NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|23200455]
View 

Chain B, CYTOCHROME C OXIDASE

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11446855)

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

CATH:  1.10.287.90|2.60.40.420
EC:  7.1.1.9
Gene Ontology:  GO:0042773|GO:0004129|GO:0005507
SCOP:  4002011|4002191

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
14-258 1.02e-83

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


:

Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 250.13  E-value: 1.02e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455  14 GGTGFQPSASPVATQIHWLDGFILVIIAAITIFVTLLILYAVWRFHEKRNK-VPARFTHNSPLEIAWTIVPIVILVAIGA 92
Cdd:COG1622  17 GQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIRYRRRKGDaDPAQFHHNTKLEIVWTVIPIIIVIVLAV 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455  93 FSLPVLFNQQEIPEADVTVKVTGYQWYWGYEYPDEEISFESYM---IGSPAtggdnrmspeveqqlieagysrdEFLLat 169
Cdd:COG1622  97 PTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIATVNELvlpVGRPV-----------------------RFLL-- 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455 170 dtamvvpvnktvvvqvTGADVIHSWTVPAFGVKQDAVPGRLAQLWFRAEREGIFFGQCSELCGISHAYMPITVKVVSEEA 249
Cdd:COG1622 152 ----------------TSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEE 215


                ....*....
gi 23200455 250 YAAWLEQAR 258
Cdd:COG1622 216 FDAWLAEQK 224
 
Name Accession Description Interval E-value
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
14-258 1.02e-83

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 250.13  E-value: 1.02e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455  14 GGTGFQPSASPVATQIHWLDGFILVIIAAITIFVTLLILYAVWRFHEKRNK-VPARFTHNSPLEIAWTIVPIVILVAIGA 92
Cdd:COG1622  17 GQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIRYRRRKGDaDPAQFHHNTKLEIVWTVIPIIIVIVLAV 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455  93 FSLPVLFNQQEIPEADVTVKVTGYQWYWGYEYPDEEISFESYM---IGSPAtggdnrmspeveqqlieagysrdEFLLat 169
Cdd:COG1622  97 PTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIATVNELvlpVGRPV-----------------------RFLL-- 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455 170 dtamvvpvnktvvvqvTGADVIHSWTVPAFGVKQDAVPGRLAQLWFRAEREGIFFGQCSELCGISHAYMPITVKVVSEEA 249
Cdd:COG1622 152 ----------------TSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEE 215


                ....*....
gi 23200455 250 YAAWLEQAR 258
Cdd:COG1622 216 FDAWLAEQK 224
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 14-255 1.54e-65

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 203.63  E-value: 1.54e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455   14 GGTGFQPSASPVATQIHWLDGFILVIIAAITIFVTLLILYAVWrfhekrNKVPARFTHNSP-LEIAWTIVPIVILVAIGA 92
Cdd:MTH00140   5 GQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLF------NKFSCRTILEAQkLETIWTIVPALILVFLAL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455   93 FSLPVLFNQQEIPEADVTVKVTGYQWYWGYEYPD-EEISFESYMIgspatggdnrmsPEVEqqlIEAGYSRdefLLATDT 171
Cdd:MTH00140  79 PSLRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDfSVIEFDSYMV------------PENE---LELGDFR---LLEVDN 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455  172 AMVVPVNKTVVVQVTGADVIHSWTVPAFGVKQDAVPGRLAQLWFRAEREGIFFGQCSELCGISHAYMPITVKVVSEEAYA 251
Cdd:MTH00140 141 RLVLPYSVDTRVLVTSADVIHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFV 220


                 ....
gi 23200455  252 AWLE 255
Cdd:MTH00140 221 KWLE 224
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 108-253 4.59e-61

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: 188.93  E-value: 4.59e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455 108 DVTVKVTGYQWYWGYEYPD-EEISFESYMIgspatggdnrmsPEVEqqlIEAGYSRdefLLATDTAMVVPVNKTVVVQVT 186
Cdd:cd13912   2 SLTIKAIGHQWYWSYEYSDfNDLEFDSYMI------------PEDD---LEKGQLR---LLEVDNRLVVPVNTHIRVLVT 63

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23200455 187 GADVIHSWTVPAFGVKQDAVPGRLAQLWFRAEREGIFFGQCSELCGISHAYMPITVKVVSEEAYAAW 253
Cdd:cd13912  64 SADVIHSWAVPSLGIKVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
110-245 2.72e-50

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 161.04  E-value: 2.72e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455   110 TVKVTGYQWYWGYEYPD-EEISFESYMIGspatggdnrmspevEQQLIEAGYSrdefLLATDTAMVVPVNKTVVVQVTGA 188
Cdd:pfam00116   2 TIKAIGHQWYWSYEYTDfGDLEFDSYMIP--------------TEDLEEGQLR----LLEVDNRVVLPVETHIRVIVTAA 63

