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Conserved domains on  [gi|63025098|ref|YP_232792|]
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cytochrome c oxidase subunit II (mitochondrion) [Geodia neptuni]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11475883)

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 MTH00051
cytochrome c oxidase subunit II; Provisional
 14-247 2.26e-170

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 468.88  E-value: 2.26e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098   14 RDAPEPWQLGFQDAASPVMEEIIFFHDQIMFILTIIVTIVLWLLIRALTLKHYYKYLFEGTLIEIIWTLVPACVLIFIAF 93
Cdd:MTH00051   1 KDAPEPWQLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098   94 PSLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYGTNTIEFDSYMVPTSDLNKGDLRLLEVDNRLIVPIQTQVRVLVTA 173
Cdd:MTH00051  81 PSLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYGTDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 63025098  174 ADVLHAFAVPSLGVKVDAVPGRLNQTSFFLKRPGVFYGQCSELCGANHSFMPIVIEGVSLEKYVSWVATQSEEA 247
Cdd:MTH00051 161 ADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQSEEI 234
 
Name Accession Description Interval E-value
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 14-247 2.26e-170

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 468.88  E-value: 2.26e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098   14 RDAPEPWQLGFQDAASPVMEEIIFFHDQIMFILTIIVTIVLWLLIRALTLKHYYKYLFEGTLIEIIWTLVPACVLIFIAF 93
Cdd:MTH00051   1 KDAPEPWQLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098   94 PSLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYGTNTIEFDSYMVPTSDLNKGDLRLLEVDNRLIVPIQTQVRVLVTA 173
Cdd:MTH00051  81 PSLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYGTDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 63025098  174 ADVLHAFAVPSLGVKVDAVPGRLNQTSFFLKRPGVFYGQCSELCGANHSFMPIVIEGVSLEKYVSWVATQSEEA 247
Cdd:MTH00051 161 ADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQSEEI 234
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 108-239 7.53e-97

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: 278.68  E-value: 7.53e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098 108 PALTIKAIGHQWYWSYEYSDYgtNTIEFDSYMVPTSDLNKGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHAFAVPSLGV 187
Cdd:cd13912   1 PSLTIKAIGHQWYWSYEYSDF--NDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGI 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 63025098 188 KVDAVPGRLNQTSFFLKRPGVFYGQCSELCGANHSFMPIVIEGVSLEKYVSW 239
Cdd:cd13912  79 KVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
110-231 7.74e-83

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 243.09  E-value: 7.74e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098   110 LTIKAIGHQWYWSYEYSDYGTntIEFDSYMVPTSDLNKGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHAFAVPSLGVKV 189
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGD--LEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKT 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 63025098   190 DAVPGRLNQTSFFLKRPGVFYGQCSELCGANHSFMPIVIEGV 231
Cdd:pfam00116  79 DAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-247 3.95e-68

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 209.68  E-value: 3.95e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098   1 MENFVLSTSLIVLRDApepWQLGFQDAASPVMEEIIFFHDQIMFILTIIVTIVLWLLIRALtLKHYYK-------YLFEG 73
Cdd:COG1622   1 MKRLLLALLLLALLLS---GQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFA-IRYRRRkgdadpaQFHHN 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098  74 TLIEIIWTLVPACVLIFIAFPSLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYGTntiefdsymvptsdlnkgdlrll 153
Cdd:COG1622  77 TKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGI----------------------- 133

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098 154 EVDNRLIVPIQTQVRVLVTAADVLHAFAVPSLGVKVDAVPGRLNQTSFFLKRPGVFYGQCSELCGANHSFMPIVIEGVSL 233
Cdd:COG1622 134 ATVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSP 213

                       250
                ....*....|....
gi 63025098 234 EKYVSWVATQSEEA 247
Cdd:COG1622 214 EEFDAWLAEQKASA 227
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 27-241 7.27e-50

