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Conserved domains on  [gi|1089667455|dbj|BAV82673|]
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cytochrome c oxidase subunit II (mitochondrion) [Cylicostephanus goldi]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11475892)

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 MTH00080
cytochrome c oxidase subunit II; Provisional
 3-231 2.09e-135

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 379.74  E-value: 2.09e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1089667455   3 NYFQGYNLNFSNSLFSSYMDWFHSFNCS--LLLGVLVFVVLLFIYLMMNNYYFKSKKIEYQFGELLCSVFPTLILLMQMI 80
Cdd:MTH00080    1 NYFQGYNLNFSNSLFSSYMDWFHNFNCSllFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1089667455  81 PSLSLLYYYGLMNLDSNLTIKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLNLGEPRLLEVDNRCVVPCDTNIRFCITSA 160
Cdd:MTH00080   81 PSLSLLYYYGLMNLDSNLTVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSS 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1089667455 161 DVIHSWALPSMSIKLDAMSGILSTLCYSFPMVGVFYGQCSEICGANHSFMPIAVEVTLLDNFKSWCYLNMD 231
Cdd:MTH00080  161 DVIHSWALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWCKLLLD 231
 
Name Accession Description Interval E-value
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 3-231 2.09e-135

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 379.74  E-value: 2.09e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1089667455   3 NYFQGYNLNFSNSLFSSYMDWFHSFNCS--LLLGVLVFVVLLFIYLMMNNYYFKSKKIEYQFGELLCSVFPTLILLMQMI 80
Cdd:MTH00080    1 NYFQGYNLNFSNSLFSSYMDWFHNFNCSllFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1089667455  81 PSLSLLYYYGLMNLDSNLTIKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLNLGEPRLLEVDNRCVVPCDTNIRFCITSA 160
Cdd:MTH00080   81 PSLSLLYYYGLMNLDSNLTVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSS 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1089667455 161 DVIHSWALPSMSIKLDAMSGILSTLCYSFPMVGVFYGQCSEICGANHSFMPIAVEVTLLDNFKSWCYLNMD 231
Cdd:MTH00080  161 DVIHSWALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWCKLLLD 231
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 96-225 3.12e-81

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


Pssm-ID: 259979 [Multi-domain]  Cd Length: 130  Bit Score: 238.62  E-value: 3.12e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1089667455  96 SNLTIKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLNLGEPRLLEVDNRCVVPCDTNIRFCITSADVIHSWALPSMSIKL 175
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1089667455 176 DAMSGILSTLCYSFPMVGVFYGQCSEICGANHSFMPIAVEVTLLDNFKSW 225
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
98-215 5.07e-60

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 184.54  E-value: 5.07e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1089667455  98 LTIKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLNLGEPRLLEVDNRCVVPCDTNIRFCITSADVIHSWALPSMSIKLDA 177
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1089667455 178 MSGILSTLCYSFPMVGVFYGQCSEICGANHSFMPIAVE 215
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIE 118
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
64-225 4.92e-36

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 126.87  E-value: 4.92e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1089667455  64 ELLCSVFPTLILLMQMIPSLSLLYYYGLMNlDSNLTIKVTGHQWYWSYEFSDIPGLefdsymksldqlnlgeprlleVDN 143
Cdd:COG1622    80 EIVWTVIPIIIVIVLAVPTLRVLHALDDAP-EDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVN 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1089667455 144 RCVVPCDTNIRFCITSADVIHSWALPSMSIKLDAMSGILSTLCYSFPMVGVFYGQCSEICGANHSFMPIAVEVTLLDNFK 223
Cdd:COG1622   138 ELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFD 217


                  ..
gi 1089667455 224 SW 225
Cdd:COG1622   218 AW 219
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 64-225 8.48e-31

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: 112.47  E-value: 8.48e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1089667455  64 ELLCSVFPTLILLMQMIPSLSLLYYYgLMNLDSN-LTIKVTGHQWYWSYEFSDipglefdsymksldqlnlgepRLLEVD 142
Cdd:TIGR02866  57 EYVWTVIPLIIVVGLFAATAKGLLYL-ERPIPKDaLKVKVTGYQWWWDFEYPE---------------------SGFTTV 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1089667455 143 NRCVVPCDTNIRFCITSADVIHSWALPSMSIKLDAMSGILSTLCYSFPMVGVFYGQCSEICGANHSFMPIAVEVTLLDNF 222
Cdd:TIGR02866 115 NELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEF 194