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 23200455   189 DVIHSWTVPAFGVKQDAVPGRLAQLWFRAEREGIFFGQCSELCGISHAYMPITVKVV 245
Cdd:pfam00116  64 DVIHSWAVPSLGIKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 22-255 2.72e-50

cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions. [Energy metabolism, Electron transport]


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 163.71  E-value: 2.72e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455    22 ASPVATQIHWLDGFILVIIAAITIFVTLLILYAVWRFHEK-RNKVPARFTHNSPLEIAWTIVPIVILVAIGAFSLPVLFN 100
Cdd:TIGR02866   2 GGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVWKFRRKgDEEKPSQIHGNRRLEYVWTVIPLIIVVGLFAATAKGLLY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455   101 QQE-IPEADVTVKVTGYQWYWGYEYPDEeisfesymigspATGGDNrmspeveqqlieagysrdEFLLATDTamvvpvnk 179
Cdd:TIGR02866  82 LERpIPKDALKVKVTGYQWWWDFEYPES------------GFTTVN------------------ELVLPAGT-------- 123

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23200455   180 TVVVQVTGADVIHSWTVPAFGVKQDAVPGRLAQLWFRAEREGIFFGQCSELCGISHAYMPITVKVVSEEAYAAWLE 255
Cdd:TIGR02866 124 PVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
 
Name Accession Description Interval E-value
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
14-258 1.02e-83

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 250.13  E-value: 1.02e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455  14 GGTGFQPSASPVATQIHWLDGFILVIIAAITIFVTLLILYAVWRFHEKRNK-VPARFTHNSPLEIAWTIVPIVILVAIGA 92
Cdd:COG1622  17 GQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIRYRRRKGDaDPAQFHHNTKLEIVWTVIPIIIVIVLAV 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455  93 FSLPVLFNQQEIPEADVTVKVTGYQWYWGYEYPDEEISFESYM---IGSPAtggdnrmspeveqqlieagysrdEFLLat 169
Cdd:COG1622  97 PTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIATVNELvlpVGRPV-----------------------RFLL-- 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455 170 dtamvvpvnktvvvqvTGADVIHSWTVPAFGVKQDAVPGRLAQLWFRAEREGIFFGQCSELCGISHAYMPITVKVVSEEA 249
Cdd:COG1622 152 ----------------TSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEE 215


                ....*....
gi 23200455 250 YAAWLEQAR 258
Cdd:COG1622 216 FDAWLAEQK 224
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 14-255 1.54e-65

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 203.63  E-value: 1.54e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455   14 GGTGFQPSASPVATQIHWLDGFILVIIAAITIFVTLLILYAVWrfhekrNKVPARFTHNSP-LEIAWTIVPIVILVAIGA 92
Cdd:MTH00140   5 GQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLF------NKFSCRTILEAQkLETIWTIVPALILVFLAL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455   93 FSLPVLFNQQEIPEADVTVKVTGYQWYWGYEYPD-EEISFESYMIgspatggdnrmsPEVEqqlIEAGYSRdefLLATDT 171
Cdd:MTH00140  79 PSLRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDfSVIEFDSYMV------------PENE---LELGDFR---LLEVDN 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455  172 AMVVPVNKTVVVQVTGADVIHSWTVPAFGVKQDAVPGRLAQLWFRAEREGIFFGQCSELCGISHAYMPITVKVVSEEAYA 251
Cdd:MTH00140 141 RLVLPYSVDTRVLVTSADVIHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFV 220


                 ....
gi 23200455  252 AWLE 255
Cdd:MTH00140 221 KWLE 224
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 17-254 1.93e-65

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 203.52  E-value: 1.93e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455   17 GFQPSASPVATQIHWLDGFILVIIAAITIFVTLLILYAVWrfhekrNKVPARF-THNSPLEIAWTIVPIVILVAIGAFSL 95
Cdd:MTH00154   8 SFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLF------NKFTNRFlLEGQEIEIIWTILPAIILIFIALPSL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455   96 PVLFNQQEIPEADVTVKVTGYQWYWGYEYPD-EEISFESYMIGSpatggdNRMSPEveqqlieagysrdEF-LLATDTAM 173
Cdd:MTH00154  82 RLLYLLDEVNNPSITLKTIGHQWYWSYEYSDfKNIEFDSYMIPT------NELENN-------------GFrLLDVDNRL 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455  174 VVPVNKTVVVQVTGADVIHSWTVPAFGVKQDAVPGRLAQLWFRAEREGIFFGQCSELCGISHAYMPITVKVVSEEAYAAW 253
Cdd:MTH00154 143 VLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINW 222


