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Conserved domains on  [gi|1916858828|gb|QOL00597|]
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cytochrome c oxidase subunit II (mitochondrion) [Gryllotalpa sp. YH-2020]

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
 1-227 1.42e-144

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 402.28  E-value: 1.42e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828   1 MATWSNLNLQNAASPIMEQLSFFHDHTLMILIMITVLVAYIMLSLLPNNLVHRYLLEGQNIEIIWTILPAITLIFIALPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828  81 LRLLYLLDESMTPLISLKSTGHQWYWSYEYMDFKNpIEFDSYMIPFNELPLNGFRVLDVDNRTTLPMNIQTRILVTASDV 160
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKN-IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1916858828 161 IHSWTVPSMGLKVDATPGRLNQLNLLMSRPGIFFGQCSEICGANHSFMPIVLESVGVKLFTKWIMNL 227
Cdd:MTH00154  160 IHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNM 226
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-227 1.42e-144

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 402.28  E-value: 1.42e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828   1 MATWSNLNLQNAASPIMEQLSFFHDHTLMILIMITVLVAYIMLSLLPNNLVHRYLLEGQNIEIIWTILPAITLIFIALPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828  81 LRLLYLLDESMTPLISLKSTGHQWYWSYEYMDFKNpIEFDSYMIPFNELPLNGFRVLDVDNRTTLPMNIQTRILVTASDV 160
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKN-IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1916858828 161 IHSWTVPSMGLKVDATPGRLNQLNLLMSRPGIFFGQCSEICGANHSFMPIVLESVGVKLFTKWIMNL 227
Cdd:MTH00154  160 IHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNM 226
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-223 2.63e-81

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: 238.62  E-value: 2.63e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828  93 PLISLKSTGHQWYWSYEYMDFkNPIEFDSYMIPFNELPLNGFRVLDVDNRTTLPMNIQTRILVTASDVIHSWTVPSMGLK 172
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDF-NDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIK 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1916858828 173 VDATPGRLNQLNLLMSRPGIFFGQCSEICGANHSFMPIVLESVGVKLFTKW 223
Cdd:cd13912    80 VDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-215 2.03e-69

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 208.42  E-value: 2.03e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828  95 ISLKSTGHQWYWSYEYMDFKNpIEFDSYMIPFNELPLNGFRVLDVDNRTTLPMNIQTRILVTASDVIHSWTVPSMGLKVD 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGD-LEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1916858828 175 ATPGRLNQLNLLMSRPGIFFGQCSEICGANHSFMPIVLESV 215
Cdd:pfam00116  80 AVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-224 4.32e-42

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 142.27  E-value: 4.32e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828   6 NLNLQNAASPIMEQLSFFHDHTLMILIMITVLV-AYIMLSLL-----PNNLVHRYLLEGQNIEIIWTILPAITLIFIALP 79
Cdd:COG1622    18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVfGLLLYFAIryrrrKGDADPAQFHHNTKLEIVWTVIPIIIVIVLAVP 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828  80 SLRLLYLLDESMTPLISLKSTGHQWYWSYEYMDFKNpiefdsymipfnelplngfrvlDVDNRTTLPMNIQTRILVTASD 159
Cdd:COG1622    98 TLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGI----------------------ATVNELVLPVGRPVRFLLTSAD 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1916858828 160 VIHSWTVPSMGLKVDATPGRLNQLNLLMSRPGIFFGQCSEICGANHSFMPIVLESVGVKLFTKWI 224
Cdd:COG1622   156 VIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWL 220
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-224 3.18e-35

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: 123.64  E-value: 3.18e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828  12 AASPIMEQLSFFHDHTLMILIMITVLV-AYIMLSLL-----PNNLVHRYLLEGQNIEIIWTILPAITLIFIALPSLRLLY 85
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVaALLAYVVWkfrrkGDEEKPSQIHGNRRLEYVWTVIPLIIVVGLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828  86 LLDESMTP-LISLKSTGHQWYWSYEYmdfknpiefdsymipfnelPLNGFRVldvDNRTTLPMNIQTRILVTASDVIHSW 164
Cdd:TIGR02866  81 YLERPIPKdALKVKVTGYQWWWDFEY-------------------PESGFTT---VNELVLPAGTPVELQVTSKDVIHSF 138

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828 165 TVPSMGLKVDATPGRLNQLNLLMSRPGIFFGQCSEICGANHSFMPIVLESVGVKLFTKWI 224
Cdd:TIGR02866 139 WVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYV 198
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-227 1.42e-144