                  ...
gi 1089667455 223 KSW 225
Cdd:TIGR02866 195 DAY 197
 
Name Accession Description Interval E-value
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 3-231 2.09e-135

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 379.74  E-value: 2.09e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1089667455   3 NYFQGYNLNFSNSLFSSYMDWFHSFNCS--LLLGVLVFVVLLFIYLMMNNYYFKSKKIEYQFGELLCSVFPTLILLMQMI 80
Cdd:MTH00080    1 NYFQGYNLNFSNSLFSSYMDWFHNFNCSllFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1089667455  81 PSLSLLYYYGLMNLDSNLTIKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLNLGEPRLLEVDNRCVVPCDTNIRFCITSA 160
Cdd:MTH00080   81 PSLSLLYYYGLMNLDSNLTVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSS 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1089667455 161 DVIHSWALPSMSIKLDAMSGILSTLCYSFPMVGVFYGQCSEICGANHSFMPIAVEVTLLDNFKSWCYLNMD 231
Cdd:MTH00080  161 DVIHSWALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWCKLLLD 231
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 96-225 3.12e-81

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


Pssm-ID: 259979 [Multi-domain]  Cd Length: 130  Bit Score: 238.62  E-value: 3.12e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1089667455  96 SNLTIKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLNLGEPRLLEVDNRCVVPCDTNIRFCITSADVIHSWALPSMSIKL 175
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1089667455 176 DAMSGILSTLCYSFPMVGVFYGQCSEICGANHSFMPIAVEVTLLDNFKSW 225
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 5-226 3.17e-73

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 221.78  E-value: 3.17e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1089667455   5 FQGYNLNFSNSLFSSYMDWFHSFNCSLLLGVLVFVVLLFIYLMMNNYYFKSKKiEYQFGELLCSVFPTLILLMQMIPSLS 84
Cdd:MTH00168    4 YSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLL-DSQMIEFVWTIIPAFILISLALPSLR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1089667455  85 LLYYyglM--NLDSNLTIKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLNLGEPRLLEVDNRCVVPCDTNIRFCITSADV 162
Cdd:MTH00168   83 LLYL---MdeIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1089667455 163 IHSWALPSMSIKLDAMSGILSTLCYSFPMVGVFYGQCSEICGANHSFMPIAVEVTLLDNFKSWC 226
Cdd:MTH00168  160 LHSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWV 223
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 10-226 3.29e-73

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 221.74  E-value: 3.29e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1089667455  10 LNF--SNSLFSSYMDWFHSFNCSLLLGVLVFVVLLFIYLMMNNYYFKSKKiEYQFGELLCSVFPTLILLMQMIPSLSLLY 87
Cdd:MTH00140    7 LGFqdPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTIL-EAQKLETIWTIVPALILVFLALPSLRLLY 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1089667455  88 YYGLMNlDSNLTIKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLNLGEPRLLEVDNRCVVPCDTNIRFCITSADVIHSWA 167
Cdd:MTH00140   86 LLDETN-NPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWT 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1089667455 168 LPSMSIKLDAMSGILSTLCYSFPMVGVFYGQCSEICGANHSFMPIAVEVTLLDNFKSWC 226
Cdd:MTH00140  165 VPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWL 223
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 9-230 2.85e-72

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 219.31  E-value: 2.85e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1089667455   9 NLNF--SNSLFSSYMDWFHSFNCSLLLGVLVFVVLLFIYLMMNNYYFKSKkIEYQFGELLCSVFPTLILLMQMIPSLSLL 86
Cdd:MTH00154    6 NLSFqdSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFL-LEGQEIEIIWTILPAIILIFIALPSLRLL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1089667455  87 YYYGLMNlDSNLTIKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLNLGEPRLLEVDNRCVVPCDTNIRFCITSADVIHSW 166
Cdd:MTH00154   85 YLLDEVN-NPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSW 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1089667455 167 ALPSMSIKLDAMSGILSTLCYSFPMVGVFYGQCSEICGANHSFMPIAVEVTLLDNFKSWCYLNM 230
Cdd:MTH00154  164 TVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 64-225 1.02e-69

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 212.85  E-value: 1.02e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1089667455  64 ELLCSVFPTLILLMQMIPSLSLLYyygLMN--LDSNLTIKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLNLGEPRLLEV 141
Cdd:MTH00117   62 ELIWTILPAIVLILLALPSLRILY---LMDeiNNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEV 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1089667455 142 DNRCVVPCDTNIRFCITSADVIHSWALPSMSIKLDAMSGILSTLCYSFPMVGVFYGQCSEICGANHSFMPIAVEVTLLDN 221
Cdd:MTH00117  139 DHRMVIPMESPIRILITAEDVLHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKH 218