                 .
gi 23200455  254 L 254
Cdd:MTH00154 223 I 223
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 13-254 3.24e-61

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 192.50  E-value: 3.24e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455   13 PGGTGFQPSASPVATQIHWLDGFILVIIAAITIFVtLLILYAVwrfheKRNKVPARFTHNSP-LEIAWTIVPIVILVAIG 91
Cdd:MTH00168   4 YSQLGLQDAASPVMEELILFHDHALLILVLILTLV-LYSLLVL-----VTSKYTNRFLLDSQmIEFVWTIIPAFILISLA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455   92 AFSLPVLFNQQEIPEADVTVKVTGYQWYWGYEYPD-EEISFESYMIGSPA-TGGDNRMSpEVEQQLIeagysrdeflLAT 169
Cdd:MTH00168  78 LPSLRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDyNDLEFDSYMVPTQDlSPGQFRLL-EVDNRLV----------LPM 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455  170 DTAMVVPvnktvvvqVTGADVIHSWTVPAFGVKQDAVPGRLAQLWFRAEREGIFFGQCSELCGISHAYMPITVKVVSEEA 249
Cdd:MTH00168 147 DSKIRVL--------VTSADVLHSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWET 218


                 ....*
gi 23200455  250 YAAWL 254
Cdd:MTH00168 219 FENWV 223
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 108-253 4.59e-61

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: 188.93  E-value: 4.59e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455 108 DVTVKVTGYQWYWGYEYPD-EEISFESYMIgspatggdnrmsPEVEqqlIEAGYSRdefLLATDTAMVVPVNKTVVVQVT 186
Cdd:cd13912   2 SLTIKAIGHQWYWSYEYSDfNDLEFDSYMI------------PEDD---LEKGQLR---LLEVDNRLVVPVNTHIRVLVT 63

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23200455 187 GADVIHSWTVPAFGVKQDAVPGRLAQLWFRAEREGIFFGQCSELCGISHAYMPITVKVVSEEAYAAW 253
Cdd:cd13912  64 SADVIHSWAVPSLGIKVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 17-254 6.94e-61

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 191.85  E-value: 6.94e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455   17 GFQPSASPVATQIHWLDGFILVIIAAITIFVTLLILYAVWrfhekrNKVPAR-FTHNSPLEIAWTIVPIVILVAIGAFSL 95
Cdd:MTH00139   8 GFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMS------NKFTSRsLLESQEVETIWTVLPAFILLFLALPSL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455   96 PVLFNQQEIPEADVTVKVTGYQWYWGYEYPD-EEISFESYMIGSP-ATGGDNRmspeveqqlieagysrdefLLATDTAM 173
Cdd:MTH00139  82 RLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDfKNLSFDSYMIPTEdLSSGEFR-------------------LLEVDNRL 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455  174 VVPVNKTVVVQVTGADVIHSWTVPAFGVKQDAVPGRLAQLWFRAEREGIFFGQCSELCGISHAYMPITVKVVSEEAYAAW 253
Cdd:MTH00139 143 VLPYKSNIRALITAADVLHSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEW 222


                 .
gi 23200455  254 L 254
Cdd:MTH00139 223 I 223
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 11-254 3.10e-59

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 188.04  E-value: 3.10e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455   11 PQPGGTGFQPSASPVATQIHWLDGFILVIIAAITIFVTLLILYAVwrfhekRNKVPARF-THNSPLEIAWTIVPIVILVA 89
Cdd:MTH00023  11 PEPWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEAL------NGKFYDRFlVDGTFLEIVWTIIPAVILVF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455   90 IGAFSLPVLFNQQEIPEADVTVKVTGYQWYWGYEYPD---EEISFESYMI-GSPATGGDNRmspeveqqlieagysrdef 165
Cdd:MTH00023  85 IALPSLKLLYLMDEVVSPALTIKAIGHQWYWSYEYSDyegETLEFDSYMVpTSDLNSGDFR------------------- 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455  166 LLATDTAMVVPVNKTVVVQVTGADVIHSWTVPAFGVKQDAVPGRLAQLWFRAEREGIFFGQCSELCGISHAYMPITVKVV 245
Cdd:MTH00023 146 LLEVDNRLVVPINTHVRILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAV 225


                 ....*....
gi 23200455  246 SEEAYAAWL 254
Cdd:MTH00023 226 SLDKYINWL 234
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 11-255 7.35e-59

