NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|27543030|gb|AAO16257|]
View 

cytochrome oxidase subunit II (mitochondrion) [Caenorhabditis elegans]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 3-231 1.75e-134

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 377.43  E-value: 1.75e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27543030    3 NFFQGYNLLFQHSLFASYMDWFHSFNCSLLLG--VLVFVTLLFGYLIFGTFYFKSKKIEYQFGELLCSIFPTIILLMQMV 80
Cdd:MTH00080   1 NYFQGYNLNFSNSLFSSYMDWFHNFNCSLLFGefVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27543030   81 PSLSLLYYYGLMNLDSNLTVKVTGHQWYWSYEYSDIPGLEFDSYMKSLD*LSLGEPRLLEVDNRCVIPCDTNIRFCITSA 160
Cdd:MTH00080  81 PSLSLLYYYGLMNLDSNLTVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSS 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27543030  161 DVIHAWALNSLSVKLDAMSGILSTFNYSFPMVGVFYGQCSEICGANHSFMPIALEVTLLDNFKSWCFGTME 231
Cdd:MTH00080 161 DVIHSWALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWCKLLLD 231
 
Name Accession Description Interval E-value
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 3-231 1.75e-134

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 377.43  E-value: 1.75e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27543030    3 NFFQGYNLLFQHSLFASYMDWFHSFNCSLLLG--VLVFVTLLFGYLIFGTFYFKSKKIEYQFGELLCSIFPTIILLMQMV 80
Cdd:MTH00080   1 NYFQGYNLNFSNSLFSSYMDWFHNFNCSLLFGefVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27543030   81 PSLSLLYYYGLMNLDSNLTVKVTGHQWYWSYEYSDIPGLEFDSYMKSLD*LSLGEPRLLEVDNRCVIPCDTNIRFCITSA 160
Cdd:MTH00080  81 PSLSLLYYYGLMNLDSNLTVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSS 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27543030  161 DVIHAWALNSLSVKLDAMSGILSTFNYSFPMVGVFYGQCSEICGANHSFMPIALEVTLLDNFKSWCFGTME 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 7.17e-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: 237.85  E-value: 7.17e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27543030  96 SNLTVKVTGHQWYWSYEYSDIPGLEFDSYMKSLD*LSLGEPRLLEVDNRCVIPCDTNIRFCITSADVIHAWALNSLSVKL 175
Cdd:cd13912   1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 27543030 176 DAMSGILSTFNYSFPMVGVFYGQCSEICGANHSFMPIALEVTLLDNFKSW 225
Cdd:cd13912  81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
98-215 2.16e-58

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 180.30  E-value: 2.16e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27543030    98 LTVKVTGHQWYWSYEYSDIPGLEFDSYMKSLD*LSLGEPRLLEVDNRCVIPCDTNIRFCITSADVIHAWALNSLSVKLDA 177
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 27543030   178 MSGILSTFNYSFPMVGVFYGQCSEICGANHSFMPIALE 215
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIE 118
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
7-225 3.83e-39

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 134.96  E-value: 3.83e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27543030   7 GYNLLFQHSLFASYMDWFHSFncSLLLGVLVFVtLLFGYLIFGTFYFKSKKIEY---QFG-----ELLCSIFPTIILLMQ 78
Cdd:COG1622  18 QLSLPDPAGPIAEEIDDLFWV--SLIIMLVIFV-LVFGLLLYFAIRYRRRKGDAdpaQFHhntklEIVWTVIPIIIVIVL 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27543030  79 MVPSLSLLYYYGLMNlDSNLTVKVTGHQWYWSYEYSDIPGLefdsymksld*lslgeprlleVDNRCVIPCDTNIRFCIT 158
Cdd:COG1622  95 AVPTLRVLHALDDAP-EDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVNELVLPVGRPVRFLLT 152

