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Conserved domains on  [gi|2172609360|ref|YP_010230727|]
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cytochrome c oxidase subunit II (mitochondrion) [Cacatua alba]

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
 1-225 1.99e-164

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 452.45  E-value: 1.99e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172609360   1 MANQSQLAFQDASSPIMEELVEFHDHALMVALMICSLVLYLLTLMLMEKLS-SNTVDAQEIELIWTILPAIVLILLALPS 79
Cdd:MTH00117    1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLThTNTVDAQEVELIWTILPAIVLILLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172609360  80 LQILYMMDEIDEPDLTLKAIGHQWYWSYEYTDFKDLSFDSYMLPTTELPLGHFRLLEVDHRVVLPMESPIRIIVTADDVL 159
Cdd:MTH00117   81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2172609360 160 HSWTVPTLGVKTDAIPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESTPLTYFENWSSLL 225
Cdd:MTH00117  161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLL 226
 
Name Accession Description Interval E-value
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-225 1.99e-164

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 452.45  E-value: 1.99e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172609360   1 MANQSQLAFQDASSPIMEELVEFHDHALMVALMICSLVLYLLTLMLMEKLS-SNTVDAQEIELIWTILPAIVLILLALPS 79
Cdd:MTH00117    1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLThTNTVDAQEVELIWTILPAIVLILLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172609360  80 LQILYMMDEIDEPDLTLKAIGHQWYWSYEYTDFKDLSFDSYMLPTTELPLGHFRLLEVDHRVVLPMESPIRIIVTADDVL 159
Cdd:MTH00117   81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2172609360 160 HSWTVPTLGVKTDAIPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESTPLTYFENWSSLL 225
Cdd:MTH00117  161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLL 226
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 92-221 1.05e-95

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: 275.22  E-value: 1.05e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172609360  92 PDLTLKAIGHQWYWSYEYTDFKDLSFDSYMLPTTELPLGHFRLLEVDHRVVLPMESPIRIIVTADDVLHSWTVPTLGVKT 171
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2172609360 172 DAIPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESTPLTYFENW 221
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
94-213 8.68e-86

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 249.63  E-value: 8.68e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172609360  94 LTLKAIGHQWYWSYEYTDFKDLSFDSYMLPTTELPLGHFRLLEVDHRVVLPMESPIRIIVTADDVLHSWTVPTLGVKTDA 173
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2172609360 174 IPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVEST 213
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
60-221 7.66e-55

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 175.02  E-value: 7.66e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172609360  60 IELIWTILPAIVLILLALPSLQILYMMDEIDEPDLTLKAIGHQWYWSYEYTDFKDLsfdsymlpttelplghfrlleVDH 139
Cdd:COG1622    79 LEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVN 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172609360 140 RVVLPMESPIRIIVTADDVLHSWTVPTLGVKTDAIPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESTPLTYFE 219
Cdd:COG1622   138 ELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFD 217


                  ..
gi 2172609360 220 NW 221
Cdd:COG1622   218 AW 219
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-221 2.93e-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: 144.45  E-value: 2.93e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172609360  12 ASSPIMEELVEFHDHALMVALMICSLVLYLLTLMLM-------EKLSSNTVDAQEIELIWTILPA-IVLILLALPSLQIL 83
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVWkfrrkgdEEKPSQIHGNRRLEYVWTVIPLiIVVGLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172609360  84 YMMDEIDEPDLTLKAIGHQWYWSYEYTDFkdlsfdsymlpttelplghfrLLEVDHRVVLPMESPIRIIVTADDVLHSWT 163
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFW 139

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2172609360 164 VPTLGVKTDAIPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESTPLTYFENW 221
Cdd:TIGR02866 140 VPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAY 197
 
Name Accession Description Interval E-value
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-225 1.99e-164