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 186.66  E-value: 7.35e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455   11 PQPGGTGFQPSASPVATQIHWLDGFILVIIAAITIFVTLLILYAVwrfhekrnkvPARFTHNSP-----LEIAWTIVPIV 85
Cdd:MTH00117   2 ANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLML----------TTKLTHTNTvdaqeVELIWTILPAI 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455   86 ILVAIGAFSLPVLFNQQEIPEADVTVKVTGYQWYWGYEYPDEE-ISFESYMIgspatggdnrmsPEVEQQLieaGYSRde 164
Cdd:MTH00117  72 VLILLALPSLRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKdLSFDSYMI------------PTQDLPN---GHFR-- 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455  165 fLLATDTAMVVPVNKTVVVQVTGADVIHSWTVPAFGVKQDAVPGRLAQLWFRAEREGIFFGQCSELCGISHAYMPITVKV 244
Cdd:MTH00117 135 -LLEVDHRMVIPMESPIRILITAEDVLHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVES 213

                        250
                 ....*....|.
gi 23200455  245 VSEEAYAAWLE 255
Cdd:MTH00117 214 VPLKHFENWSS 224
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 17-256 3.08e-57

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 182.59  E-value: 3.08e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455   17 GFQPSASPVATQIHWLDGFILVIIAAITIFV-----TLLILYAVWRFhekrnkvparFTHNSPLEIAWTIVPIVILVAIG 91
Cdd:MTH00038   8 GLQDASSPLMEELIYFHDYALIILTLITILVfyglaSLLFSSPTNRF----------FLEGQELETIWTIVPAFILIFIA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455   92 AFSLPVLFNQQEIPEADVTVKVTGYQWYWGYEYPD-EEISFESYMIG-SPATGGDNRMSpEVEQQLIeagysrdeflLAT 169
Cdd:MTH00038  78 LPSLQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDyNDLEFDSYMVPtSDLSTGLPRLL-EVDNRLV----------LPY 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455  170 DTAMVVPvnktvvvqVTGADVIHSWTVPAFGVKQDAVPGRLAQLWFRAEREGIFFGQCSELCGISHAYMPITVKVVSEEA 249
Cdd:MTH00038 147 QTPIRVL--------VSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNT 218


                 ....*..
gi 23200455  250 YAAWLEQ 256
Cdd:MTH00038 219 FENWVSN 225
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 11-255 2.19e-55

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 178.05  E-value: 2.19e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455   11 PQPGGTGFQPSASPVATQIHWLDGFILVIIAAITIFVTLLILYAVWRFHEKRNkvparFTHNSPLEIAWTIVPIVILVAI 90
Cdd:MTH00051   4 PEPWQLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKY-----LFEGTLIEIIWTLIPAAILIFI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455   91 GAFSLPVLFNQQEIPEADVTVKVTGYQWYWGYEYPD---EEISFESYMIGSPATG-GDNRMSpEVEQQLIEAGYSRDEFL 166
Cdd:MTH00051  79 AFPSLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDygtDTIEFDSYMIPTSDLNsGDLRLL-EVDNRLIVPIQTQVRVL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455  167 latdtamvvpvnktvvvqVTGADVIHSWTVPAFGVKQDAVPGRLAQLWFRAEREGIFFGQCSELCGISHAYMPITVKVVS 246
Cdd:MTH00051 158 ------------------VTAADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVS 219


                 ....*....
gi 23200455  247 EEAYAAWLE 255
Cdd:MTH00051 220 LDKYINWVA 228
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 13-253 7.17e-54

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 174.13  E-value: 7.17e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455   13 PGGTGFQPSASPVATQIHWLDGFILVIIAAITIFVTLLILYAVwrfhekRNKVPARFTHNS-PLEIAWTIVPIVILVAIG 91
Cdd:MTH00129   4 PSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMV------STKLTNKYILDSqEIEIIWTVLPAVILILIA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455   92 AFSLPVLFNQQEIPEADVTVKVTGYQWYWGYEYPD-EEISFESYMIGSpatggdnrmspeveQQLIEAGYSrdefLLATD 170
Cdd:MTH00129  78 LPSLRILYLMDEINDPHLTIKAMGHQWYWSYEYTDyEDLGFDSYMIPT--------------QDLTPGQFR----LLEAD 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455  171 TAMVVPVNKTVVVQVTGADVIHSWTVPAFGVKQDAVPGRLAQLWFRAEREGIFFGQCSELCGISHAYMPITVKVVSEEAY 250
Cdd:MTH00129 140 HRMVVPVESPIRVLVSAEDVLHSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHF 219


                 ...
gi 23200455  251 AAW 253
Cdd:MTH00129 220 ENW 222
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 12-253 2.03e-51