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27543030 159 SADVIHAWALNSLSVKLDAMSGILSTFNYSFPMVGVFYGQCSEICGANHSFMPIALEVTLLDNFKSW 225
Cdd:COG1622 153 SADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAW 219
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 24-225 9.14e-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: 9.14e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27543030    24 FHSFNCSLLLGVLVFVtLLFGYLIFGTFYFKSK----KIEYQFG----ELLCSIFPTIILLMQMVPSLSLLYYYgLMNLD 95
Cdd:TIGR02866  10 AFLFLFVLAVSTLISL-LVAALLAYVVWKFRRKgdeeKPSQIHGnrrlEYVWTVIPLIIVVGLFAATAKGLLYL-ERPIP 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27543030    96 SN-LTVKVTGHQWYWSYEYSDIpglefdsymksld*lslgeprLLEVDNRCVIPCDTNIRFCITSADVIHAWALNSLSVK 174
Cdd:TIGR02866  88 KDaLKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGK 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 27543030   175 LDAMSGILS--TFNYSFPmvGVFYGQCSEICGANHSFMPIALEVTLLDNFKSW 225
Cdd:TIGR02866 147 IDAIPGQTNalWFNADEP--GVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAY 197
 
Name Accession Description Interval E-value
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 3-231 1.75e-134

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 377.43  E-value: 1.75e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27543030    3 NFFQGYNLLFQHSLFASYMDWFHSFNCSLLLG--VLVFVTLLFGYLIFGTFYFKSKKIEYQFGELLCSIFPTIILLMQMV 80
Cdd:MTH00080   1 NYFQGYNLNFSNSLFSSYMDWFHNFNCSLLFGefVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27543030   81 PSLSLLYYYGLMNLDSNLTVKVTGHQWYWSYEYSDIPGLEFDSYMKSLD*LSLGEPRLLEVDNRCVIPCDTNIRFCITSA 160
Cdd:MTH00080  81 PSLSLLYYYGLMNLDSNLTVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSS 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27543030  161 DVIHAWALNSLSVKLDAMSGILSTFNYSFPMVGVFYGQCSEICGANHSFMPIALEVTLLDNFKSWCFGTME 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 7.17e-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: 237.85  E-value: 7.17e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27543030  96 SNLTVKVTGHQWYWSYEYSDIPGLEFDSYMKSLD*LSLGEPRLLEVDNRCVIPCDTNIRFCITSADVIHAWALNSLSVKL 175
Cdd:cd13912   1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 27543030 176 DAMSGILSTFNYSFPMVGVFYGQCSEICGANHSFMPIALEVTLLDNFKSW 225
Cdd:cd13912  81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 15-229 8.35e-76

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 228.67  E-value: 8.35e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27543030   15 SLFASYMDWFHSFNCSLLLGVLVFVTLLFGYLIFGTFYFKSKKiEYQFGELLCSIFPTIILLMQMVPSLSLLYYYGLMNl 94
Cdd:MTH00140  14 SPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTIL-EAQKLETIWTIVPALILVFLALPSLRLLYLLDETN- 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27543030   95 DSNLTVKVTGHQWYWSYEYSDIPGLEFDSYMKSLD*LSLGEPRLLEVDNRCVIPCDTNIRFCITSADVIHAWALNSLSVK 174
Cdd:MTH00140  92 NPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVPSLGVK 171

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 27543030  175 LDAMSGILSTFNYSFPMVGVFYGQCSEICGANHSFMPIALEVTLLDNFKSWCFGT 229
Cdd:MTH00140 172 VDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELM 226
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 9-225 8.53e-76

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 228.56  E-value: 8.53e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27543030    9 NLLFQHSlfASY----MDWFHSFNCSLLLGVLVFVTLLFGYLIFGTFYFKSKkIEYQFGELLCSIFPTIILLMQMVPSLS 84
Cdd:MTH00154   6 NLSFQDS--ASPlmeqLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFL-LEGQEIEIIWTILPAIILIFIALPSLR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27543030   85 LLYYYGLMNlDSNLTVKVTGHQWYWSYEYSDIPGLEFDSYMKSLD*LSLGEPRLLEVDNRCVIPCDTNIRFCITSADVIH 164
Cdd:MTH00154  83 LLYLLDEVN-NPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIH 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27543030  165 AWALNSLSVKLDAMSGILSTFNYSFPMVGVFYGQCSEICGANHSFMPIALEVTLLDNFKSW 225
Cdd:MTH00154 162 SWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINW 222
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 4-227 1.45e-74