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 452.45  E-value: 1.99e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172609360   1 MANQSQLAFQDASSPIMEELVEFHDHALMVALMICSLVLYLLTLMLMEKLS-SNTVDAQEIELIWTILPAIVLILLALPS 79
Cdd:MTH00117    1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLThTNTVDAQEVELIWTILPAIVLILLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172609360  80 LQILYMMDEIDEPDLTLKAIGHQWYWSYEYTDFKDLSFDSYMLPTTELPLGHFRLLEVDHRVVLPMESPIRIIVTADDVL 159
Cdd:MTH00117   81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2172609360 160 HSWTVPTLGVKTDAIPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESTPLTYFENWSSLL 225
Cdd:MTH00117  161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLL 226
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-225 3.25e-133

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 373.67  E-value: 3.25e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172609360   1 MANQSQLAFQDASSPIMEELVEFHDHALMVALMICSLVLYLLTLMLMEKLS-SNTVDAQEIELIWTILPAIVLILLALPS 79
Cdd:MTH00098    1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLThTSTMDAQEVETIWTILPAIILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172609360  80 LQILYMMDEIDEPDLTLKAIGHQWYWSYEYTDFKDLSFDSYMLPTTELPLGHFRLLEVDHRVVLPMESPIRIIVTADDVL 159
Cdd:MTH00098   81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2172609360 160 HSWTVPTLGVKTDAIPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESTPLTYFENWSSLL 225
Cdd:MTH00098  161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASM 226
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-223 7.27e-133

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 372.62  E-value: 7.27e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172609360   1 MANQSQLAFQDASSPIMEELVEFHDHALMVALMICSLVLYLLTLMLMEKLSS-NTVDAQEIELIWTILPAIVLILLALPS 79
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNrFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172609360  80 LQILYMMDEIDEPDLTLKAIGHQWYWSYEYTDFKDLSFDSYMLPTTELPLGHFRLLEVDHRVVLPMESPIRIIVTADDVL 159
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2172609360 160 HSWTVPTLGVKTDAIPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESTPLTYFENWSS 223
Cdd:MTH00154  161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIK 224
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-225 1.63e-132

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 372.12  E-value: 1.63e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172609360   1 MANQSQLAFQDASSPIMEELVEFHDHALMVALMICSLVLYLLTLMLMEKLSS-NTVDAQEIELIWTILPAIVLILLALPS 79
Cdd:MTH00129    1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNkYILDSQEIEIIWTVLPAVILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172609360  80 LQILYMMDEIDEPDLTLKAIGHQWYWSYEYTDFKDLSFDSYMLPTTELPLGHFRLLEVDHRVVLPMESPIRIIVTADDVL 159
Cdd:MTH00129   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2172609360 160 HSWTVPTLGVKTDAIPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESTPLTYFENWSSLL 225
Cdd:MTH00129  161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLM 226
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-224 2.22e-131

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 369.11  E-value: 2.22e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172609360   1 MANQSQLAFQDASSPIMEELVEFHDHALMVALMICSLVLYLLTLMLMEKLSS-NTVDAQEIELIWTILPAIVLILLALPS 79
Cdd:MTH00076    1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNtNTMDAQEIEMVWTIMPAIILIVIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172609360  80 LQILYMMDEIDEPDLTLKAIGHQWYWSYEYTDFKDLSFDSYMLPTTELPLGHFRLLEVDHRVVLPMESPIRIIVTADDVL 159
Cdd:MTH00076   81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2172609360 160 HSWTVPTLGVKTDAIPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESTPLTYFENWSSL 224
Cdd:MTH00076  161 HSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSS 225
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-225 3.02e-123

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 348.80  E-value: 3.02e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172609360   1 MANQSQLAFQDASSPIMEELVEFHDHALMVALMICSLVLYLLTLMLMEKLSSN-TVDAQEIELIWTILPAIVLILLALPS 79
Cdd:MTH00185    1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKyILDSQEIEIVWTILPAIILIMIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172609360  80 LQILYMMDEIDEPDLTLKAIGHQWYWSYEYTDFKDLSFDSYMLPTTELPLGHFRLLEVDHRVVLPMESPIRIIVTADDVL 159
Cdd:MTH00185   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2172609360 160 HSWTVPTLGVKTDAIPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESTPLTYFENWSSLL 225
Cdd:MTH00185  161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLM 226
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-223 2.20e-122