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 167.75  E-value: 2.03e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455   12 QPGGTGFQPSASPVATQIHWLDGFILVIIAAITIFVTLLILYAVwrfhekRNKVPARFTHNS-PLEIAWTIVPIVILVAI 90
Cdd:MTH00185   3 HPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMV------TTKLTNKYILDSqEIEIVWTILPAIILIMI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455   91 GAFSLPVLFNQQEIPEADVTVKVTGYQWYWGYEYPD-EEISFESYMIgspatggdnrmspevEQQLIEAGYSRdefLLAT 169
Cdd:MTH00185  77 ALPSLRILYLMDEINDPHLTIKAMGHQWYWSYEYTDyEQLEFDSYMT---------------PTQDLTPGQFR---LLET 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455  170 DTAMVVPVNKTVVVQVTGADVIHSWTVPAFGVKQDAVPGRLAQLWFRAEREGIFFGQCSELCGISHAYMPITVKVVSEEA 249
Cdd:MTH00185 139 DHRMVVPMESPIRVLITAEDVLHSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEH 218


                 ....
gi 23200455  250 YAAW 253
Cdd:MTH00185 219 FENW 222
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
110-245 2.72e-50

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 161.04  E-value: 2.72e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455   110 TVKVTGYQWYWGYEYPD-EEISFESYMIGspatggdnrmspevEQQLIEAGYSrdefLLATDTAMVVPVNKTVVVQVTGA 188
Cdd:pfam00116   2 TIKAIGHQWYWSYEYTDfGDLEFDSYMIP--------------TEDLEEGQLR----LLEVDNRVVLPVETHIRVIVTAA 63

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 23200455   189 DVIHSWTVPAFGVKQDAVPGRLAQLWFRAEREGIFFGQCSELCGISHAYMPITVKVV 245
Cdd:pfam00116  64 DVIHSWAVPSLGIKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 22-255 2.72e-50

cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions. [Energy metabolism, Electron transport]


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 163.71  E-value: 2.72e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455    22 ASPVATQIHWLDGFILVIIAAITIFVTLLILYAVWRFHEK-RNKVPARFTHNSPLEIAWTIVPIVILVAIGAFSLPVLFN 100
Cdd:TIGR02866   2 GGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVWKFRRKgDEEKPSQIHGNRRLEYVWTVIPLIIVVGLFAATAKGLLY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455   101 QQE-IPEADVTVKVTGYQWYWGYEYPDEeisfesymigspATGGDNrmspeveqqlieagysrdEFLLATDTamvvpvnk 179
Cdd:TIGR02866  82 LERpIPKDALKVKVTGYQWWWDFEYPES------------GFTTVN------------------ELVLPAGT-------- 123

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23200455   180 TVVVQVTGADVIHSWTVPAFGVKQDAVPGRLAQLWFRAEREGIFFGQCSELCGISHAYMPITVKVVSEEAYAAWLE 255
Cdd:TIGR02866 124 PVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 18-254 7.76e-50

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 163.49  E-value: 7.76e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455   18 FQPSASPVATQ-IHWLDGFILVIIAAITIFVTLLILYAVwrfhekrNKVPARFTHNS-PLEIAWTIVPIVILVAIGAFSL 95
Cdd:MTH00008   9 FQDAASPVMLQlISFHDHALLILTLVLTVVGYAMTSLMF-------NKLSNRYILEAqQIETIWTILPALILLFLAFPSL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455   96 PVLFNQQEIPEADVTVKVTGYQWYWGYEYPD-EEISFESYMIGspatggDNRMSPEveqqlieagysrDEFLLATDTAMV 174
Cdd:MTH00008  82 RLLYLMDEVSNPSITLKTIGHQWYWSYEYSDfSNLEFDSYMLP------TSDLSPG------------QFRLLEVDNRAV 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455  175 VPVNKTVVVQVTGADVIHSWTVPAFGVKQDAVPGRLAQLWFRAEREGIFFGQCSELCGISHAYMPITVKVVSEEAYAAWL 254
Cdd:MTH00008 144 LPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWV 223
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 12-257 6.71e-49

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 161.10  E-value: 6.71e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455   12 QPGGTGFQPSASPVATQ-IHWLDGFILVIIaaitiFVTLLILYAVWRFHEKR----NKVPARfthnsPLEIAWTIVPIVI 86
Cdd:MTH00076   3 HPSQLGFQDAASPIMEElLHFHDHALMAVF-----LISTLVLYIITIMMTTKltntNTMDAQ-----EIEMVWTIMPAII 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455   87 LVAIGAFSLPVLFNQQEIPEADVTVKVTGYQWYWGYEYPD-EEISFESYMIGSpatggdNRMSPeveqqlieaGYSRdef 165
Cdd:MTH00076  73 LIVIALPSLRILYLMDEINDPHLTVKAIGHQWYWSYEYTDyEDLSFDSYMIPT------QDLTP---------GQFR--- 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455  166 LLATDTAMVVPVNKTVVVQVTGADVIHSWTVPAFGVKQDAVPGRLAQLWFRAEREGIFFGQCSELCGISHAYMPITVKVV 245
Cdd:MTH00076 135 LLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEAT 214

