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Conserved domains on  [gi|564813666|gb|AHC03924|]
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cytochrome c oxidase subunit II (mitochondrion) [Molothrus rufoaxillaris]

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 9.33e-166

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 455.91  E-value: 9.33e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666   1 MANHSQLNFQDAASPIMEELMGFHDHALMIALAICSLVLYLLTHTLTEKLS-SNTVNAQVIELVWTILPALVLVTLALPS 79
Cdd:MTH00117   1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLThTNTVDAQEVELIWTILPAIVLILLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666  80 LRILYMMDELNEPDLTLKAIGHQWYWTYEYTDLKDLTFDSYMIPTTDLPLGHFRLLEVDHRVIVPMTSTIRVIVTADDVL 159
Cdd:MTH00117  81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564813666 160 HSWAVPSLGVKTDAIPGRLNQTSFLASRPGVFYGQCSEICGANHSFMPIVVESTPLANFENWSSLMS 226
Cdd:MTH00117 161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLLS 227
 
Name Accession Description Interval E-value
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-226 9.33e-166

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 455.91  E-value: 9.33e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666   1 MANHSQLNFQDAASPIMEELMGFHDHALMIALAICSLVLYLLTHTLTEKLS-SNTVNAQVIELVWTILPALVLVTLALPS 79
Cdd:MTH00117   1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLThTNTVDAQEVELIWTILPAIVLILLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666  80 LRILYMMDELNEPDLTLKAIGHQWYWTYEYTDLKDLTFDSYMIPTTDLPLGHFRLLEVDHRVIVPMTSTIRVIVTADDVL 159
Cdd:MTH00117  81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564813666 160 HSWAVPSLGVKTDAIPGRLNQTSFLASRPGVFYGQCSEICGANHSFMPIVVESTPLANFENWSSLMS 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 1.31e-96

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: 277.53  E-value: 1.31e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666  92 PDLTLKAIGHQWYWTYEYTDLKDLTFDSYMIPTTDLPLGHFRLLEVDHRVIVPMTSTIRVIVTADDVLHSWAVPSLGVKT 171
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 564813666 172 DAIPGRLNQTSFLASRPGVFYGQCSEICGANHSFMPIVVESTPLANFENW 221
Cdd:cd13912   81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
94-213 5.46e-85

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 247.71  E-value: 5.46e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666   94 LTLKAIGHQWYWTYEYTDLKDLTFDSYMIPTTDLPLGHFRLLEVDHRVIVPMTSTIRVIVTADDVLHSWAVPSLGVKTDA 173
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 564813666  174 IPGRLNQTSFLASRPGVFYGQCSEICGANHSFMPIVVEST 213
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-221 8.45e-60

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 187.73  E-value: 8.45e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666   6 QLNFQDAASPIMEELMGFHDHALMIALAICSLVLYLL-----------THTLTEKLSSNTVnaqvIELVWTILPALVLVT 74
Cdd:COG1622   18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLlyfairyrrrkGDADPAQFHHNTK----LEIVWTVIPIIIVIV 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666  75 LALPSLRILYMMDELNEPDLTLKAIGHQWYWTYEYTDLKDLTfdsymipttdlplghfrllevDHRVIVPMTSTIRVIVT 154
Cdd:COG1622   94 LAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIAT---------------------VNELVLPVGRPVRFLLT 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564813666 155 ADDVLHSWAVPSLGVKTDAIPGRLNQTSFLASRPGVFYGQCSEICGANHSFMPIVVESTPLANFENW 221
Cdd:COG1622  153 SADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAW 219
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-221 5.55e-43

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


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 143.68  E-value: 5.55e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666   12 AASPIMEELMGFHDHALMIALAICSLVLYLLTHTL-------TEKLSSNTVNAQVIELVWTILPALVLVTL-ALPSLRIL 83
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVwkfrrkgDEEKPSQIHGNRRLEYVWTVIPLIIVVGLfAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666   84 YMMDELNEPDLTLKAIGHQWYWTYEYTDLkdltfdsymipttdlplghfrLLEVDHRVIVPMTSTIRVIVTADDVLHSWA 163
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFW 139

