfdsyMTPTSdlpmghfrllevdhrviVPMNSTVRVIVTANDVLHSWAVPS----LGVK 170
Cdd:cd13916    2 VVAVTGHQWYWE--------------LSRTE-----------------IPAGKPVEFRVTSADVNHGFGIYDpdmrLLAQ 50

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 470227334 171 TDAIPGRLNQTSFMAPRPGVYYGQCSEICGANHSFM 206
Cdd:cd13916   51 TQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 148-206 7.94e-07

The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase participates in nitrogen metabolism and catalyzes the last step in dissimilatory nitrate reduction, the two-electron reduction of N2O to N2. It contains copper ions as cofactors in the form of a binuclear CuA center at the site of electron entry and a tetranuclear CuZ centre at the active site. The C-terminus of Nitrous-oxide reductase is a cupredoxin domain.


Pssm-ID: 259885 [Multi-domain]  Cd Length: 95  Bit Score: 46.07  E-value: 7.94e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 470227334 148 TVRVIVT----ANDVLHSWAVPSLGVKTDAIPGRLNQTSFMAPRPGVYYGQCSEICGANHSFM 206
Cdd:cd04223   25 EVTVHLTnleqDEDITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALHLEM 87
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 132-211 1.60e-06

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: 45.68  E-value: 1.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334 132 FRLLEVDHRVIVPMNSTVRVIVT-ANDVLHSWAVPSLGVKTDAI---------------PGRLNQTSFMAPRPGVYYGQC 195
Cdd:cd00920   16 GVLLFGPPVLVVPVGDTVRVQFVnKLGENHSVTIAGFGVPVVAMagganpglvntlvigPGESAEVTFTTDQAGVYWFYC 95

                         90
                 ....*....|....*.
gi 470227334 196 SEICGaNHSFMPIVVE 211
Cdd:cd00920   96 TIPGH-NHAGMVGTIN 110
PRK02888 PRK02888
nitrous-oxide reductase; Validated
 120-206 3.02e-04

nitrous-oxide reductase; Validated


Pssm-ID: 235082 [Multi-domain]  Cd Length: 635  Bit Score: 41.50  E-value: 3.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334 120 YMT---PTSDLPmgHFRLLEVDHrvivpmnstVRVIVT----ANDVLHSWAVPSLGVKTDAIPGRLNQTSFMAPRPGVYY 192
Cdd:PRK02888 544 YMTsqaPAFGLR--EFTVKQGDE---------VTVIVTnldkVEDLTHGFAIPNYGVNMEVAPQATASVTFTADKPGVYW 612

                         90
                 ....*....|....
gi 470227334 193 GQCSEICGANHSFM 206
Cdd:PRK02888 613 YYCTWFCHALHMEM 626
PRK10525 PRK10525
cytochrome o ubiquinol oxidase subunit II; Provisional
 48-221 9.72e-04

cytochrome o ubiquinol oxidase subunit II; Provisional


Pssm-ID: 182518 [Multi-domain]  Cd Length: 315  Bit Score: 39.40  E-value: 9.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334  48 SKLTANTVNAQVMELV-WTIlPAMVLIALALPSLRILYLMD-----EVNEPDMTLKAIGHQWYWTYEYTDFKDLTFDSYM 121
Cdd:PRK10525  76 AKYSPNWSHSNKVEAVvWTV-PILIIIFLAVLTWKTTHALEpskplAHDEKPITIEVVSMDWKWFFIYPEQGIATVNEIA 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470227334 122 TPTsdlpmghfrllevdhrvivpmNSTVRVIVTANDVLHSWAVPSLGVKTDAIPGRLNQTSFMAPRPGVYYGQCSEICGA 201
Cdd:PRK10525 155 FPA---------------------NVPVYFKVTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIANEPGTYDGISASYSGP 213

                        170       180
                 ....*....|....*....|.
gi 470227334 202 NHSFMPIVVESTP-LANFENW 221
Cdd:PRK10525 214 GFSGMKFKAIATPdRAEFDQW 234
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 143-213 2.58e-03

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: 35.99  E-value: 2.58e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 470227334 143 VPMNSTVRVIVTANDVLHSWAVPSLGVKTDAIPGRLNQTSFMAPRPGVYYGQCSEICGANHSFMPIVVEST 213
Cdd:cd04212   29 IPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDMKFKVLAV 99
 
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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