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 402.28  E-value: 1.42e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828   1 MATWSNLNLQNAASPIMEQLSFFHDHTLMILIMITVLVAYIMLSLLPNNLVHRYLLEGQNIEIIWTILPAITLIFIALPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828  81 LRLLYLLDESMTPLISLKSTGHQWYWSYEYMDFKNpIEFDSYMIPFNELPLNGFRVLDVDNRTTLPMNIQTRILVTASDV 160
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKN-IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1916858828 161 IHSWTVPSMGLKVDATPGRLNQLNLLMSRPGIFFGQCSEICGANHSFMPIVLESVGVKLFTKWIMNL 227
Cdd:MTH00154  160 IHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNM 226
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-227 1.80e-114

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 326.51  E-value: 1.80e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828   1 MATWSNLNLQNAASPIMEQLSFFHDHTLMILIMITVLVAYIMLSLLPNNLVHRYLLEGQNIEIIWTILPAITLIFIALPS 80
Cdd:MTH00140    1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828  81 LRLLYLLDESMTPLISLKSTGHQWYWSYEYMDFKNpIEFDSYMIPFNELPLNGFRVLDVDNRTTLPMNIQTRILVTASDV 160
Cdd:MTH00140   81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSV-IEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1916858828 161 IHSWTVPSMGLKVDATPGRLNQLNLLMSRPGIFFGQCSEICGANHSFMPIVLESVGVKLFTKWIMNL 227
Cdd:MTH00140  160 IHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELM 226
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-227 7.26e-113

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 322.25  E-value: 7.26e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828   1 MATWSNLNLQNAASPIMEQLSFFHDHTLMILIMITVLVAYIMLSLLPNNLVHRYLLEGQNIEIIWTILPAITLIFIALPS 80
Cdd:MTH00117    1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828  81 LRLLYLLDESMTPLISLKSTGHQWYWSYEYMDFKNpIEFDSYMIPFNELPLNGFRVLDVDNRTTLPMNIQTRILVTASDV 160
Cdd:MTH00117   81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKD-LSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1916858828 161 IHSWTVPSMGLKVDATPGRLNQLNLLMSRPGIFFGQCSEICGANHSFMPIVLESVGVKLFTKWIMNL 227
Cdd:MTH00117  160 LHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLL 226
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-226 6.25e-111

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 317.43  E-value: 6.25e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828   1 MATWSNLNLQNAASPIMEQLSFFHDHTLMILIMITVLVAYIMLSLLPNNLVHRYLLEGQNIEIIWTILPAITLIFIALPS 80
Cdd:MTH00139    1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828  81 LRLLYLLDESMTPLISLKSTGHQWYWSYEYMDFKNpIEFDSYMIPFNELPLNGFRVLDVDNRTTLPMNIQTRILVTASDV 160
Cdd:MTH00139   81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKN-LSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1916858828 161 IHSWTVPSMGLKVDATPGRLNQLNLLMSRPGIFFGQCSEICGANHSFMPIVLESVGVKLFTKWIMN 226
Cdd:MTH00139  160 LHSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILE 225
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-226 5.33e-107

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 307.29  E-value: 5.33e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828   1 MATWSNLNLQNAASPIMEQLSFFHDHTLMILIMITVLVAYIMLSLLPNNLVHRYLLEGQNIEIIWTILPAITLIFIALPS 80
Cdd:MTH00168    1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828  81 LRLLYLLDESMTPLISLKSTGHQWYWSYEYMDFkNPIEFDSYMIPFNELPLNGFRVLDVDNRTTLPMNIQTRILVTASDV 160
Cdd:MTH00168   81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDY-NDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1916858828 161 IHSWTVPSMGLKVDATPGRLNQLNLLMSRPGIFFGQCSEICGANHSFMPIVLESVGVKLFTKWIMN 226
Cdd:MTH00168  160 LHSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVDS 225
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-226 1.07e-105

