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Conserved domains on  [gi|830261325|gb|AKL83114|]
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cytochrome c oxidase subunit 2 (mitochondrion) [Saccharomyces cerevisiae]

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
 24-249 1.03e-104

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 302.52  E-value: 1.03e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325  24 YFQDSATPNQEGILELHDNIMFYLLVILGLVSWMLYTIVMTYSKNpiayKYIKHGQTIEVIWTIFPAVILLIIAFPSFIL 103
Cdd:MTH00154   8 SFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTN----RFLLEGQEIEIIWTILPAIILIFIALPSLRL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325 104 LYLCDEVISPAMTIKAIGYQWYWKYEYSDFINdsgetVEFESYVIPDELLEEGQLRLLDTDTSMVVPVDTHIRFVVTAAD 183
Cdd:MTH00154  84 LYLLDEVNNPSITLKTIGHQWYWSYEYSDFKN-----IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAAD 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 830261325 184 VIHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTGHANMPIKIEAVSLPKFLEWLN 249
Cdd:MTH00154 159 VIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIK 224
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 24-249 1.03e-104

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 302.52  E-value: 1.03e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325  24 YFQDSATPNQEGILELHDNIMFYLLVILGLVSWMLYTIVMTYSKNpiayKYIKHGQTIEVIWTIFPAVILLIIAFPSFIL 103
Cdd:MTH00154   8 SFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTN----RFLLEGQEIEIIWTILPAIILIFIALPSLRL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325 104 LYLCDEVISPAMTIKAIGYQWYWKYEYSDFINdsgetVEFESYVIPDELLEEGQLRLLDTDTSMVVPVDTHIRFVVTAAD 183
Cdd:MTH00154  84 LYLLDEVNNPSITLKTIGHQWYWSYEYSDFKN-----IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAAD 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 830261325 184 VIHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTGHANMPIKIEAVSLPKFLEWLN 249
Cdd:MTH00154 159 VIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIK 224
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 113-247 1.67e-85

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: 250.18  E-value: 1.67e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325 113 PAMTIKAIGYQWYWKYEYSDFindsgETVEFESYVIPDELLEEGQLRLLDTDTSMVVPVDTHIRFVVTAADVIHDFAIPS 192
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDF-----NDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPS 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 830261325 193 LGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTGHANMPIKIEAVSLPKFLEW 247
Cdd:cd13912   76 LGIKVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
115-239 1.36e-80

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 237.69  E-value: 1.36e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325  115 MTIKAIGYQWYWKYEYSDFINdsgetVEFESYVIPDELLEEGQLRLLDTDTSMVVPVDTHIRFVVTAADVIHDFAIPSLG 194
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGD-----LEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLG 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 830261325  195 IKVDATPGRLNQVSALIQREGVFYGQCSELCGTGHANMPIKIEAV 239
Cdd:pfam00116  76 IKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
24-251 2.16e-63

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 197.74  E-value: 2.16e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325  24 YFQDSATPNQEGILELHdNIMFYLLVILGLVSW--MLYTIVM-TYSKNPIAYKYIKHGQTIEVIWTIFPAVILLIIAFPS 100
Cdd:COG1622   20 SLPDPAGPIAEEIDDLF-WVSLIIMLVIFVLVFglLLYFAIRyRRRKGDADPAQFHHNTKLEIVWTVIPIIIVIVLAVPT 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325 101 FILLYLCDEVISPAMTIKAIGYQWYWKYEYsdfindsgetvefesyvipdelLEEGQLrlldTDTSMVVPVDTHIRFVVT 180
Cdd:COG1622   99 LRVLHALDDAPEDPLTVEVTGYQWKWLFRY----------------------PDQGIA----TVNELVLPVGRPVRFLLT 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 830261325 181 AADVIHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTGHANMPIKIEAVSLPKFLEWLNEQ 251
Cdd:COG1622  153 SADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQ 223
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 29-249 3.77e-42