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: 162.16  E-value: 7.27e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098    27 AASPVMEEIIFFHdQIMFILTIIVTIVLWLLIRALTLKHYYK-------YLFEGTLIEIIWTLVPAC-VLIFIAFPSLKL 98
Cdd:TIGR02866   1 PGGEIAQQIAFLF-LFVLAVSTLISLLVAALLAYVVWKFRRKgdeekpsQIHGNRRLEYVWTVIPLIiVVGLFAATAKGL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098    99 LYLMDEVIDPALTIKAIGHQWYWSYEYSDYGTNTiefdsymvptsdlnkgdlrllevDNRLIVPIQTQVRVLVTAADVLH 178
Cdd:TIGR02866  80 LYLERPIPKDALKVKVTGYQWWWDFEYPESGFTT-----------------------VNELVLPAGTPVELQVTSKDVIH 136

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 63025098   179 AFAVPSLGVKVDAVPGRLNQTSFFLKRPGVFYGQCSELCGANHSFMPIVIEGVSLEKYVSWVA 241
Cdd:TIGR02866 137 SFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
 
Name Accession Description Interval E-value
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 14-247 2.26e-170

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 468.88  E-value: 2.26e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098   14 RDAPEPWQLGFQDAASPVMEEIIFFHDQIMFILTIIVTIVLWLLIRALTLKHYYKYLFEGTLIEIIWTLVPACVLIFIAF 93
Cdd:MTH00051   1 KDAPEPWQLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098   94 PSLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYGTNTIEFDSYMVPTSDLNKGDLRLLEVDNRLIVPIQTQVRVLVTA 173
Cdd:MTH00051  81 PSLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYGTDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 63025098  174 ADVLHAFAVPSLGVKVDAVPGRLNQTSFFLKRPGVFYGQCSELCGANHSFMPIVIEGVSLEKYVSWVATQSEEA 247
Cdd:MTH00051 161 ADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQSEEI 234
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 11-246 4.17e-156

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 433.02  E-value: 4.17e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098   11 IVLRDAPEPWQLGFQDAASPVMEEIIFFHDQIMFILTIIVTIVLWLLIRALTLKHYYKYLFEGTLIEIIWTLVPACVLIF 90
Cdd:MTH00023   5 FFYRDIPEPWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098   91 IAFPSLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYGTNTIEFDSYMVPTSDLNKGDLRLLEVDNRLIVPIQTQVRVL 170
Cdd:MTH00023  85 IALPSLKLLYLMDEVVSPALTIKAIGHQWYWSYEYSDYEGETLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRIL 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 63025098  171 VTAADVLHAFAVPSLGVKVDAVPGRLNQTSFFLKRPGVFYGQCSELCGANHSFMPIVIEGVSLEKYVSWVATQSEE 246
Cdd:MTH00023 165 VTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLSLSND 240
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 21-240 1.43e-139

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 390.73  E-value: 1.43e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098   21 QLGFQDAASPVMEEIIFFHDQIMFILTIIVTIVLWLLIRALTLKHYYKYLFEGTLIEIIWTLVPACVLIFIAFPSLKLLY 100
Cdd:MTH00154   6 NLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098  101 LMDEVIDPALTIKAIGHQWYWSYEYSDYgtNTIEFDSYMVPTSDLNKGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHAF 180
Cdd:MTH00154  86 LLDEVNNPSITLKTIGHQWYWSYEYSDF--KNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSW 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098  181 AVPSLGVKVDAVPGRLNQTSFFLKRPGVFYGQCSELCGANHSFMPIVIEGVSLEKYVSWV 240
Cdd:MTH00154 164 TVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWI 223
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 17-244 2.76e-130

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 367.32  E-value: 2.76e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098   17 PEPWQLGFQDAASPVMEEIIFFHDQIMFILTIIVTIVLWLLIRALTLKHYYKYLFEGTLIEIIWTLVPACVLIFIAFPSL 96
Cdd:MTH00117   2 ANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPSL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098   97 KLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYgtNTIEFDSYMVPTSDLNKGDLRLLEVDNRLIVPIQTQVRVLVTAADV 176
Cdd:MTH00117  82 RILYLMDEINNPHLTIKAIGHQWYWSYEYTDY--KDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 63025098  177 LHAFAVPSLGVKVDAVPGRLNQTSFFLKRPGVFYGQCSELCGANHSFMPIVIEGVSLEKYVSWVATQS 244
Cdd:MTH00117 160 LHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLLS 227
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 21-245 5.97e-128

