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Conserved domains on  [gi|162951843|ref|YP_001621413|]
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cytochrome c oxidase subunit 2 (mitochondrion) [Debaryomyces hansenii]

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
 10-237 6.17e-96

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 280.18  E-value: 6.17e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843  10 WG-MRFQDAATPNAEGMHELYDHMMYYLALMLGLVSYMLYVMMKdyknNTFAYKYIKHGQTLEIMWTMFPAVMLLLMAFP 88
Cdd:MTH00154   4 WSnLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLF----NKFTNRFLLEGQEIEIIWTILPAIILIFIALP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843  89 SFMLLYLCDEVLTPAMTVKVVGLQWYWKYEYSDFVSetgetVEYESYVMPEDMLEEGQLRLLDTDTSMVVPVDTHVRFMV 168
Cdd:MTH00154  80 SLRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKN-----IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILI 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 162951843 169 TANDVLHCFTMPSLGIKVDACPGRLNQVSALMQRTGVYYGQCSELCGVNHGLMPIKTECVPIGDFVEWL 237
Cdd:MTH00154 155 TAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWI 223
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 10-237 6.17e-96

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 280.18  E-value: 6.17e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843  10 WG-MRFQDAATPNAEGMHELYDHMMYYLALMLGLVSYMLYVMMKdyknNTFAYKYIKHGQTLEIMWTMFPAVMLLLMAFP 88
Cdd:MTH00154   4 WSnLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLF----NKFTNRFLLEGQEIEIIWTILPAIILIFIALP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843  89 SFMLLYLCDEVLTPAMTVKVVGLQWYWKYEYSDFVSetgetVEYESYVMPEDMLEEGQLRLLDTDTSMVVPVDTHVRFMV 168
Cdd:MTH00154  80 SLRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKN-----IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILI 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 162951843 169 TANDVLHCFTMPSLGIKVDACPGRLNQVSALMQRTGVYYGQCSELCGVNHGLMPIKTECVPIGDFVEWL 237
Cdd:MTH00154 155 TAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWI 223
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 102-236 5.46e-77

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: 228.61  E-value: 5.46e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843 102 PAMTVKVVGLQWYWKYEYSDFVsetgeTVEYESYVMPEDMLEEGQLRLLDTDTSMVVPVDTHVRFMVTANDVLHCFTMPS 181
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFN-----DLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPS 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 162951843 182 LGIKVDACPGRLNQVSALMQRTGVYYGQCSELCGVNHGLMPIKTECVPIGDFVEW 236
Cdd:cd13912   76 LGIKVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
104-228 1.80e-68

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 206.49  E-value: 1.80e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843  104 MTVKVVGLQWYWKYEYSDFVsetgeTVEYESYVMPEDMLEEGQLRLLDTDTSMVVPVDTHVRFMVTANDVLHCFTMPSLG 183
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFG-----DLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLG 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 162951843  184 IKVDACPGRLNQVSALMQRTGVYYGQCSELCGVNHGLMPIKTECV 228
Cdd:pfam00116  76 IKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
10-240 9.46e-55

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 175.40  E-value: 9.46e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843  10 WGMRFQDAATPNAEGMHELYDhMMYYLALMLGLV--SYMLYVMMK-DYKNNTFAYKYIKHGQTLEIMWTMFPAVMLLLMA 86
Cdd:COG1622   17 GQLSLPDPAGPIAEEIDDLFW-VSLIIMLVIFVLvfGLLLYFAIRyRRRKGDADPAQFHHNTKLEIVWTVIPIIIVIVLA 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843  87 FPSFMLLYLCDEVLTPAMTVKVVGLQWYWKYEYsdfvsetgetveyesyvmpedmLEEGQLrlldTDTSMVVPVDTHVRF 166
Cdd:COG1622   96 VPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRY----------------------PDQGIA----TVNELVLPVGRPVRF 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162951843 167 MVTANDVLHCFTMPSLGIKVDACPGRLNQVSALMQRTGVYYGQCSELCGVNHGLMPIKTECVPIGDFVEWLGEQ 240
Cdd:COG1622  150 LLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQ 223
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 17-237 1.11e-39