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 564813666  164 VPSLGVKTDAIPGRLNQTSFLASRPGVFYGQCSEICGANHSFMPIVVESTPLANFENW 221
Cdd:TIGR02866 140 VPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAY 197
 
Name Accession Description Interval E-value
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-226 9.33e-166

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 455.91  E-value: 9.33e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666   1 MANHSQLNFQDAASPIMEELMGFHDHALMIALAICSLVLYLLTHTLTEKLS-SNTVNAQVIELVWTILPALVLVTLALPS 79
Cdd:MTH00117   1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLThTNTVDAQEVELIWTILPAIVLILLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666  80 LRILYMMDELNEPDLTLKAIGHQWYWTYEYTDLKDLTFDSYMIPTTDLPLGHFRLLEVDHRVIVPMTSTIRVIVTADDVL 159
Cdd:MTH00117  81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564813666 160 HSWAVPSLGVKTDAIPGRLNQTSFLASRPGVFYGQCSEICGANHSFMPIVVESTPLANFENWSSLMS 226
Cdd:MTH00117 161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLLS 227
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-225 1.51e-135

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 379.83  E-value: 1.51e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666   1 MANHSQLNFQDAASPIMEELMGFHDHALMIALAICSLVLYLLTHTLTEKLS-SNTVNAQVIELVWTILPALVLVTLALPS 79
Cdd:MTH00098   1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLThTSTMDAQEVETIWTILPAIILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666  80 LRILYMMDELNEPDLTLKAIGHQWYWTYEYTDLKDLTFDSYMIPTTDLPLGHFRLLEVDHRVIVPMTSTIRVIVTADDVL 159
Cdd:MTH00098  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564813666 160 HSWAVPSLGVKTDAIPGRLNQTSFLASRPGVFYGQCSEICGANHSFMPIVVESTPLANFENWSSLM 225
Cdd:MTH00098 161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASM 226
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-225 1.69e-135

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 379.51  E-value: 1.69e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666   1 MANHSQLNFQDAASPIMEELMGFHDHALMIALAICSLVLYLLTHTLTEKLSS-NTVNAQVIELVWTILPALVLVTLALPS 79
Cdd:MTH00076   1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNtNTMDAQEIEMVWTIMPAIILIVIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666  80 LRILYMMDELNEPDLTLKAIGHQWYWTYEYTDLKDLTFDSYMIPTTDLPLGHFRLLEVDHRVIVPMTSTIRVIVTADDVL 159
Cdd:MTH00076  81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564813666 160 HSWAVPSLGVKTDAIPGRLNQTSFLASRPGVFYGQCSEICGANHSFMPIVVESTPLANFENWSSLM 225
Cdd:MTH00076 161 HSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSM 226
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-226 1.44e-134

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 377.25  E-value: 1.44e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666   1 MANHSQLNFQDAASPIMEELMGFHDHALMIALAICSLVLYLLTHTLTEKLSSNTVN-AQVIELVWTILPALVLVTLALPS 79
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLeGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666  80 LRILYMMDELNEPDLTLKAIGHQWYWTYEYTDLKDLTFDSYMIPTTDLPLGHFRLLEVDHRVIVPMTSTIRVIVTADDVL 159
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564813666 160 HSWAVPSLGVKTDAIPGRLNQTSFLASRPGVFYGQCSEICGANHSFMPIVVESTPLANFENWSSLMS 226
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-225 1.48e-134

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 377.13  E-value: 1.48e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666   1 MANHSQLNFQDAASPIMEELMGFHDHALMIALAICSLVLYLLTHTLTEKLSS-NTVNAQVIELVWTILPALVLVTLALPS 79
Cdd:MTH00129   1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNkYILDSQEIEIIWTVLPAVILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666  80 LRILYMMDELNEPDLTLKAIGHQWYWTYEYTDLKDLTFDSYMIPTTDLPLGHFRLLEVDHRVIVPMTSTIRVIVTADDVL 159
Cdd:MTH00129  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564813666 160 HSWAVPSLGVKTDAIPGRLNQTSFLASRPGVFYGQCSEICGANHSFMPIVVESTPLANFENWSSLM 225
Cdd:MTH00129 161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLM 226
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-227 2.17e-125

