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Conserved domains on  [gi|2431513845|ref|YP_010614742|]
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Cox3 (mitochondrion) [Theileria luwenshuni]

Protein Classification

cytochrome c oxidase subunit 3( domain architecture ID 10086888)

cytochrome c oxidase subunit 3 is a component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 38-211 4.26e-20

Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). 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. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. This group additionally contains proteins which are fusions between subunits I and III, such as Sulfolobus acidocaldarius SoxM, a subunit of the SoxM terminal oxidase complex. It also includes NorE which has been speculated to be a subunit of nitric oxide reductase. Some archaebacterial cytochrome oxidases lack subunit III. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria.


:

Pssm-ID: 238227  Cd Length: 183  Bit Score: 83.41  E-value: 4.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431513845  38 TSSTAIMYSIFGMFIFSEIMVFSTFIWGYLHLRLSNP----MLLAELNVEAYLQISDVLNIGSVLVSIILHRIQEGASFE 113
Cdd:cd00386     3 ASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPvefgAGLDPLDLPLLNTNTLLLSGSSVTWAHASLAARRGNRKK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431513845 114 VDFFMEQLLLVGVIFLSLQNDEYSLLLSYVNNYWMTLYFFILTGLHSLHVCMGGVF---VLIQSYLYDDDGSLRDEDFNA 190
Cdd:cd00386    83 ARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFllvVLIRLRRGHFTPRHHLGLEAA 162

                         170       180
                  ....*....|....*....|.
gi 2431513845 191 GVYWHFVEMIWIALTLLLFLV 211
Cdd:cd00386   163 ALYWHFVDVVWLFLFPLVYLW 183
 
Name Accession Description Interval E-value
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 38-211 4.26e-20

Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). 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. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. This group additionally contains proteins which are fusions between subunits I and III, such as Sulfolobus acidocaldarius SoxM, a subunit of the SoxM terminal oxidase complex. It also includes NorE which has been speculated to be a subunit of nitric oxide reductase. Some archaebacterial cytochrome oxidases lack subunit III. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria.


Pssm-ID: 238227  Cd Length: 183  Bit Score: 83.41  E-value: 4.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431513845  38 TSSTAIMYSIFGMFIFSEIMVFSTFIWGYLHLRLSNP----MLLAELNVEAYLQISDVLNIGSVLVSIILHRIQEGASFE 113
Cdd:cd00386     3 ASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPvefgAGLDPLDLPLLNTNTLLLSGSSVTWAHASLAARRGNRKK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431513845 114 VDFFMEQLLLVGVIFLSLQNDEYSLLLSYVNNYWMTLYFFILTGLHSLHVCMGGVF---VLIQSYLYDDDGSLRDEDFNA 190
Cdd:cd00386    83 ARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFllvVLIRLRRGHFTPRHHLGLEAA 162

                         170       180
                  ....*....|....*....|.
gi 2431513845 191 GVYWHFVEMIWIALTLLLFLV 211
Cdd:cd00386   163 ALYWHFVDVVWLFLFPLVYLW 183
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
48-211 1.11e-12

Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];


Pssm-ID: 441450  Cd Length: 192  Bit Score: 63.72  E-value: 1.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431513845  48 FGMFIFSEIMVFSTFIWGYLHLRLSN---PMLLAELNVEAYLQISDVLNIGSVLVSIILHRIQEGASFEVDFFMEQLLLV 124
Cdd:COG1845    20 MWLFLASEVMLFAALFAAYFVLRASApdwPAGAELLDLPLPLINTLLLLLSSFTVALAVRAARRGDRKGLRLWLLLTLLL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431513845 125 GVIFLSLQNDEYSLLLS-----YVNNYWMTlyFFILTGLHSLHVCMGGVF---VLIQSYLYDDDGSLRDEDFNAGVYWHF 196
Cdd:COG1845   100 GLAFLGLQAYEYSHLIAegltpTSNAFGSF--FFLLTGFHGLHVIIGLIWllvVLVRALRGGFTPENHTGVEAAALYWHF 177

