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Conserved domains on  [gi|1511244826|ref|YP_009531182|]
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cytochrome c oxidase subunit II (mitochondrion) [Ornebius fuscicerci]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11475927)

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 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-224 1.81e-128

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 361.84  E-value: 1.81e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511244826   1 MSTWSNLNFQNGSSPLMEQLTFFHDHSIVILIIISVSVLHLMTSLSYNSWIHRSLLEDQSLESIWTVMPGIVLIFIALPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511244826  81 LVILYLTDESFNPLITIKSIGHQWYWSYELMDSNsSIEIDSYMIPSE--TNNTFRLLDVDNQIKLPIKTQIRLLTTAADV 158
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFK-NIEFDSYMIPTNelENNGFRLLDVDNRLVLPMNTQIRILITAADV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1511244826 159 IHSWTIPSLGIKIDSTPGRLNQGSFSINRPGILFGQCSEICGANHSFMPITIQATNLHDFCNWIKS 224
Cdd:MTH00154  160 IHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKN 225
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-224 1.81e-128

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 361.84  E-value: 1.81e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511244826   1 MSTWSNLNFQNGSSPLMEQLTFFHDHSIVILIIISVSVLHLMTSLSYNSWIHRSLLEDQSLESIWTVMPGIVLIFIALPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511244826  81 LVILYLTDESFNPLITIKSIGHQWYWSYELMDSNsSIEIDSYMIPSE--TNNTFRLLDVDNQIKLPIKTQIRLLTTAADV 158
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFK-NIEFDSYMIPTNelENNGFRLLDVDNRLVLPMNTQIRILITAADV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1511244826 159 IHSWTIPSLGIKIDSTPGRLNQGSFSINRPGILFGQCSEICGANHSFMPITIQATNLHDFCNWIKS 224
Cdd:MTH00154  160 IHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKN 225
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-221 3.19e-76

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: 225.91  E-value: 3.19e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511244826  93 PLITIKSIGHQWYWSYELMDsNSSIEIDSYMIPSETNNT--FRLLDVDNQIKLPIKTQIRLLTTAADVIHSWTIPSLGIK 170
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSD-FNDLEFDSYMIPEDDLEKgqLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIK 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1511244826 171 IDSTPGRLNQGSFSINRPGILFGQCSEICGANHSFMPITIQATNLHDFCNW 221
Cdd:cd13912    80 VDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-213 6.32e-65

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 196.86  E-value: 6.32e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511244826  95 ITIKSIGHQWYWSYELMDSNSsIEIDSYMIPSE--TNNTFRLLDVDNQIKLPIKTQIRLLTTAADVIHSWTIPSLGIKID 172
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGD-LEFDSYMIPTEdlEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1511244826 173 STPGRLNQGSFSINRPGILFGQCSEICGANHSFMPITIQAT 213
Cdd:pfam00116  80 AVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
61-224 6.05e-45

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 149.59  E-value: 6.05e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511244826  61 LESIWTVMPGIVLIFIALPSLVILYLTDESFNPLITIKSIGHQWYWSYELMDSNSsieidsymipsetnntfrllDVDNQ 140
Cdd:COG1622    79 LEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGI--------------------ATVNE 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511244826 141 IKLPIKTQIRLLTTAADVIHSWTIPSLGIKIDSTPGRLNQGSFSINRPGILFGQCSEICGANHSFMPITIQATNLHDFCN 220
Cdd:COG1622   139 LVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDA 218


                  ....
gi 1511244826 221 WIKS 224
Cdd:COG1622   219 WLAE 222
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 44-222 2.60e-37

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: 129.04  E-value: 2.60e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511244826  44 SLSYNSWIHRSLLEDQS---------LESIWTVMPG-IVLIFIALPSLVILYLTDESFNPLITIKSIGHQWYWSYELMDS 113
Cdd:TIGR02866  30 LLAYVVWKFRRKGDEEKpsqihgnrrLEYVWTVIPLiIVVGLFAATAKGLLYLERPIPKDALKVKVTGYQWWWDFEYPES 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511244826 114 nssieidsymipsetnnTFRlldVDNQIKLPIKTQIRLLTTAADVIHSWTIPSLGIKIDSTPGRLNQGSFSINRPGILFG 193
Cdd:TIGR02866 110 -----------------GFT---TVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYG 169

                         170       180
                  ....*....|....*....|....*....
gi 1511244826 194 QCSEICGANHSFMPITIQATNLHDFCNWI 222
Cdd:TIGR02866 170 FCAELCGAGHSLMLFKVVVVPKEEFDAYV 198
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-224 1.81e-128

