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Conserved domains on  [gi|528750217|gb|AGS44344|]
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cytochrome c oxidase subunit 2 (mitochondrion) [Candida albicans]

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 8.35e-104

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 300.59  E-value: 8.35e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217  10 WG-IRLQDSATPNAEGIHELYDHIMFYLCLILGLVSYILYVIIKdykdNRFAYKYVRHGQVIEIIWTIFPAVILLLIAFP 88
Cdd:MTH00154   4 WSnLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLF----NKFTNRFLLEGQEIEIIWTILPAIILIFIALP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217  89 SFILLYLCDEVLTPAMTIKVIGLQWYWKYEYSDFVDsigetIEFESYVIPDDMLEPGALRLLDTDTSIVVPVDTHIRFVV 168
Cdd:MTH00154  80 SLRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKN-----IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILI 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528750217 169 TANDVIHSFTIPSLGMKIDATPGRLNQVSALIQRTGVYYGQCSELCGVNHGMMPIKLECVSIEDFIEWL 237
Cdd:MTH00154 155 TAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWI 223
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 10-237 8.35e-104

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 300.59  E-value: 8.35e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217  10 WG-IRLQDSATPNAEGIHELYDHIMFYLCLILGLVSYILYVIIKdykdNRFAYKYVRHGQVIEIIWTIFPAVILLLIAFP 88
Cdd:MTH00154   4 WSnLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLF----NKFTNRFLLEGQEIEIIWTILPAIILIFIALP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217  89 SFILLYLCDEVLTPAMTIKVIGLQWYWKYEYSDFVDsigetIEFESYVIPDDMLEPGALRLLDTDTSIVVPVDTHIRFVV 168
Cdd:MTH00154  80 SLRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKN-----IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILI 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528750217 169 TANDVIHSFTIPSLGMKIDATPGRLNQVSALIQRTGVYYGQCSELCGVNHGMMPIKLECVSIEDFIEWL 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 1.36e-81

C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the binuclear center (active site) in subunit I.


Pssm-ID: 259979 [Multi-domain]  Cd Length: 130  Bit Score: 240.94  E-value: 1.36e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217 102 PAMTIKVIGLQWYWKYEYSDFVDsigetIEFESYVIPDDMLEPGALRLLDTDTSIVVPVDTHIRFVVTANDVIHSFTIPS 181
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFND-----LEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPS 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 528750217 182 LGMKIDATPGRLNQVSALIQRTGVYYGQCSELCGVNHGMMPIKLECVSIEDFIEW 236
Cdd:cd13912   76 LGIKVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
104-228 2.60e-72

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 216.89  E-value: 2.60e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217  104 MTIKVIGLQWYWKYEYSDFVDsigetIEFESYVIPDDMLEPGALRLLDTDTSIVVPVDTHIRFVVTANDVIHSFTIPSLG 183
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGD-----LEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLG 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 528750217  184 MKIDATPGRLNQVSALIQRTGVYYGQCSELCGVNHGMMPIKLECV 228
Cdd:pfam00116  76 IKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
10-239 4.69e-64

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 199.67  E-value: 4.69e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217  10 WGIRLQDSATPNAEGIHELYDhIMFYLCLILGLV--SYILYVIIKdYKDNRFAYK--YVRHGQVIEIIWTIFPAVILLLI 85
Cdd:COG1622   17 GQLSLPDPAGPIAEEIDDLFW-VSLIIMLVIFVLvfGLLLYFAIR-YRRRKGDADpaQFHHNTKLEIVWTVIPIIIVIVL 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217  86 AFPSFILLYLCDEVLTPAMTIKVIGLQWYWKYEYsdfvdsigetiefesyvipddmLEPGALrlldTDTSIVVPVDTHIR 165
Cdd:COG1622   95 AVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRY----------------------PDQGIA----TVNELVLPVGRPVR 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528750217 166 FVVTANDVIHSFTIPSLGMKIDATPGRLNQVSALIQRTGVYYGQCSELCGVNHGMMPIKLECVSIEDFIEWLGE 239
Cdd:COG1622  149 FLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAE 222
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 18-237 4.07e-44