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: 135.97  E-value: 1.11e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843   17 AATPNAEGMHELYDHMMYYLALMLGLV-SYMLYVMMKDYKNNTFAY-KYIKHGQTLEIMWTMFPAVMLL-LMAFPSFMLL 93
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVaALLAYVVWKFRRKGDEEKpSQIHGNRRLEYVWTVIPLIIVVgLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843   94 YLCDEVLTPAMTVKVVGLQWYWKYEYSDFVSETGETVeyesyvmpedmleegqlrlldtdtsmVVPVDTHVRFMVTANDV 173
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPESGFTTVNEL--------------------------VLPAGTPVELQVTSKDV 134

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162951843  174 LHCFTMPSLGIKVDACPGRLNQVSALMQRTGVYYGQCSELCGVNHGLMPIKTECVPIGDFVEWL 237
Cdd:TIGR02866 135 IHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYV 198
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 10-237 6.17e-96

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 280.18  E-value: 6.17e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843  10 WG-MRFQDAATPNAEGMHELYDHMMYYLALMLGLVSYMLYVMMKdyknNTFAYKYIKHGQTLEIMWTMFPAVMLLLMAFP 88
Cdd:MTH00154   4 WSnLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLF----NKFTNRFLLEGQEIEIIWTILPAIILIFIALP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843  89 SFMLLYLCDEVLTPAMTVKVVGLQWYWKYEYSDFVSetgetVEYESYVMPEDMLEEGQLRLLDTDTSMVVPVDTHVRFMV 168
Cdd:MTH00154  80 SLRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKN-----IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILI 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 162951843 169 TANDVLHCFTMPSLGIKVDACPGRLNQVSALMQRTGVYYGQCSELCGVNHGLMPIKTECVPIGDFVEWL 237
Cdd:MTH00154 155 TAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWI 223
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 8-237 7.05e-90

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 264.92  E-value: 7.05e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843   8 TPWGMRFQDAATPNAEGMHELYDHMMYYLALMLGLVSYMLYVMMKdyknNTFAYKYIKHGQTLEIMWTMFPAVMLLLMAF 87
Cdd:MTH00168   3 TYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVT----SKYTNRFLLDSQMIEFVWTIIPAFILISLAL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843  88 PSFMLLYLCDEVLTPAMTVKVVGLQWYWKYEYSDFVSetgetVEYESYVMPEDMLEEGQLRLLDTDTSMVVPVDTHVRFM 167
Cdd:MTH00168  79 PSLRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYND-----LEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVL 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843 168 VTANDVLHCFTMPSLGIKVDACPGRLNQVSALMQRTGVYYGQCSELCGVNHGLMPIKTECVPIGDFVEWL 237
Cdd:MTH00168 154 VTSADVLHSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWV 223
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 5-237 1.48e-89

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 264.69  E-value: 1.48e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843   5 DVPTPWGMRFQDAATPNAEGMHELYDHMMYYLALMLGLVSYMLYVMMkdykNNTFAYKYIKHGQTLEIMWTMFPAVMLLL 84
Cdd:MTH00023   9 DIPEPWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEAL----NGKFYDRFLVDGTFLEIVWTIIPAVILVF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843  85 MAFPSFMLLYLCDEVLTPAMTVKVVGLQWYWKYEYSDFvseTGETVEYESYVMPEDMLEEGQLRLLDTDTSMVVPVDTHV 164
Cdd:MTH00023  85 IALPSLKLLYLMDEVVSPALTIKAIGHQWYWSYEYSDY---EGETLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHV 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162951843 165 RFMVTANDVLHCFTMPSLGIKVDACPGRLNQVSALMQRTGVYYGQCSELCGVNHGLMPIKTECVPIGDFVEWL 237
Cdd:MTH00023 162 RILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWL 234
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 10-238 9.92e-88

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 259.49  E-value: 9.92e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843  10 WG-MRFQDAATPNAEGMHELYDHMMYYLALMLGLVSYMLYVMMKdyknNTFAYKYIKHGQTLEIMWTMFPAVMLLLMAFP 88
Cdd:MTH00140   4 WGqLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLF----NKFSCRTILEAQKLETIWTIVPALILVFLALP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843  89 SFMLLYLCDEVLTPAMTVKVVGLQWYWKYEYSDFVSetgetVEYESYVMPEDMLEEGQLRLLDTDTSMVVPVDTHVRFMV 168
Cdd:MTH00140  80 SLRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSV-----IEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLV 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843 169 TANDVLHCFTMPSLGIKVDACPGRLNQVSALMQRTGVYYGQCSELCGVNHGLMPIKTECVPIGDFVEWLG 238
Cdd:MTH00140 155 TSADVIHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLE 224
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 5-242 5.76e-86