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 361.18  E-value: 5.97e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098   21 QLGFQDAASPVMEEIIFFHDQIMFILTIIVTIVLWLLIRALTLKHYYKYLFEGTLIEIIWTLVPACVLIFIAFPSLKLLY 100
Cdd:MTH00140   6 QLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPSLRLLY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098  101 LMDEVIDPALTIKAIGHQWYWSYEYSDygTNTIEFDSYMVPTSDLNKGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHAF 180
Cdd:MTH00140  86 LLDETNNPLLTVKAIGHQWYWSYEYSD--FSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSW 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 63025098  181 AVPSLGVKVDAVPGRLNQTSFFLKRPGVFYGQCSELCGANHSFMPIVIEGVSLEKYVSWVATQSE 245
Cdd:MTH00140 164 TVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELMSE 228
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 19-246 1.96e-125

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 355.16  E-value: 1.96e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098   19 PWQLGFQDAASPVMEEIIFFHDQIMFILTIIVTIVLWLLIRALTLKHYYKYLFEGTLIEIIWTLVPACVLIFIAFPSLKL 98
Cdd:MTH00038   4 WLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPSLQL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098   99 LYLMDEVIDPALTIKAIGHQWYWSYEYSDYgtNTIEFDSYMVPTSDLNKGDLRLLEVDNRLIVPIQTQVRVLVTAADVLH 178
Cdd:MTH00038  84 LYLMDEVNNPFLTIKAIGHQWYWSYEYTDY--NDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLH 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 63025098  179 AFAVPSLGVKVDAVPGRLNQTSFFLKRPGVFYGQCSELCGANHSFMPIVIEGVSLEKYVSWVATQSEE 246
Cdd:MTH00038 162 SWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFLEE 229
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 21-242 2.37e-122

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 346.97  E-value: 2.37e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098   21 QLGFQDAASPVMEEIIFFHDQIMFILTIIVTIVLWLLIRALTLKHYYKYLFEGTLIEIIWTLVPACVLIFIAFPSLKLLY 100
Cdd:MTH00168   6 QLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPSLRLLY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098  101 LMDEVIDPALTIKAIGHQWYWSYEYSDYgtNTIEFDSYMVPTSDLNKGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHAF 180
Cdd:MTH00168  86 LMDEIDKPDLTIKAVGHQWYWSYEYTDY--NDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSW 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 63025098  181 AVPSLGVKVDAVPGRLNQTSFFLKRPGVFYGQCSELCGANHSFMPIVIEGVSLEKYVSWVAT 242
Cdd:MTH00168 164 TLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVDS 225
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 21-240 1.68e-118

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 337.46  E-value: 1.68e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098   21 QLGFQDAASPVMEEIIFFHDQIMFILTIIVTIVLWLLIRALTLKHYYKYLFEGTLIEIIWTLVPACVLIFIAFPSLKLLY 100
Cdd:MTH00139   6 QLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPSLRLLY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098  101 LMDEVIDPALTIKAIGHQWYWSYEYSDygTNTIEFDSYMVPTSDLNKGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHAF 180
Cdd:MTH00139  86 LMDEVSDPYLTFKAVGHQWYWSYEYSD--FKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSW 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098  181 AVPSLGVKVDAVPGRLNQTSFFLKRPGVFYGQCSELCGANHSFMPIVIEGVSLEKYVSWV 240
Cdd:MTH00139 164 TVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWI 223
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 19-247 6.45e-118