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: 142.52  E-value: 3.77e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325   29 ATPNQEGILELHDNIMFYLLVILGLVSWMLYTIVMTY---SKNPIAyKYIKHGQTIEVIWTIFPAVILL-IIAFPSFILL 104
Cdd:TIGR02866   2 GGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVWKFrrkGDEEKP-SQIHGNRRLEYVWTVIPLIIVVgLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325  105 YLCDEVISPAMTIKAIGYQWYWKYEYSDFindsgetvefesyvipdelleegqlrLLDTDTSMVVPVDTHIRFVVTAADV 184
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPES--------------------------GFTTVNELVLPAGTPVELQVTSKDV 134

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 830261325  185 IHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTGHANMPIKIEAVSLPKFLEWLN 249
Cdd:TIGR02866 135 IHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 24-249 1.03e-104

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 302.52  E-value: 1.03e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325  24 YFQDSATPNQEGILELHDNIMFYLLVILGLVSWMLYTIVMTYSKNpiayKYIKHGQTIEVIWTIFPAVILLIIAFPSFIL 103
Cdd:MTH00154   8 SFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTN----RFLLEGQEIEIIWTILPAIILIFIALPSLRL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325 104 LYLCDEVISPAMTIKAIGYQWYWKYEYSDFINdsgetVEFESYVIPDELLEEGQLRLLDTDTSMVVPVDTHIRFVVTAAD 183
Cdd:MTH00154  84 LYLLDEVNNPSITLKTIGHQWYWSYEYSDFKN-----IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAAD 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 830261325 184 VIHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTGHANMPIKIEAVSLPKFLEWLN 249
Cdd:MTH00154 159 VIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIK 224
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 9-248 4.10e-100

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 291.65  E-value: 4.10e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325   9 LTTFIMNDVPTPYACYFQDSATPNQEGILELHDNIMFYLLVILGLVSWMLYTIVmtysKNPIAYKYIKHGQTIEVIWTIF 88
Cdd:MTH00023   2 FNNFFYRDIPEPWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEAL----NGKFYDRFLVDGTFLEIVWTII 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325  89 PAVILLIIAFPSFILLYLCDEVISPAMTIKAIGYQWYWKYEYSDFindSGETVEFESYVIPDELLEEGQLRLLDTDTSMV 168
Cdd:MTH00023  78 PAVILVFIALPSLKLLYLMDEVVSPALTIKAIGHQWYWSYEYSDY---EGETLEFDSYMVPTSDLNSGDFRLLEVDNRLV 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325 169 VPVDTHIRFVVTAADVIHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTGHANMPIKIEAVSLPKFLEWL 248
Cdd:MTH00023 155 VPINTHVRILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWL 234
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 21-249 4.00e-96

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 281.06  E-value: 4.00e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325  21 YACYFQDSATPNQEGILELHDNIMFYLLVILGLVSWMLYTIVMtyskNPIAYKYIKHGQTIEVIWTIFPAVILLIIAFPS 100
Cdd:MTH00140   5 GQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLF----NKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325 101 FILLYLCDEVISPAMTIKAIGYQWYWKYEYSDFINdsgetVEFESYVIPDELLEEGQLRLLDTDTSMVVPVDTHIRFVVT 180
Cdd:MTH00140  81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSV-----IEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVT 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 830261325 181 AADVIHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTGHANMPIKIEAVSLPKFLEWLN 249
Cdd:MTH00140 156 SADVIHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLE 224
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 15-251 6.17e-94

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 275.51  E-value: 6.17e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325  15 NDVPTPYACYFQDSATPNQEGILELHDNIMFYLLVILGLVSWMLYTIVMTysKNPiaYKYIKHGQTIEVIWTIFPAVILL 94
Cdd:MTH00051   1 KDAPEPWQLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTT--KYY--HKYLFEGTLIEIIWTLIPAAILI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325  95 IIAFPSFILLYLCDEVISPAMTIKAIGYQWYWKYEYSDFindSGETVEFESYVIPDELLEEGQLRLLDTDTSMVVPVDTH 174
Cdd:MTH00051  77 FIAFPSLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDY---GTDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQ 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 830261325 175 IRFVVTAADVIHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTGHANMPIKIEAVSLPKFLEWLNEQ 251
Cdd:MTH00051 154 VRVLVTAADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQ 230
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 25-250 4.49e-91