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 361.84  E-value: 1.81e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511244826   1 MSTWSNLNFQNGSSPLMEQLTFFHDHSIVILIIISVSVLHLMTSLSYNSWIHRSLLEDQSLESIWTVMPGIVLIFIALPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511244826  81 LVILYLTDESFNPLITIKSIGHQWYWSYELMDSNsSIEIDSYMIPSE--TNNTFRLLDVDNQIKLPIKTQIRLLTTAADV 158
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFK-NIEFDSYMIPTNelENNGFRLLDVDNRLVLPMNTQIRILITAADV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1511244826 159 IHSWTIPSLGIKIDSTPGRLNQGSFSINRPGILFGQCSEICGANHSFMPITIQATNLHDFCNWIKS 224
Cdd:MTH00154  160 IHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKN 225
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-224 4.02e-106

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 305.32  E-value: 4.02e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511244826   1 MSTWSNLNFQNGSSPLMEQLTFFHDHSIVILIIISVSVLHLMTSLSYNSWIHRSLLEDQSLESIWTVMPGIVLIFIALPS 80
Cdd:MTH00140    1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511244826  81 LVILYLTDESFNPLITIKSIGHQWYWSYELMDSNSsIEIDSYMIPSETNNT--FRLLDVDNQIKLPIKTQIRLLTTAADV 158
Cdd:MTH00140   81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSV-IEFDSYMVPENELELgdFRLLEVDNRLVLPYSVDTRVLVTSADV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1511244826 159 IHSWTIPSLGIKIDSTPGRLNQGSFSINRPGILFGQCSEICGANHSFMPITIQATNLHDFCNWIKS 224
Cdd:MTH00140  160 IHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLEL 225
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-224 5.52e-105

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 302.41  E-value: 5.52e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511244826   1 MSTWSNLNFQNGSSPLMEQLTFFHDHSIVILIIISVSVLHLMTSLSYNSWIHRSLLEDQSLESIWTVMPGIVLIFIALPS 80
Cdd:MTH00139    1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511244826  81 LVILYLTDESFNPLITIKSIGHQWYWSYELMDSNsSIEIDSYMIPSE--TNNTFRLLDVDNQIKLPIKTQIRLLTTAADV 158
Cdd:MTH00139   81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFK-NLSFDSYMIPTEdlSSGEFRLLEVDNRLVLPYKSNIRALITAADV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1511244826 159 IHSWTIPSLGIKIDSTPGRLNQGSFSINRPGILFGQCSEICGANHSFMPITIQATNLHDFCNWIKS 224
Cdd:MTH00139  160 LHSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILE 225
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-222 1.16e-100

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 291.11  E-value: 1.16e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511244826   1 MSTWSNLNFQNGSSPLMEQLTFFHDHSIVILIIISVSVLHLMTSLSYNSWIHRSLLEDQSLESIWTVMPGIVLIFIALPS 80
Cdd:MTH00168    1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511244826  81 LVILYLTDESFNPLITIKSIGHQWYWSYELMDSNSsIEIDSYMIPSE--TNNTFRLLDVDNQIKLPIKTQIRLLTTAADV 158
Cdd:MTH00168   81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYND-LEFDSYMVPTQdlSPGQFRLLEVDNRLVLPMDSKIRVLVTSADV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1511244826 159 IHSWTIPSLGIKIDSTPGRLNQGSFSINRPGILFGQCSEICGANHSFMPITIQATNLHDFCNWI 222
Cdd:MTH00168  160 LHSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWV 223
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-222 4.97e-100

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 289.68  E-value: 4.97e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511244826   1 MSTWSNLNFQNGSSPLMEQLTFFHDHSIVILIIISVSVLHLMTSLSYNSWIHRSLLEDQSLESIWTVMPGIVLIFIALPS 80
Cdd:MTH00038    1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511244826  81 LVILYLTDESFNPLITIKSIGHQWYWSYELMDSNsSIEIDSYMIPSE--TNNTFRLLDVDNQIKLPIKTQIRLLTTAADV 158
Cdd:MTH00038   81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYN-DLEFDSYMVPTSdlSTGLPRLLEVDNRLVLPYQTPIRVLVSSADV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1511244826 159 IHSWTIPSLGIKIDSTPGRLNQGSFSINRPGILFGQCSEICGANHSFMPITIQATNLHDFCNWI 222
Cdd:MTH00038  160 LHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWV 223
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-226 7.93e-100