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 255.09  E-value: 5.76e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843   5 DVPTPWGMRFQDAATPNAEGMHELYDHMMYYLALMLGLVsymLYVMMKDYkNNTFAYKYIKHGQTLEIMWTMFPAVMLLL 84
Cdd:MTH00051   2 DAPEPWQLGFQDAASPVMEEIIFFHDQIMFILTIIITTV---LWLIIRAL-TTKYYHKYLFEGTLIEIIWTLIPAAILIF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843  85 MAFPSFMLLYLCDEVLTPAMTVKVVGLQWYWKYEYSDFvseTGETVEYESYVMPEDMLEEGQLRLLDTDTSMVVPVDTHV 164
Cdd:MTH00051  78 IAFPSLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDY---GTDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQV 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162951843 165 RFMVTANDVLHCFTMPSLGIKVDACPGRLNQVSALMQRTGVYYGQCSELCGVNHGLMPIKTECVPIGDFVEWLGEQEN 242
Cdd:MTH00051 155 RVLVTAADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQSE 232
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 10-239 6.78e-83

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 246.94  E-value: 6.78e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843  10 WGM-RFQDAATPNAEGMHELYDHMMYYLALMLGLVSYMLYVMMKdyknNTFAYKYIKHGQTLEIMWTMFPAVMLLLMAFP 88
Cdd:MTH00139   4 WGQlGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMS----NKFTSRSLLESQEVETIWTVLPAFILLFLALP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843  89 SFMLLYLCDEVLTPAMTVKVVGLQWYWKYEYSDFvsetgETVEYESYVMPEDMLEEGQLRLLDTDTSMVVPVDTHVRFMV 168
Cdd:MTH00139  80 SLRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDF-----KNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALI 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 162951843 169 TANDVLHCFTMPSLGIKVDACPGRLNQVSALMQRTGVYYGQCSELCGVNHGLMPIKTECVPIGDFVEWLGE 239
Cdd:MTH00139 155 TAADVLHSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILE 225
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 14-237 4.34e-80

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 239.82  E-value: 4.34e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843  14 FQDAATPNAEGMHELYDHMMYYLALMLGLVSYMLYVMM--KDYKNNTfaykyiKHGQTLEIMWTMFPAVMLLLMAFPSFM 91
Cdd:MTH00117   9 FQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLttKLTHTNT------VDAQEVELIWTILPAIVLILLALPSLR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843  92 LLYLCDEVLTPAMTVKVVGLQWYWKYEYSDFvsetgETVEYESYVMPEDMLEEGQLRLLDTDTSMVVPVDTHVRFMVTAN 171
Cdd:MTH00117  83 ILYLMDEINNPHLTIKAIGHQWYWSYEYTDY-----KDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAE 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 162951843 172 DVLHCFTMPSLGIKVDACPGRLNQVSALMQRTGVYYGQCSELCGVNHGLMPIKTECVPIGDFVEWL 237
Cdd:MTH00117 158 DVLHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWS 223
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 10-237 3.85e-78

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 235.14  E-value: 3.85e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843  10 WG-MRFQDAATPNAEGMHELYDHMMYYLALMLGLVSYMLYVMMKdyknNTFAYKYIKHGQTLEIMWTMFPAVMLLLMAFP 88
Cdd:MTH00008   4 WGqLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMF----NKLSNRYILEAQQIETIWTILPALILLFLAFP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843  89 SFMLLYLCDEVLTPAMTVKVVGLQWYWKYEYSDFVSetgetVEYESYVMPEDMLEEGQLRLLDTDTSMVVPVDTHVRFMV 168
Cdd:MTH00008  80 SLRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSN-----LEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLV 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 162951843 169 TANDVLHCFTMPSLGIKVDACPGRLNQVSALMQRTGVYYGQCSELCGVNHGLMPIKTECVPIGDFVEWL 237
Cdd:MTH00008 155 TAADVIHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWV 223
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 102-236 5.46e-77

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: 228.61  E-value: 5.46e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843 102 PAMTVKVVGLQWYWKYEYSDFVsetgeTVEYESYVMPEDMLEEGQLRLLDTDTSMVVPVDTHVRFMVTANDVLHCFTMPS 181
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFN-----DLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPS 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 162951843 182 LGIKVDACPGRLNQVSALMQRTGVYYGQCSELCGVNHGLMPIKTECVPIGDFVEW 236
Cdd:cd13912   76 LGIKVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 9-236 1.28e-76