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: 147.91  E-value: 4.07e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217   18 ATPNAEGIHELYDHIMFYLCLILGLV-SYILYVIIK--DYKDNRFAyKYVRHGQVIEIIWTIFPAVILL-LIAFPSFILL 93
Cdd:TIGR02866   2 GGEIAQQIAFLFLFVLAVSTLISLLVaALLAYVVWKfrRKGDEEKP-SQIHGNRRLEYVWTVIPLIIVVgLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217   94 YLCDEVLTPAMTIKVIGLQWYWKYEYSDFvdsigetiefesyvipddmlepgalrLLDTDTSIVVPVDTHIRFVVTANDV 173
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPES--------------------------GFTTVNELVLPAGTPVELQVTSKDV 134

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528750217  174 IHSFTIPSLGMKIDATPGRLNQVSALIQRTGVYYGQCSELCGVNHGMMPIKLECVSIEDFIEWL 237
Cdd:TIGR02866 135 IHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYV 198
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 10-237 8.35e-104

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 300.59  E-value: 8.35e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217  10 WG-IRLQDSATPNAEGIHELYDHIMFYLCLILGLVSYILYVIIKdykdNRFAYKYVRHGQVIEIIWTIFPAVILLLIAFP 88
Cdd:MTH00154   4 WSnLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLF----NKFTNRFLLEGQEIEIIWTILPAIILIFIALP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217  89 SFILLYLCDEVLTPAMTIKVIGLQWYWKYEYSDFVDsigetIEFESYVIPDDMLEPGALRLLDTDTSIVVPVDTHIRFVV 168
Cdd:MTH00154  80 SLRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKN-----IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILI 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528750217 169 TANDVIHSFTIPSLGMKIDATPGRLNQVSALIQRTGVYYGQCSELCGVNHGMMPIKLECVSIEDFIEWL 237
Cdd:MTH00154 155 TAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWI 223
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 8-237 5.90e-96

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 280.71  E-value: 5.90e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217   8 TPWGIRLQDSATPNAEGIHELYDHIMFYLCLILGLVSYILYVIIKdykdNRFAYKYVRHGQVIEIIWTIFPAVILLLIAF 87
Cdd:MTH00168   3 TYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVT----SKYTNRFLLDSQMIEFVWTIIPAFILISLAL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217  88 PSFILLYLCDEVLTPAMTIKVIGLQWYWKYEYSDFVDsigetIEFESYVIPDDMLEPGALRLLDTDTSIVVPVDTHIRFV 167
Cdd:MTH00168  79 PSLRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYND-----LEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVL 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217 168 VTANDVIHSFTIPSLGMKIDATPGRLNQVSALIQRTGVYYGQCSELCGVNHGMMPIKLECVSIEDFIEWL 237
Cdd:MTH00168 154 VTSADVLHSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWV 223
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 5-237 1.12e-94

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 278.17  E-value: 1.12e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217   5 DVPTPWGIRLQDSATPNAEGIHELYDHIMFYLCLILGLVsyiLYVIIKDYKdNRFAYKYVRHGQVIEIIWTIFPAVILLL 84
Cdd:MTH00023   9 DIPEPWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVV---LWLIVEALN-GKFYDRFLVDGTFLEIVWTIIPAVILVF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217  85 IAFPSFILLYLCDEVLTPAMTIKVIGLQWYWKYEYSDFVdsiGETIEFESYVIPDDMLEPGALRLLDTDTSIVVPVDTHI 164
Cdd:MTH00023  85 IALPSLKLLYLMDEVVSPALTIKAIGHQWYWSYEYSDYE---GETLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHV 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528750217 165 RFVVTANDVIHSFTIPSLGMKIDATPGRLNQVSALIQRTGVYYGQCSELCGVNHGMMPIKLECVSIEDFIEWL 237
Cdd:MTH00023 162 RILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWL 234
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 10-238 4.28e-93