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 353.86  E-value: 2.17e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666   1 MANHSQLNFQDAASPIMEELMGFHDHALMIALAICSLVLYLLTHTLTEKLSSNTV-NAQVIELVWTILPALVLVTLALPS 79
Cdd:MTH00140   1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTIlEAQKLETIWTIVPALILVFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666  80 LRILYMMDELNEPDLTLKAIGHQWYWTYEYTDLKDLTFDSYMIPTTDLPLGHFRLLEVDHRVIVPMTSTIRVIVTADDVL 159
Cdd:MTH00140  81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564813666 160 HSWAVPSLGVKTDAIPGRLNQTSFLASRPGVFYGQCSEICGANHSFMPIVVESTPLANFENWSSLMSS 227
Cdd:MTH00140 161 HSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELMSE 228
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-223 2.75e-125

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 353.52  E-value: 2.75e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666   1 MANHSQLNFQDAASPIMEELMGFHDHALMIALAICSLVLYLLTHTLTEKLSSNTVN-AQVIELVWTILPALVLVTLALPS 79
Cdd:MTH00168   1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLdSQMIEFVWTIIPAFILISLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666  80 LRILYMMDELNEPDLTLKAIGHQWYWTYEYTDLKDLTFDSYMIPTTDLPLGHFRLLEVDHRVIVPMTSTIRVIVTADDVL 159
Cdd:MTH00168  81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564813666 160 HSWAVPSLGVKTDAIPGRLNQTSFLASRPGVFYGQCSEICGANHSFMPIVVESTPLANFENWSS 223
Cdd:MTH00168 161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVD 224
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-225 2.68e-124

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 351.50  E-value: 2.68e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666   1 MANHSQLNFQDAASPIMEELMGFHDHALMIALAICSLVLYLLTHTLTEKLSSN-TVNAQVIELVWTILPALVLVTLALPS 79
Cdd:MTH00185   1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKyILDSQEIEIVWTILPAIILIMIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666  80 LRILYMMDELNEPDLTLKAIGHQWYWTYEYTDLKDLTFDSYMIPTTDLPLGHFRLLEVDHRVIVPMTSTIRVIVTADDVL 159
Cdd:MTH00185  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564813666 160 HSWAVPSLGVKTDAIPGRLNQTSFLASRPGVFYGQCSEICGANHSFMPIVVESTPLANFENWSSLM 225
Cdd:MTH00185 161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLM 226
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-223 6.66e-122

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 345.15  E-value: 6.66e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666   1 MANHSQLNFQDAASPIMEELMGFHDHALMIALAICSLVLYLLTHTLtekLSSNT----VNAQVIELVWTILPALVLVTLA 76
Cdd:MTH00038   1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLL---FSSPTnrffLEGQELETIWTIVPAFILIFIA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666  77 LPSLRILYMMDELNEPDLTLKAIGHQWYWTYEYTDLKDLTFDSYMIPTTDLPLGHFRLLEVDHRVIVPMTSTIRVIVTAD 156
Cdd:MTH00038  78 LPSLQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSA 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564813666 157 DVLHSWAVPSLGVKTDAIPGRLNQTSFLASRPGVFYGQCSEICGANHSFMPIVVESTPLANFENWSS 223
Cdd:MTH00038 158 DVLHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVS 224
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-221 1.14e-118

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 337.07  E-value: 1.14e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666   1 MANHSQLNFQDAASPIMEELMGFHDHALMIALAICSLVLYLLTHTLTEKLSSNT-VNAQVIELVWTILPALVLVTLALPS 79
Cdd:MTH00139   1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSlLESQEVETIWTVLPAFILLFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666  80 LRILYMMDELNEPDLTLKAIGHQWYWTYEYTDLKDLTFDSYMIPTTDLPLGHFRLLEVDHRVIVPMTSTIRVIVTADDVL 159
Cdd:MTH00139  81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564813666 160 HSWAVPSLGVKTDAIPGRLNQTSFLASRPGVFYGQCSEICGANHSFMPIVVESTPLANFENW 221
Cdd:MTH00139 161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEW 222
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-227 1.15e-112