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 231.31  E-value: 1.28e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843   9 PWGMRFQDAATPNAEGMHELYDHMMYYLALMLGLVSYMLYVMMkdykNNTFAYKYIKHGQTLEIMWTMFPAVMLLLMAFP 88
Cdd:MTH00185   4 PSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMV----TTKLTNKYILDSQEIEIVWTILPAIILIMIALP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843  89 SFMLLYLCDEVLTPAMTVKVVGLQWYWKYEYSDFvsetgETVEYESYVMPEDMLEEGQLRLLDTDTSMVVPVDTHVRFMV 168
Cdd:MTH00185  80 SLRILYLMDEINDPHLTIKAMGHQWYWSYEYTDY-----EQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLI 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162951843 169 TANDVLHCFTMPSLGIKVDACPGRLNQVSALMQRTGVYYGQCSELCGVNHGLMPIKTECVPIGDFVEW 236
Cdd:MTH00185 155 TAEDVLHSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 8-239 4.27e-76

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 229.97  E-value: 4.27e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843   8 TPWGMRFQDAATPNAEGMHELYDHMMYYLALMLGLVSYMLYVMMkdykNNTFAYKYIKHGQTLEIMWTMFPAVMLLLMAF 87
Cdd:MTH00038   3 TWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLL----FSSPTNRFFLEGQELETIWTIVPAFILIFIAL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843  88 PSFMLLYLCDEVLTPAMTVKVVGLQWYWKYEYSDFvsetgETVEYESYVMPEDMLEEGQLRLLDTDTSMVVPVDTHVRFM 167
Cdd:MTH00038  79 PSLQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDY-----NDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVL 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 162951843 168 VTANDVLHCFTMPSLGIKVDACPGRLNQVSALMQRTGVYYGQCSELCGVNHGLMPIKTECVPIGDFVEWLGE 239
Cdd:MTH00038 154 VSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSN 225
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 9-242 4.93e-76

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 229.67  E-value: 4.93e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843   9 PWGMRFQDAATPNAEGMHELYDHMMYYLALMLGLVSYMLYVMMKDYKNNTFAYKyikhGQTLEIMWTMFPAVMLLLMAFP 88
Cdd:MTH00076   4 PSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMD----AQEIEMVWTIMPAIILIVIALP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843  89 SFMLLYLCDEVLTPAMTVKVVGLQWYWKYEYSDFvsetgETVEYESYVMPEDMLEEGQLRLLDTDTSMVVPVDTHVRFMV 168
Cdd:MTH00076  80 SLRILYLMDEINDPHLTVKAIGHQWYWSYEYTDY-----EDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLI 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162951843 169 TANDVLHCFTMPSLGIKVDACPGRLNQVSALMQRTGVYYGQCSELCGVNHGLMPIKTECVPIGDFVEWLGEQEN 242
Cdd:MTH00076 155 TAEDVLHSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSMLE 228
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 14-236 7.97e-76

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 229.22  E-value: 7.97e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843  14 FQDAATPNAEGMHELYDHMMYYLALMLGLVSYMLYVMMKDYKNNtfayKYIKHGQTLEIMWTMFPAVMLLLMAFPSFMLL 93
Cdd:MTH00129   9 FQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTN----KYILDSQEIEIIWTVLPAVILILIALPSLRIL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843  94 YLCDEVLTPAMTVKVVGLQWYWKYEYSDFvsetgETVEYESYVMPEDMLEEGQLRLLDTDTSMVVPVDTHVRFMVTANDV 173
Cdd:MTH00129  85 YLMDEINDPHLTIKAMGHQWYWSYEYTDY-----EDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162951843 174 LHCFTMPSLGIKVDACPGRLNQVSALMQRTGVYYGQCSELCGVNHGLMPIKTECVPIGDFVEW 236
Cdd:MTH00129 160 LHSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 7-236 4.46e-72