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 225.24  E-value: 1.45e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27543030    4 FFQGYNLLFQHSLFASYMDWFHSFNCSLLLGVLVFVTLLFGYLIFGTFYFKSKKiEYQFGELLCSIFPTIILLMQMVPSL 83
Cdd:MTH00168   3 TYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLL-DSQMIEFVWTIIPAFILISLALPSL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27543030   84 SLLYYyglM--NLDSNLTVKVTGHQWYWSYEYSDIPGLEFDSYMKSLD*LSLGEPRLLEVDNRCVIPCDTNIRFCITSAD 161
Cdd:MTH00168  82 RLLYL---MdeIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSAD 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27543030  162 VIHAWALNSLSVKLDAMSGILSTFNYSFPMVGVFYGQCSEICGANHSFMPIALEVTLLDNFKSWCF 227
Cdd:MTH00168 159 VLHSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVD 224
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 23-231 2.89e-71

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 216.88  E-value: 2.89e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27543030   23 WFHSFncslLLGVLVFVTLLFGY----LIFGTFYFKsKKIEYQFGELLCSIFPTIILLMQMVPSLSLLYYYGLMNlDSNL 98
Cdd:MTH00038  22 YFHDY----ALIILTLITILVFYglasLLFSSPTNR-FFLEGQELETIWTIVPAFILIFIALPSLQLLYLMDEVN-NPFL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27543030   99 TVKVTGHQWYWSYEYSDIPGLEFDSYMKSLD*LSLGEPRLLEVDNRCVIPCDTNIRFCITSADVIHAWALNSLSVKLDAM 178
Cdd:MTH00038  96 TIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLHSWAVPSLGVKMDAV 175

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 27543030  179 SGILSTFNYSFPMVGVFYGQCSEICGANHSFMPIALEVTLLDNFKSWCFGTME 231
Cdd:MTH00038 176 PGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFLE 228
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 24-226 2.04e-70

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 214.97  E-value: 2.04e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27543030   24 FHSFNCSLLLGVLVFVTLLFGYLIFGTFYFKSKkIEYQFGELLCSIFPTIILLMQMVPSLSLLYyygLMN--LDSNLTVK 101
Cdd:MTH00139  23 FHDHAMVILIMILSFVGYISLSLMSNKFTSRSL-LESQEVETIWTVLPAFILLFLALPSLRLLY---LMDevSDPYLTFK 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27543030  102 VTGHQWYWSYEYSDIPGLEFDSYMKSLD*LSLGEPRLLEVDNRCVIPCDTNIRFCITSADVIHAWALNSLSVKLDAMSGI 181
Cdd:MTH00139  99 AVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSWTVPSLGVKIDAVPGR 178

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 27543030  182 LSTFNYSFPMVGVFYGQCSEICGANHSFMPIALEVTLLDNFKSWC 226
Cdd:MTH00139 179 LNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWI 223
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 25-225 1.26e-67

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 207.84  E-value: 1.26e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27543030   25 HSFNCSLLLGVLVFVTLLfgyLIFGTFYFKSKKIEYQFGELLCSIFPTIILLMQMVPSLSLLYyygLMN--LDSNLTVKV 102
Cdd:MTH00117  26 HALMVALLISSLVLYLLT---LMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPSLRILY---LMDeiNNPHLTIKA 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27543030  103 TGHQWYWSYEYSDIPGLEFDSYMKSLD*LSLGEPRLLEVDNRCVIPCDTNIRFCITSADVIHAWALNSLSVKLDAMSGIL 182
Cdd:MTH00117 100 IGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVPSLGVKTDAVPGRL 179

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 27543030  183 STFNYSFPMVGVFYGQCSEICGANHSFMPIALEVTLLDNFKSW 225
Cdd:MTH00117 180 NQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENW 222
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 10-225 1.07e-62