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 335.92  E-value: 6.45e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098   19 PWQLGFQDAASPVMEEIIFFHDQIMFILTIIVTIVLWLLIRALTLKHYYKYLFEGTLIEIIWTLVPACVLIFIAFPSLKL 98
Cdd:MTH00129   4 PSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098   99 LYLMDEVIDPALTIKAIGHQWYWSYEYSDYgtNTIEFDSYMVPTSDLNKGDLRLLEVDNRLIVPIQTQVRVLVTAADVLH 178
Cdd:MTH00129  84 LYLMDEINDPHLTIKAMGHQWYWSYEYTDY--EDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLH 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 63025098  179 AFAVPSLGVKVDAVPGRLNQTSFFLKRPGVFYGQCSELCGANHSFMPIVIEGVSLEKYVSWVATQSEEA 247
Cdd:MTH00129 162 SWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLMLEDA 230
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 12-243 3.75e-117

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 335.46  E-value: 3.75e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098   12 VLRDAPEPWQLGFQDAASPVMEEIIFFHDQIMFILTIIVTIVLWLLIRALTLKHYYKYLF---EGTLIEIIWTLVPACVL 88
Cdd:MTH00027  25 MIKDANEPWQLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLGNNYYSYYWnklDGSLIEVIWTLIPAFIL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098   89 IFIAFPSLKLLYLMDE-VIDPALTIKAIGHQWYWSYEYSDYGTNTIEFDSYMVPTSDLNKGDLRLLEVDNRLIVPIQTQV 167
Cdd:MTH00027 105 ILIAFPSLRLLYIMDEcGFSANITIKVTGHQWYWSYSYEDYGEKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNV 184

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 63025098  168 RVLVTAADVLHAFAVPSLGVKVDAVPGRLNQTSFFLKRPGVFYGQCSELCGANHSFMPIVIEGVSLEKYVSWVATQ 243
Cdd:MTH00027 185 RVLITAADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWIGRE 260
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 17-242 1.10e-112

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 322.82  E-value: 1.10e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098   17 PEPWQLGFQDAASPVMEEIIFFHDQIMFILTIIVTIVLWLLIRALTLKHYYKYLFEGTLIEIIWTLVPACVLIFIAFPSL 96
Cdd:MTH00098   2 AYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098   97 KLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYGTntIEFDSYMVPTSDLNKGDLRLLEVDNRLIVPIQTQVRVLVTAADV 176
Cdd:MTH00098  82 RILYMMDEINNPSLTVKTMGHQWYWSYEYTDYED--LSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 63025098  177 LHAFAVPSLGVKVDAVPGRLNQTSFFLKRPGVFYGQCSELCGANHSFMPIVIEGVSLEKYVSWVAT 242
Cdd:MTH00098 160 LHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSAS 225
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 21-245 9.24e-112

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 320.26  E-value: 9.24e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098   21 QLGFQDAASPVMEEIIFFHDQIMFILTIIVTIVLWLLIRALTLKHYYKYLFEGTLIEIIWTLVPACVLIFIAFPSLKLLY 100
Cdd:MTH00008   6 QLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSLRLLY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098  101 LMDEVIDPALTIKAIGHQWYWSYEYSDYgtNTIEFDSYMVPTSDLNKGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHAF 180
Cdd:MTH00008  86 LMDEVSNPSITLKTIGHQWYWSYEYSDF--SNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSW 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 63025098  181 AVPSLGVKVDAVPGRLNQTSFFLKRPGVFYGQCSELCGANHSFMPIVIEGVSLEKYVSWVATQSE 245
Cdd:MTH00008 164 TVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSSFAE 228
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 18-247 2.51e-111

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 319.52  E-value: 2.51e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098   18 EPWQLGFQDAASPVMEEIIFFHDQIMFILTIIVTIVLWLLIRALTLKHYYKYLFEGTLIEIIWTLVPACVLIFIAFPSLK 97
Cdd:MTH00185   3 HPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098   98 LLYLMDEVIDPALTIKAIGHQWYWSYEYSDYgtNTIEFDSYMVPTSDLNKGDLRLLEVDNRLIVPIQTQVRVLVTAADVL 177
Cdd:MTH00185  83 ILYLMDEINDPHLTIKAMGHQWYWSYEYTDY--EQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098  178 HAFAVPSLGVKVDAVPGRLNQTSFFLKRPGVFYGQCSELCGANHSFMPIVIEGVSLEKYVSWVATQSEEA 247
Cdd:MTH00185 161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLMLEEA 230
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 19-245 1.03e-108