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 346.20  E-value: 2.20e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172609360   1 MANQSQLAFQDASSPIMEELVEFHDHALMVALMICSLVLYLLTLMLMEKLSSNTV-DAQEIELIWTILPAIVLILLALPS 79
Cdd:MTH00168    1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLlDSQMIEFVWTIIPAFILISLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172609360  80 LQILYMMDEIDEPDLTLKAIGHQWYWSYEYTDFKDLSFDSYMLPTTELPLGHFRLLEVDHRVVLPMESPIRIIVTADDVL 159
Cdd:MTH00168   81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2172609360 160 HSWTVPTLGVKTDAIPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESTPLTYFENWSS 223
Cdd:MTH00168  161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVD 224
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-227 9.46e-121

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 342.30  E-value: 9.46e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172609360   1 MANQSQLAFQDASSPIMEELVEFHDHALMVALMICSLVLYLLTLMLMEKLSSNTV-DAQEIELIWTILPAIVLILLALPS 79
Cdd:MTH00140    1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTIlEAQKLETIWTIVPALILVFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172609360  80 LQILYMMDEIDEPDLTLKAIGHQWYWSYEYTDFKDLSFDSYMLPTTELPLGHFRLLEVDHRVVLPMESPIRIIVTADDVL 159
Cdd:MTH00140   81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2172609360 160 HSWTVPTLGVKTDAIPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESTPLTYFENWSSLLAS 227
Cdd:MTH00140  161 HSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELMSE 228
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-223 1.22e-118

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 337.06  E-value: 1.22e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172609360   1 MANQSQLAFQDASSPIMEELVEFHDHALMVALMICSLVLYLLTLMLmekLSSNT----VDAQEIELIWTILPAIVLILLA 76
Cdd:MTH00038    1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLL---FSSPTnrffLEGQELETIWTIVPAFILIFIA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172609360  77 LPSLQILYMMDEIDEPDLTLKAIGHQWYWSYEYTDFKDLSFDSYMLPTTELPLGHFRLLEVDHRVVLPMESPIRIIVTAD 156
Cdd:MTH00038   78 LPSLQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSA 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2172609360 157 DVLHSWTVPTLGVKTDAIPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESTPLTYFENWSS 223
Cdd:MTH00038  158 DVLHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVS 224
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-221 2.78e-115

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 328.21  E-value: 2.78e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172609360   1 MANQSQLAFQDASSPIMEELVEFHDHALMVALMICSLVLYLLTLMLMEKLSSNT-VDAQEIELIWTILPAIVLILLALPS 79
Cdd:MTH00139    1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSlLESQEVETIWTVLPAFILLFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172609360  80 LQILYMMDEIDEPDLTLKAIGHQWYWSYEYTDFKDLSFDSYMLPTTELPLGHFRLLEVDHRVVLPMESPIRIIVTADDVL 159
Cdd:MTH00139   81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2172609360 160 HSWTVPTLGVKTDAIPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESTPLTYFENW 221
Cdd:MTH00139  161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEW 222
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-227 3.49e-112

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 320.65  E-value: 3.49e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172609360   1 MANQSQLAFQDASSPIMEELVEFHDHALMVALMICSLVLYLLTLMLMEKLSSNTV-DAQEIELIWTILPAIVLILLALPS 79
Cdd:MTH00008    1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYIlEAQQIETIWTILPALILLFLAFPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172609360  80 LQILYMMDEIDEPDLTLKAIGHQWYWSYEYTDFKDLSFDSYMLPTTELPLGHFRLLEVDHRVVLPMESPIRIIVTADDVL 159
Cdd:MTH00008   81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2172609360 160 HSWTVPTLGVKTDAIPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESTPLTYFENWSSLLAS 227
Cdd:MTH00008  161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSSFAE 228
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 6-227 1.94e-99