                        250
                 ....*....|..
gi 23200455  246 SEEAYAAWLEQA 257
Cdd:MTH00076 215 PLNNFLNWSSSM 226
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 11-253 7.10e-49

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 161.04  E-value: 7.10e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455   11 PQPGGTGFQPSASPVATQ-IHWLDG--FILVIIAAITIFVTLLILyavwrfhekrnkvPARFTHNSPL-----EIAWTIV 82
Cdd:MTH00098   2 AYPFQLGFQDATSPIMEElLHFHDHtlMIVFLISSLVLYIISLML-------------TTKLTHTSTMdaqevETIWTIL 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455   83 PIVILVAIGAFSLPVLFNQQEIPEADVTVKVTGYQWYWGYEYPD-EEISFESYMIGSpatggdnrmspeveqQLIEAGYS 161
Cdd:MTH00098  69 PAIILILIALPSLRILYMMDEINNPSLTVKTMGHQWYWSYEYTDyEDLSFDSYMIPT---------------SDLKPGEL 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455  162 RdefLLATDTAMVVPVNKTVVVQVTGADVIHSWTVPAFGVKQDAVPGRLAQLWFRAEREGIFFGQCSELCGISHAYMPIT 241
Cdd:MTH00098 134 R---LLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIV 210

                        250
                 ....*....|..
gi 23200455  242 VKVVSEEAYAAW 253
Cdd:MTH00098 211 LELVPLKYFEKW 222
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 12-254 1.00e-44

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 151.33  E-value: 1.00e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455   12 QPGGTGFQPSASPVATQIHWLDG---FILVIIAAITIFVTLLILYAVWRFHEKRNKVPARFthnspLEIAWTIVPIVILV 88
Cdd:MTH00027  31 EPWQLGFQDAGSPVMEEIIMLHDqilFILTIIVGVVLWLIIRILLGNNYYSYYWNKLDGSL-----IEVIWTLIPAFILI 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455   89 AIGAFSLPVLFNQQE-IPEADVTVKVTGYQWYWGYEYPD---EEISFESYMIGSPATG-GDNRMSpEVEQQLIeagysrd 163
Cdd:MTH00027 106 LIAFPSLRLLYIMDEcGFSANITIKVTGHQWYWSYSYEDygeKNIEFDSYMIPTADLEfGDLRLL-EVDNRLI------- 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455  164 eflLATDTAMVVPvnktvvvqVTGADVIHSWTVPAFGVKQDAVPGRLAQLWFRAEREGIFFGQCSELCGISHAYMPITVK 243
Cdd:MTH00027 178 ---LPVDTNVRVL--------ITAADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVE 246

                        250
                 ....*....|.
gi 23200455  244 VVSEEAYAAWL 254
Cdd:MTH00027 247 SVSLSKYIDWI 257
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 31-254 7.62e-43

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 145.54  E-value: 7.62e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455   31 WLDGF--ILVIIAAITIFVTLLILYAV---WRFHEKRnkvparfTHNSPLEIAWTIVPIVILVAIGAFSLPVLFNQQEIP 105
Cdd:MTH00080  21 WFHNFncSLLFGEFVLAFVVFLFLYLIsnnFYFKSKK-------IEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMN 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455  106 -EADVTVKVTGYQWYWGYEYPD-EEISFESYMigspatggdNRMSpeveqQLiEAGYSRdefLLATDTAMVVPVNKTVVV 183
Cdd:MTH00080  94 lDSNLTVKVTGHQWYWSYEFSDiPGLEFDSYM---------KSLD-----QL-RLGEPR---LLEVDNRCVLPCDTNIRF 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23200455  184 QVTGADVIHSWTVPAFGVKQDAVPGRLAQLWFRAEREGIFFGQCSELCGISHAYMPITVKVVSEEAYAAWL 254
Cdd:MTH00080 156 CITSSDVIHSWALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWC 226
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 35-245 3.01e-37

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 130.07  E-value: 3.01e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455   35 FILVIIAAITIFVTLLILYAVwrfhEKRNKVPARFTHNSPLEIAWTIVPIVILVAIGAFSLPVLFNQQEIpEADVTVKVT 114
Cdd:MTH00047  13 YILALCVFIPCWVYIMLCWQV----VSGNGSVNFGSENQVLELLWTVVPTLLVLVLCFLNLNFITSDLDC-FSSETIKVI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455  115 GYQWYWGYEYPDEeISFESYMIGspatggdnrmspeveqqlieagysrdeFLLATDTAMVVPVNKTVVVQVTGADVIHSW 194
Cdd:MTH00047  88 GHQWYWSYEYSFG-GSYDSFMTD---------------------------DIFGVDKPLRLVYGVPYHLLVTSSDVIHSF 139