                         170
                  ....*....|....*
gi 2431513845 197 VEMIWIALTLLLFLV 211
Cdd:COG1845   178 VDVVWIFLFALVYLL 192
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 48-204 1.83e-08

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 52.97  E-value: 1.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431513845  48 FGMFIFSEIMVFSTFIWGYLHLRLSN---------PMLLAELNV-EAYLQISDVLNIGSVLVSIILHRIQEGASFEVDFF 117
Cdd:MTH00141   81 FILFIVSEVCFFFAFFWAYFHSSLAPsveigccwpPVGIEPLNPfQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQG 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431513845 118 MEQLLLVGVIFLSLQNDEYslllsYVNNYWM--TLY---FFILTGLHSLHVCMGGVFV---LIQSYLYDDDGSlRDEDFN 189
Cdd:MTH00141  161 LGLTIILGVYFTFLQAGEY-----YEASFSIadGVYgstFFVLTGFHGLHVIIGTTFLlvcLVRLLLGHFSTN-HHFGFE 234

                         170
                  ....*....|....*.
gi 2431513845 190 AGV-YWHFVEMIWIAL 204
Cdd:MTH00141  235 AAAwYWHFVDVVWLFL 250
COX3 pfam00510
Cytochrome c oxidase subunit III;
48-204 1.00e-05

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 45.09  E-value: 1.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431513845  48 FGMFIFSEIMVFSTFIWGYLHLRLS---------NPMLLAELN-VEAYLQISDVLNIGSVLVSIILHRIQEGASFEVDFF 117
Cdd:pfam00510  80 MILFIISEVFFFLGIFWAFFHSALSptvelgaqwPPVGIHPVNpFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQG 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431513845 118 MEQLLLVGVIFLSLQNDEYSLLLSYVNNYWMTLYFFILTGLHSLHVCMGGVFVL-----IQSYLYDDDGSLRDEdfNAGV 192
Cdd:pfam00510 160 LILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAvcflrLLKYHLTDNHHFGFE--AAIL 237

                         170
                  ....*....|..
gi 2431513845 193 YWHFVEMIWIAL 204
Cdd:pfam00510 238 YWHFVDVVWLFL 249
 
Name Accession Description Interval E-value
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 38-211 4.26e-20

Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). 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. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. This group additionally contains proteins which are fusions between subunits I and III, such as Sulfolobus acidocaldarius SoxM, a subunit of the SoxM terminal oxidase complex. It also includes NorE which has been speculated to be a subunit of nitric oxide reductase. Some archaebacterial cytochrome oxidases lack subunit III. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria.


Pssm-ID: 238227  Cd Length: 183  Bit Score: 83.41  E-value: 4.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431513845  38 TSSTAIMYSIFGMFIFSEIMVFSTFIWGYLHLRLSNP----MLLAELNVEAYLQISDVLNIGSVLVSIILHRIQEGASFE 113
Cdd:cd00386     3 ASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPvefgAGLDPLDLPLLNTNTLLLSGSSVTWAHASLAARRGNRKK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431513845 114 VDFFMEQLLLVGVIFLSLQNDEYSLLLSYVNNYWMTLYFFILTGLHSLHVCMGGVF---VLIQSYLYDDDGSLRDEDFNA 190
Cdd:cd00386    83 ARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFllvVLIRLRRGHFTPRHHLGLEAA 162

                         170       180
                  ....*....|....*....|.
gi 2431513845 191 GVYWHFVEMIWIALTLLLFLV 211
Cdd:cd00386   163 ALYWHFVDVVWLFLFPLVYLW 183
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
48-211 1.11e-12

Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];


Pssm-ID: 441450  Cd Length: 192  Bit Score: 63.72  E-value: 1.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431513845  48 FGMFIFSEIMVFSTFIWGYLHLRLSN---PMLLAELNVEAYLQISDVLNIGSVLVSIILHRIQEGASFEVDFFMEQLLLV 124
Cdd:COG1845    20 MWLFLASEVMLFAALFAAYFVLRASApdwPAGAELLDLPLPLINTLLLLLSSFTVALAVRAARRGDRKGLRLWLLLTLLL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431513845 125 GVIFLSLQNDEYSLLLS-----YVNNYWMTlyFFILTGLHSLHVCMGGVF---VLIQSYLYDDDGSLRDEDFNAGVYWHF 196
Cdd:COG1845   100 GLAFLGLQAYEYSHLIAegltpTSNAFGSF--FFLLTGFHGLHVIIGLIWllvVLVRALRGGFTPENHTGVEAAALYWHF 177