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 288.96  E-value: 1.94e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172609360   6 QLAFQDASSPIMEELVEFHDHALMVALMICSLVLYLLTLMLMEK-LSSNTVDAQEIELIWTILPAIVLILLALPSLQILY 84
Cdd:MTH00023   15 QLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKfYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLY 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172609360  85 MMDEIDEPDLTLKAIGHQWYWSYEYTDFKD--LSFDSYMLPTTELPLGHFRLLEVDHRVVLPMESPIRIIVTADDVLHSW 162
Cdd:MTH00023   95 LMDEVVSPALTIKAIGHQWYWSYEYSDYEGetLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSF 174

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2172609360 163 TVPTLGVKTDAIPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESTPLTYFENWSSLLAS 227
Cdd:MTH00023  175 AVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLSLSN 239
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 92-221 1.05e-95

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: 275.22  E-value: 1.05e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172609360  92 PDLTLKAIGHQWYWSYEYTDFKDLSFDSYMLPTTELPLGHFRLLEVDHRVVLPMESPIRIIVTADDVLHSWTVPTLGVKT 171
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2172609360 172 DAIPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESTPLTYFENW 221
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 6-221 7.09e-95

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 277.05  E-value: 7.09e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172609360   6 QLAFQDASSPIMEELVEFHDHALMVALMICSLVLYLLTLMLMEKLSSNTV-DAQEIELIWTILPAIVLILLALPSLQILY 84
Cdd:MTH00051    8 QLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLfEGTLIEIIWTLIPAAILIFIAFPSLKLLY 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172609360  85 MMDEIDEPDLTLKAIGHQWYWSYEYTDF--KDLSFDSYMLPTTELPLGHFRLLEVDHRVVLPMESPIRIIVTADDVLHSW 162
Cdd:MTH00051   88 LMDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSF 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2172609360 163 TVPTLGVKTDAIPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESTPLTYFENW 221
Cdd:MTH00051  168 AVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINW 226
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
94-213 8.68e-86

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 249.63  E-value: 8.68e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172609360  94 LTLKAIGHQWYWSYEYTDFKDLSFDSYMLPTTELPLGHFRLLEVDHRVVLPMESPIRIIVTADDVLHSWTVPTLGVKTDA 173
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2172609360 174 IPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVEST 213
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 6-221 1.05e-81

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 244.55  E-value: 1.05e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172609360   6 QLAFQDASSPIMEELVEFHDHALMVALMICSLVLYLLTLMLM----EKLSSNTVDAQEIELIWTILPAIVLILLALPSLQ 81
Cdd:MTH00027   34 QLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLgnnyYSYYWNKLDGSLIEVIWTLIPAFILILIAFPSLR 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172609360  82 ILYMMDE-IDEPDLTLKAIGHQWYWSYEYTDF--KDLSFDSYMLPTTELPLGHFRLLEVDHRVVLPMESPIRIIVTADDV 158
Cdd:MTH00027  114 LLYIMDEcGFSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADV 193

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2172609360 159 LHSWTVPTLGVKTDAIPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESTPLTYFENW 221
Cdd:MTH00027  194 LHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDW 256
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 49-225 7.88e-74

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 223.35  E-value: 7.88e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172609360  49 KLSSNTVDAQEIELIWTILPAIVLILLALPSLQILYMMDEID-EPDLTLKAIGHQWYWSYEYTDFKDLSFDSYMLPTTEL 127
Cdd:MTH00080   52 YFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMNlDSNLTVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQL 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172609360 128 PLGHFRLLEVDHRVVLPMESPIRIIVTADDVLHSWTVPTLGVKTDAIPGRLNQTSFITTRPGVFYGQCSEICGANHSFMP 207
Cdd:MTH00080  132 RLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMP 211

                         170
                  ....*....|....*...
gi 2172609360 208 IVVESTPLTYFENWSSLL 225
Cdd:MTH00080  212 IAVEVTLLDNFKEWCKLL 229
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
60-221 7.66e-55