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 23200455  195 TVPAFGVKQDAVPGRLAQLWFRAEREGIFFGQCSELCGISHAYMPITVKVV 245
Cdd:MTH00047 140 SVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVV 190
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 185-252 2.11e-29

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 108.75  E-value: 2.11e-29
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23200455  185 VTGADVIHSWTVPAFGVKQDAVPGRLAQLWFRAEREGIFFGQCSELCGISHAYMPITVKVVSEEAYAA 252
Cdd:PTZ00047  87 ITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCSEMCGTLHGFMPIVVEAVSPEAYAA 154
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 108-245 1.21e-25

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


Pssm-ID: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 97.33  E-value: 1.21e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455 108 DVTVKVTGYQWYWGYEYPDEEISFesymigspaTGGDNRMSPEVEqqlIEAGySRDEFLLATDtamvvpvnktvvvqvtg 187
Cdd:cd13919   1 ALVVEVTAQQWAWTFRYPGGDGKL---------GTDDDVTSPELH---LPVG-RPVLFNLRSK----------------- 50

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 23200455 188 aDVIHSWTVPAFGVKQDAVPGRLAQLWFRAEREGIFFGQCSELCGISHAYMPITVKVV 245
Cdd:cd13919  51 -DVIHSFWVPEFRVKQDAVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRMRATVKVV 107
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 11-97 4.84e-25

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: 95.09  E-value: 4.84e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455    11 PQPGGTGFQPSASPVATQIHWLDGFILVIIAAITIFVTLLILYAVWRFHEKRNKVPARFT-HNSPLEIAWTIVPIVILVA 89
Cdd:pfam02790   2 PTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRFNRRKNPITARYTtHGQTIEIIWTIIPAVILIL 81


                  ....*...
gi 23200455    90 IGAFSLPV 97
Cdd:pfam02790  82 IALPSFKL 89
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 108-245 5.05e-23

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: 89.99  E-value: 5.05e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455 108 DVTVKVTGYQWYWGYEYPDEEisfesymiGSPATGGdnrmspeveQQL-IEAGysRDEFLlatdtamvvpvnktvvvQVT 186
Cdd:cd04213   1 ALTIEVTGHQWWWEFRYPDEP--------GRGIVTA---------NELhIPVG--RPVRL-----------------RLT 44

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 23200455 187 GADVIHSWTVPAFGVKQDAVPGRLAQLWFRAEREGIFFGQCSELCGISHAYMPITVKVV 245
Cdd:cd04213  45 SADVIHSFWVPSLAGKMDMIPGRTNRLWLQADEPGVYRGQCAEFCGASHALMRFKVIAL 103
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 110-244 5.76e-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: 87.30  E-value: 5.76e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455 110 TVKVTGYQWYWGYEYPdeeisfesymigspatgGDNRMSPEVEqqlIEAGysRDEFLLatdtamvvpvnktvvvqVTGAD 189
Cdd:cd13915   3 EIQVTGRQWMWEFTYP-----------------NGKREINELH---VPVG--KPVRLI-----------------LTSKD 43

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 23200455 190 VIHSWTVPAFGVKQDAVPGRLAQLWFRAEREGIFFGQCSELCGISHAYMPITVKV 244
Cdd:cd13915  44 VIHSFYVPAFRIKQDVVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGMIGKVRV 98
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 109-254 2.72e-21

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: 85.92  E-value: 2.72e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455 109 VTVKVTGYQWYWGYEYPDEEISfesymigspatggdnrmspeveqqlieagySRDEFLLATDTAMVVpvnktvvvQVTGA 188
Cdd:cd13914   1 VEIEVEAYQWGWEFSYPEANVT------------------------------TSEQLVIPADRPVYF--------RITSR 42

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23200455 189 DVIHSWTVPAFGVKQDAVPGRLAQLWFRAEREGIFFGQCSELCGISHAYMPITVKVVSEEAYAAWL 254
Cdd:cd13914  43 DVIHAFHVPELGLKQDAFPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 106-254 3.07e-21

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: 86.74  E-value: 3.07e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455 106 EADVTVKVTGYQWYWGYEYPDEeisfesymigspatggdnrmspeveqqlieaGYSRDEFLLATDTAMVVpvnktvvvQV 185
Cdd:cd13918  30 EDALEVEVEGFQFGWQFEYPNG-------------------------------VTTGNTLRVPADTPIAL--------RV 70

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23200455 186 TGADVIHSWTVPAFGVKQDAVPGRLAQLWFRAEREGIFFGQCSELCGISHAYMPITVKVVSEEAYAAWL 254
Cdd:cd13918  71 TSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAWY 139
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 109-243 3.60e-21