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 289.12  E-value: 7.93e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511244826   1 MSTWSNLNFQNGSSPLMEQLTFFHDHSIVILIIISVSVLHLMTSLSYNSWIHRSLLEDQSLESIWTVMPGIVLIFIALPS 80
Cdd:MTH00117    1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511244826  81 LVILYLTDESFNPLITIKSIGHQWYWSYELMDsNSSIEIDSYMIPSE--TNNTFRLLDVDNQIKLPIKTQIRLLTTAADV 158
Cdd:MTH00117   81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTD-YKDLSFDSYMIPTQdlPNGHFRLLEVDHRMVIPMESPIRILITAEDV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1511244826 159 IHSWTIPSLGIKIDSTPGRLNQGSFSINRPGILFGQCSEICGANHSFMPITIQATNLHDFCNWIKSCL 226
Cdd:MTH00117  160 LHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLLS 227
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-224 1.93e-97

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 283.29  E-value: 1.93e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511244826   1 MSTWSNLNFQNGSSPLMEQLTFFHDHSIVILIIISVSVLHLMTSLSYNSWIHRSLLEDQSLESIWTVMPGIVLIFIALPS 80
Cdd:MTH00008    1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511244826  81 LVILYLTDESFNPLITIKSIGHQWYWSYELMDSnSSIEIDSYMIPSE--TNNTFRLLDVDNQIKLPIKTQIRLLTTAADV 158
Cdd:MTH00008   81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDF-SNLEFDSYMLPTSdlSPGQFRLLEVDNRAVLPMQTEIRVLVTAADV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1511244826 159 IHSWTIPSLGIKIDSTPGRLNQGSFSINRPGILFGQCSEICGANHSFMPITIQATNLHDFCNWIKS 224
Cdd:MTH00008  160 IHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSS 225
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 7-224 5.50e-89

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 262.02  E-value: 5.50e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511244826   7 LNFQNGSSPLMEQLTFFHDHSIVILIIISVSVLHLMTSLSYNSWIHRSLLEDQSLESIWTVMPGIVLIFIALPSLVILYL 86
Cdd:MTH00051    9 LGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511244826  87 TDESFNPLITIKSIGHQWYWSYELMDSNS-SIEIDSYMIPSE--TNNTFRLLDVDNQIKLPIKTQIRLLTTAADVIHSWT 163
Cdd:MTH00051   89 MDEVIDPALTIKAIGHQWYWSYEYSDYGTdTIEFDSYMIPTSdlNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFA 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1511244826 164 IPSLGIKIDSTPGRLNQGSFSINRPGILFGQCSEICGANHSFMPITIQATNLHDFCNWIKS 224
Cdd:MTH00051  169 VPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVAT 229
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 7-224 4.54e-88

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 260.07  E-value: 4.54e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511244826   7 LNFQNGSSPLMEQLTFFHDHSIVILIIISVSVLHLMTSLSYNSWIHRSLLEDQSLESIWTVMPGIVLIFIALPSLVILYL 86
Cdd:MTH00023   16 LGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511244826  87 TDESFNPLITIKSIGHQWYWSYELMD-SNSSIEIDSYMIPSETNNT--FRLLDVDNQIKLPIKTQIRLLTTAADVIHSWT 163
Cdd:MTH00023   96 MDEVVSPALTIKAIGHQWYWSYEYSDyEGETLEFDSYMVPTSDLNSgdFRLLEVDNRLVVPINTHVRILVTGADVLHSFA 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1511244826 164 IPSLGIKIDSTPGRLNQGSFSINRPGILFGQCSEICGANHSFMPITIQATNLHDFCNWIKS 224
Cdd:MTH00023  176 VPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLS 236
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-226 3.74e-87

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 257.33  E-value: 3.74e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511244826   1 MSTWSNLNFQNGSSPLMEQLTFFHDHSIVILIIISVSVLHLMTSLSYNSWIHRSLLEDQSLESIWTVMPGIVLIFIALPS 80
Cdd:MTH00129    1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511244826  81 LVILYLTDESFNPLITIKSIGHQWYWSYELMDSNSsIEIDSYMIPSE--TNNTFRLLDVDNQIKLPIKTQIRLLTTAADV 158
Cdd:MTH00129   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYED-LGFDSYMIPTQdlTPGQFRLLEADHRMVVPVESPIRVLVSAEDV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1511244826 159 IHSWTIPSLGIKIDSTPGRLNQGSFSINRPGILFGQCSEICGANHSFMPITIQATNLHDFCNWIKSCL 226
Cdd:MTH00129  160 LHSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLML 227
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-226 9.90e-87