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 273.74  E-value: 4.28e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217  10 WG-IRLQDSATPNAEGIHELYDHIMFYLCLILGLVSYILYVIIKdykdNRFAYKYVRHGQVIEIIWTIFPAVILLLIAFP 88
Cdd:MTH00140   4 WGqLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLF----NKFSCRTILEAQKLETIWTIVPALILVFLALP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217  89 SFILLYLCDEVLTPAMTIKVIGLQWYWKYEYSDFVDsigetIEFESYVIPDDMLEPGALRLLDTDTSIVVPVDTHIRFVV 168
Cdd:MTH00140  80 SLRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSV-----IEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLV 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217 169 TANDVIHSFTIPSLGMKIDATPGRLNQVSALIQRTGVYYGQCSELCGVNHGMMPIKLECVSIEDFIEWLG 238
Cdd:MTH00140 155 TSADVIHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLE 224
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 5-237 4.26e-91

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 268.96  E-value: 4.26e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217   5 DVPTPWGIRLQDSATPNAEGIHELYDHIMFYLCLIlglVSYILYVIIKDYKdNRFAYKYVRHGQVIEIIWTIFPAVILLL 84
Cdd:MTH00051   2 DAPEPWQLGFQDAASPVMEEIIFFHDQIMFILTII---ITTVLWLIIRALT-TKYYHKYLFEGTLIEIIWTLIPAAILIF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217  85 IAFPSFILLYLCDEVLTPAMTIKVIGLQWYWKYEYSDFVdsiGETIEFESYVIPDDMLEPGALRLLDTDTSIVVPVDTHI 164
Cdd:MTH00051  78 IAFPSLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYG---TDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQV 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528750217 165 RFVVTANDVIHSFTIPSLGMKIDATPGRLNQVSALIQRTGVYYGQCSELCGVNHGMMPIKLECVSIEDFIEWL 237
Cdd:MTH00051 155 RVLVTAADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWV 227
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 10-239 4.21e-87

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 258.49  E-value: 4.21e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217  10 WG-IRLQDSATPNAEGIHELYDHIMFYLCLILGLVSYILYVIIKdykdNRFAYKYVRHGQVIEIIWTIFPAVILLLIAFP 88
Cdd:MTH00139   4 WGqLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMS----NKFTSRSLLESQEVETIWTVLPAFILLFLALP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217  89 SFILLYLCDEVLTPAMTIKVIGLQWYWKYEYSDFvdsigETIEFESYVIPDDMLEPGALRLLDTDTSIVVPVDTHIRFVV 168
Cdd:MTH00139  80 SLRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDF-----KNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALI 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528750217 169 TANDVIHSFTIPSLGMKIDATPGRLNQVSALIQRTGVYYGQCSELCGVNHGMMPIKLECVSIEDFIEWLGE 239
Cdd:MTH00139 155 TAADVLHSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILE 225
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 14-237 3.35e-84

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 250.99  E-value: 3.35e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217  14 LQDSATPNAEGIHELYDHIMFYLCLILGLVSYILYVII--KDYKDNrfaykyVRHGQVIEIIWTIFPAVILLLIAFPSFI 91
Cdd:MTH00117   9 FQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLttKLTHTN------TVDAQEVELIWTILPAIVLILLALPSLR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217  92 LLYLCDEVLTPAMTIKVIGLQWYWKYEYSDFvdsigETIEFESYVIPDDMLEPGALRLLDTDTSIVVPVDTHIRFVVTAN 171
Cdd:MTH00117  83 ILYLMDEINNPHLTIKAIGHQWYWSYEYTDY-----KDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAE 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528750217 172 DVIHSFTIPSLGMKIDATPGRLNQVSALIQRTGVYYGQCSELCGVNHGMMPIKLECVSIEDFIEWL 237
Cdd:MTH00117 158 DVLHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWS 223
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 10-240 1.55e-83