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 195.07  E-value: 1.07e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27543030   10 LLFQHSLfASYMDWFHSFNCSLLLgVLVFVTLLFGYLIFGTFYFKSKK---IEYQFGELLCSIFPTIILLMQMVPSLSLL 86
Cdd:MTH00008   7 LMFQDAA-SPVMLQLISFHDHALL-ILTLVLTVVGYAMTSLMFNKLSNryiLEAQQIETIWTILPALILLFLAFPSLRLL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27543030   87 YyygLMNLDSN--LTVKVTGHQWYWSYEYSDIPGLEFDSYMKSLD*LSLGEPRLLEVDNRCVIPCDTNIRFCITSADVIH 164
Cdd:MTH00008  85 Y---LMDEVSNpsITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIH 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27543030  165 AWALNSLSVKLDAMSGILSTFNYSFPMVGVFYGQCSEICGANHSFMPIALEVTLLDNFKSW 225
Cdd:MTH00008 162 SWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKW 222
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 64-225 1.72e-61

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 192.24  E-value: 1.72e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27543030   64 ELLCSIFPTIILLMQMVPSLSLLYYYGLMNlDSNLTVKVTGHQWYWSYEYSDIPGLEFDSYMKSLD*LSLGEPRLLEVDN 143
Cdd:MTH00098  62 ETIWTILPAIILILIALPSLRILYMMDEIN-NPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDN 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27543030  144 RCVIPCDTNIRFCITSADVIHAWALNSLSVKLDAMSGILSTFNYSFPMVGVFYGQCSEICGANHSFMPIALEVTLLDNFK 223
Cdd:MTH00098 141 RVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFE 220


                 ..
gi 27543030  224 SW 225
Cdd:MTH00098 221 KW 222
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 58-225 2.51e-61

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 191.53  E-value: 2.51e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27543030   58 IEYQFGELLCSIFPTIILLMQMVPSLSLLYYYGLMNlDSNLTVKVTGHQWYWSYEYSDIPGLEFDSYMKSLD*LSLGEPR 137
Cdd:MTH00076  56 MDAQEIEMVWTIMPAIILIVIALPSLRILYLMDEIN-DPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFR 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27543030  138 LLEVDNRCVIPCDTNIRFCITSADVIHAWALNSLSVKLDAMSGILSTFNYSFPMVGVFYGQCSEICGANHSFMPIALEVT 217
Cdd:MTH00076 135 LLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEAT 214


                 ....*...
gi 27543030  218 LLDNFKSW 225
Cdd:MTH00076 215 PLNNFLNW 222
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 25-225 3.56e-61

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 191.25  E-value: 3.56e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27543030   25 HSFNCSLLLGVLVFvtllfgYLIFG--TFYFKSKKI-EYQFGELLCSIFPTIILLMQMVPSLSLLYYYGLMNlDSNLTVK 101
Cdd:MTH00185  26 HTLMIVFLISTLVL------YIIVAmvTTKLTNKYIlDSQEIEIVWTILPAIILIMIALPSLRILYLMDEIN-DPHLTIK 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27543030  102 VTGHQWYWSYEYSDIPGLEFDSYMKSLD*LSLGEPRLLEVDNRCVIPCDTNIRFCITSADVIHAWALNSLSVKLDAMSGI 181
Cdd:MTH00185  99 AMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVPALGVKMDAVPGR 178

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 27543030  182 LSTFNYSFPMVGVFYGQCSEICGANHSFMPIALEVTLLDNFKSW 225
Cdd:MTH00185 179 LNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 23-225 2.11e-60

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 189.58  E-value: 2.11e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27543030   23 WFHSFNCSLLLGVLVFVTLLFGYLIFGTFYFKSKkIEYQFGELLCSIFPTIILLMQMVPSLSLLYyygLM--NLDSNLTV 100
Cdd:MTH00023  31 FFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFL-VDGTFLEIVWTIIPAVILVFIALPSLKLLY---LMdeVVSPALTI 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27543030  101 KVTGHQWYWSYEYSDIPG--LEFDSYMKSLD*LSLGEPRLLEVDNRCVIPCDTNIRFCITSADVIHAWALNSLSVKLDAM 178
Cdd:MTH00023 107 KAIGHQWYWSYEYSDYEGetLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVPSLGLKIDAV 186