                         170
                  ....*....|....*
gi 2431513845 197 VEMIWIALTLLLFLV 211
Cdd:COG1845   178 VDVVWIFLFALVYLL 192
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 48-204 1.83e-08

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 52.97  E-value: 1.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431513845  48 FGMFIFSEIMVFSTFIWGYLHLRLSN---------PMLLAELNV-EAYLQISDVLNIGSVLVSIILHRIQEGASFEVDFF 117
Cdd:MTH00141   81 FILFIVSEVCFFFAFFWAYFHSSLAPsveigccwpPVGIEPLNPfQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQG 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431513845 118 MEQLLLVGVIFLSLQNDEYslllsYVNNYWM--TLY---FFILTGLHSLHVCMGGVFV---LIQSYLYDDDGSlRDEDFN 189
Cdd:MTH00141  161 LGLTIILGVYFTFLQAGEY-----YEASFSIadGVYgstFFVLTGFHGLHVIIGTTFLlvcLVRLLLGHFSTN-HHFGFE 234

                         170
                  ....*....|....*.
gi 2431513845 190 AGV-YWHFVEMIWIAL 204
Cdd:MTH00141  235 AAAwYWHFVDVVWLFL 250
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 48-209 2.18e-08

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 52.87  E-value: 2.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431513845  48 FGM--FIFSEIMVFSTFIWGYLHLRLSN---------PMLLAELNVEAYLQISDVLNIGS-VLVSIILHRIQEGASFEVD 115
Cdd:MTH00052   82 YGMilFIVSEVCLFFSFFWAFFHSSLAPtieigavwpPRGVDPLNPFSVPLLNTAVLLSSgATVTWAHHGIISGKRKEAI 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431513845 116 FFMEQLLLVGVIFLSLQNDEYSLLLSYVNNYWMTLYFFILTGLHSLHVCMGGVFVLIQSYLYDDDGSLRDEDFN---AGV 192
Cdd:MTH00052  162 IGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGfeaAAW 241

                         170
                  ....*....|....*..
gi 2431513845 193 YWHFVEMIWIALTLLLF 209
Cdd:MTH00052  242 YWHFVDVVWLFLFIFMY 258
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 48-204 3.57e-08

Cytochrome c oxidase subunit III. 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. CcO 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, but subunit III, which is also conserved, is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. 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 III contains bound phospholipids in several crystal structures and is proposed to contain a "lipid pool." These phospholipids are believed to intrinsic constituents similar to cofactors of the enzyme.


Pssm-ID: 238834  Cd Length: 243  Bit Score: 52.13  E-value: 3.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431513845  48 FGMFIFSEIMVFSTFIWGYLHLRLS-----------------NPMLLAELNveaylqiSDVLNIGSVLVSIILHRIQEGA 110
Cdd:cd01665    67 MILFILSEVMFFFSFFWAFFHSSLSpsvelggtwppvgieplNPFGIPLLN-------TIILLSSGATVTWAHHALLLGN 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431513845 111 SFEVDFFMEQLLLVGVIFLSLQNDEYSLLLSYVNNYWMTLYFFILTGLHSLHVCMGGVFVLIQSYLYDDDGSLRDEDFN- 189
Cdd:cd01665   140 RKKAILGLILTILLGVYFTGLQAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGf 219

                         170
                  ....*....|....*..
gi 2431513845 190 --AGVYWHFVEMIWIAL 204
Cdd:cd01665   220 eaAIWYWHFVDVVWLFL 236
NorE_like cd02862
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ...
 51-211 4.26e-08

NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include cytochrome c and ubiquinol oxidases. Alcaligenes faecalis norE is found in a gene cluster containing norCB. norCB encodes the cytochrome c and cytochrome b subunits of nitric oxide reductase (NOR). Based on this and on its similarity to subunit III of cytochrome c oxidase (CcO) and ubiquinol oxidase, NorE has been speculated to be a subunit of NOR.