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 256.35  E-value: 9.90e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511244826   1 MSTWSNLNFQNGSSPLMEQLTFFHDHSIVILIIISVSVLHLMTSLSYNSWIHRSLLEDQSLESIWTVMPGIVLIFIALPS 80
Cdd:MTH00185    1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511244826  81 LVILYLTDESFNPLITIKSIGHQWYWSYELMDSNSsIEIDSYMIPSE--TNNTFRLLDVDNQIKLPIKTQIRLLTTAADV 158
Cdd:MTH00185   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQ-LEFDSYMTPTQdlTPGQFRLLETDHRMVVPMESPIRVLITAEDV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1511244826 159 IHSWTIPSLGIKIDSTPGRLNQGSFSINRPGILFGQCSEICGANHSFMPITIQATNLHDFCNWIKSCL 226
Cdd:MTH00185  160 LHSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLML 227
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-226 9.95e-87

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 256.18  E-value: 9.95e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511244826   1 MSTWSNLNFQNGSSPLMEQLTFFHDHSIVILIIISVSVLHLMTSLSYNSWIHRSLLEDQSLESIWTVMPGIVLIFIALPS 80
Cdd:MTH00098    1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511244826  81 LVILYLTDESFNPLITIKSIGHQWYWSYELMDSNsSIEIDSYMIPSETNNT--FRLLDVDNQIKLPIKTQIRLLTTAADV 158
Cdd:MTH00098   81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYE-DLSFDSYMIPTSDLKPgeLRLLEVDNRVVLPMEMPIRMLISSEDV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1511244826 159 IHSWTIPSLGIKIDSTPGRLNQGSFSINRPGILFGQCSEICGANHSFMPITIQATNLHDFCNWIKSCL 226
Cdd:MTH00098  160 LHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASML 227
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-224 1.93e-85

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 252.78  E-value: 1.93e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511244826   1 MSTWSNLNFQNGSSPLMEQLTFFHDHSIVILIIISVSVLHLMTSLSYNSWIHRSLLEDQSLESIWTVMPGIVLIFIALPS 80
Cdd:MTH00076    1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511244826  81 LVILYLTDESFNPLITIKSIGHQWYWSYELMDSNSsIEIDSYMIPSE--TNNTFRLLDVDNQIKLPIKTQIRLLTTAADV 158
Cdd:MTH00076   81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYED-LSFDSYMIPTQdlTPGQFRLLEVDNRMVVPMESPIRMLITAEDV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1511244826 159 IHSWTIPSLGIKIDSTPGRLNQGSFSINRPGILFGQCSEICGANHSFMPITIQATNLHDFCNWIKS 224
Cdd:MTH00076  160 LHSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSS 225
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-221 3.19e-76

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: 225.91  E-value: 3.19e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511244826  93 PLITIKSIGHQWYWSYELMDsNSSIEIDSYMIPSETNNT--FRLLDVDNQIKLPIKTQIRLLTTAADVIHSWTIPSLGIK 170
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSD-FNDLEFDSYMIPEDDLEKgqLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIK 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1511244826 171 IDSTPGRLNQGSFSINRPGILFGQCSEICGANHSFMPITIQATNLHDFCNW 221
Cdd:cd13912    80 VDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-213 6.32e-65

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 196.86  E-value: 6.32e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511244826  95 ITIKSIGHQWYWSYELMDSNSsIEIDSYMIPSE--TNNTFRLLDVDNQIKLPIKTQIRLLTTAADVIHSWTIPSLGIKID 172
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGD-LEFDSYMIPTEdlEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1511244826 173 STPGRLNQGSFSINRPGILFGQCSEICGANHSFMPITIQAT 213
Cdd:pfam00116  80 AVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 7-222 2.54e-64

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 200.25  E-value: 2.54e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511244826   7 LNFQNGSSPLMEQLTFFHDHSIVILIIISVSVLHLMTSLSYNSWIHR---SLLEDQSLESIWTVMPGIVLIFIALPSLVI 83
Cdd:MTH00027   35 LGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLGNNYYSyywNKLDGSLIEVIWTLIPAFILILIAFPSLRL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511244826  84 LYLTDES-FNPLITIKSIGHQWYWSYELMD-SNSSIEIDSYMIPSE--TNNTFRLLDVDNQIKLPIKTQIRLLTTAADVI 159
Cdd:MTH00027  115 LYIMDECgFSANITIKVTGHQWYWSYSYEDyGEKNIEFDSYMIPTAdlEFGDLRLLEVDNRLILPVDTNVRVLITAADVL 194