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 304.32  E-value: 1.07e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828   1 MATWSNLNLQNAASPIMEQLSFFHDHTLMILIMITVLVAYIMLSLLPNNLVHRYLLEGQNIEIIWTILPAITLIFIALPS 80
Cdd:MTH00038    1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828  81 LRLLYLLDESMTPLISLKSTGHQWYWSYEYMDFkNPIEFDSYMIPFNELPLNGFRVLDVDNRTTLPMNIQTRILVTASDV 160
Cdd:MTH00038   81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDY-NDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1916858828 161 IHSWTVPSMGLKVDATPGRLNQLNLLMSRPGIFFGQCSEICGANHSFMPIVLESVGVKLFTKWIMN 226
Cdd:MTH00038  160 LHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSN 225
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-227 9.03e-105

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 301.78  E-value: 9.03e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828   1 MATWSNLNLQNAASPIMEQLSFFHDHTLMILIMITVLVAYIMLSLLPNNLVHRYLLEGQNIEIIWTILPAITLIFIALPS 80
Cdd:MTH00008    1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828  81 LRLLYLLDESMTPLISLKSTGHQWYWSYEYMDFKNpIEFDSYMIPFNELPLNGFRVLDVDNRTTLPMNIQTRILVTASDV 160
Cdd:MTH00008   81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSN-LEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1916858828 161 IHSWTVPSMGLKVDATPGRLNQLNLLMSRPGIFFGQCSEICGANHSFMPIVLESVGVKLFTKWIMNL 227
Cdd:MTH00008  160 IHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSSF 226
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-223 1.35e-99

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 288.54  E-value: 1.35e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828   1 MATWSNLNLQNAASPIMEQLSFFHDHTLMILIMITVLVAYIMLSLLPNNLVHRYLLEGQNIEIIWTILPAITLIFIALPS 80
Cdd:MTH00098    1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828  81 LRLLYLLDESMTPLISLKSTGHQWYWSYEYMDFKNpIEFDSYMIPFNELPLNGFRVLDVDNRTTLPMNIQTRILVTASDV 160
Cdd:MTH00098   81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYED-LSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1916858828 161 IHSWTVPSMGLKVDATPGRLNQLNLLMSRPGIFFGQCSEICGANHSFMPIVLESVGVKLFTKW 223
Cdd:MTH00098  160 LHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKW 222
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-223 2.56e-97

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 283.14  E-value: 2.56e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828   1 MATWSNLNLQNAASPIMEQLSFFHDHTLMILIMITVLVAYIMLSLLPNNLVHRYLLEGQNIEIIWTILPAITLIFIALPS 80
Cdd:MTH00129    1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828  81 LRLLYLLDESMTPLISLKSTGHQWYWSYEYMDFKNpIEFDSYMIPFNELPLNGFRVLDVDNRTTLPMNIQTRILVTASDV 160
Cdd:MTH00129   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYED-LGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1916858828 161 IHSWTVPSMGLKVDATPGRLNQLNLLMSRPGIFFGQCSEICGANHSFMPIVLESVGVKLFTKW 223
Cdd:MTH00129  160 LHSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 7-227 1.96e-95

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 278.56  E-value: 1.96e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828   7 LNLQNAASPIMEQLSFFHDHTLMILIMITVLVAYIMLSLLPNNLVHRYLLEGQNIEIIWTILPAITLIFIALPSLRLLYL 86
Cdd:MTH00023   16 LGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828  87 LDESMTPLISLKSTGHQWYWSYEYMDFKNP-IEFDSYMIPFNELPLNGFRVLDVDNRTTLPMNIQTRILVTASDVIHSWT 165
Cdd:MTH00023   96 MDEVVSPALTIKAIGHQWYWSYEYSDYEGEtLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFA 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1916858828 166 VPSMGLKVDATPGRLNQLNLLMSRPGIFFGQCSEICGANHSFMPIVLESVGVKLFTKWIMNL 227
Cdd:MTH00023  176 VPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLSL 237
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-223 1.06e-94

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 276.38  E-value: 1.06e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828   1 MATWSNLNLQNAASPIMEQLSFFHDHTLMILIMITVLVAYIMLSLLPNNLVHRYLLEGQNIEIIWTILPAITLIFIALPS 80
Cdd:MTH00185    1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828  81 LRLLYLLDESMTPLISLKSTGHQWYWSYEYMDFKNpIEFDSYMIPFNELPLNGFRVLDVDNRTTLPMNIQTRILVTASDV 160
Cdd:MTH00185   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQ-LEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1916858828 161 IHSWTVPSMGLKVDATPGRLNQLNLLMSRPGIFFGQCSEICGANHSFMPIVLESVGVKLFTKW 223
Cdd:MTH00185  160 LHSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-224 1.10e-92