                  ....
gi 1089667455 222 FKSW 225
Cdd:MTH00117  219 FENW 222
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 4-226 3.46e-69

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 211.50  E-value: 3.46e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1089667455   4 YFQGYNLNFSNSLFSSYMDWFHSFNCSLLLGVLVFVVLLFIYLMMNNYYFKSKkIEYQFGELLCSVFPTLILLMQMIPSL 83
Cdd:MTH00139    3 YWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSL-LESQEVETIWTVLPAFILLFLALPSL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1089667455  84 SLLYyygLMN--LDSNLTIKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLNLGEPRLLEVDNRCVVPCDTNIRFCITSAD 161
Cdd:MTH00139   82 RLLY---LMDevSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAAD 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1089667455 162 VIHSWALPSMSIKLDAMSGILSTLCYSFPMVGVFYGQCSEICGANHSFMPIAVEVTLLDNFKSWC 226
Cdd:MTH00139  159 VLHSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWI 223
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 58-227 1.10e-68

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 210.33  E-value: 1.10e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1089667455  58 IEYQFGELLCSVFPTLILLMQMIPSLSLLYYYGLMNlDSNLTIKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLNLGEPR 137
Cdd:MTH00038   56 LEGQELETIWTIVPAFILIFIALPSLQLLYLMDEVN-NPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPR 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1089667455 138 LLEVDNRCVVPCDTNIRFCITSADVIHSWALPSMSIKLDAMSGILSTLCYSFPMVGVFYGQCSEICGANHSFMPIAVEVT 217
Cdd:MTH00038  135 LLEVDNRLVLPYQTPIRVLVSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESV 214

                         170
                  ....*....|
gi 1089667455 218 LLDNFKSWCY 227
Cdd:MTH00038  215 PFNTFENWVS 224
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 44-225 4.64e-63

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 196.15  E-value: 4.64e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1089667455  44 IYLMMNNYYFKSKKIEYQFGELLCSVFPTLILLMQMIPSLSLLYYYGLMNlDSNLTIKVTGHQWYWSYEFSDIPGLEFDS 123
Cdd:MTH00076   42 ITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRILYLMDEIN-DPHLTVKAIGHQWYWSYEYTDYEDLSFDS 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1089667455 124 YMKSLDQLNLGEPRLLEVDNRCVVPCDTNIRFCITSADVIHSWALPSMSIKLDAMSGILSTLCYSFPMVGVFYGQCSEIC 203
Cdd:MTH00076  121 YMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEIC 200

                         170       180
                  ....*....|....*....|..
gi 1089667455 204 GANHSFMPIAVEVTLLDNFKSW 225
Cdd:MTH00076  201 GANHSFMPIVVEATPLNNFLNW 222
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 47-225 7.17e-63

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 195.87  E-value: 7.17e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1089667455  47 MMNNYYFKSKKIEyqfgeLLCSVFPTLILLMQMIPSLSLLYYYGLMNlDSNLTIKVTGHQWYWSYEFSDIPGLEFDSYMK 126
Cdd:MTH00185   50 LTNKYILDSQEIE-----IVWTILPAIILIMIALPSLRILYLMDEIN-DPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMT 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1089667455 127 SLDQLNLGEPRLLEVDNRCVVPCDTNIRFCITSADVIHSWALPSMSIKLDAMSGILSTLCYSFPMVGVFYGQCSEICGAN 206
Cdd:MTH00185  124 PTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGAN 203

                         170
                  ....*....|....*....
gi 1089667455 207 HSFMPIAVEVTLLDNFKSW 225
Cdd:MTH00185  204 HSFMPIVVEAVPLEHFENW 222
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 47-225 9.05e-62

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 192.76  E-value: 9.05e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1089667455  47 MMNNYYFKSKKIEYQFGELLCSVFPTLILLMQMIPSLSLLYyygLMNLDSN--LTIKVTGHQWYWSYEFSDIPGLEFDSY 124
Cdd:MTH00008   45 LMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSLRLLY---LMDEVSNpsITLKTIGHQWYWSYEYSDFSNLEFDSY 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1089667455 125 MKSLDQLNLGEPRLLEVDNRCVVPCDTNIRFCITSADVIHSWALPSMSIKLDAMSGILSTLCYSFPMVGVFYGQCSEICG 204
Cdd:MTH00008  122 MLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICG 201