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 27543030  179 SGILSTFNYSFPMVGVFYGQCSEICGANHSFMPIALEVTLLDNFKSW 225
Cdd:MTH00023 187 PGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINW 233
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 64-226 5.15e-60

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 188.38  E-value: 5.15e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27543030   64 ELLCSIFPTIILLMQMVPSLSLLYYYGLMNlDSNLTVKVTGHQWYWSYEYSDIPGLEFDSYMKSLD*LSLGEPRLLEVDN 143
Cdd:MTH00129  62 EIIWTVLPAVILILIALPSLRILYLMDEIN-DPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADH 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27543030  144 RCVIPCDTNIRFCITSADVIHAWALNSLSVKLDAMSGIL--STFNYSFPmvGVFYGQCSEICGANHSFMPIALEVTLLDN 221
Cdd:MTH00129 141 RMVVPVESPIRVLVSAEDVLHSWAVPALGVKMDAVPGRLnqTAFIASRP--GVFYGQCSEICGANHSFMPIVVEAVPLEH 218


                 ....*
gi 27543030  222 FKSWC 226
Cdd:MTH00129 219 FENWS 223
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
98-215 2.16e-58

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 180.30  E-value: 2.16e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27543030    98 LTVKVTGHQWYWSYEYSDIPGLEFDSYMKSLD*LSLGEPRLLEVDNRCVIPCDTNIRFCITSADVIHAWALNSLSVKLDA 177
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 27543030   178 MSGILSTFNYSFPMVGVFYGQCSEICGANHSFMPIALE 215
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIE 118
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 24-225 3.03e-58

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 184.21  E-value: 3.03e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27543030   24 FHSFNCSLLLGVLVFVTLLFGYLIFGTFYFKSKkIEYQFGELLCSIFPTIILLMQMVPSLSLLYyygLMN--LDSNLTVK 101
Cdd:MTH00051  25 FHDQIMFILTIIITTVLWLIIRALTTKYYHKYL-FEGTLIEIIWTLIPAAILIFIAFPSLKLLY---LMDevIDPALTIK 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27543030  102 VTGHQWYWSYEYSDIPG--LEFDSYMKSLD*LSLGEPRLLEVDNRCVIPCDTNIRFCITSADVIHAWALNSLSVKLDAMS 179
Cdd:MTH00051 101 AIGHQWYWSYEYSDYGTdtIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPSLSVKIDAVP 180

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 27543030  180 GILSTFNYSFPMVGVFYGQCSEICGANHSFMPIALEVTLLDNFKSW 225
Cdd:MTH00051 181 GRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINW 226
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 27-225 1.21e-53

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 173.29  E-value: 1.21e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27543030   27 FNCSLLLGVLVFVTLlfgYLIFGTFYFKS--KKIEYQFGELLCSIFPTIILLMQMVPSLSLLYYYGLMNLDSNLTVKVTG 104
Cdd:MTH00027  57 FILTIIVGVVLWLII---RILLGNNYYSYywNKLDGSLIEVIWTLIPAFILILIAFPSLRLLYIMDECGFSANITIKVTG 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27543030  105 HQWYWSYEYSDI--PGLEFDSYMKSLD*LSLGEPRLLEVDNRCVIPCDTNIRFCITSADVIHAWALNSLSVKLDAMSGIL 182
Cdd:MTH00027 134 HQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVLHSWTVPSLAVKMDAVPGRI 213

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 27543030  183 STFNYSFPMVGVFYGQCSEICGANHSFMPIALEVTLLDNFKSW 225
Cdd:MTH00027 214 NETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDW 256
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
7-225 3.83e-39