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 249.39  E-value: 1.55e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217  10 WG-IRLQDSATPNAEGIHELYDHIMFYLCLILGLVSYILYVIIKdykdNRFAYKYVRHGQVIEIIWTIFPAVILLLIAFP 88
Cdd:MTH00008   4 WGqLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMF----NKLSNRYILEAQQIETIWTILPALILLFLAFP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217  89 SFILLYLCDEVLTPAMTIKVIGLQWYWKYEYSDFVDsigetIEFESYVIPDDMLEPGALRLLDTDTSIVVPVDTHIRFVV 168
Cdd:MTH00008  80 SLRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSN-----LEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLV 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528750217 169 TANDVIHSFTIPSLGMKIDATPGRLNQVSALIQRTGVYYGQCSELCGVNHGMMPIKLECVSIEDFIEWLGEN 240
Cdd:MTH00008 155 TAADVIHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSSF 226
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 8-240 1.10e-81

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 244.61  E-value: 1.10e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217   8 TPWGIRLQDSATPNAEGIHELYDHIMFYLCLILGLVSYILYVIIKDYKDNRFAYKyvrhGQVIEIIWTIFPAVILLLIAF 87
Cdd:MTH00038   3 TWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLE----GQELETIWTIVPAFILIFIAL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217  88 PSFILLYLCDEVLTPAMTIKVIGLQWYWKYEYSDFVDsigetIEFESYVIPDDMLEPGALRLLDTDTSIVVPVDTHIRFV 167
Cdd:MTH00038  79 PSLQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYND-----LEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVL 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528750217 168 VTANDVIHSFTIPSLGMKIDATPGRLNQVSALIQRTGVYYGQCSELCGVNHGMMPIKLECVSIEDFIEWLGEN 240
Cdd:MTH00038 154 VSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNF 226
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 102-236 1.36e-81

C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the binuclear center (active site) in subunit I.


Pssm-ID: 259979 [Multi-domain]  Cd Length: 130  Bit Score: 240.94  E-value: 1.36e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217 102 PAMTIKVIGLQWYWKYEYSDFVDsigetIEFESYVIPDDMLEPGALRLLDTDTSIVVPVDTHIRFVVTANDVIHSFTIPS 181
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFND-----LEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPS 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 528750217 182 LGMKIDATPGRLNQVSALIQRTGVYYGQCSELCGVNHGMMPIKLECVSIEDFIEW 236
Cdd:cd13912   76 LGIKVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 14-236 1.65e-80

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 241.71  E-value: 1.65e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217  14 LQDSATPNAEGIHELYDHIMFYLCLILGLVSYILYVIIKdykdNRFAYKYVRHGQVIEIIWTIFPAVILLLIAFPSFILL 93
Cdd:MTH00185   9 LQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVT----TKLTNKYILDSQEIEIVWTILPAIILIMIALPSLRIL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217  94 YLCDEVLTPAMTIKVIGLQWYWKYEYSDFvdsigETIEFESYVIPDDMLEPGALRLLDTDTSIVVPVDTHIRFVVTANDV 173
Cdd:MTH00185  85 YLMDEINDPHLTIKAMGHQWYWSYEYTDY-----EQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528750217 174 IHSFTIPSLGMKIDATPGRLNQVSALIQRTGVYYGQCSELCGVNHGMMPIKLECVSIEDFIEW 236
Cdd:MTH00185 160 LHSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 14-236 6.79e-79

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 237.69  E-value: 6.79e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217  14 LQDSATPNAEGIHELYDHIMFYLCLILGLVSYILYVIIKdykdNRFAYKYVRHGQVIEIIWTIFPAVILLLIAFPSFILL 93
Cdd:MTH00129   9 FQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVS----TKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRIL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217  94 YLCDEVLTPAMTIKVIGLQWYWKYEYSDFvdsigETIEFESYVIPDDMLEPGALRLLDTDTSIVVPVDTHIRFVVTANDV 173
Cdd:MTH00129  85 YLMDEINDPHLTIKAMGHQWYWSYEYTDY-----EDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528750217 174 IHSFTIPSLGMKIDATPGRLNQVSALIQRTGVYYGQCSELCGVNHGMMPIKLECVSIEDFIEW 236
Cdd:MTH00129 160 LHSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 7-236 4.61e-78