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 175.02  E-value: 7.66e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172609360  60 IELIWTILPAIVLILLALPSLQILYMMDEIDEPDLTLKAIGHQWYWSYEYTDFKDLsfdsymlpttelplghfrlleVDH 139
Cdd:COG1622    79 LEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVN 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172609360 140 RVVLPMESPIRIIVTADDVLHSWTVPTLGVKTDAIPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESTPLTYFE 219
Cdd:COG1622   138 ELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFD 217


                  ..
gi 2172609360 220 NW 221
Cdd:COG1622   218 AW 219
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 56-211 2.57e-47

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 154.73  E-value: 2.57e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172609360  56 DAQEIELIWTILPA-IVLILLALPSLQILYMMDeiDEPDLTLKAIGHQWYWSYEYTDfkDLSFDSYMlptTELPLGhfrl 134
Cdd:MTH00047   45 ENQVLELLWTVVPTlLVLVLCFLNLNFITSDLD--CFSSETIKVIGHQWYWSYEYSF--GGSYDSFM---TDDIFG---- 113

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2172609360 135 leVDHRVVLPMESPIRIIVTADDVLHSWTVPTLGVKTDAIPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVE 211
Cdd:MTH00047  114 --VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIE 188
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-221 2.93e-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: 144.45  E-value: 2.93e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172609360  12 ASSPIMEELVEFHDHALMVALMICSLVLYLLTLMLM-------EKLSSNTVDAQEIELIWTILPA-IVLILLALPSLQIL 83
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVWkfrrkgdEEKPSQIHGNRRLEYVWTVIPLiIVVGLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172609360  84 YMMDEIDEPDLTLKAIGHQWYWSYEYTDFkdlsfdsymlpttelplghfrLLEVDHRVVLPMESPIRIIVTADDVLHSWT 163
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFW 139

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2172609360 164 VPTLGVKTDAIPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESTPLTYFENW 221
Cdd:TIGR02866 140 VPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAY 197
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 116-217 1.60e-38

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 131.10  E-value: 1.60e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172609360 116 SFDSYMLPTTELPLGHFRLLEVDHRVVLPMESPIRIIVTADDVLHSWTVPTLGVKTDAIPGRLNQTSFITTRPGVFYGQC 195
Cdd:PTZ00047   50 SFQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQC 129

                          90       100
                  ....*....|....*....|...
gi 2172609360 196 SEICGANHSFMPIVVES-TPLTY 217
Cdd:PTZ00047  130 SEMCGTLHGFMPIVVEAvSPEAY 152
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 94-211 1.84e-32

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: 113.16  E-value: 1.84e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172609360  94 LTLKAIGHQWYWSYEYTDfkdlsfdsymlpttelplghfrlLEVDHRVVLPMESPIRIIVTADDVLHSWTVPTLGVKTDA 173
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2172609360 174 IPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVE 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 1.12e-28

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


Pssm-ID: 259875 [Multi-domain]  Cd Length: 103  Bit Score: 103.85  E-value: 1.12e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172609360  93 DLTLKAIGHQWYWSYEYTDFKDLSFDSymlpTTELplghfrllevdhrvVLPMESPIRIIVTADDVLHSWTVPTLGVKTD 172
Cdd:cd04213     1 ALTIEVTGHQWWWEFRYPDEPGRGIVT----ANEL--------------HIPVGRPVRLRLTSADVIHSFWVPSLAGKMD 62

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2172609360 173 AIPGRLNQTSFITTRPGVFYGQCSEICGANHSFM 206
Cdd:cd04213    63 MIPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 70-221 1.10e-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: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 94.83  E-value: 1.10e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172609360  70 IVLILLALPSLQILYMMD---EIDEPDLTLKAIGHQWYWSYEYTDfkDLSFDSYMlpttelplghfrllevdhrvVLPME 146
Cdd:cd13918     6 IVISLIVWTYGMLLYVEDppdEADEDALEVEVEGFQFGWQFEYPN--GVTTGNTL--------------------RVPAD 63