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 268.00  E-value: 4.49e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325  25 FQDSATPNQEGILELHDNIMFYLLVILGLVSWMLYTIvmtySKNPIAYKYIKHGQTIEVIWTIFPAVILLIIAFPSFILL 104
Cdd:MTH00168   9 LQDAASPVMEELILFHDHALLILVLILTLVLYSLLVL----VTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPSLRLL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325 105 YLCDEVISPAMTIKAIGYQWYWKYEYSDFINdsgetVEFESYVIPDELLEEGQLRLLDTDTSMVVPVDTHIRFVVTAADV 184
Cdd:MTH00168  85 YLMDEIDKPDLTIKAVGHQWYWSYEYTDYND-----LEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 830261325 185 IHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTGHANMPIKIEAVSLPKFLEWLNE 250
Cdd:MTH00168 160 LHSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVDS 225
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 25-250 2.36e-87

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 258.49  E-value: 2.36e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325  25 FQDSATPNQEGILELHDNIMFYLLVILGLVSWMLYTIVmtysKNPIAYKYIKHGQTIEVIWTIFPAVILLIIAFPSFILL 104
Cdd:MTH00139   9 FQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLM----SNKFTSRSLLESQEVETIWTVLPAFILLFLALPSLRLL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325 105 YLCDEVISPAMTIKAIGYQWYWKYEYSDFINdsgetVEFESYVIPDELLEEGQLRLLDTDTSMVVPVDTHIRFVVTAADV 184
Cdd:MTH00139  85 YLMDEVSDPYLTFKAVGHQWYWSYEYSDFKN-----LSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 830261325 185 IHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTGHANMPIKIEAVSLPKFLEWLNE 250
Cdd:MTH00139 160 LHSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILE 225
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 25-249 8.68e-86

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 254.45  E-value: 8.68e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325  25 FQDSATPNQEGILELHDNIMFYLLVILGLVSWMLYTIVMTysknPIAYKYIKHGQTIEVIWTIFPAVILLIIAFPSFILL 104
Cdd:MTH00117   9 FQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTT----KLTHTNTVDAQEVELIWTILPAIVLILLALPSLRIL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325 105 YLCDEVISPAMTIKAIGYQWYWKYEYSDFindsgETVEFESYVIPDELLEEGQLRLLDTDTSMVVPVDTHIRFVVTAADV 184
Cdd:MTH00117  85 YLMDEINNPHLTIKAIGHQWYWSYEYTDY-----KDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 830261325 185 IHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTGHANMPIKIEAVSLPKFLEWLN 249
Cdd:MTH00117 160 LHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSS 224
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 113-247 1.67e-85

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: 250.18  E-value: 1.67e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325 113 PAMTIKAIGYQWYWKYEYSDFindsgETVEFESYVIPDELLEEGQLRLLDTDTSMVVPVDTHIRFVVTAADVIHDFAIPS 192
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDF-----NDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPS 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 830261325 193 LGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTGHANMPIKIEAVSLPKFLEW 247
Cdd:cd13912   76 LGIKVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 25-248 7.24e-84

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 249.77  E-value: 7.24e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325  25 FQDSATPNQEGILELHDNIMFYLLVILGLVSWMLYTIVMtyskNPIAYKYIKHGQTIEVIWTIFPAVILLIIAFPSFILL 104
Cdd:MTH00008   9 FQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMF----NKLSNRYILEAQQIETIWTILPALILLFLAFPSLRLL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325 105 YLCDEVISPAMTIKAIGYQWYWKYEYSDFINdsgetVEFESYVIPDELLEEGQLRLLDTDTSMVVPVDTHIRFVVTAADV 184
Cdd:MTH00008  85 YLMDEVSNPSITLKTIGHQWYWSYEYSDFSN-----LEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 830261325 185 IHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTGHANMPIKIEAVSLPKFLEWL 248
Cdd:MTH00008 160 IHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWV 223
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 25-247 1.75e-82