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 235.38  E-value: 4.61e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217   7 PTPWGIRLQDSATPNAEGIHELYDHIMFYLCLILGLVSYILYVIIKdykdNRFAYKYVRHGQVIEIIWTIFPAVILLLIA 86
Cdd:MTH00098   2 AYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLT----TKLTHTSTMDAQEVETIWTILPAIILILIA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217  87 FPSFILLYLCDEVLTPAMTIKVIGLQWYWKYEYSDFvdsigETIEFESYVIPDDMLEPGALRLLDTDTSIVVPVDTHIRF 166
Cdd:MTH00098  78 LPSLRILYMMDEINNPSLTVKTMGHQWYWSYEYTDY-----EDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRM 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217 167 VVTANDVIHSFTIPSLGMKIDATPGRLNQVSALIQRTGVYYGQCSELCGVNHGMMPIKLECVSIEDFIEW 236
Cdd:MTH00098 153 LISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKW 222
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 7-241 3.40e-77

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 233.52  E-value: 3.40e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217   7 PTPWGirLQDSATPNAEGIHELYDHIMFYLCLILGLVSYILYVIIKDYKDNRFAYKyvrhGQVIEIIWTIFPAVILLLIA 86
Cdd:MTH00076   4 PSQLG--FQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMD----AQEIEMVWTIMPAIILIVIA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217  87 FPSFILLYLCDEVLTPAMTIKVIGLQWYWKYEYSDFVDsigetIEFESYVIPDDMLEPGALRLLDTDTSIVVPVDTHIRF 166
Cdd:MTH00076  78 LPSLRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYED-----LSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRM 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528750217 167 VVTANDVIHSFTIPSLGMKIDATPGRLNQVSALIQRTGVYYGQCSELCGVNHGMMPIKLECVSIEDFIEWLGENE 241
Cdd:MTH00076 153 LITAEDVLHSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSML 227
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
104-228 2.60e-72

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 216.89  E-value: 2.60e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217  104 MTIKVIGLQWYWKYEYSDFVDsigetIEFESYVIPDDMLEPGALRLLDTDTSIVVPVDTHIRFVVTANDVIHSFTIPSLG 183
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGD-----LEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLG 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 528750217  184 MKIDATPGRLNQVSALIQRTGVYYGQCSELCGVNHGMMPIKLECV 228
Cdd:pfam00116  76 IKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 5-242 6.08e-72

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 221.05  E-value: 6.08e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217   5 DVPTPWGIRLQDSATPNAEGIHELYDHIMFYLCLILGLVSYILYVIIkdYKDNRFAYKYVR-HGQVIEIIWTIFPAVILL 83
Cdd:MTH00027  28 DANEPWQLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRIL--LGNNYYSYYWNKlDGSLIEVIWTLIPAFILI 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217  84 LIAFPSFILLYLCDE-VLTPAMTIKVIGLQWYWKYEYSDFVDsigETIEFESYVIPDDMLEPGALRLLDTDTSIVVPVDT 162
Cdd:MTH00027 106 LIAFPSLRLLYIMDEcGFSANITIKVTGHQWYWSYSYEDYGE---KNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDT 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217 163 HIRFVVTANDVIHSFTIPSLGMKIDATPGRLNQVSALIQRTGVYYGQCSELCGVNHGMMPIKLECVSIEDFIEWLGENEV 242
Cdd:MTH00027 183 NVRVLITAADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWIGREDV 262
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
10-239 4.69e-64

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 199.67  E-value: 4.69e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217  10 WGIRLQDSATPNAEGIHELYDhIMFYLCLILGLV--SYILYVIIKdYKDNRFAYK--YVRHGQVIEIIWTIFPAVILLLI 85
Cdd:COG1622   17 GQLSLPDPAGPIAEEIDDLFW-VSLIIMLVIFVLvfGLLLYFAIR-YRRRKGDADpaQFHHNTKLEIVWTVIPIIIVIVL 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217  86 AFPSFILLYLCDEVLTPAMTIKVIGLQWYWKYEYsdfvdsigetiefesyvipddmLEPGALrlldTDTSIVVPVDTHIR 165
Cdd:COG1622   95 AVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRY----------------------PDQGIA----TVNELVLPVGRPVR 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528750217 166 FVVTANDVIHSFTIPSLGMKIDATPGRLNQVSALIQRTGVYYGQCSELCGVNHGMMPIKLECVSIEDFIEWLGE 239
Cdd:COG1622  149 FLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAE 222
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 25-237 3.70e-63