Pssm-ID: 239213  Cd Length: 186  Bit Score: 51.08  E-value: 4.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431513845  51 FIFSEIMVFSTFIWGYLHLRLSNPMLLA----ELNVEAYLQISDVLNIGSVLVSIILHRIQEGASFEVDFFMEQLLLVGV 126
Cdd:cd02862    16 FILSELLAFGALFIAYAVYRALYPELFAagsaHLDLLLGALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431513845 127 IFLSLQNDEYSLLLSYVN----NYWMTLYFFiLTGLHSLHVCMGGVFVLI-------QSYLYDDDGSLRdedfNAGVYWH 195
Cdd:cd02862    96 VFLVIKYFEYAHKIAAGIdpdaGLFFTLYFL-LTGFHLLHVLIGLGILLWvawrarrGRYSARDYEGVE----AAALYWH 170

                         170
                  ....*....|....*.
gi 2431513845 196 FVEMIWIALTLLLFLV 211
Cdd:cd02862   171 MVDLVWIVLFPLLYLV 186
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 50-209 1.11e-07

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 50.61  E-value: 1.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431513845  50 MFIFSEIMVFSTFIWGYLHLRLSN---------PMLLAELN-VEAYLQISDVLNIGSVLVSIILHRIQEGASFEVDFFME 119
Cdd:MTH00009   83 LFIASEVMFFFAFFWAFFHSSLAPtpelgcswpPTGIEPLNpFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALI 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431513845 120 QLLLVGVIFLSLQNDEYSLLLSYVNNYWMTLYFFILTGLHSLHVCMGGVFVLI-----QSYLYDDDGSLRDEdfNAGVYW 194
Cdd:MTH00009  163 LTVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVcllrtWSHHFSTGHHFGFE--AAAWYW 240

                         170
                  ....*....|....*
gi 2431513845 195 HFVEMIWIALTLLLF 209
Cdd:MTH00009  241 HFVDVVWIFLYLCIY 255
Heme_Cu_Oxidase_III_1 cd02864
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 42-211 4.63e-07

Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). 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. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria.


Pssm-ID: 239215  Cd Length: 202  Bit Score: 48.27  E-value: 4.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431513845  42 AIMYSIFGMFIF--SEIMVFSTFIWGYLHLRLSNPMLLAELNVEAYLQISDVlNIGSVLVSII--------------LHR 105
Cdd:cd02864     5 KVSWGKAMMWFFllSDAFIFSSFLIAYMTARISTTEPWPLPSDVFALRIGHF-NIPLVLIAIMtfilitssgtmamaVNF 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431513845 106 IQEGASFEVDFFMEQLLLVGVIFLSLQNDEYSLLLS------YVNNYWMTLY---FFILTGLHSLHVCMGGVFVLIQSYL 176
Cdd:cd02864    84 GYRGNRKAAARLMLATALLGATFVGMQAFEWTKLIVeegvrpWGNPWGAAQFgasFFMITGFHGTHVTIGVIYLIIIARK 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2431513845 177 -----YDDDGSLRDEDFnAGVYWHFVEMIWIALTLLLFLV 211
Cdd:cd02864   164 vwrgkYQRIGRYEIVEI-AGLYWHFVDLVWVFIFAFFYLW 202
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 48-204 6.26e-06

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 45.52  E-value: 6.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431513845  48 FGM--FIFSEIMVFSTFIWGYLHLRLSN---------PMLLAELN-VEAYLQISDVLNIGSVLVSIILHRIQEGASFEVD 115
Cdd:MTH00130   81 YGMilFITSEVFFFLGFFWAFYHSSLAPtpelggcwpPTGITTLDpFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAI 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431513845 116 FFMEQLLLVGVIFLSLQNDEYSLLLSYVNNYWMTLYFFILTGLHSLHVCMGGVFV---LIQSYLYDDDGSLRDEDFNAGV 192
Cdd:MTH00130  161 QSLTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLavcLLRQIQYHFTSEHHFGFEAAAW 240