                         170       180
                  ....*....|....*....|.
gi 1089667455 205 ANHSFMPIAVEVTLLDNFKSW 225
Cdd:MTH00008  202 ANHSFMPIVLEAVDTKSFMKW 222
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 47-228 9.23e-62

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 193.01  E-value: 9.23e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1089667455  47 MMNNYYFKSKKIEyqfgeLLCSVFPTLILLMQMIPSLSLLYYYGLMNlDSNLTIKVTGHQWYWSYEFSDIPGLEFDSYMK 126
Cdd:MTH00129   50 LTNKYILDSQEIE-----IIWTVLPAVILILIALPSLRILYLMDEIN-DPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMI 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1089667455 127 SLDQLNLGEPRLLEVDNRCVVPCDTNIRFCITSADVIHSWALPSMSIKLDAMSGILSTLCYSFPMVGVFYGQCSEICGAN 206
Cdd:MTH00129  124 PTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGAN 203

                         170       180
                  ....*....|....*....|..
gi 1089667455 207 HSFMPIAVEVTLLDNFKSWCYL 228
Cdd:MTH00129  204 HSFMPIVVEAVPLEHFENWSSL 225
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 47-225 3.19e-61

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 191.53  E-value: 3.19e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1089667455  47 MMNNYYFKSKkIEYQFGELLCSVFPTLILLMQMIPSLSLLYyygLMN--LDSNLTIKVTGHQWYWSYEFSDIPG--LEFD 122
Cdd:MTH00051   48 LTTKYYHKYL-FEGTLIEIIWTLIPAAILIFIAFPSLKLLY---LMDevIDPALTIKAIGHQWYWSYEYSDYGTdtIEFD 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1089667455 123 SYMKSLDQLNLGEPRLLEVDNRCVVPCDTNIRFCITSADVIHSWALPSMSIKLDAMSGILSTLCYSFPMVGVFYGQCSEI 202
Cdd:MTH00051  124 SYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEI 203

                         170       180
                  ....*....|....*....|...
gi 1089667455 203 CGANHSFMPIAVEVTLLDNFKSW 225
Cdd:MTH00051  204 CGANHSFMPIVIEGVSLDKYINW 226
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 48-225 3.32e-61

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 191.89  E-value: 3.32e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1089667455  48 MNNYYFKSKKIEYQFGELLCSVFPTLILLMQMIPSLSLLYyygLM--NLDSNLTIKVTGHQWYWSYEFSDIPG--LEFDS 123
Cdd:MTH00023   55 LNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLY---LMdeVVSPALTIKAIGHQWYWSYEYSDYEGetLEFDS 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1089667455 124 YMKSLDQLNLGEPRLLEVDNRCVVPCDTNIRFCITSADVIHSWALPSMSIKLDAMSGILSTLCYSFPMVGVFYGQCSEIC 203
Cdd:MTH00023  132 YMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEIC 211

                         170       180
                  ....*....|....*....|..
gi 1089667455 204 GANHSFMPIAVEVTLLDNFKSW 225
Cdd:MTH00023  212 GANHSFMPIVIEAVSLDKYINW 233
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 44-225 2.07e-60

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 189.16  E-value: 2.07e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1089667455  44 IYLMMNNYYFKSKKIEYQFGELLCSVFPTLILLMQMIPSLSLLYYYGLMNlDSNLTIKVTGHQWYWSYEFSDIPGLEFDS 123
Cdd:MTH00098   42 ISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRILYMMDEIN-NPSLTVKTMGHQWYWSYEYTDYEDLSFDS 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1089667455 124 YMKSLDQLNLGEPRLLEVDNRCVVPCDTNIRFCITSADVIHSWALPSMSIKLDAMSGIL--STLCYSFPmvGVFYGQCSE 201
Cdd:MTH00098  121 YMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLnqTTLMSTRP--GLYYGQCSE 198

                         170       180
                  ....*....|....*....|....
gi 1089667455 202 ICGANHSFMPIAVEVTLLDNFKSW 225
Cdd:MTH00098  199 ICGSNHSFMPIVLELVPLKYFEKW 222
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
98-215 5.07e-60

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 184.54  E-value: 5.07e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1089667455  98 LTIKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLNLGEPRLLEVDNRCVVPCDTNIRFCITSADVIHSWALPSMSIKLDA 177
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1089667455 178 MSGILSTLCYSFPMVGVFYGQCSEICGANHSFMPIAVE 215
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIE 118
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 46-225 1.07e-55