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 197.54  E-value: 3.70e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217  25 IHELYDHIMFYLCLILGLVSYILYVIIkdykdNRFAYKYVR-HGQVIEIIWTIFPAVILLLIAFPSFILLYLCDEV-LTP 102
Cdd:MTH00080  22 FHNFNCSLLFGEFVLAFVVFLFLYLIS-----NNFYFKSKKiEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMnLDS 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217 103 AMTIKVIGLQWYWKYEYSDFVDsigetIEFESYVIPDDMLEPGALRLLDTDTSIVVPVDTHIRFVVTANDVIHSFTIPSL 182
Cdd:MTH00080  97 NLTVKVTGHQWYWSYEFSDIPG-----LEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSL 171

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 528750217 183 GMKIDATPGRLNQVSALIQRTGVYYGQCSELCGVNHGMMPIKLECVSIEDFIEWL 237
Cdd:MTH00080 172 SIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWC 226
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 118-233 2.03e-44

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 147.27  E-value: 2.03e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217 118 EYSDFVDSIGETIEFESYVIPDDMLEPGALRLLDTDTSIVVPVDTHIRFVVTANDVIHSFTIPSLGMKIDATPGRLNQVS 197
Cdd:PTZ00047  37 KYLEDPDLIPKYYSFQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKIN 116

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 528750217 198 ALIQRTGVYYGQCSELCGVNHGMMPIKLECVSIEDF 233
Cdd:PTZ00047 117 TFILREGVFYGQCSEMCGTLHGFMPIVVEAVSPEAY 152
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 18-237 4.07e-44

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: 147.91  E-value: 4.07e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217   18 ATPNAEGIHELYDHIMFYLCLILGLV-SYILYVIIK--DYKDNRFAyKYVRHGQVIEIIWTIFPAVILL-LIAFPSFILL 93
Cdd:TIGR02866   2 GGEIAQQIAFLFLFVLAVSTLISLLVaALLAYVVWKfrRKGDEEKP-SQIHGNRRLEYVWTVIPLIIVVgLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217   94 YLCDEVLTPAMTIKVIGLQWYWKYEYSDFvdsigetiefesyvipddmlepgalrLLDTDTSIVVPVDTHIRFVVTANDV 173
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPES--------------------------GFTTVNELVLPAGTPVELQVTSKDV 134

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528750217  174 IHSFTIPSLGMKIDATPGRLNQVSALIQRTGVYYGQCSELCGVNHGMMPIKLECVSIEDFIEWL 237
Cdd:TIGR02866 135 IHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYV 198
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 28-228 2.79e-39

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 135.08  E-value: 2.79e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217  28 LYDHIMFYL----CLILGLVSYILYVIIKDYKDNrfaykyVRHG---QVIEIIWTIFPAVILLLIAFpsFILLYL-CDEV 99
Cdd:MTH00047   6 LYYDIVCYIlalcVFIPCWVYIMLCWQVVSGNGS------VNFGsenQVLELLWTVVPTLLVLVLCF--LNLNFItSDLD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217 100 LTPAMTIKVIGLQWYWKYEYSDfvdsigeTIEFESYVIPDDMLEPGALRLLdtdtsivvpVDTHIRFVVTANDVIHSFTI 179
Cdd:MTH00047  78 CFSSETIKVIGHQWYWSYEYSF-------GGSYDSFMTDDIFGVDKPLRLV---------YGVPYHLLVTSSDVIHSFSV 141

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 528750217 180 PSLGMKIDATPGRLNQVSALIQRTGVYYGQCSELCGVNHGMMPIKLECV 228
Cdd:MTH00047 142 PDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVV 190
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 6-92 4.09e-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: 113.20  E-value: 4.09e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217    6 VPTPWGIRLQDSATPNAEGIHELYDHIMFYLCLILGLVSYILYVIIKDY--KDNRFAYKYVRHGQVIEIIWTIFPAVILL 83
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRFnrRKNPITARYTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 528750217   84 LIAFPSFIL 92
Cdd:pfam02790  81 LIALPSFKL 89
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 103-221 5.63e-27