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 246.55  E-value: 1.75e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325  25 FQDSATPNQEGILELHDNIMFYLLVILGLVSWMLYTIVMTYSKNpiayKYIKHGQTIEVIWTIFPAVILLIIAFPSFILL 104
Cdd:MTH00129   9 FQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTN----KYILDSQEIEIIWTVLPAVILILIALPSLRIL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325 105 YLCDEVISPAMTIKAIGYQWYWKYEYSDFindsgETVEFESYVIPDELLEEGQLRLLDTDTSMVVPVDTHIRFVVTAADV 184
Cdd:MTH00129  85 YLMDEINDPHLTIKAMGHQWYWSYEYTDY-----EDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 830261325 185 IHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTGHANMPIKIEAVSLPKFLEW 247
Cdd:MTH00129 160 LHSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 25-250 2.32e-82

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 246.15  E-value: 2.32e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325  25 FQDSATPNQEGILELHDNIMFYLLVILGLVSWMLYTIVMTYSKNpiayKYIKHGQTIEVIWTIFPAVILLIIAFPSFILL 104
Cdd:MTH00038   9 LQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTN----RFFLEGQELETIWTIVPAFILIFIALPSLQLL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325 105 YLCDEVISPAMTIKAIGYQWYWKYEYSDFindsgETVEFESYVIPDELLEEGQLRLLDTDTSMVVPVDTHIRFVVTAADV 184
Cdd:MTH00038  85 YLMDEVNNPFLTIKAIGHQWYWSYEYTDY-----NDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 830261325 185 IHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTGHANMPIKIEAVSLPKFLEWLNE 250
Cdd:MTH00038 160 LHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSN 225
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
115-239 1.36e-80

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 237.69  E-value: 1.36e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325  115 MTIKAIGYQWYWKYEYSDFINdsgetVEFESYVIPDELLEEGQLRLLDTDTSMVVPVDTHIRFVVTAADVIHDFAIPSLG 194
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGD-----LEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLG 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 830261325  195 IKVDATPGRLNQVSALIQREGVFYGQCSELCGTGHANMPIKIEAV 239
Cdd:pfam00116  76 IKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 25-251 1.62e-80

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 241.22  E-value: 1.62e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325  25 FQDSATPNQEGILELHDNIMFYLLVILGLVSWMLyTIVMTY---SKNPIaykyikHGQTIEVIWTIFPAVILLIIAFPSF 101
Cdd:MTH00076   9 FQDAASPIMEELLHFHDHALMAVFLISTLVLYII-TIMMTTkltNTNTM------DAQEIEMVWTIMPAIILIVIALPSL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325 102 ILLYLCDEVISPAMTIKAIGYQWYWKYEYSDFINDSgetveFESYVIPDELLEEGQLRLLDTDTSMVVPVDTHIRFVVTA 181
Cdd:MTH00076  82 RILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLS-----FDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITA 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325 182 ADVIHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTGHANMPIKIEAVSLPKFLEWLNEQ 251
Cdd:MTH00076 157 EDVLHSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSM 226
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 25-247 5.89e-80

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 240.17  E-value: 5.89e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325  25 FQDSATPNQEGILELHDNIMFYLLVILGLVSWMLYTIVMTYSKNpiayKYIKHGQTIEVIWTIFPAVILLIIAFPSFILL 104
Cdd:MTH00185   9 LQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTN----KYILDSQEIEIVWTILPAIILIMIALPSLRIL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325 105 YLCDEVISPAMTIKAIGYQWYWKYEYSDFindsgETVEFESYVIPDELLEEGQLRLLDTDTSMVVPVDTHIRFVVTAADV 184
Cdd:MTH00185  85 YLMDEINDPHLTIKAMGHQWYWSYEYTDY-----EQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 830261325 185 IHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTGHANMPIKIEAVSLPKFLEW 247
Cdd:MTH00185 160 LHSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 18-247 1.35e-76