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 271.27  E-value: 1.10e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828   1 MATWSNLNLQNAASPIMEQLSFFHDHTLMILIMITVLVAYIMLSLLPNNLVHRYLLEGQNIEIIWTILPAITLIFIALPS 80
Cdd:MTH00076    1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828  81 LRLLYLLDESMTPLISLKSTGHQWYWSYEYMDFKNpIEFDSYMIPFNELPLNGFRVLDVDNRTTLPMNIQTRILVTASDV 160
Cdd:MTH00076   81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYED-LSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1916858828 161 IHSWTVPSMGLKVDATPGRLNQLNLLMSRPGIFFGQCSEICGANHSFMPIVLESVGVKLFTKWI 224
Cdd:MTH00076  160 LHSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWS 223
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 7-227 4.51e-91

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 267.42  E-value: 4.51e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828   7 LNLQNAASPIMEQLSFFHDHTLMILIMITVLVAYIMLSLLPNNLVHRYLLEGQNIEIIWTILPAITLIFIALPSLRLLYL 86
Cdd:MTH00051    9 LGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828  87 LDESMTPLISLKSTGHQWYWSYEYMDF-KNPIEFDSYMIPFNELPLNGFRVLDVDNRTTLPMNIQTRILVTASDVIHSWT 165
Cdd:MTH00051   89 MDEVIDPALTIKAIGHQWYWSYEYSDYgTDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFA 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1916858828 166 VPSMGLKVDATPGRLNQLNLLMSRPGIFFGQCSEICGANHSFMPIVLESVGVKLFTKWIMNL 227
Cdd:MTH00051  169 VPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQ 230
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-223 2.63e-81

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: 238.62  E-value: 2.63e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828  93 PLISLKSTGHQWYWSYEYMDFkNPIEFDSYMIPFNELPLNGFRVLDVDNRTTLPMNIQTRILVTASDVIHSWTVPSMGLK 172
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDF-NDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIK 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1916858828 173 VDATPGRLNQLNLLMSRPGIFFGQCSEICGANHSFMPIVLESVGVKLFTKW 223
Cdd:cd13912    80 VDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 7-224 9.53e-71

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 216.82  E-value: 9.53e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828   7 LNLQNAASPIMEQLSFFHDHTLMILIMITVLVAYIMLSLLPNNLVHRYL---LEGQNIEIIWTILPAITLIFIALPSLRL 83
Cdd:MTH00027   35 LGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLGNNYYSYYwnkLDGSLIEVIWTLIPAFILILIAFPSLRL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828  84 LYLLDES-MTPLISLKSTGHQWYWSYEYMDF-KNPIEFDSYMIPFNELPLNGFRVLDVDNRTTLPMNIQTRILVTASDVI 161
Cdd:MTH00027  115 LYIMDECgFSANITIKVTGHQWYWSYSYEDYgEKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVL 194

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1916858828 162 HSWTVPSMGLKVDATPGRLNQLNLLMSRPGIFFGQCSEICGANHSFMPIVLESVGVKLFTKWI 224
Cdd:MTH00027  195 HSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWI 257
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-215 2.03e-69

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 208.42  E-value: 2.03e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828  95 ISLKSTGHQWYWSYEYMDFKNpIEFDSYMIPFNELPLNGFRVLDVDNRTTLPMNIQTRILVTASDVIHSWTVPSMGLKVD 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGD-LEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1916858828 175 ATPGRLNQLNLLMSRPGIFFGQCSEICGANHSFMPIVLESV 215
Cdd:pfam00116  80 AVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 6-227 8.93e-60

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 187.52  E-value: 8.93e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828   6 NLNLQNAASPI-MEQLSFFHDHTLMILIMITVLVAYIMLSLLPNNLVHRYLLEGQNIEIIWTILPAITLIFIALPSLRLL 84
Cdd:MTH00080    7 NLNFSNSLFSSyMDWFHNFNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828  85 YLLDESMTPL-ISLKSTGHQWYWSYEYMDFKNpIEFDSYMIPFNELPLNGFRVLDVDNRTTLPMNIQTRILVTASDVIHS 163
Cdd:MTH00080   87 YYYGLMNLDSnLTVKVTGHQWYWSYEFSDIPG-LEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHS 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1916858828 164 WTVPSMGLKVDATPGRLNQLNLLMSRPGIFFGQCSEICGANHSFMPIVLESVGVKLFTKWIMNL 227
Cdd:MTH00080  166 WALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWCKLL 229
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 30-217 3.72e-44