                         170
                  ....*....|..
gi 2431513845 193 YWHFVEMIWIAL 204
Cdd:MTH00130  241 YWHFVDVVWLFL 252
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 48-204 7.15e-06

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 45.49  E-value: 7.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431513845  48 FGM--FIFSEIMVFSTFIWGYLHLRLS-----------------NPMLLAELNveaylqiSDVLNIGSVLVSIILHRIQE 108
Cdd:MTH00039   80 YGMilFITSEVCFFFAFFWAFFHSSLAptveigvswpptginpiNPFLVPLLN-------TAVLLSSGVTITWSHHSILE 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431513845 109 GASFEVDFFMEQLLLVGVIFLSLQNDEYSLLLSYVNNYWMTLYFFILTGLHSLHVCMGGVFVLI-----QSYLYDDDGSL 183
Cdd:MTH00039  153 GNRTEAIQALFLTVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVclfrlINHHFSNNHHF 232

                         170       180
                  ....*....|....*....|.
gi 2431513845 184 RDEdfNAGVYWHFVEMIWIAL 204
Cdd:MTH00039  233 GFE--AAAWYWHFVDVVWLFL 251
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 122-209 8.54e-06

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 45.44  E-value: 8.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431513845 122 LLVGVIFLSLQNDEYSLLLSYVNNYWMTLYFFILTGLHSLHVCMGGVFVLIQSY--LYDDDGSLRDEDFNAGV-YWHFVE 198
Cdd:MTH00028  203 ILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVLVGTTFLIVCFIrlLSNQFTNSHHLGLEAAIwYWHFVD 282

                          90
                  ....*....|.
gi 2431513845 199 MIWIALTLLLF 209
Cdd:MTH00028  283 VVWLFLYVFVY 293
PLN02194 PLN02194
cytochrome-c oxidase
 50-209 9.59e-06

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 45.04  E-value: 9.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431513845  50 MFIFSEIMVFSTFIWGYLHLRLSNPMLLAELNVEAYLQISD----------VLNIGSVLVSIILHRIQEGASFEVDFFME 119
Cdd:PLN02194   88 LFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDpweipflntpILPSSGAAVTWAHHAILAGKEKRAVYALV 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431513845 120 QLLLVGVIFLSLQNDEYSLLLSYVNNYWMTLYFFILTGLHSLHVCMGGVFVLI---QSYLydddGSLRDEDF----NAGV 192
Cdd:PLN02194  168 ATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIIcgiRQYL----GHLTKEHHvgfeAAAW 243

                         170
                  ....*....|....*..
gi 2431513845 193 YWHFVEMIWIALTLLLF 209
Cdd:PLN02194  244 YWHFVDVVWLFLFVSIY 260
COX3 pfam00510
Cytochrome c oxidase subunit III;
48-204 1.00e-05

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 45.09  E-value: 1.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431513845  48 FGMFIFSEIMVFSTFIWGYLHLRLS---------NPMLLAELN-VEAYLQISDVLNIGSVLVSIILHRIQEGASFEVDFF 117
Cdd:pfam00510  80 MILFIISEVFFFLGIFWAFFHSALSptvelgaqwPPVGIHPVNpFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQG 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431513845 118 MEQLLLVGVIFLSLQNDEYSLLLSYVNNYWMTLYFFILTGLHSLHVCMGGVFVL-----IQSYLYDDDGSLRDEdfNAGV 192
Cdd:pfam00510 160 LILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAvcflrLLKYHLTDNHHFGFE--AAIL 237

                         170
                  ....*....|..
gi 2431513845 193 YWHFVEMIWIAL 204
Cdd:pfam00510 238 YWHFVDVVWLFL 249
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 48-204 2.17e-05

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 43.95  E-value: 2.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431513845  48 FGM--FIFSEIMVFSTFIWGYLHLRLSN---------PMLLAELN-VEAYLQISDVLNIGSVLVSIILHRIQEGASFEVD 115
Cdd:MTH00099   81 YGMilFIISEVFFFAGFFWAFYHSSLAPtpelggcwpPTGITPLNpLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHML 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431513845 116 FFMEQLLLVGVIFLSLQNDEYSLLLSYVNNYWMTLYFFILTGLHSLHVCMGGVFV---LIQSYLYDDDGSLRDEDFNAGV 192
Cdd:MTH00099  161 QALFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLivcFLRQLKFHFTSNHHFGFEAAAW 240