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 231.15  E-value: 1.35e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325  18 PTPYACYFQDSATPNQEGILELHDNIMFYLLVILGLVswmLYTIVMTYSKNpIAYKYIKHGQTIEVIWTIFPAVILLIIA 97
Cdd:MTH00098   2 AYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLV---LYIISLMLTTK-LTHTSTMDAQEVETIWTILPAIILILIA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325  98 FPSFILLYLCDEVISPAMTIKAIGYQWYWKYEYSDFindsgETVEFESYVIPDELLEEGQLRLLDTDTSMVVPVDTHIRF 177
Cdd:MTH00098  78 LPSLRILYMMDEINNPSLTVKTMGHQWYWSYEYTDY-----EDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRM 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325 178 VVTAADVIHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTGHANMPIKIEAVSLPKFLEW 247
Cdd:MTH00098 153 LISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKW 222
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 13-251 4.41e-74

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 226.06  E-value: 4.41e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325  13 IMNDVPTPYACYFQDSATPNQEGILELHDNIMFYLLVILGLVSWMLYTIVMtySKNPIAYKYIK-HGQTIEVIWTIFPAV 91
Cdd:MTH00027  25 MIKDANEPWQLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILL--GNNYYSYYWNKlDGSLIEVIWTLIPAF 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325  92 ILLIIAFPSFILLYLCDE-VISPAMTIKAIGYQWYWKYEYSDFindSGETVEFESYVIPDELLEEGQLRLLDTDTSMVVP 170
Cdd:MTH00027 103 ILILIAFPSLRLLYIMDEcGFSANITIKVTGHQWYWSYSYEDY---GEKNIEFDSYMIPTADLEFGDLRLLEVDNRLILP 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325 171 VDTHIRFVVTAADVIHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTGHANMPIKIEAVSLPKFLEWLNE 250
Cdd:MTH00027 180 VDTNVRVLITAADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWIGR 259


                 .
gi 830261325 251 Q 251
Cdd:MTH00027 260 E 260
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
24-251 2.16e-63

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 197.74  E-value: 2.16e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325  24 YFQDSATPNQEGILELHdNIMFYLLVILGLVSW--MLYTIVM-TYSKNPIAYKYIKHGQTIEVIWTIFPAVILLIIAFPS 100
Cdd:COG1622   20 SLPDPAGPIAEEIDDLF-WVSLIIMLVIFVLVFglLLYFAIRyRRRKGDADPAQFHHNTKLEIVWTVIPIIIVIVLAVPT 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325 101 FILLYLCDEVISPAMTIKAIGYQWYWKYEYsdfindsgetvefesyvipdelLEEGQLrlldTDTSMVVPVDTHIRFVVT 180
Cdd:COG1622   99 LRVLHALDDAPEDPLTVEVTGYQWKWLFRY----------------------PDQGIA----TVNELVLPVGRPVRFLLT 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 830261325 181 AADVIHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTGHANMPIKIEAVSLPKFLEWLNEQ 251
Cdd:COG1622  153 SADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQ 223
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 41-248 1.98e-59

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 187.52  E-value: 1.98e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325  41 DNIMFYLLVILGLVSWMLYTIVMTYSknpiaYKYIK-HGQTIEVIWTIFPAVILLIIAFPSFILLYLCDEV-ISPAMTIK 118
Cdd:MTH00080  27 CSLLFGEFVLAFVVFLFLYLISNNFY-----FKSKKiEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMnLDSNLTVK 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325 119 AIGYQWYWKYEYSDFINdsgetVEFESYVIPDELLEEGQLRLLDTDTSMVVPVDTHIRFVVTAADVIHDFAIPSLGIKVD 198
Cdd:MTH00080 102 VTGHQWYWSYEFSDIPG-----LEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMD 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 830261325 199 ATPGRLNQVSALIQREGVFYGQCSELCGTGHANMPIKIEAVSLPKFLEWL 248
Cdd:MTH00080 177 AMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWC 226
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 143-244 1.38e-45