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 219.59  E-value: 4.46e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843   7 PTPWGMRFQDAATPNAEGMHELYDHMMYYLALMLGLVSYMLYVMMKDYKNNTfaykYIKHGQTLEIMWTMFPAVMLLLMA 86
Cdd:MTH00098   2 AYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHT----STMDAQEVETIWTILPAIILILIA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843  87 FPSFMLLYLCDEVLTPAMTVKVVGLQWYWKYEYSDFvsetgETVEYESYVMPEDMLEEGQLRLLDTDTSMVVPVDTHVRF 166
Cdd:MTH00098  78 LPSLRILYMMDEINNPSLTVKTMGHQWYWSYEYTDY-----EDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRM 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843 167 MVTANDVLHCFTMPSLGIKVDACPGRLNQVSALMQRTGVYYGQCSELCGVNHGLMPIKTECVPIGDFVEW 236
Cdd:MTH00098 153 LISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKW 222
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 5-241 1.43e-69

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 214.50  E-value: 1.43e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843   5 DVPTPWGMRFQDAATPNAEGMHELYDHMMYYLALMLGLVSYMLYVMMkdYKNNTFAYKYIK-HGQTLEIMWTMFPAVMLL 83
Cdd:MTH00027  28 DANEPWQLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRIL--LGNNYYSYYWNKlDGSLIEVIWTLIPAFILI 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843  84 LMAFPSFMLLYLCDE-VLTPAMTVKVVGLQWYWKYEYSDFvsetGE-TVEYESYVMPEDMLEEGQLRLLDTDTSMVVPVD 161
Cdd:MTH00027 106 LIAFPSLRLLYIMDEcGFSANITIKVTGHQWYWSYSYEDY----GEkNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVD 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843 162 THVRFMVTANDVLHCFTMPSLGIKVDACPGRLNQVSALMQRTGVYYGQCSELCGVNHGLMPIKTECVPIGDFVEWLGEQE 241
Cdd:MTH00027 182 TNVRVLITAADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWIGRED 261
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
104-228 1.80e-68

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 206.49  E-value: 1.80e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843  104 MTVKVVGLQWYWKYEYSDFVsetgeTVEYESYVMPEDMLEEGQLRLLDTDTSMVVPVDTHVRFMVTANDVLHCFTMPSLG 183
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFG-----DLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLG 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 162951843  184 IKVDACPGRLNQVSALMQRTGVYYGQCSELCGVNHGLMPIKTECV 228
Cdd:pfam00116  76 IKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 25-237 5.32e-55

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 176.35  E-value: 5.32e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843  25 MHELYDHMMYYLALMLGLVSYMLYVMMkdyknNTFAYKYIK-HGQTLEIMWTMFPAVMLLLMAFPSFMLLYLCDEV-LTP 102
Cdd:MTH00080  22 FHNFNCSLLFGEFVLAFVVFLFLYLIS-----NNFYFKSKKiEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMnLDS 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843 103 AMTVKVVGLQWYWKYEYSDFVSetgetVEYESYVMPEDMLEEGQLRLLDTDTSMVVPVDTHVRFMVTANDVLHCFTMPSL 182
Cdd:MTH00080  97 NLTVKVTGHQWYWSYEFSDIPG-----LEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSL 171

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 162951843 183 GIKVDACPGRLNQVSALMQRTGVYYGQCSELCGVNHGLMPIKTECVPIGDFVEWL 237
Cdd:MTH00080 172 SIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWC 226
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
10-240 9.46e-55

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 175.40  E-value: 9.46e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843  10 WGMRFQDAATPNAEGMHELYDhMMYYLALMLGLV--SYMLYVMMK-DYKNNTFAYKYIKHGQTLEIMWTMFPAVMLLLMA 86
Cdd:COG1622   17 GQLSLPDPAGPIAEEIDDLFW-VSLIIMLVIFVLvfGLLLYFAIRyRRRKGDADPAQFHHNTKLEIVWTVIPIIIVIVLA 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843  87 FPSFMLLYLCDEVLTPAMTVKVVGLQWYWKYEYsdfvsetgetveyesyvmpedmLEEGQLrlldTDTSMVVPVDTHVRF 166
Cdd:COG1622   96 VPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRY----------------------PDQGIA----TVNELVLPVGRPVRF 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162951843 167 MVTANDVLHCFTMPSLGIKVDACPGRLNQVSALMQRTGVYYGQCSELCGVNHGLMPIKTECVPIGDFVEWLGEQ 240
Cdd:COG1622  150 LLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQ 223
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 17-237 1.11e-39