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1511244826 160 HSWTIPSLGIKIDSTPGRLNQGSFSINRPGILFGQCSEICGANHSFMPITIQATNLHDFCNWI 222
Cdd:MTH00027  195 HSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWI 257
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 6-226 2.82e-59

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 186.37  E-value: 2.82e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511244826   6 NLNFQNGS-SPLMEQLTFFHDHSIVILIIISVSVLHLMTSLSYNSWIHRSLLEDQSLESIWTVMPGIVLIFIALPSLVIL 84
Cdd:MTH00080    7 NLNFSNSLfSSYMDWFHNFNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511244826  85 YLTD-ESFNPLITIKSIGHQWYWSYELMDsNSSIEIDSYMIPSETNN--TFRLLDVDNQIKLPIKTQIRLLTTAADVIHS 161
Cdd:MTH00080   87 YYYGlMNLDSNLTVKVTGHQWYWSYEFSD-IPGLEFDSYMKSLDQLRlgEPRLLEVDNRCVLPCDTNIRFCITSSDVIHS 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1511244826 162 WTIPSLGIKIDSTPGRLNQGSFSINRPGILFGQCSEICGANHSFMPITIQATNLHDFCNWIKSCL 226
Cdd:MTH00080  166 WALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWCKLLL 230
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
61-224 6.05e-45

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 149.59  E-value: 6.05e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511244826  61 LESIWTVMPGIVLIFIALPSLVILYLTDESFNPLITIKSIGHQWYWSYELMDSNSsieidsymipsetnntfrllDVDNQ 140
Cdd:COG1622    79 LEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGI--------------------ATVNE 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511244826 141 IKLPIKTQIRLLTTAADVIHSWTIPSLGIKIDSTPGRLNQGSFSINRPGILFGQCSEICGANHSFMPITIQATNLHDFCN 220
Cdd:COG1622   139 LVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDA 218


                  ....
gi 1511244826 221 WIKS 224
Cdd:COG1622   219 WLAE 222
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 57-213 4.03e-42

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 141.25  E-value: 4.03e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511244826  57 EDQSLESIWTVMP-GIVLIFIALPSLVILYltDESFNPLITIKSIGHQWYWSYELmdsNSSIEIDSYMipseTNNTFrll 135
Cdd:MTH00047   45 ENQVLELLWTVVPtLLVLVLCFLNLNFITS--DLDCFSSETIKVIGHQWYWSYEY---SFGGSYDSFM----TDDIF--- 112

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1511244826 136 DVDNQIKLPIKTQIRLLTTAADVIHSWTIPSLGIKIDSTPGRLNQGSFSINRPGILFGQCSEICGANHSFMPITIQAT 213
Cdd:MTH00047  113 GVDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVV 190
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 44-222 2.60e-37

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: 129.04  E-value: 2.60e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511244826  44 SLSYNSWIHRSLLEDQS---------LESIWTVMPG-IVLIFIALPSLVILYLTDESFNPLITIKSIGHQWYWSYELMDS 113
Cdd:TIGR02866  30 LLAYVVWKFRRKGDEEKpsqihgnrrLEYVWTVIPLiIVVGLFAATAKGLLYLERPIPKDALKVKVTGYQWWWDFEYPES 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511244826 114 nssieidsymipsetnnTFRlldVDNQIKLPIKTQIRLLTTAADVIHSWTIPSLGIKIDSTPGRLNQGSFSINRPGILFG 193
Cdd:TIGR02866 110 -----------------GFT---TVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYG 169

                         170       180
                  ....*....|....*....|....*....
gi 1511244826 194 QCSEICGANHSFMPITIQATNLHDFCNWI 222
Cdd:TIGR02866 170 FCAELCGAGHSLMLFKVVVVPKEEFDAYV 198
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 133-212 1.96e-34

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 120.70  E-value: 1.96e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511244826 133 RLLDVDNQIKLPIKTQIRLLTTAADVIHSWTIPSLGIKIDSTPGRLNQGSFSINRPGILFGQCSEICGANHSFMPITIQA 212
Cdd:PTZ00047   67 RQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCSEMCGTLHGFMPIVVEA 146
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-210 3.32e-24