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


Pssm-ID: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 100.41  E-value: 5.63e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217 103 AMTIKVIGLQWYWKYEYsdfvdsIGETIEFesyvIPDDMLEPGALRLldtdtsivvPVDTHIRFVVTANDVIHSFTIPSL 182
Cdd:cd13919    1 ALVVEVTAQQWAWTFRY------PGGDGKL----GTDDDVTSPELHL---------PVGRPVLFNLRSKDVIHSFWVPEF 61

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 528750217 183 GMKIDATPGRLNQVSALIQRTGVYYGQCSELCGVNHGMM 221
Cdd:cd13919   62 RVKQDAVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 103-221 8.41e-27

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: 100.00  E-value: 8.41e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217 103 AMTIKVIGLQWYWKYEYsdfVDSIGETIEfesyvipddmlepgalrlldTDTSIVVPVDTHIRFVVTANDVIHSFTIPSL 182
Cdd:cd04213    1 ALTIEVTGHQWWWEFRY---PDEPGRGIV--------------------TANELHIPVGRPVRLRLTSADVIHSFWVPSL 57

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 528750217 183 GMKIDATPGRLNQVSALIQRTGVYYGQCSELCGVNHGMM 221
Cdd:cd04213   58 AGKMDMIPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 104-226 1.01e-25

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


Pssm-ID: 259911 [Multi-domain]  Cd Length: 95  Bit Score: 96.98  E-value: 1.01e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217 104 MTIKVIGLQWYWKYEYSDfvdsigetiefesyvipddmlepgalrlLDTDTSIVVPVDTHIRFVVTANDVIHSFTIPSLG 183
Cdd:cd13842    1 LTVYVTGVQWSWTFIYPN----------------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLG 52

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 528750217 184 MKIDATPGRLNQVSALIQRTGVYYGQCSELCGVNHGMMPIKLE 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 1.77e-23

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: 91.32  E-value: 1.77e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217 105 TIKVIGLQWYWKYEYSDfvdsigETIefesyvipddmlepgalrllDTDTSIVVPVDTHIRFVVTANDVIHSFTIPSLGM 184
Cdd:cd13914    2 EIEVEAYQWGWEFSYPE------ANV--------------------TTSEQLVIPADRPVYFRITSRDVIHAFHVPELGL 55

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 528750217 185 KIDATPGRLNQVSALIQRTGVYYGQCSELCGVNHGMMPIKLECVSIEDFIEWL 237
Cdd:cd13914   56 KQDAFPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 79-237 5.24e-23

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: 91.36  E-value: 5.24e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217  79 AVILL-LIAFPSFILLYLCDEVLTP---AMTIKVIGLQWYWKYEYSDFVDSIGEtiefesyvipddmlepgalrlldtdt 154
Cdd:cd13918    4 AIIVIsLIVWTYGMLLYVEDPPDEAdedALEVEVEGFQFGWQFEYPNGVTTGNT-------------------------- 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217 155 sIVVPVDTHIRFVVTANDVIHSFTIPSLGMKIDATPGRLNQVSALIQRTGVYYGQCSELCGVNHGMMPIKLECVSIEDFI 234
Cdd:cd13918   58 -LRVPADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFE 136


                 ...
gi 528750217 235 EWL 237
Cdd:cd13918  137 AWY 139
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 103-221 1.99e-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: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 88.45  E-value: 1.99e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217 103 AMTIKVIGLQWYWKYEYsdfvdsigetiefesyvipddmlePGALRLLDTdtsIVVPVDTHIRFVVTANDVIHSFTIPSL 182
Cdd:cd13915    1 ALEIQVTGRQWMWEFTY------------------------PNGKREINE---LHVPVGKPVRLILTSKDVIHSFYVPAF 53

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 528750217 183 GMKIDATPGRLNQVSALIQRTGVYYGQCSELCGVNHGMM 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 8.42e-13