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: 135.97  E-value: 1.11e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843   17 AATPNAEGMHELYDHMMYYLALMLGLV-SYMLYVMMKDYKNNTFAY-KYIKHGQTLEIMWTMFPAVMLL-LMAFPSFMLL 93
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVaALLAYVVWKFRRKGDEEKpSQIHGNRRLEYVWTVIPLIIVVgLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843   94 YLCDEVLTPAMTVKVVGLQWYWKYEYSDFVSETGETVeyesyvmpedmleegqlrlldtdtsmVVPVDTHVRFMVTANDV 173
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPESGFTTVNEL--------------------------VLPAGTPVELQVTSKDV 134

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162951843  174 LHCFTMPSLGIKVDACPGRLNQVSALMQRTGVYYGQCSELCGVNHGLMPIKTECVPIGDFVEWL 237
Cdd:TIGR02866 135 IHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYV 198
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 29-228 1.75e-36

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 127.38  E-value: 1.75e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843  29 YDHMMYYLAL---MLGLVSYMLYVMMKDYKNNtfaykyIKHG---QTLEIMWTMFPAVMLLLMAFpsFMLLYL-CDEVLT 101
Cdd:MTH00047   8 YDIVCYILALcvfIPCWVYIMLCWQVVSGNGS------VNFGsenQVLELLWTVVPTLLVLVLCF--LNLNFItSDLDCF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843 102 PAMTVKVVGLQWYWKYEYSDfvsetgeTVEYESYVMPEDMLEEGQLRLLdtdtsmvvpVDTHVRFMVTANDVLHCFTMPS 181
Cdd:MTH00047  80 SSETIKVIGHQWYWSYEYSF-------GGSYDSFMTDDIFGVDKPLRLV---------YGVPYHLLVTSSDVIHSFSVPD 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 162951843 182 LGIKVDACPGRLNQVSALMQRTGVYYGQCSELCGVNHGLMPIKTECV 228
Cdd:MTH00047 144 LNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVV 190
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 132-228 1.72e-35

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 123.78  E-value: 1.72e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843 132 YESYVMPEDMLEEGQLRLLDTDTSMVVPVDTHVRFMVTANDVLHCFTMPSLGIKVDACPGRLNQVSALMQRTGVYYGQCS 211
Cdd:PTZ00047  51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                         90
                 ....*....|....*..
gi 162951843 212 ELCGVNHGLMPIKTECV 228
Cdd:PTZ00047 131 EMCGTLHGFMPIVVEAV 147
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 6-92 6.91e-32

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: 112.43  E-value: 6.91e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843    6 VPTPWGMRFQDAATPNAEGMHELYDHMMYYLALMLGLVSYMLYVMMKDY--KNNTFAYKYIKHGQTLEIMWTMFPAVMLL 83
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRFnrRKNPITARYTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 162951843   84 LMAFPSFML 92
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), ...
 103-221 1.42e-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: 88.45  E-value: 1.42e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843 103 AMTVKVVGLQWYWKYEYSDfvsETGETVEyesyvmpedmleegqlrlldTDTSMVVPVDTHVRFMVTANDVLHCFTMPSL 182
Cdd:cd04213    1 ALTIEVTGHQWWWEFRYPD---EPGRGIV--------------------TANELHIPVGRPVRLRLTSADVIHSFWVPSL 57

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 162951843 183 GIKVDACPGRLNQVSALMQRTGVYYGQCSELCGVNHGLM 221
Cdd:cd04213   58 AGKMDMIPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 84-237 4.62e-22

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: 88.28  E-value: 4.62e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843  84 LMAFPSFMLLYLCDEVLTP---AMTVKVVGLQWYWKYEYSDFVSETGEtveyesyvmpedmleegqlrlldtdtsMVVPV 160
Cdd:cd13918   10 LIVWTYGMLLYVEDPPDEAdedALEVEVEGFQFGWQFEYPNGVTTGNT---------------------------LRVPA 62

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162951843 161 DTHVRFMVTANDVLHCFTMPSLGIKVDACPGRLNQVSALMQRTGVYYGQCSELCGVNHGLMPIKTECVPIGDFVEWL 237
Cdd:cd13918   63 DTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAWY 139
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 103-221 5.88e-22