                         170
                  ....*....|..
gi 2431513845 193 YWHFVEMIWIAL 204
Cdd:MTH00099  241 YWHFVDVVWLFL 252
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 48-204 9.85e-05

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 41.86  E-value: 9.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431513845  48 FGM--FIFSEIMVFSTFIWGYLHLRLS-----------------NPMLLAELNveaylqiSDVLNIGSVLVSIILHRIQE 108
Cdd:MTH00118   81 YGMilFITSEVFFFLGFFWAFYHSSLAptpelggqwpptgikplNPFEVPLLN-------TAVLLASGVTVTWAHHSIME 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431513845 109 GASFEVDFFMEQLLLVGVIFLSLQNDEYSLLLSYVNNYWMTLYFFILTGLHSLHVCMGGVFVLIqsylydddGSLRDEDF 188
Cdd:MTH00118  154 GNRKQAIQALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIV--------CLLRLIKF 225

                         170       180
                  ....*....|....*....|....*..
gi 2431513845 189 N-----------AGVYWHFVEMIWIAL 204
Cdd:MTH00118  226 HfttnhhfgfeaAAWYWHFVDVVWLFL 252
Ubiquinol_oxidase_III cd02863
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ...
 48-202 1.12e-04

Ubiquinol oxidase subunit III subfamily. 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. Ubiquinol oxidases feature four subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of bovine CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in bovine CcO. Although not required for catalytic activity, subunit III appears to be involved in assembly of the multimer complex.


Pssm-ID: 239214  Cd Length: 186  Bit Score: 41.46  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431513845  48 FGMFIFSEIMVFSTFIWGYLHLRLS---NPMLLAELNVEAYLQISDVLNIGSVLVSIILHRIQEGASFEVDFFMEQLLLV 124
Cdd:cd02863    13 FWIYLMSDCILFATLFATYAVLSGNtagGPPGHELFELPLVFIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431513845 125 GVIFLSLQNDEYSLLLSY-----VNNYWMTlyFFILTGLHSLHVCMGGVFVL---IQSYLYDDDGSLRDEDFNAGVYWHF 196
Cdd:cd02863    93 GLGFVGMEIYEFHHLIAEgagpdRSAFLSA--FFTLVGTHGLHVTFGLIWILvmiIQLKKRGLTPDTARRLFCLSLFWHF 170


                  ....*.
gi 2431513845 197 VEMIWI 202
Cdd:cd02863   171 LDIVWI 176
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 48-204 1.30e-04

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 41.65  E-value: 1.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431513845  48 FGM--FIFSEIMVFSTFIWGYLHLRLSN---------PMLLAELN-VEAYLQISDVLNIGSVLVSIILHRIQEGASFEVD 115
Cdd:MTH00075   81 YGMilFITSEVFFFLGFFWAFYNSSLAPtpelgecwpPTGITPLDpFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAI 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431513845 116 FFMEQLLLVGVIFLSLQNDEYSLLLSYVNNYWMTLYFFILTGLHSLHVCMGGVFVLIqsylydddGSLRDEDFN------ 189
Cdd:MTH00075  161 QSLALTIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLV--------CLLRQINFHftsqhh 232

                         170       180
                  ....*....|....*....|
gi 2431513845 190 -----AGVYWHFVEMIWIAL 204
Cdd:MTH00075  233 fgfeaAAWYWHFVDVVWLFL 252
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 50-209 1.44e-04

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 41.70  E-value: 1.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431513845  50 MFIFSEIMVFSTFIWGYLHLRLSNPMLLAE---------LNVEAYLQISDVLNIGS-VLVSIILHRIQEGASFEVDFFME 119
Cdd:MTH00219   86 LFIVSEILFFFAFFWAFFHSSLAPTIELGScwpptginpLNPFQVPLLNTAVLLASgVTVTWAHHSLMESNHKEAQQGLL 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431513845 120 QLLLVGVIFLSLQNDEYSLLLSYVNNYWMTLYFFILTGLHSLHVCMGGVFVLI--QSYLYDDDGSLRDEDFNAGV-YWHF 196
Cdd:MTH00219  166 FTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVcfMRGLMLHFSKNHHFGFEAAAwYWHF 245