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 312.87  E-value: 1.03e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098   19 PWQLGFQDAASPVMEEIIFFHDQIMFILTIIVTIVLWLLIRALTLKHYYKYLFEGTLIEIIWTLVPACVLIFIAFPSLKL 98
Cdd:MTH00076   4 PSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098   99 LYLMDEVIDPALTIKAIGHQWYWSYEYSDYgtNTIEFDSYMVPTSDLNKGDLRLLEVDNRLIVPIQTQVRVLVTAADVLH 178
Cdd:MTH00076  84 LYLMDEINDPHLTVKAIGHQWYWSYEYTDY--EDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLH 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 63025098  179 AFAVPSLGVKVDAVPGRLNQTSFFLKRPGVFYGQCSELCGANHSFMPIVIEGVSLEKYVSWVATQSE 245
Cdd:MTH00076 162 SWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSMLE 228
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 108-239 7.53e-97

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: 278.68  E-value: 7.53e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098 108 PALTIKAIGHQWYWSYEYSDYgtNTIEFDSYMVPTSDLNKGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHAFAVPSLGV 187
Cdd:cd13912   1 PSLTIKAIGHQWYWSYEYSDF--NDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGI 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 63025098 188 KVDAVPGRLNQTSFFLKRPGVFYGQCSELCGANHSFMPIVIEGVSLEKYVSW 239
Cdd:cd13912  79 KVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
110-231 7.74e-83

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 243.09  E-value: 7.74e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098   110 LTIKAIGHQWYWSYEYSDYGTntIEFDSYMVPTSDLNKGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHAFAVPSLGVKV 189
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGD--LEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKT 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 63025098   190 DAVPGRLNQTSFFLKRPGVFYGQCSELCGANHSFMPIVIEGV 231
Cdd:pfam00116  79 DAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 38-239 7.81e-73

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 221.81  E-value: 7.81e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098   38 FHDQIMFILTIIVTIVLWLLIRALTLKHYYKYLFEGTLIEIIWTLVPACVLIFIAFPSLKLLYLMDEV-IDPALTIKAIG 116
Cdd:MTH00080  25 FNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMnLDSNLTVKVTG 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098  117 HQWYWSYEYSDYGTntIEFDSYMVPTSDLNKGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHAFAVPSLGVKVDAVPGRL 196
Cdd:MTH00080 105 HQWYWSYEFSDIPG--LEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGIL 182

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 63025098  197 NQTSFFLKRPGVFYGQCSELCGANHSFMPIVIEGVSLEKYVSW 239
Cdd:MTH00080 183 STLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEW 225
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-247 3.95e-68

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 209.68  E-value: 3.95e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098   1 MENFVLSTSLIVLRDApepWQLGFQDAASPVMEEIIFFHDQIMFILTIIVTIVLWLLIRALtLKHYYK-------YLFEG 73
Cdd:COG1622   1 MKRLLLALLLLALLLS---GQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFA-IRYRRRkgdadpaQFHHN 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098  74 TLIEIIWTLVPACVLIFIAFPSLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYGTntiefdsymvptsdlnkgdlrll 153
Cdd:COG1622  77 TKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGI----------------------- 133

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098 154 EVDNRLIVPIQTQVRVLVTAADVLHAFAVPSLGVKVDAVPGRLNQTSFFLKRPGVFYGQCSELCGANHSFMPIVIEGVSL 233
Cdd:COG1622 134 ATVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSP 213

                       250
                ....*....|....
gi 63025098 234 EKYVSWVATQSEEA 247
Cdd:COG1622 214 EEFDAWLAEQKASA 227
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 27-241 7.27e-50