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: 86.93  E-value: 5.88e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843 103 AMTVKVVGLQWYWKYEYSDfvsetgetveYESYVMPEDMLEEGQLRLldtdtsmvvPVDTHVRFMVTANDVLHCFTMPSL 182
Cdd:cd13919    1 ALVVEVTAQQWAWTFRYPG----------GDGKLGTDDDVTSPELHL---------PVGRPVLFNLRSKDVIHSFWVPEF 61

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 162951843 183 GIKVDACPGRLNQVSALMQRTGVYYGQCSELCGVNHGLM 221
Cdd:cd13919   62 RVKQDAVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 104-226 4.38e-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: 84.27  E-value: 4.38e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843 104 MTVKVVGLQWYWKYEYSDfvsetgetveyesyvmpedmleegqlrlLDTDTSMVVPVDTHVRFMVTANDVLHCFTMPSLG 183
Cdd:cd13842    1 LTVYVTGVQWSWTFIYPN----------------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLG 52

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 162951843 184 IKVDACPGRLNQVSALMQRTGVYYGQCSELCGVNHGLMPIKTE 226
Cdd:cd13842   53 VKVDAVPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 105-237 2.97e-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: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 82.84  E-value: 2.97e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843 105 TVKVVGLQWYWKYEYSDfvsetgETVeyesyvmpedmleegqlrllDTDTSMVVPVDTHVRFMVTANDVLHCFTMPSLGI 184
Cdd:cd13914    2 EIEVEAYQWGWEFSYPE------ANV--------------------TTSEQLVIPADRPVYFRITSRDVIHAFHVPELGL 55

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 162951843 185 KVDACPGRLNQVSALMQRTGVYYGQCSELCGVNHGLMPIKTECVPIGDFVEWL 237
Cdd:cd13914   56 KQDAFPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 103-221 5.47e-19

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: 78.82  E-value: 5.47e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843 103 AMTVKVVGLQWYWKYEYSDFVSETGEtveyesyvmpedmleegqlrlldtdtsMVVPVDTHVRFMVTANDVLHCFTMPSL 182
Cdd:cd13915    1 ALEIQVTGRQWMWEFTYPNGKREINE---------------------------LHVPVGKPVRLILTSKDVIHSFYVPAF 53

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 162951843 183 GIKVDACPGRLNQVSALMQRTGVYYGQCSELCGVNHGLM 221
Cdd:cd13915   54 RIKQDVVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 152-221 3.29e-11

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: 58.35  E-value: 3.29e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843 152 TDTSMVVPVDTHVRFMVTANDVLHCFTMPSLGIKVDACPGRLNQVSALMQRTGVYYGQCSELCGVNHGLM 221
Cdd:cd13913   23 NPNEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 105-221 4.92e-05

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


Pssm-ID: 259983 [Multi-domain]  Cd Length: 93  Bit Score: 41.21  E-value: 4.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843 105 TVKVVGLQWYWkyeysdfvsetgetveyesyVMPEDMLEEGQLrlldtdtsmvvpvdthVRFMVTANDVLHCFTM--PSL 182
Cdd:cd13916    2 VVAVTGHQWYW--------------------ELSRTEIPAGKP----------------VEFRVTSADVNHGFGIydPDM 45

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 162951843 183 GI--KVDACPGRLNQVSALMQRTGVYYGQCSELCGVNHGLM 221
Cdd:cd13916   46 RLlaQTQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 104-215 3.47e-04

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


Pssm-ID: 259874 [Multi-domain]  Cd Length: 99  Bit Score: 38.68  E-value: 3.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951843 104 MTVKVVGLQWYWKYEYSDfvsETGETVEYesyvmpedmleegqlrlldtdtsMVVPVDTHVRFMVTANDVLHCFTMPSLG 183
Cdd:cd04212    1 LEIQVVSLDWKWLFIYPE---QGIATVNE-----------------------LVIPVGRPVNFRLTSDSVMNSFFIPQLG 54

                         90       100       110
                 ....*....|....*....|....*....|..
gi 162951843 184 IKVDACPGRLNQVSALMQRTGVYYGQCSELCG 215
Cdd:cd04212   55 GQIYAMAGMQTQLHLIADKPGTYQGLSANYSG 86
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 165-221 4.06e-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: 35.42  E-value: 4.06e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 162951843 165 RFMVTANDVLHCFTMPSLGIKVDACPGRLNQVSALMQRTGVYYGQCSELCGVNHGLM 221
Cdd:cd13917   25 RLHLSSLDVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIICNEYCGIGHHTM 81
 
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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