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: 91.97  E-value: 3.32e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511244826  95 ITIKSIGHQWYWSYELMDSNSsieidsymipsetnntfrlldvDNQIKLPIKTQIRLLTTAADVIHSWTIPSLGIKIDST 174
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPNVRT----------------------PNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDAV 58

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1511244826 175 PGRLNQGSFSINRPGILFGQCSEICGANHSFMPITI 210
Cdd:cd13842    59 PGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKV 94
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 95-212 4.72e-24

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: 91.91  E-value: 4.72e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511244826  95 ITIKSIGHQWYWSYELMDSNSSIEIDSymipsetnntfrlldvdNQIKLPIKTQIRLLTTAADVIHSWTIPSLGIKIDST 174
Cdd:cd04213     2 LTIEVTGHQWWWEFRYPDEPGRGIVTA-----------------NELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDMI 64

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1511244826 175 PGRLNQGSFSINRPGILFGQCSEICGANHSFMPITIQA 212
Cdd:cd04213    65 PGRTNRLWLQADEPGVYRGQCAEFCGASHALMRFKVIA 102
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-206 1.17e-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: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 78.07  E-value: 1.17e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511244826  95 ITIKSIGHQWYWSYelmdsnssieidSYMIPSETNNTFRLLDVdNQIKLPIKTQIRLLTTAADVIHSWTIPSLGIKIDST 174
Cdd:cd13919     2 LVVEVTAQQWAWTF------------RYPGGDGKLGTDDDVTS-PELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDAV 68

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1511244826 175 PGRLNQGSFSINRPGILFGQCSEICGANHSFM 206
Cdd:cd13919    69 PGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 71-221 7.88e-17

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: 74.03  E-value: 7.88e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511244826  71 IVLIFIALPSLVILYL----TDESFNPLiTIKSIGHQWYWSYElmdsnssieidsYMIPSETNNTFRLldvdnqiklPIK 146
Cdd:cd13918     6 IVISLIVWTYGMLLYVedppDEADEDAL-EVEVEGFQFGWQFE------------YPNGVTTGNTLRV---------PAD 63

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1511244826 147 TQIRLLTTAADVIHSWTIPSLGIKIDSTPGRLNQGSFSINRPGILFGQCSEICGANHSFMPITIQATNLHDFCNW 221
Cdd:cd13918    64 TPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAW 138
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-206 1.25e-16

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: 72.28  E-value: 1.25e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511244826  95 ITIKSIGHQWYWSYELMDSNSSIeidsymipsetnntfrlldvdNQIKLPIKTQIRLLTTAADVIHSWTIPSLGIKIDST 174
Cdd:cd13915     2 LEIQVTGRQWMWEFTYPNGKREI---------------------NELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDVV 60

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1511244826 175 PGRLNQGSFSINRPGILFGQCSEICGANHSFM 206
Cdd:cd13915    61 PGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-222 2.37e-16

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: 72.06  E-value: 2.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511244826  95 ITIKSIGHQWYWSYELMDSNssieidsymipsetnntfrlLDVDNQIKLPIKTQIRLLTTAADVIHSWTIPSLGIKIDST 174
Cdd:cd13914     1 VEIEVEAYQWGWEFSYPEAN--------------------VTTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAF 60

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1511244826 175 PGRLNQGSFSINRPGILFGQCSEICGANHSFMPITIQATNLHDFCNWI 222
Cdd:cd13914    61 PGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-83 1.05e-14

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: 66.97  E-value: 1.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511244826   1 MSTWSNLNFQNGSSPLMEQLTFFHDHSIVILIIISVSVLHLMTSL------SYNSWIHRSLLEDQSLESIWTVMPGIVLI 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTClirfnrRKNPITARYTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 1511244826  75 FIALPSLVI 83
Cdd:pfam02790  81 LIALPSFKL 89
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 139-210 7.12e-08

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: 48.72  E-value: 7.12e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1511244826 139 NQIKLPIKTQIRLLTTAADVIHSWTIPSLGIKIDSTPGRLNQGSFSINRPG---ILfgqCSEICGANHSFMPITI 210
Cdd:cd13913    25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGeylII---CNEYCGAGHHNMYGKI 96
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 139-206 9.60e-06

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: 42.92  E-value: 9.60e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1511244826 139 NQIKLPIKTQIRLLTTAADVIHSWTIPSLGIKIDSTPGRLNQGSFSINRPGILFGQCSEICGANHSFM 206
Cdd:cd04212    25 NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDM 92
 
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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