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 146.64  E-value: 3.72e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828  30 ILIMITVLVAYIMLSLLPNnlvhryllEGQNIEIIWTILPA-ITLIFIALPSLRLLYLLDESMTPLIslKSTGHQWYWSY 108
Cdd:MTH00047   26 YIMLCWQVVSGNGSVNFGS--------ENQVLELLWTVVPTlLVLVLCFLNLNFITSDLDCFSSETI--KVIGHQWYWSY 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828 109 EYmdfKNPIEFDSYMIPFnelplngfrVLDVDNRTTLPMNIQTRILVTASDVIHSWTVPSMGLKVDATPGRLNQLNLLMS 188
Cdd:MTH00047   96 EY---SFGGSYDSFMTDD---------IFGVDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPD 163

                         170       180
                  ....*....|....*....|....*....
gi 1916858828 189 RPGIFFGQCSEICGANHSFMPIVLESVGV 217
Cdd:MTH00047  164 RHGVFVGYCSELCGVGHSYMPIVIEVVDV 192
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-224 4.32e-42

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 142.27  E-value: 4.32e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828   6 NLNLQNAASPIMEQLSFFHDHTLMILIMITVLV-AYIMLSLL-----PNNLVHRYLLEGQNIEIIWTILPAITLIFIALP 79
Cdd:COG1622    18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVfGLLLYFAIryrrrKGDADPAQFHHNTKLEIVWTVIPIIIVIVLAVP 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828  80 SLRLLYLLDESMTPLISLKSTGHQWYWSYEYMDFKNpiefdsymipfnelplngfrvlDVDNRTTLPMNIQTRILVTASD 159
Cdd:COG1622    98 TLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGI----------------------ATVNELVLPVGRPVRFLLTSAD 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1916858828 160 VIHSWTVPSMGLKVDATPGRLNQLNLLMSRPGIFFGQCSEICGANHSFMPIVLESVGVKLFTKWI 224
Cdd:COG1622   156 VIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWL 220
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 119-215 8.73e-38

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 129.17  E-value: 8.73e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828 119 FDSYMIPFNELPLNGFRVLDVDNRTTLPMNIQTRILVTASDVIHSWTVPSMGLKVDATPGRLNQLNLLMSRPGIFFGQCS 198
Cdd:PTZ00047   51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                          90
                  ....*....|....*..
gi 1916858828 199 EICGANHSFMPIVLESV 215
Cdd:PTZ00047  131 EMCGTLHGFMPIVVEAV 147
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-224 3.18e-35

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: 123.64  E-value: 3.18e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828  12 AASPIMEQLSFFHDHTLMILIMITVLV-AYIMLSLL-----PNNLVHRYLLEGQNIEIIWTILPAITLIFIALPSLRLLY 85
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVaALLAYVVWkfrrkGDEEKPSQIHGNRRLEYVWTVIPLIIVVGLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828  86 LLDESMTP-LISLKSTGHQWYWSYEYmdfknpiefdsymipfnelPLNGFRVldvDNRTTLPMNIQTRILVTASDVIHSW 164
Cdd:TIGR02866  81 YLERPIPKdALKVKVTGYQWWWDFEY-------------------PESGFTT---VNELVLPAGTPVELQVTSKDVIHSF 138

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828 165 TVPSMGLKVDATPGRLNQLNLLMSRPGIFFGQCSEICGANHSFMPIVLESVGVKLFTKWI 224
Cdd:TIGR02866 139 WVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYV 198
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-77 1.37e-23

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: 90.08  E-value: 1.37e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828   1 MATWSNLNLQNAASPIMEQLSFFHDHTLMILIMITVLVAYIMLSLL------PNNLVHRYLLEGQNIEIIWTILPAITLI 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLirfnrrKNPITARYTTHGQTIEIIWTIIPAVILI 80


                  ...
gi 1916858828  75 FIA 77
Cdd:pfam02790  81 LIA 83
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 100-208 1.46e-22

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: 88.06  E-value: 1.46e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828 100 TGHQWYWSYEYMDfknpiEFDSYMIPFNELplngfrvldvdnrtTLPMNIQTRILVTASDVIHSWTVPSMGLKVDATPGR 179
Cdd:cd04213     7 TGHQWWWEFRYPD-----EPGRGIVTANEL--------------HIPVGRPVRLRLTSADVIHSFWVPSLAGKMDMIPGR 67