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2172609360 147 SPIRIIVTADDVLHSWTVPTLGVKTDAIPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESTPLTYFENW 221
Cdd:cd13918    64 TPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAW 138
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 93-211 1.24e-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: 93.47  E-value: 1.24e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172609360  93 DLTLKAIGHQWYWSYEYTDFKDLSFDSYMLPTTELplghfrllevdhrvVLPMESPIRIIVTADDVLHSWTVPTLGVKTD 172
Cdd:cd13919     1 ALVVEVTAQQWAWTFRYPGGDGKLGTDDDVTSPEL--------------HLPVGRPVLFNLRSKDVIHSFWVPEFRVKQD 66

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2172609360 173 AIPGRLNQTSFITTRPGVFYGQCSEICGANHSFM--PIVVE 211
Cdd:cd13919    67 AVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRMraTVKVV 107
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-82 9.03e-22

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: 85.46  E-value: 9.03e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172609360   1 MANQSQLAFQDASSPIMEELVEFHDHALMVALMICSLVLYLLTLMLMEKLSS-------NTVDAQEIELIWTILPAIVLI 73
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRFNRRknpitarYTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 2172609360  74 LLALPSLQI 82
Cdd:pfam02790  81 LIALPSFKL 89
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 93-210 8.43e-21

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


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 83.45  E-value: 8.43e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172609360  93 DLTLKAIGHQWYWSYEYTDFKdlsfdsymlpttelplghfrllEVDHRVVLPMESPIRIIVTADDVLHSWTVPTLGVKTD 172
Cdd:cd13915     1 ALEIQVTGRQWMWEFTYPNGK----------------------REINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQD 58

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2172609360 173 AIPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVV 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 2.52e-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: 77.06  E-value: 2.52e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172609360  95 TLKAIGHQWYWSYEYTDFKDLSFDsymlpttelplghfrllevdhRVVLPMESPIRIIVTADDVLHSWTVPTLGVKTDAI 174
Cdd:cd13914     2 EIEVEAYQWGWEFSYPEANVTTSE---------------------QLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAF 60

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2172609360 175 PGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESTPLTYFENW 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 ...
 141-211 7.16e-10

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: 54.50  E-value: 7.16e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2172609360 141 VVLPMESPIRIIVTADDVLHSWTVPTLGVKTDAIPGRLNQTSFITTRPGVFYGQCSEICGANHSFM--PIVVE 211
Cdd:cd13913    27 IEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNMygKIIVE 99
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-206 3.44e-06

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: 44.29  E-value: 3.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172609360  95 TLKAIGHQWYWSyeytdfkdlsfdsymLPTTELPLGhfrllevdhrvvlpmeSPIRIIVTADDVLHSWTV----PTLGVK 170
Cdd:cd13916     2 VVAVTGHQWYWE---------------LSRTEIPAG----------------KPVEFRVTSADVNHGFGIydpdMRLLAQ 50

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2172609360 171 TDAIPGRLNQTSFITTRPGVFYGQCSEICGANHSFM 206
Cdd:cd13916    51 TQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 151-211 1.30e-04

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: 40.29  E-value: 1.30e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2172609360 151 IIVTADDVLHSWTVPTLGVKTDAI---------------PGRLNQTSFITTRPGVFYGQCSEICGaNHSFMPIVVE 211
Cdd:cd00920    36 QFVNKLGENHSVTIAGFGVPVVAMagganpglvntlvigPGESAEVTFTTDQAGVYWFYCTIPGH-NHAGMVGTIN 110
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 149-206 1.53e-04

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: 39.53  E-value: 1.53e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2172609360 149 IRIIVT----ADDVLHSWTVPTLGVKTDAIPGRLNQTSFITTRPGVFYGQCSEICGANHSFM 206
Cdd:cd04223    26 VTVHLTnleqDEDITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALHLEM 87
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 141-213 2.88e-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: 38.68  E-value: 2.88e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2172609360 141 VVLPMESPIRIIVTADDVLHSWTVPTLGVKTDAIPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVEST 213
Cdd:cd04212    27 LVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDMKFKVLAV 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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