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: 62.97  E-value: 8.42e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217 152 TDTSIVVPVDTHIRFVVTANDVIHSFTIPSLGMKIDATPGRLNQVSALIQRTGVYYGQCSELCGVNHGMM 221
Cdd:cd13913   23 NPNEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 104-215 1.25e-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: 51.39  E-value: 1.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217 104 MTIKVIGLQWYWKYEYSDF-VDSIGEtiefesyvipddmlepgalrlldtdtsIVVPVDTHIRFVVTANDVIHSFTIPSL 182
Cdd:cd04212    1 LEIQVVSLDWKWLFIYPEQgIATVNE---------------------------LVIPVGRPVNFRLTSDSVMNSFFIPQL 53

                         90       100       110
                 ....*....|....*....|....*....|...
gi 528750217 183 GMKIDATPGRLNQVSALIQRTGVYYGQCSELCG 215
Cdd:cd04212   54 GGQIYAMAGMQTQLHLIADKPGTYQGLSANYSG 86
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 105-221 1.17e-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: 45.84  E-value: 1.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217 105 TIKVIGLQWYWKyeysdfvdsigetiefesyvipddmlepgalrlLDTDTsivVPVDTHIRFVVTANDVIHSFTIPSLGM 184
Cdd:cd13916    2 VVAVTGHQWYWE---------------------------------LSRTE---IPAGKPVEFRVTSADVNHGFGIYDPDM 45

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 528750217 185 KI----DATPGRLNQVSALIQRTGVYYGQCSELCGV-NHGMM 221
Cdd:cd13916   46 RLlaqtQAMPGYTNVLRYTFDKPGTYTILCLEYCGLaHHVMM 87
PRK10525 PRK10525
cytochrome o ubiquinol oxidase subunit II; Provisional
 59-246 1.55e-05

cytochrome o ubiquinol oxidase subunit II; Provisional


Pssm-ID: 182518 [Multi-domain]  Cd Length: 315  Bit Score: 45.18  E-value: 1.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217  59 FAYKYV------------RHGQVIE-IIWTIfPAVILLLIAfpsfILLYLCDEVLTPA---------MTIKVIGLQWYWK 116
Cdd:PRK10525  65 FAWKYRasnkdakyspnwSHSNKVEaVVWTV-PILIIIFLA----VLTWKTTHALEPSkplahdekpITIEVVSMDWKWF 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217 117 YEYSDfvdsigetiefesyvipddmlepgalRLLDTDTSIVVPVDTHIRFVVTANDVIHSFTIPSLGMKIDATPGRLNQV 196
Cdd:PRK10525 140 FIYPE--------------------------QGIATVNEIAFPANVPVYFKVTSNSVMNSFFIPRLGSQIYAMAGMQTRL 193

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 528750217 197 SALIQRTGVYYGQCSELCGvnHGMMPIKLECVSI---EDFIEWLGENEVSLNS 246
Cdd:PRK10525 194 HLIANEPGTYDGISASYSG--PGFSGMKFKAIATpdrAEFDQWVAKAKQSPNT 244
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 144-221 5.18e-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: 41.45  E-value: 5.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528750217 144 PGALRLLDTDTSIVVPVDTHIRFVVT-ANDVIHSFTIPSLGMKIDA---------------TPGRLNQVSALIQRTGVYY 207
Cdd:cd00920   13 TYNGVLLFGPPVLVVPVGDTVRVQFVnKLGENHSVTIAGFGVPVVAmagganpglvntlviGPGESAEVTFTTDQAGVYW 92

                         90
                 ....*....|....
gi 528750217 208 GQCSELCGVNHGMM 221
Cdd:cd00920   93 FYCTIPGHNHAGMV 106
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 156-221 8.53e-04

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: 37.35  E-value: 8.53e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528750217 156 IVVPVDTHIRFVVTANDVIHSFTIPSLGMKIDATPGRLNQVSALIQRTGVYYGQCSELCGVNHGMM 221
Cdd:cd13917   16 LVLKKGKTYRLHLSSLDVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIICNEYCGIGHHTM 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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