                         170
                  ....*....|...
gi 2431513845 197 VEMIWIALTLLLF 209
Cdd:MTH00219  246 VDVVWLFLYVSIY 258
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
 48-209 5.30e-04

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 39.94  E-value: 5.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431513845  48 FGM--FIFSEIMVFSTFIWGYLHLRLS---------NPMLLAELNVEAYLQISDVLNIGSVLVSIILHRIQEGASFEVDF 116
Cdd:MTH00083   77 FGMilFIFSEFMFFFSIFWTFFDAALVpvhelggvwSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSNKSCTN 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431513845 117 FMEQLLLVGVIFLSLQNDEYSLLLSYVNNYWMTLYFFILTGLHSLHVCMGGVFVLIQSY--LYDDDGSLRDEDFNAGV-Y 193
Cdd:MTH00083  157 SLLLTCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLrlLKSHFNYNHHLGLEFAIlY 236

                         170
                  ....*....|....*.
gi 2431513845 194 WHFVEMIWIALTLLLF 209
Cdd:MTH00083  237 WHFVDVVWLFLFVFVY 252
Heme_Cu_Oxidase_III_2 cd02865
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 122-204 6.68e-04

Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). 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. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria.


Pssm-ID: 239216  Cd Length: 184  Bit Score: 38.89  E-value: 6.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431513845 122 LLVGVIFLSLQNDEYSLLlsYVNNYWMTL-----YFFILTGLHSLHVCMGGVF---VLIQSYLYDDDGSLRDEDFNAGVY 193
Cdd:cd02865    89 GALALAFLAGQLLAWHAL--NDAGYGPTSnpagsFFYLLTGLHGLHVIGGLVAlaiVLAGLIRGHYGPRRRLPVELCALY 166

                          90
                  ....*....|.
gi 2431513845 194 WHFVEMIWIAL 204
Cdd:cd02865   167 WHFLLLVWLVL 177
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 50-204 1.01e-03

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 39.01  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431513845  50 MFIFSEIMVFSTFIWGYLHLRLS-----------------NPMLLAELNveaylqiSDVLNIGSVLVSIILHRIQEGASF 112
Cdd:MTH00155   83 LFIVSEVFFFISFFWAFFHSSLSpnielgmiwppkgiipfNPFQIPLLN-------TIILLSSGVTVTWAHHSLMENNYK 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431513845 113 EVDFFMEQLLLVGVIFLSLQNDEYSLLLSYVNNYWMTLYFFILTGLHSLHVCMGGVFVLIQSYLYDDDGSLRDEDFN--- 189
Cdd:MTH00155  156 QATQSLFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGfea 235

                         170
                  ....*....|....*
gi 2431513845 190 AGVYWHFVEMIWIAL 204
Cdd:MTH00155  236 AAWYWHFVDVVWLFL 250
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 49-204 1.65e-03

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 38.42  E-value: 1.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431513845  49 GM--FIFSEIMVFSTFIWGYLHLRLSN---------PMLLAELNVEAYLQISDVLNIGS-VLVSIILHRIQEGASFEVDF 116
Cdd:MTH00189   81 GMilFITSEVFFFLGFFWAFFHSSLAPtvelgmcwpPTGIEPLNPFEVPLLNTAVLLSSgVTVTWAHHSLMEGNRKEAIQ 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431513845 117 FMEQLLLVGVIFLSLQNDEYSLLLSYVNNYWMTLYFFILTGLHSLHVCMGGVFVLIQSY--LYDDDGSLRDEDFNAGV-Y 193
Cdd:MTH00189  161 ALTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLrqIQGHFTSSHHFGFEAAAwY 240

                         170
                  ....*....|.
gi 2431513845 194 WHFVEMIWIAL 204
Cdd:MTH00189  241 WHFVDVVWLFL 251
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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