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 149.97  E-value: 1.38e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325 143 FESYVIPDELLEEGQLRLLDTDTSMVVPVDTHIRFVVTAADVIHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGQCS 222
Cdd:PTZ00047  51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                         90       100
                 ....*....|....*....|..
gi 830261325 223 ELCGTGHANMPIKIEAVSLPKF 244
Cdd:PTZ00047 131 EMCGTLHGFMPIVVEAVSPEAY 152
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 29-249 3.77e-42

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: 142.52  E-value: 3.77e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325   29 ATPNQEGILELHDNIMFYLLVILGLVSWMLYTIVMTY---SKNPIAyKYIKHGQTIEVIWTIFPAVILL-IIAFPSFILL 104
Cdd:TIGR02866   2 GGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVWKFrrkGDEEKP-SQIHGNRRLEYVWTVIPLIIVVgLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325  105 YLCDEVISPAMTIKAIGYQWYWKYEYSDFindsgetvefesyvipdelleegqlrLLDTDTSMVVPVDTHIRFVVTAADV 184
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPES--------------------------GFTTVNELVLPAGTPVELQVTSKDV 134

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 830261325  185 IHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTGHANMPIKIEAVSLPKFLEWLN 249
Cdd:TIGR02866 135 IHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 79-239 2.13e-39

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 135.08  E-value: 2.13e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325  79 QTIEVIWTIFPAVILLIIAFpsFILLYL-CDEVISPAMTIKAIGYQWYWKYEYSDFIndsgetvEFESYVIPDELLEEGQ 157
Cdd:MTH00047  47 QVLELLWTVVPTLLVLVLCF--LNLNFItSDLDCFSSETIKVIGHQWYWSYEYSFGG-------SYDSFMTDDIFGVDKP 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325 158 LRLLdtdtsmvvpVDTHIRFVVTAADVIHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTGHANMPIKIE 237
Cdd:MTH00047 118 LRLV---------YGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIE 188


                 ..
gi 830261325 238 AV 239
Cdd:MTH00047 189 VV 190
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 17-103 4.15e-39

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: 130.91  E-value: 4.15e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325   17 VPTPYACYFQDSATPNQEGILELHDNIMFYLLVILGLVSWMLYTIVMTY--SKNPIAYKYIKHGQTIEVIWTIFPAVILL 94
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRFnrRKNPITARYTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 830261325   95 IIAFPSFIL 103
Cdd:pfam02790  81 LIALPSFKL 89
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 114-239 3.86e-30

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: 108.48  E-value: 3.86e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325 114 AMTIKAIGYQWYWKYEYSDfinDSGETVEfesyvipdelleegqlrlldTDTSMVVPVDTHIRFVVTAADVIHDFAIPSL 193
Cdd:cd04213    1 ALTIEVTGHQWWWEFRYPD---EPGRGIV--------------------TANELHIPVGRPVRLRLTSADVIHSFWVPSL 57

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 830261325 194 GIKVDATPGRLNQVSALIQREGVFYGQCSELCGTGHANMPIKIEAV 239
Cdd:cd04213   58 AGKMDMIPGRTNRLWLQADEPGVYRGQCAEFCGASHALMRFKVIAL 103
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 114-232 1.92e-27

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: 101.56  E-value: 1.92e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325 114 AMTIKAIGYQWYWKYEYSDfindSGETVEFESYVIPDELleegqlrlldtdtsmVVPVDTHIRFVVTAADVIHDFAIPSL 193
Cdd:cd13919    1 ALVVEVTAQQWAWTFRYPG----GDGKLGTDDDVTSPEL---------------HLPVGRPVLFNLRSKDVIHSFWVPEF 61

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 830261325 194 GIKVDATPGRLNQVSALIQREGVFYGQCSELCGTGHANM 232
Cdd:cd13919   62 RVKQDAVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 115-237 1.57e-25