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 321.81  E-value: 1.15e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666   1 MANHSQLNFQDAASPIMEELMGFHDHALMIALAICSLVLYLLTHTLTEKLSSNTV-NAQVIELVWTILPALVLVTLALPS 79
Cdd:MTH00008   1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYIlEAQQIETIWTILPALILLFLAFPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666  80 LRILYMMDELNEPDLTLKAIGHQWYWTYEYTDLKDLTFDSYMIPTTDLPLGHFRLLEVDHRVIVPMTSTIRVIVTADDVL 159
Cdd:MTH00008  81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564813666 160 HSWAVPSLGVKTDAIPGRLNQTSFLASRPGVFYGQCSEICGANHSFMPIVVESTPLANFENWSSLMSS 227
Cdd:MTH00008 161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSSFAE 228
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 6-227 3.82e-105

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 303.21  E-value: 3.82e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666   6 QLNFQDAASPIMEELMGFHDHALMIALAICSLVLYLLTHTLTEK-LSSNTVNAQVIELVWTILPALVLVTLALPSLRILY 84
Cdd:MTH00023  15 QLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKfYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLY 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666  85 MMDELNEPDLTLKAIGHQWYWTYEYTDLKD--LTFDSYMIPTTDLPLGHFRLLEVDHRVIVPMTSTIRVIVTADDVLHSW 162
Cdd:MTH00023  95 LMDEVVSPALTIKAIGHQWYWSYEYSDYEGetLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSF 174

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564813666 163 AVPSLGVKTDAIPGRLNQTSFLASRPGVFYGQCSEICGANHSFMPIVVESTPLANFENWSSLMSS 227
Cdd:MTH00023 175 AVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLSLSN 239
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 6-221 1.11e-102

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 296.69  E-value: 1.11e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666   6 QLNFQDAASPIMEELMGFHDHALMIALAICSLVLYLLTHTLTEKLSSNTV-NAQVIELVWTILPALVLVTLALPSLRILY 84
Cdd:MTH00051   8 QLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLfEGTLIEIIWTLIPAAILIFIAFPSLKLLY 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666  85 MMDELNEPDLTLKAIGHQWYWTYEYTDL--KDLTFDSYMIPTTDLPLGHFRLLEVDHRVIVPMTSTIRVIVTADDVLHSW 162
Cdd:MTH00051  88 LMDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSF 167

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 564813666 163 AVPSLGVKTDAIPGRLNQTSFLASRPGVFYGQCSEICGANHSFMPIVVESTPLANFENW 221
Cdd:MTH00051 168 AVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINW 226
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 92-221 1.31e-96

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: 277.53  E-value: 1.31e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666  92 PDLTLKAIGHQWYWTYEYTDLKDLTFDSYMIPTTDLPLGHFRLLEVDHRVIVPMTSTIRVIVTADDVLHSWAVPSLGVKT 171
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 564813666 172 DAIPGRLNQTSFLASRPGVFYGQCSEICGANHSFMPIVVESTPLANFENW 221
Cdd:cd13912   81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 6-221 2.68e-85

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 253.79  E-value: 2.68e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666   6 QLNFQDAASPIMEELMGFHDHALMIALAICSLVLYLLTHTLT----EKLSSNTVNAQVIELVWTILPALVLVTLALPSLR 81
Cdd:MTH00027  34 QLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLgnnyYSYYWNKLDGSLIEVIWTLIPAFILILIAFPSLR 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666  82 ILYMMDELN-EPDLTLKAIGHQWYWTYEYTDL--KDLTFDSYMIPTTDLPLGHFRLLEVDHRVIVPMTSTIRVIVTADDV 158
Cdd:MTH00027 114 LLYIMDECGfSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADV 193

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564813666 159 LHSWAVPSLGVKTDAIPGRLNQTSFLASRPGVFYGQCSEICGANHSFMPIVVESTPLANFENW 221
Cdd:MTH00027 194 LHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDW 256
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
94-213 5.46e-85

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 247.71  E-value: 5.46e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666   94 LTLKAIGHQWYWTYEYTDLKDLTFDSYMIPTTDLPLGHFRLLEVDHRVIVPMTSTIRVIVTADDVLHSWAVPSLGVKTDA 173
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 564813666  174 IPGRLNQTSFLASRPGVFYGQCSEICGANHSFMPIVVEST 213
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 7-225 1.81e-78