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 178.68  E-value: 1.07e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1089667455  46 LMMNNYY-FKSKKIEYQFGELLCSVFPTLILLMQMIPSLSLLYYYGLMNLDSNLTIKVTGHQWYWSYEFSDI--PGLEFD 122
Cdd:MTH00027   74 LLGNNYYsYYWNKLDGSLIEVIWTLIPAFILILIAFPSLRLLYIMDECGFSANITIKVTGHQWYWSYSYEDYgeKNIEFD 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1089667455 123 SYMKSLDQLNLGEPRLLEVDNRCVVPCDTNIRFCITSADVIHSWALPSMSIKLDAMSGILSTLCYSFPMVGVFYGQCSEI 202
Cdd:MTH00027  154 SYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEI 233

                         170       180
                  ....*....|....*....|...
gi 1089667455 203 CGANHSFMPIAVEVTLLDNFKSW 225
Cdd:MTH00027  234 CGANHSFMPIVVESVSLSKYIDW 256
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
64-225 4.92e-36

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 126.87  E-value: 4.92e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1089667455  64 ELLCSVFPTLILLMQMIPSLSLLYYYGLMNlDSNLTIKVTGHQWYWSYEFSDIPGLefdsymksldqlnlgeprlleVDN 143
Cdd:COG1622    80 EIVWTVIPIIIVIVLAVPTLRVLHALDDAP-EDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVN 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1089667455 144 RCVVPCDTNIRFCITSADVIHSWALPSMSIKLDAMSGILSTLCYSFPMVGVFYGQCSEICGANHSFMPIAVEVTLLDNFK 223
Cdd:COG1622   138 ELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFD 217


                  ..
gi 1089667455 224 SW 225
Cdd:COG1622   218 AW 219
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 59-221 1.43e-34

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 121.99  E-value: 1.43e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1089667455  59 EYQFGELLCSVFPTLILLMQMIPSLSLLYYYglMNLDSNLTIKVTGHQWYWSYEFSDipGLEFDSYMKSLdqlnlgeprL 138
Cdd:MTH00047   45 ENQVLELLWTVVPTLLVLVLCFLNLNFITSD--LDCFSSETIKVIGHQWYWSYEYSF--GGSYDSFMTDD---------I 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1089667455 139 LEVDNRCVVPCDTNIRFCITSADVIHSWALPSMSIKLDAMSGILSTLCYSFPMVGVFYGQCSEICGANHSFMPIAVEVTL 218
Cdd:MTH00047  112 FGVDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVVD 191


                  ...
gi 1089667455 219 LDN 221
Cdd:MTH00047  192 VDS 194
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 121-215 2.29e-31

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 112.99  E-value: 2.29e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1089667455 121 FDSYMKSLDQLNLGEPRLLEVDNRCVVPCDTNIRFCITSADVIHSWALPSMSIKLDAMSGILSTLCYSFPMVGVFYGQCS 200
Cdd:PTZ00047   51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                          90
                  ....*....|....*
gi 1089667455 201 EICGANHSFMPIAVE 215
Cdd:PTZ00047  131 EMCGTLHGFMPIVVE 145
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 64-225 8.48e-31

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: 112.47  E-value: 8.48e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1089667455  64 ELLCSVFPTLILLMQMIPSLSLLYYYgLMNLDSN-LTIKVTGHQWYWSYEFSDipglefdsymksldqlnlgepRLLEVD 142
Cdd:TIGR02866  57 EYVWTVIPLIIVVGLFAATAKGLLYL-ERPIPKDaLKVKVTGYQWWWDFEYPE---------------------SGFTTV 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1089667455 143 NRCVVPCDTNIRFCITSADVIHSWALPSMSIKLDAMSGILSTLCYSFPMVGVFYGQCSEICGANHSFMPIAVEVTLLDNF 222
Cdd:TIGR02866 115 NELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEF 194


                  ...
gi 1089667455 223 KSW 225
Cdd:TIGR02866 195 DAY 197
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 98-215 1.22e-23

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: 90.82  E-value: 1.22e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1089667455  98 LTIKVTGHQWYWSYEFSDIpglefdsymksldqlnlgeprllEVDNRCVVPCDTNIRFCITSADVIHSWALPSMSIKLDA 177
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPNV-----------------------RTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1089667455 178 MSGILSTLCYSFPMVGVFYGQCSEICGANHSFMPIAVE 215
Cdd:cd13842    58 VPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 98-216 3.35e-22

The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of most bacteria, is a multi-chain transmembrane protein located in the inner membrane the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. Caa3 type of CcO Subunit II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the cytochromes a, a3 and CuB active site in subunit I.