                          90       100
                  ....*....|....*....|....*....
gi 1916858828 180 LNQLNLLMSRPGIFFGQCSEICGANHSFM 208
Cdd:cd04213    68 TNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 100-213 6.53e-21

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: 83.50  E-value: 6.53e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828 100 TGHQWYWSYEYMDFKNPiefdsymipfnelplngfrvldvdNRTTLPMNIQTRILVTASDVIHSWTVPSMGLKVDATPGR 179
Cdd:cd13842     6 TGVQWSWTFIYPNVRTP------------------------NEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDAVPGY 61

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1916858828 180 LNQLNLLMSRPGIFFGQCSEICGANHSFMPIVLE 213
Cdd:cd13842    62 TSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 100-208 4.25e-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: 76.53  E-value: 4.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828 100 TGHQWYWSYEYmdfknpiefdsymipFNELPLNGFRVLDVDNRTTLPMNIQTRILVTASDVIHSWTVPSMGLKVDATPGR 179
Cdd:cd13919     7 TAQQWAWTFRY---------------PGGDGKLGTDDDVTSPELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDAVPGR 71

                          90       100
                  ....*....|....*....|....*....
gi 1916858828 180 LNQLNLLMSRPGIFFGQCSEICGANHSFM 208
Cdd:cd13919    72 TTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 101-208 6.42e-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: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 73.60  E-value: 6.42e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828 101 GHQWYWSYEYMDFKNpiefdsymipfnelplngfrvlDVDNRTTLPMNIQTRILVTASDVIHSWTVPSMGLKVDATPGRL 180
Cdd:cd13914     7 AYQWGWEFSYPEANV----------------------TTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAFPGQY 64

                          90       100
                  ....*....|....*....|....*...
gi 1916858828 181 NQLNLLMSRPGIFFGQCSEICGANHSFM 208
Cdd:cd13914    65 NTIKTEATEEGEYQLYCAEYCGAGHSQM 92
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 100-208 1.94e-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: 71.89  E-value: 1.94e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828 100 TGHQWYWSYEYmdfknpiefdsymipfnelpLNGFRVldvDNRTTLPMNIQTRILVTASDVIHSWTVPSMGLKVDATPGR 179
Cdd:cd13915     7 TGRQWMWEFTY--------------------PNGKRE---INELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDVVPGR 63

                          90       100
                  ....*....|....*....|....*....
gi 1916858828 180 LNQLNLLMSRPGIFFGQCSEICGANHSFM 208
Cdd:cd13915    64 YTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 100-223 8.50e-13

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: 63.24  E-value: 8.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828 100 TGHQWYWSYEYmdfknPIEFDSymipfnelpLNGFRVldvdnrttlPMNIQTRILVTASDVIHSWTVPSMGLKVDATPGR 179
Cdd:cd13918    38 EGFQFGWQFEY-----PNGVTT---------GNTLRV---------PADTPIALRVTSTDVFHTFGIPELRVKADAIPGE 94

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1916858828 180 LNQLNLLMSRPGIFFGQCSEICGANHSFMPIVLESVGVKLFTKW 223
Cdd:cd13918    95 YTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAW 138
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 141-208 7.64e-07

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: 46.02  E-value: 7.64e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1916858828 141 NRTTLPMNIQTRILVTASDVIHSWTVPSMGLKVDATPGRLNQLNLLMSRPGIFFGQCSEICGANHSFM 208
Cdd:cd13913    25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 100-208 4.83e-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: 43.52  E-value: 4.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916858828 100 TGHQWYWSyeyMDfknpiefdsymipfnelplngfrvldvdnRTTLPMNIQTRILVTASDVIHSWTV--PSMGL--KVDA 175
Cdd:cd13916     6 TGHQWYWE---LS-----------------------------RTEIPAGKPVEFRVTSADVNHGFGIydPDMRLlaQTQA 53

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1916858828 176 TPGRLNQLNLLMSRPGIFFGQCSEICGANHSFM 208
Cdd:cd13916    54 MPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 141-215 2.77e-05

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: 41.76  E-value: 2.77e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1916858828 141 NRTTLPMNIQTRILVTASDVIHSWTVPSMGLKVDATPGRLNQLNLLMSRPGIFFGQCSEICGANHSFMPIVLESV 215
Cdd:cd04212    25 NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDMKFKVLAV 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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