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 235.29  E-value: 1.81e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666   7 LNFQDAASPI-MEELMGFHDHALMIALAICSLV-LYLLTHTLTEKLSSNTVNAQVIELVWTILPALVLVTLALPSLRILY 84
Cdd:MTH00080   8 LNFSNSLFSSyMDWFHNFNCSLLFGEFVLAFVVfLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLY 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666  85 MMDELN-EPDLTLKAIGHQWYWTYEYTDLKDLTFDSYMIPTTDLPLGHFRLLEVDHRVIVPMTSTIRVIVTADDVLHSWA 163
Cdd:MTH00080  88 YYGLMNlDSNLTVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWA 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564813666 164 VPSLGVKTDAIPGRLNQTSFLASRPGVFYGQCSEICGANHSFMPIVVESTPLANFENWSSLM 225
Cdd:MTH00080 168 LPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWCKLL 229
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-221 8.45e-60

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 187.73  E-value: 8.45e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666   6 QLNFQDAASPIMEELMGFHDHALMIALAICSLVLYLL-----------THTLTEKLSSNTVnaqvIELVWTILPALVLVT 74
Cdd:COG1622   18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLlyfairyrrrkGDADPAQFHHNTK----LEIVWTVIPIIIVIV 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666  75 LALPSLRILYMMDELNEPDLTLKAIGHQWYWTYEYTDLKDLTfdsymipttdlplghfrllevDHRVIVPMTSTIRVIVT 154
Cdd:COG1622   94 LAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIAT---------------------VNELVLPVGRPVRFLLT 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564813666 155 ADDVLHSWAVPSLGVKTDAIPGRLNQTSFLASRPGVFYGQCSEICGANHSFMPIVVESTPLANFENW 221
Cdd:COG1622  153 SADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAW 219
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 57-211 3.94e-46

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 151.65  E-value: 3.94e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666  57 AQVIELVWTILPA-LVLVTLALPSLRILYMMDelNEPDLTLKAIGHQWYWTYEYTDlkDLTFDSYMiptTDLPLGhfrll 135
Cdd:MTH00047  46 NQVLELLWTVVPTlLVLVLCFLNLNFITSDLD--CFSSETIKVIGHQWYWSYEYSF--GGSYDSFM---TDDIFG----- 113

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564813666 136 eVDHRVIVPMTSTIRVIVTADDVLHSWAVPSLGVKTDAIPGRLNQTSFLASRPGVFYGQCSEICGANHSFMPIVVE 211
Cdd:MTH00047 114 -VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIE 188
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-221 5.55e-43

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


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 143.68  E-value: 5.55e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666   12 AASPIMEELMGFHDHALMIALAICSLVLYLLTHTL-------TEKLSSNTVNAQVIELVWTILPALVLVTL-ALPSLRIL 83
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVwkfrrkgDEEKPSQIHGNRRLEYVWTVIPLIIVVGLfAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666   84 YMMDELNEPDLTLKAIGHQWYWTYEYTDLkdltfdsymipttdlplghfrLLEVDHRVIVPMTSTIRVIVTADDVLHSWA 163
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFW 139

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 564813666  164 VPSLGVKTDAIPGRLNQTSFLASRPGVFYGQCSEICGANHSFMPIVVESTPLANFENW 221
Cdd:TIGR02866 140 VPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAY 197
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 116-212 1.71e-39

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 133.41  E-value: 1.71e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666 116 TFDSYMIPTTDLPLGHFRLLEVDHRVIVPMTSTIRVIVTADDVLHSWAVPSLGVKTDAIPGRLNQTSFLASRPGVFYGQC 195
Cdd:PTZ00047  50 SFQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQC 129

                         90
                 ....*....|....*..
gi 564813666 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 1.61e-30

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: 108.15  E-value: 1.61e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666  94 LTLKAIGHQWYWTYEYTDLkdltfdsymipttdlplghfrllEVDHRVIVPMTSTIRVIVTADDVLHSWAVPSLGVKTDA 173
Cdd:cd13842    1 LTVYVTGVQWSWTFIYPNV-----------------------RTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 564813666 174 IPGRLNQTSFLASRPGVFYGQCSEICGANHSFMPIVVE 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 7.41e-28