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: 162.16  E-value: 7.27e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098    27 AASPVMEEIIFFHdQIMFILTIIVTIVLWLLIRALTLKHYYK-------YLFEGTLIEIIWTLVPAC-VLIFIAFPSLKL 98
Cdd:TIGR02866   1 PGGEIAQQIAFLF-LFVLAVSTLISLLVAALLAYVVWKFRRKgdeekpsQIHGNRRLEYVWTVIPLIiVVGLFAATAKGL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098    99 LYLMDEVIDPALTIKAIGHQWYWSYEYSDYGTNTiefdsymvptsdlnkgdlrllevDNRLIVPIQTQVRVLVTAADVLH 178
Cdd:TIGR02866  80 LYLERPIPKDALKVKVTGYQWWWDFEYPESGFTT-----------------------VNELVLPAGTPVELQVTSKDVIH 136

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 63025098   179 AFAVPSLGVKVDAVPGRLNQTSFFLKRPGVFYGQCSELCGANHSFMPIVIEGVSLEKYVSWVA 241
Cdd:TIGR02866 137 SFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 72-231 6.63e-48

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 156.65  E-value: 6.63e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098   72 EGTLIEIIWTLVPACVLIFIAFpsLKLLYLM-DEVIDPALTIKAIGHQWYWSYEYSDYGtntiEFDSYMvptSDLNKGdl 150
Cdd:MTH00047  45 ENQVLELLWTVVPTLLVLVLCF--LNLNFITsDLDCFSSETIKVIGHQWYWSYEYSFGG----SYDSFM---TDDIFG-- 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098  151 rlleVDNRLIVPIQTQVRVLVTAADVLHAFAVPSLGVKVDAVPGRLNQTSFFLKRPGVFYGQCSELCGANHSFMPIVIEG 230
Cdd:MTH00047 114 ----VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEV 189


                 .
gi 63025098  231 V 231
Cdd:MTH00047 190 V 190
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 135-236 3.01e-46

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 151.51  E-value: 3.01e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098  135 FDSYMVPTSDLNKGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHAFAVPSLGVKVDAVPGRLNQTSFFLKRPGVFYGQCS 214
Cdd:PTZ00047  51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                         90       100
                 ....*....|....*....|..
gi 63025098  215 ELCGANHSFMPIVIEGVSLEKY 236
Cdd:PTZ00047 131 EMCGTLHGFMPIVVEAVSPEAY 152
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 109-224 8.25e-31

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: 110.02  E-value: 8.25e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098 109 ALTIKAIGHQWYWSYEYSDYGTNTIEfdsymvpTSdlnkgdlrllevdNRLIVPIQTQVRVLVTAADVLHAFAVPSLGVK 188
Cdd:cd04213   1 ALTIEVTGHQWWWEFRYPDEPGRGIV-------TA-------------NELHIPVGRPVRLRLTSADVIHSFWVPSLAGK 60

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 63025098 189 VDAVPGRLNQTSFFLKRPGVFYGQCSELCGANHSFM 224
Cdd:cd04213  61 MDMIPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 16-98 1.17e-29

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: 106.65  E-value: 1.17e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098    16 APEPWQLGFQDAASPVMEEIIFFHDQIMFILTIIVTIVLWLLIRALTLKHY------YKYLFEGTLIEIIWTLVPACVLI 89
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRFNRrknpitARYTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 63025098    90 FIAFPSLKL 98
Cdd:pfam02790  81 LIALPSFKL 89
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 110-229 1.34e-29

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: 106.61  E-value: 1.34e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098 110 LTIKAIGHQWYWSYEYSDYGTntiefdsymvptsdlnkgdlrllevDNRLIVPIQTQVRVLVTAADVLHAFAVPSLGVKV 189
Cdd:cd13842   1 LTVYVTGVQWSWTFIYPNVRT-------------------------PNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKV 55

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 63025098 190 DAVPGRLNQTSFFLKRPGVFYGQCSELCGANHSFMPIVIE 229
Cdd:cd13842  56 DAVPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 109-224 3.16e-25