Pssm-ID: 259875 [Multi-domain]  Cd Length: 103  Bit Score: 87.29  E-value: 3.35e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1089667455  98 LTIKVTGHQWYWSYEFSDIPGLEFdsymksldqlnlgeprllEVDNRCVVPCDTNIRFCITSADVIHSWALPSMSIKLDA 177
Cdd:cd04213     2 LTIEVTGHQWWWEFRYPDEPGRGI------------------VTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDM 63

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1089667455 178 MSGILSTLCYSFPMVGVFYGQCSEICGANHSFMPIAVEV 216
Cdd:cd04213    64 IPGRTNRLWLQADEPGVYRGQCAEFCGASHALMRFKVIA 102
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 98-225 2.36e-18

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


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 78.27  E-value: 2.36e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1089667455  98 LTIKVTGHQWYWSYEFSDipGLEFDSYMksldqlnlgeprllevdnrcVVPCDTNIRFCITSADVIHSWALPSMSIKLDA 177
Cdd:cd13918    33 LEVEVEGFQFGWQFEYPN--GVTTGNTL--------------------RVPADTPIALRVTSTDVFHTFGIPELRVKADA 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1089667455 178 MSGILSTLCYSFPMVGVFYGQCSEICGANHSFMPIAVEVTLLDNFKSW 225
Cdd:cd13918    91 IPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAW 138
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 98-216 9.90e-18

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


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 75.36  E-value: 9.90e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1089667455  98 LTIKVTGHQWYWSYEFsdipglefdsymksldqlnlgePRLLEVDNRCVVPCDTNIRFCITSADVIHSWALPSMSIKLDA 177
Cdd:cd13915     2 LEIQVTGRQWMWEFTY----------------------PNGKREINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDV 59

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1089667455 178 MSGILSTLCYSFPMVGVFYGQCSEICGANHSFMPIAVEV 216
Cdd:cd13915    60 VPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGMIGKVRV 98
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 98-210 6.13e-16

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


Pssm-ID: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 70.75  E-value: 6.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1089667455  98 LTIKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLnlgeprllevdnrcVVPCDTNIRFCITSADVIHSWALPSMSIKLDA 177
Cdd:cd13919     2 LVVEVTAQQWAWTFRYPGGDGKLGTDDDVTSPEL--------------HLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1089667455 178 MSGILSTLCYSFPMVGVFYGQCSEICGANHSFM 210
Cdd:cd13919    68 VPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 99-225 2.45e-15

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: 69.36  E-value: 2.45e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1089667455  99 TIKVTGHQWYWSYEFsdiPGLEFDSymksldqlnlgeprllevDNRCVVPCDTNIRFCITSADVIHSWALPSMSIKLDAM 178
Cdd:cd13914     2 EIEVEAYQWGWEFSY---PEANVTT------------------SEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAF 60

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1089667455 179 SGILSTLCYSFPMVGVFYGQCSEICGANHSFMPIAVEVTLLDNFKSW 225
Cdd:cd13914    61 PGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQW 107
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 143-217 5.01e-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: 57.58  E-value: 5.01e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1089667455 143 NRCVVPCDTNIRFCITSADVIHSWALPSMSIKLDAMSGILSTLCYSFPMVGVFYGQCSEICGANHSFMPIAVEVT 217
Cdd:cd13913    25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNMYGKIIVE 99
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 99-217 4.80e-10

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: 54.70  E-value: 4.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1089667455  99 TIKVTGHQWYWSYefsdipglefdsymkSLDQLNLGEPrllevdnrcvvpcdtnIRFCITSADVIHSWAL--PSMSI--K 174
Cdd:cd13916     2 VVAVTGHQWYWEL---------------SRTEIPAGKP----------------VEFRVTSADVNHGFGIydPDMRLlaQ 50

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1089667455 175 LDAMSGILSTLCYSFPMVGVFYGQCSEICGANHSFMPIAVEVT 217
Cdd:cd13916    51 TQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVMMAEFTVV 93
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 143-217 2.21e-03

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: 36.37  E-value: 2.21e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1089667455 143 NRCVVPCDTNIRFCITSADVIHSWALPSMSIKLDAMSGILSTLCYSFPMVGVFYGQCSEICGANHSFMPIAVEVT 217
Cdd:cd04212    25 NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDMKFKVLAV 99
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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