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


Pssm-ID: 259875 [Multi-domain]  Cd Length: 103  Bit Score: 101.54  E-value: 7.41e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666  93 DLTLKAIGHQWYWTYEYTDLKDLTFdsymipttdlplghfrllEVDHRVIVPMTSTIRVIVTADDVLHSWAVPSLGVKTD 172
Cdd:cd04213    1 ALTIEVTGHQWWWEFRYPDEPGRGI------------------VTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMD 62

                         90       100       110
                 ....*....|....*....|....*....|....
gi 564813666 173 AIPGRLNQTSFLASRPGVFYGQCSEICGANHSFM 206
Cdd:cd04213   63 MIPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-82 1.03e-25

Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C oxidase contains two transmembrane alpha-helices.


Pssm-ID: 397083 [Multi-domain]  Cd Length: 89  Bit Score: 95.86  E-value: 1.03e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666    1 MANHSQLNFQDAASPIMEELMGFHDHALMIALAICSLVLYLLTHTLTEKLSS-------NTVNAQVIELVWTILPALVLV 73
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRFNRRknpitarYTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 564813666   74 TLALPSLRI 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 5.93e-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: 91.93  E-value: 5.93e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666  93 DLTLKAIGHQWYWTYEY--TDLKDLTFDSYMIPTTDLPLGHfrllevdhrvivpmtsTIRVIVTADDVLHSWAVPSLGVK 170
Cdd:cd13919    1 ALVVEVTAQQWAWTFRYpgGDGKLGTDDDVTSPELHLPVGR----------------PVLFNLRSKDVIHSFWVPEFRVK 64

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 564813666 171 TDAIPGRLNQTSFLASRPGVFYGQCSEICGANHSFM--PIVVE 211
Cdd:cd13919   65 QDAVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRMraTVKVV 107
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 87-221 1.53e-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: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 91.75  E-value: 1.53e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666  87 DELNEPDLTLKAIGHQWYWTYEYTDlkDLTFDSYMIpttdlplghfrllevdhrviVPMTSTIRVIVTADDVLHSWAVPS 166
Cdd:cd13918   26 DEADEDALEVEVEGFQFGWQFEYPN--GVTTGNTLR--------------------VPADTPIALRVTSTDVFHTFGIPE 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 564813666 167 LGVKTDAIPGRLNQTSFLASRPGVFYGQCSEICGANHSFMPIVVESTPLANFENW 221
Cdd:cd13918   84 LRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAW 138
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 93-210 1.20e-20

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


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 83.06  E-value: 1.20e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666  93 DLTLKAIGHQWYWTYEYTDLKdltfdsymipttdlplghfrllEVDHRVIVPMTSTIRVIVTADDVLHSWAVPSLGVKTD 172
Cdd:cd13915    1 ALEIQVTGRQWMWEFTYPNGK----------------------REINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQD 58

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 564813666 173 AIPGRLNQTSFLASRPGVFYGQCSEICGANHSFMPIVV 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 1.70e-18

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: 77.45  E-value: 1.70e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666  95 TLKAIGHQWYWTYEYTDLKDLTFDSYMIPTtDLPLghfrllevdhrvivpmtsTIRVivTADDVLHSWAVPSLGVKTDAI 174
Cdd:cd13914    2 EIEVEAYQWGWEFSYPEANVTTSEQLVIPA-DRPV------------------YFRI--TSRDVIHAFHVPELGLKQDAF 60

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 564813666 175 PGRLNQTSFLASRPGVFYGQCSEICGANHSFMPIVVESTPLANFENW 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 2.03e-09

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: 52.96  E-value: 2.03e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564813666 143 VPMTSTIRVIVTADDVLHSWAVPSLGVKTDAIPGRLNQTSFLASRPGVFYGQCSEICGANHSFM--PIVVE 211
Cdd:cd13913   29 VPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNMygKIIVE 99
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 148-206 4.66e-06

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: 43.76  E-value: 4.66e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564813666 148 TIRVIVT----ADDVLHSWAVPSLGVKTDAIPGRLNQTSFLASRPGVFYGQCSEICGANHSFM 206
Cdd:cd04223   25 EVTVHLTnleqDEDITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALHLEM 87
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 132-211 5.31e-05