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 134.96  E-value: 3.83e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27543030   7 GYNLLFQHSLFASYMDWFHSFncSLLLGVLVFVtLLFGYLIFGTFYFKSKKIEY---QFG-----ELLCSIFPTIILLMQ 78
Cdd:COG1622  18 QLSLPDPAGPIAEEIDDLFWV--SLIIMLVIFV-LVFGLLLYFAIRYRRRKGDAdpaQFHhntklEIVWTVIPIIIVIVL 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27543030  79 MVPSLSLLYYYGLMNlDSNLTVKVTGHQWYWSYEYSDIPGLefdsymksld*lslgeprlleVDNRCVIPCDTNIRFCIT 158
Cdd:COG1622  95 AVPTLRVLHALDDAP-EDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVNELVLPVGRPVRFLLT 152

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27543030 159 SADVIHAWALNSLSVKLDAMSGILSTFNYSFPMVGVFYGQCSEICGANHSFMPIALEVTLLDNFKSW 225
Cdd:COG1622 153 SADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAW 219
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 35-221 5.68e-33

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 117.75  E-value: 5.68e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27543030   35 VLVFVTLLFGYLIFGTFYFKSKKIEYQFGELLCSIFPTIILLMQMVPSLSLLYYYglMNLDSNLTVKVTGHQWYWSYEYS 114
Cdd:MTH00047  21 IPCWVYIMLCWQVVSGNGSVNFGSENQVLELLWTVVPTLLVLVLCFLNLNFITSD--LDCFSSETIKVIGHQWYWSYEYS 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27543030  115 DipGLEFDSYMKSLD*LslgeprlleVDNRCVIPCDTNIRFCITSADVIHAWALNSLSVKLDAMSGILSTFNYSFPMVGV 194
Cdd:MTH00047  99 F--GGSYDSFMTDDIFG---------VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGV 167

                        170       180
                 ....*....|....*....|....*..
gi 27543030  195 FYGQCSEICGANHSFMPIALEVTLLDN 221
Cdd:MTH00047 168 FVGYCSELCGVGHSYMPIVIEVVDVDS 194
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 24-225 9.14e-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: 9.14e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27543030    24 FHSFNCSLLLGVLVFVtLLFGYLIFGTFYFKSK----KIEYQFG----ELLCSIFPTIILLMQMVPSLSLLYYYgLMNLD 95
Cdd:TIGR02866  10 AFLFLFVLAVSTLISL-LVAALLAYVVWKFRRKgdeeKPSQIHGnrrlEYVWTVIPLIIVVGLFAATAKGLLYL-ERPIP 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27543030    96 SN-LTVKVTGHQWYWSYEYSDIpglefdsymksld*lslgeprLLEVDNRCVIPCDTNIRFCITSADVIHAWALNSLSVK 174
Cdd:TIGR02866  88 KDaLKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGK 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 27543030   175 LDAMSGILS--TFNYSFPmvGVFYGQCSEICGANHSFMPIALEVTLLDNFKSW 225
Cdd:TIGR02866 147 IDAIPGQTNalWFNADEP--GVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAY 197
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 121-215 5.54e-29

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 106.83  E-value: 5.54e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27543030  121 FDSYMKSLD*LSLGEPRLLEVDNRCVIPCDTNIRFCITSADVIHAWALNSLSVKLDAMSGILSTFNYSFPMVGVFYGQCS 200
Cdd:PTZ00047  51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                         90
                 ....*....|....*
gi 27543030  201 EICGANHSFMPIALE 215
Cdd:PTZ00047 131 EMCGTLHGFMPIVVE 145
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 98-215 6.55e-24

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: 91.20  E-value: 6.55e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27543030  98 LTVKVTGHQWYWSYEYSDIpglefdsymksld*lslgeprllEVDNRCVIPCDTNIRFCITSADVIHAWALNSLSVKLDA 177
Cdd:cd13842   1 LTVYVTGVQWSWTFIYPNV-----------------------RTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 27543030 178 MSGILSTFNYSFPMVGVFYGQCSEICGANHSFMPIALE 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), ...
 98-210 1.55e-21

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: 85.36  E-value: 1.55e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27543030  98 LTVKVTGHQWYWSYEYSDIPGLEFdsymksld*lslgeprllEVDNRCVIPCDTNIRFCITSADVIHAWALNSLSVKLDA 177
Cdd:cd04213   2 LTIEVTGHQWWWEFRYPDEPGRGI------------------VTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDM 63