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: 95.79  E-value: 3.16e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098 109 ALTIKAIGHQWYWSYEYSDYGTNTIEFDsymvptsDLNKGDLRLlevdnrlivPIQTQVRVLVTAADVLHAFAVPSLGVK 188
Cdd:cd13919   1 ALVVEVTAQQWAWTFRYPGGDGKLGTDD-------DVTSPELHL---------PVGRPVLFNLRSKDVIHSFWVPEFRVK 64

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 63025098 189 VDAVPGRLNQTSFFLKRPGVFYGQCSELCGANHSFM 224
Cdd:cd13919  65 QDAVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 109-224 3.30e-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: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 92.69  E-value: 3.30e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098 109 ALTIKAIGHQWYWSYEYSDYGTNtiefdsymvptsdlnkgdlrllevDNRLIVPIQTQVRVLVTAADVLHAFAVPSLGVK 188
Cdd:cd13915   1 ALEIQVTGRQWMWEFTYPNGKRE------------------------INELHVPVGKPVRLILTSKDVIHSFYVPAFRIK 56

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 63025098 189 VDAVPGRLNQTSFFLKRPGVFYGQCSELCGANHSFM 224
Cdd:cd13915  57 QDVVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 98-240 3.39e-24

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


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 94.06  E-value: 3.39e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098  98 LLYLMD---EVIDPALTIKAIGHQWYWSYEYSDYGTNTiefdsymvptsdlnkgdlrllevdNRLIVPIQTQVRVLVTAA 174
Cdd:cd13918  18 LLYVEDppdEADEDALEVEVEGFQFGWQFEYPNGVTTG------------------------NTLRVPADTPIALRVTST 73

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 63025098 175 DVLHAFAVPSLGVKVDAVPGRLNQTSFFLKRPGVFYGQCSELCGANHSFMPIVIEGVSLEKYVSWV 240
Cdd:cd13918  74 DVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAWY 139
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 111-240 5.99e-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: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 87.08  E-value: 5.99e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098 111 TIKAIGHQWYWSYEYSDYGTNTiefdsymvptsdlnkgdlrllevDNRLIVPIQTQVRVLVTAADVLHAFAVPSLGVKVD 190
Cdd:cd13914   2 EIEVEAYQWGWEFSYPEANVTT-----------------------SEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQD 58

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 63025098 191 AVPGRLNQTSFFLKRPGVFYGQCSELCGANHSFMPIVIEGVSLEKYVSWV 240
Cdd:cd13914  59 AFPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 157-224 2.88e-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: 2.88e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 63025098 157 NRLIVPIQTQVRVLVTAADVLHAFAVPSLGVKVDAVPGRLNQTSFFLKRPGVFYGQCSELCGANHSFM 224
Cdd:cd13913  25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 110-224 4.12e-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: 49.85  E-value: 4.12e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098 110 LTIKAIGHQWYWSYEYSDYGTNTIefdsymvptsdlnkgdlrllevdNRLIVPIQTQVRVLVTAADVLHAFAVPSLGVKV 189
Cdd:cd04212   1 LEIQVVSLDWKWLFIYPEQGIATV-----------------------NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQI 57

                        90       100       110
                ....*....|....*....|....*....|....*
gi 63025098 190 DAVPGRLNQTSFFLKRPGVFYGQCSELCGANHSFM 224
Cdd:cd04212  58 YAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDM 92
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 111-224 1.80e-06

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


Pssm-ID: 259983 [Multi-domain]  Cd Length: 93  Bit Score: 45.07  E-value: 1.80e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098 111 TIKAIGHQWYWSyeysdygtntiefdsymVPTSDLNKGDlrllevdnrlivPIQTQVrvlvTAADVLHAFAVPS----LG 186
Cdd:cd13916   2 VVAVTGHQWYWE-----------------LSRTEIPAGK------------PVEFRV----TSADVNHGFGIYDpdmrLL 48

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 63025098 187 VKVDAVPGRLNQTSFFLKRPGVFYGQCSELCGANHSFM 224
Cdd:cd13916  49 AQTQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 148-229 3.37e-05

Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in inter-molecular electron transfer reactions. Cupredoxins are blue copper proteins, having an intense blue color due to the presence of a mononuclear type 1 (T1) copper site. Structurally, the cupredoxin-like fold consists of a beta-sandwich with 7 strands in 2 beta-sheets, which is arranged in a Greek-key beta-barrel. Some of these proteins have lost the ability to bind copper. The majority of family members contain multiple cupredoxin domain repeats: ceruloplasmin and the coagulation factors V/VIII have six repeats; laccase, ascorbate oxidase, spore coat protein A, and multicopper oxidase CueO contain three repeats; and nitrite reductase has two repeats. Others are mono-domain cupredoxins, such as plastocyanin, pseudoazurin, plantacyanin, azurin, rusticyanin, stellacyanin, quinol oxidase, and the periplasmic domain of cytochrome c oxidase subunit II.


Pssm-ID: 259860 [Multi-domain]  Cd Length: 110  Bit Score: 41.83  E-value: 3.37e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098 148 GDLRLLEVDNRLIVPIQTQVRV-LVTAADVLHAFAVPSLGVKVDA---------------VPGRLNQTSFFLKRPGVFYG 211
Cdd:cd00920  14 YNGVLLFGPPVLVVPVGDTVRVqFVNKLGENHSVTIAGFGVPVVAmagganpglvntlviGPGESAEVTFTTDQAGVYWF 93

                        90
                ....*....|....*...
gi 63025098 212 QCSELCGaNHSFMPIVIE 229
Cdd:cd00920  94 YCTIPGH-NHAGMVGTIN 110
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 167-224 1.33e-04

The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase participates in nitrogen metabolism and catalyzes the last step in dissimilatory nitrate reduction, the two-electron reduction of N2O to N2. It contains copper ions as cofactors in the form of a binuclear CuA center at the site of electron entry and a tetranuclear CuZ centre at the active site. The C-terminus of Nitrous-oxide reductase is a cupredoxin domain.


Pssm-ID: 259885 [Multi-domain]  Cd Length: 95  Bit Score: 39.91  E-value: 1.33e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 63025098 167 VRVLVT----AADVLHAFAVPSLGVKVDAVPGRLNQTSFFLKRPGVFYGQCSELCGANHSFM 224
Cdd:cd04223  26 VTVHLTnleqDEDITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALHLEM 87
NosZ COG4263
Nitrous oxide reductase [Inorganic ion transport and metabolism];
167-224 3.80e-03

Nitrous oxide reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443405 [Multi-domain]  Cd Length: 621  Bit Score: 38.35  E-value: 3.80e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 63025098 167 VRVLVT----AADVLHAFAVPSLGVKVDAVPGRLNQTSFFLKRPGVFYGQCSELCGANHSFM 224
Cdd:COG4263 552 VTVHVTnldqVEDLTHGFAIPGYNINMEIMPQETASVTFVADKPGVYWYYCTWFCHALHMEM 613
PRK10525 PRK10525
cytochrome o ubiquinol oxidase subunit II; Provisional
 78-224 9.64e-03

cytochrome o ubiquinol oxidase subunit II; Provisional


Pssm-ID: 182518 [Multi-domain]  Cd Length: 315  Bit Score: 36.70  E-value: 9.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025098   78 IIWTlVPACVLIFIAFPSLKLLYLMDEV------IDPaLTIKAIGHQWYWSYEYSDYGTNTIefdsymvptsdlnkgdlr 151
Cdd:PRK10525  91 VVWT-VPILIIIFLAVLTWKTTHALEPSkplahdEKP-ITIEVVSMDWKWFFIYPEQGIATV------------------ 150

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 63025098  152 llevdNRLIVPIQTQVRVLVTAADVLHAFAVPSLGVKVDAVPGRLNQTSFFLKRPGVFYGQCSELCGANHSFM 224
Cdd:PRK10525 151 -----NEIAFPANVPVYFKVTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIANEPGTYDGISASYSGPGFSGM 218
 
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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