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: 41.06  E-value: 5.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666 132 FRLLEVDHRVIVPMTSTIRVIVT-ADDVLHSWAVPSLGVKTDAI---------------PGRLNQTSFLASRPGVFYGQC 195
Cdd:cd00920   16 GVLLFGPPVLVVPVGDTVRVQFVnKLGENHSVTIAGFGVPVVAMagganpglvntlvigPGESAEVTFTTDQAGVYWFYC 95

                         90
                 ....*....|....*.
gi 564813666 196 SEICGaNHSFMPIVVE 211
Cdd:cd00920   96 TIPGH-NHAGMVGTIN 110
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-206 5.90e-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: 40.83  E-value: 5.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666  95 TLKAIGHQWYWTyeytdlkdltfdsymIPTTDLPLGhfrllevdhrvivpmtSTIRVIVTADDVLHSWAVPS----LGVK 170
Cdd:cd13916    2 VVAVTGHQWYWE---------------LSRTEIPAG----------------KPVEFRVTSADVNHGFGIYDpdmrLLAQ 50

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 564813666 171 TDAIPGRLNQTSFLASRPGVFYGQCSEICGANHSFM 206
Cdd:cd13916   51 TQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
PRK10525 PRK10525
cytochrome o ubiquinol oxidase subunit II; Provisional
 49-221 1.80e-04

cytochrome o ubiquinol oxidase subunit II; Provisional


Pssm-ID: 182518 [Multi-domain]  Cd Length: 315  Bit Score: 41.71  E-value: 1.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666  49 KLSSNTVNAQVIELV-WTIlPALVLVTLALPSLRILYMMDEL-----NEPDLTLKAIGHQWYWTYEYTDLKDLTFDSYMI 122
Cdd:PRK10525  77 KYSPNWSHSNKVEAVvWTV-PILIIIFLAVLTWKTTHALEPSkplahDEKPITIEVVSMDWKWFFIYPEQGIATVNEIAF 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666 123 PTtDLPLgHFRllevdhrvivpmtstirviVTADDVLHSWAVPSLGVKTDAIPGRLNQTSFLASRPGVFYGQCSEICGAN 202
Cdd:PRK10525 156 PA-NVPV-YFK-------------------VTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIANEPGTYDGISASYSGPG 214

                        170       180
                 ....*....|....*....|
gi 564813666 203 HSFMPIVVESTP-LANFENW 221
Cdd:PRK10525 215 FSGMKFKAIATPdRAEFDQW 234
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 94-213 2.44e-04

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


Pssm-ID: 259874 [Multi-domain]  Cd Length: 99  Bit Score: 39.07  E-value: 2.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666  94 LTLKAIGHQWYWTYEYTDLKDLTFDSYMIPTtDLPLgHFRLlevdhrvivpmtstirvivTADDVLHSWAVPSLGVKTDA 173
Cdd:cd04212    1 LEIQVVSLDWKWLFIYPEQGIATVNELVIPV-GRPV-NFRL-------------------TSDSVMNSFFIPQLGGQIYA 59

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 564813666 174 IPGRLNQTSFLASRPGVFYGQCSEICGANHSFMPIVVEST 213
Cdd:cd04212   60 MAGMQTQLHLIADKPGTYQGLSANYSGEGFSDMKFKVLAV 99
PRK02888 PRK02888
nitrous-oxide reductase; Validated
 135-206 6.78e-04

nitrous-oxide reductase; Validated


Pssm-ID: 235082 [Multi-domain]  Cd Length: 635  Bit Score: 40.35  E-value: 6.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813666 135 LEVDHRVI-------VPMTST----------------IRVIVT----ADDVLHSWAVPSLGVKTDAIPGRLNQTSFLASR 187
Cdd:PRK02888 528 LEEDSKVIrdgnkvrVYMTSQapafglreftvkqgdeVTVIVTnldkVEDLTHGFAIPNYGVNMEVAPQATASVTFTADK 607

                         90
                 ....*....|....*....
gi 564813666 188 PGVFYGQCSEICGANHSFM 206
Cdd:PRK02888 608 PGVYWYYCTWFCHALHMEM 626
 
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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