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: 96.21  E-value: 1.57e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325 115 MTIKAIGYQWYWKYEYSDfindsgetvefesyvipdelleegqlrlLDTDTSMVVPVDTHIRFVVTAADVIHDFAIPSLG 194
Cdd:cd13842    1 LTVYVTGVQWSWTFIYPN----------------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLG 52

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 830261325 195 IKVDATPGRLNQVSALIQREGVFYGQCSELCGTGHANMPIKIE 237
Cdd:cd13842   53 VKVDAVPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 116-248 1.30e-24

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


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 94.01  E-value: 1.30e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325 116 TIKAIGYQWYWKYEYsdfiNDSGetvefesyvipdelleegqlrlLDTDTSMVVPVDTHIRFVVTAADVIHDFAIPSLGI 195
Cdd:cd13914    2 EIEVEAYQWGWEFSY----PEAN----------------------VTTSEQLVIPADRPVYFRITSRDVIHAFHVPELGL 55

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 830261325 196 KVDATPGRLNQVSALIQREGVFYGQCSELCGTGHANMPIKIEAVSLPKFLEWL 248
Cdd:cd13914   56 KQDAFPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 114-238 4.77e-24

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


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 92.31  E-value: 4.77e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325 114 AMTIKAIGYQWYWKYEYSdfiNDSGETVEfesyvipdelleegqlrlldtdtsMVVPVDTHIRFVVTAADVIHDFAIPSL 193
Cdd:cd13915    1 ALEIQVTGRQWMWEFTYP---NGKREINE------------------------LHVPVGKPVRLILTSKDVIHSFYVPAF 53

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 830261325 194 GIKVDATPGRLNQVSALIQREGVFYGQCSELCGTGHANMPIKIEA 238
Cdd:cd13915   54 RIKQDVVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGMIGKVRV 98
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 91-248 1.38e-20

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


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 84.43  E-value: 1.38e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325  91 VILLIIAfPSFILLYLCD---EVISPAMTIKAIGYQWYWKYEYSDFINDSGEtvefesyvipdelleegqlrlldtdtsM 167
Cdd:cd13918    7 VISLIVW-TYGMLLYVEDppdEADEDALEVEVEGFQFGWQFEYPNGVTTGNT---------------------------L 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325 168 VVPVDTHIRFVVTAADVIHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTGHANMPIKIEAVSLPKFLEW 247
Cdd:cd13918   59 RVPADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAW 138


                 .
gi 830261325 248 L 248
Cdd:cd13918  139 Y 139
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 163-239 5.65e-15

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: 68.37  E-value: 5.65e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 830261325 163 TDTSMVVPVDTHIRFVVTAADVIHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTGHANMPIKIEAV 239
Cdd:cd13913   23 NPNEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNMYGKIIVE 99
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 116-239 1.38e-08

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: 50.84  E-value: 1.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830261325 116 TIKAIGYQWYWKyeysdfindsgetvefesyvipdelleegqlrlLDTDTsmvVPVDTHIRFVVTAADVIHDFAI--PSL 193
Cdd:cd13916    2 VVAVTGHQWYWE---------------------------------LSRTE---IPAGKPVEFRVTSADVNHGFGIydPDM 45

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 830261325 194 GI--KVDATPGRLNQVSALIQREGVFYGQCSELCGTGHANMPIKIEAV 239
Cdd:cd13916   46 RLlaQTQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVMMAEFTVV 93
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 167-239 9.28e-08

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: 48.70  E-value: 9.28e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 830261325 167 MVVPVDTHIRFVVTAADVIHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTGHANMPIKIEAV 239
Cdd:cd04212   27 LVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDMKFKVLAV 99
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 176-236 5.37e-03

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: 259984 [Multi-domain]  Cd Length: 88  Bit Score: 35.04  E-value: 5.37e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 830261325 176 RFVVTAADVIHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTGHANMPIKI 236
Cdd:cd13917   25 RLHLSSLDVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIICNEYCGIGHHTMHGRI 85
 
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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