                        90       100       110
                ....*....|....*....|....*....|...
gi 27543030 178 MSGILSTFNYSFPMVGVFYGQCSEICGANHSFM 210
Cdd:cd04213  64 IPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 98-225 3.64e-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: 77.88  E-value: 3.64e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27543030  98 LTVKVTGHQWYWSYEYSDipGLEFDSYMksld*lslgeprllevdnrcVIPCDTNIRFCITSADVIHAWALNSLSVKLDA 177
Cdd:cd13918  33 LEVEVEGFQFGWQFEYPN--GVTTGNTL--------------------RVPADTPIALRVTSTDVFHTFGIPELRVKADA 90

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 27543030 178 MSGILSTFNYSFPMVGVFYGQCSEICGANHSFMPIALEVTLLDNFKSW 225
Cdd:cd13918  91 IPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAW 138
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 99-225 7.81e-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: 68.20  E-value: 7.81e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27543030  99 TVKVTGHQWYWSYEYsdiPGLEFDSymksld*lslgeprllevDNRCVIPCDTNIRFCITSADVIHAWALNSLSVKLDAM 178
Cdd:cd13914   2 EIEVEAYQWGWEFSY---PEANVTT------------------SEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAF 60

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 27543030 179 SGILSTFNYSFPMVGVFYGQCSEICGANHSFMPIALEVTLLDNFKSW 225
Cdd:cd13914  61 PGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQW 107
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 98-210 3.31e-14

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: 66.12  E-value: 3.31e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27543030  98 LTVKVTGHQWYWSYEYsdiPGleFDSYMKSLD*LSLGEprllevdnrCVIPCDTNIRFCITSADVIHAWALNSLSVKLDA 177
Cdd:cd13919   2 LVVEVTAQQWAWTFRY---PG--GDGKLGTDDDVTSPE---------LHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                        90       100       110
                ....*....|....*....|....*....|...
gi 27543030 178 MSGILSTFNYSFPMVGVFYGQCSEICGANHSFM 210
Cdd:cd13919  68 VPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 98-216 1.28e-13

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: 64.57  E-value: 1.28e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27543030  98 LTVKVTGHQWYWSYEYsdipglefdsymksld*lslgePRLLEVDNRCVIPCDTNIRFCITSADVIHAWALNSLSVKLDA 177
Cdd:cd13915   2 LEIQVTGRQWMWEFTY----------------------PNGKREINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDV 59

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 27543030 178 MSGILSTFNYSFPMVGVFYGQCSEICGANHSFMPIALEV 216
Cdd:cd13915  60 VPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGMIGKVRV 98
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 143-217 1.27e-09

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: 53.73  E-value: 1.27e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27543030 143 NRCVIPCDTNIRFCITSADVIHAWALNSLSVKLDAMSGILSTFNYSFPMVGVFYGQCSEICGANHSFMPIALEVT 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 8.12e-09

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: 51.23  E-value: 8.12e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27543030  99 TVKVTGHQWYWSYEYSDIPglefdsymksld*lsLGEPrllevdnrcvipcdtnIRFCITSADVIHAWALNSLSVKL--- 175
Cdd:cd13916   2 VVAVTGHQWYWELSRTEIP---------------AGKP----------------VEFRVTSADVNHGFGIYDPDMRLlaq 50

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 27543030 176 -DAMSGILSTFNYSFPMVGVFYGQCSEICGANHSFMPIALEVT 217
Cdd:cd13916  51 tQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVMMAEFTVV 93
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 8-85 2.38e-03

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: 36.16  E-value: 2.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27543030     8 YNLLFQHSLFASY--MDWFHSFNCSLLLGVLVFVTLLFGYLIFgTFYFKSKKIEYQFG------ELLCSIFPTIILLMQM 79
Cdd:pfam02790   5 WGLGFQDAASPLMegLLELHDYIMFILTLILILVLYILVTCLI-RFNRRKNPITARYTthgqtiEIIWTIIPAVILILIA 83


                  ....*.
gi 27543030    80 VPSLSL 85
Cdd:pfam02790  84 LPSFKL 89
 
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