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


Pssm-ID: 259911 [Multi-domain]  Cd Length: 95  Bit Score: 85.04  E-value: 3.60e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455 109 VTVKVTGYQWYWGYEYPDEEisfesymigspatggdnrmspeveqqlieagySRDEFLLATDTAMVVPvnktvvvqVTGA 188
Cdd:cd13842   1 LTVYVTGVQWSWTFIYPNVR--------------------------------TPNEIVVPAGTPVRFR--------VTSP 40

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 23200455 189 DVIHSWTVPAFGVKQDAVPGRLAQLWFRAEREGIFFGQCSELCGISHAYMPITVK 243
Cdd:cd13842  41 DVIHGFYIPNLGVKVDAVPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CyoA TIGR01433
cytochrome o ubiquinol oxidase subunit II; This enzyme catalyzes the oxidation of ubiquinol ...
 25-258 5.51e-07

cytochrome o ubiquinol oxidase subunit II; This enzyme catalyzes the oxidation of ubiquinol with the concomitant reduction of molecular oxygen to water. This acts as the terminal electron acceptor in the respiratory chain. Subunit II is responsible for binding and oxidation of the ubiquinone substrate. This sequence is closely related to QoxA, which oxidizes quinol in gram positive bacteria but which is in complex with subunits which utilize cytochromes a in the reduction of molecular oxygen. Slightly more distantly related is subunit II of cytochrome c oxidase which uses cyt. c as the oxidant. [Energy metabolism, Electron transport]


Pssm-ID: 213620 [Multi-domain]  Cd Length: 226  Bit Score: 49.05  E-value: 5.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455    25 VATQIHWLDGFILVIIAAITIFVTLLILYAVWRFHE--KRNKVPARFTHNSPLEIA-WTIvPIVILVAIGAFSLPVL--- 98
Cdd:TIGR01433  24 IGLEERSLILTAFGLMLLVVIPVILMTLFFAWKYRAtnKDADYSPNWHHSTKIEIVvWTI-PILIIIFLGVLTWITThkl 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455    99 --FNQQEIPEADVTVKVTGYQWYWGYEYPDEEISfesymigspatggdnrmspeveqqlieagySRDEFLLATDTAMvvp 176
Cdd:TIGR01433 103 dpYRPLASDVKPITIEVVALDWKWLFIYPEQGIA------------------------------TVNEIAFPVNTPI--- 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455   177 vnktvVVQVTGADVIHSWTVPAFGVKQDAVPGRLAQLWFRAEREGIFFGQCSELCGISHAYMPITVKVVSEEAYAAWLEQ 256
Cdd:TIGR01433 150 -----NFKITSNSVMNSFFIPQLGSQIYAMAGMQTKLHLIANEPGVYDGISANYSGPGFSGMKFKAIATDRAAFDQWVAK 224


                  ..
gi 23200455   257 AR 258
Cdd:TIGR01433 225 AK 226
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 184-245 1.44e-06

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: 45.64  E-value: 1.44e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23200455 184 QVTGADVIHSWTVPAFGVKQDAVPGRLAQLWFRAEREGIFFGQCSELCGISHAYMPITVKVV 245
Cdd:cd13913  38 YVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNMYGKIIVE 99
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 109-245 1.40e-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: 259983 [Multi-domain]  Cd Length: 93  Bit Score: 40.06  E-value: 1.40e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23200455 109 VTVKVTGYQWYWgyeypdeEISFESYMIGSPAtggdnrmspeveqqlieagysrdEFllatdtamvvpvnktvvvQVTGA 188
Cdd:cd13916   1 QVVAVTGHQWYW-------ELSRTEIPAGKPV-----------------------EF------------------RVTSA 32

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23200455 189 DVIHswtvpAFGVKQD---------AVPGRLAQLWFRAEREGIFFGQCSELCGISHAYMPITVKVV 245
Cdd:cd13916  33 DVNH-----GFGIYDPdmrllaqtqAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVMMAEFTVV 93
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 184-245 8.48e-04

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


Pssm-ID: 259874 [Multi-domain]  Cd Length: 99  Bit Score: 37.91  E-value: 8.48e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23200455 184 QVTGADVIHSWTVPAFGVKQDAVPGRLAQLWFRAEREGIFFGQCSELCGISHAYMPITVKVV 245
Cdd:cd04212  38 RLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDMKFKVLAV 99
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 187-243 5.91e-03

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: 35.67  E-value: 5.91e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23200455 187 GADVIHSWTVPAFGVKQDA---------------VPGRLAQLWFRAEREGIFFGQCSELCGIsHAYMPITVK 243
Cdd:cd00920  40 KLGENHSVTIAGFGVPVVAmagganpglvntlviGPGESAEVTFTTDQAGVYWFYCTIPGHN-HAGMVGTIN 110
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH