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Conserved domains on  [gi|157786758|ref|NP_001099208|]
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epididymal secretory glutathione peroxidase precursor [Rattus norvegicus]

Protein Classification

glutathione peroxidase( domain architecture ID 10085912)

glutathione peroxidase catalyzes the reduction of hydroperoxides using GSH as a specific electron donor

CATH:  3.40.30.10
EC:  1.11.1.-
Gene Ontology:  GO:0043295|GO:0004602|GO:0006979
SCOP:  4000042

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
39-211 3.82e-62

Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a variety of hydroperoxides including lipid peroxidases, using GSH as a specific electron donor substrate. GSH peroxidase contains one selenocysteine residue per subunit, which is involved in catalysis. Different isoenzymes are known in mammals,which are involved in protection against reactive oxygen species, redox regulation of many metabolic processes, peroxinitrite scavenging, and modulation of inflammatory processes.


:

Pssm-ID: 238207 [Multi-domain]  Cd Length: 152  Bit Score: 190.80  E-value: 3.82e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786758  39 TIYNYEALSLNGKErIPFKQYAGKHVLFVNVATYCGLTIQYPELNALQDDLKQFGLVILGFPCNQFGKQEPGDNTEILPG 118
Cdd:cd00340    1 SIYDFSVKDIDGEP-VSLSKYKGKVLLIVNVASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786758 119 LKYVRPgkgflPNFQLFAKGDVNGEKEQEIFTFLKRSCPhpsetvvtskhtfwePIKVHDIRWNFEKFLVGPNGVPVMRW 198
Cdd:cd00340   80 CETNYG-----VTFPMFAKIDVNGENAHPLYKYLKEEAP---------------GLLGKDIKWNFTKFLVDRDGEVVKRF 139
                        170
                 ....*....|...
gi 157786758 199 FHQAPVSTVKSDI 211
Cdd:cd00340  140 APTTDPEELEKDI 152
 
Name Accession Description Interval E-value
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
39-211 3.82e-62

Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a variety of hydroperoxides including lipid peroxidases, using GSH as a specific electron donor substrate. GSH peroxidase contains one selenocysteine residue per subunit, which is involved in catalysis. Different isoenzymes are known in mammals,which are involved in protection against reactive oxygen species, redox regulation of many metabolic processes, peroxinitrite scavenging, and modulation of inflammatory processes.


Pssm-ID: 238207 [Multi-domain]  Cd Length: 152  Bit Score: 190.80  E-value: 3.82e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786758  39 TIYNYEALSLNGKErIPFKQYAGKHVLFVNVATYCGLTIQYPELNALQDDLKQFGLVILGFPCNQFGKQEPGDNTEILPG 118
Cdd:cd00340    1 SIYDFSVKDIDGEP-VSLSKYKGKVLLIVNVASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786758 119 LKYVRPgkgflPNFQLFAKGDVNGEKEQEIFTFLKRSCPhpsetvvtskhtfwePIKVHDIRWNFEKFLVGPNGVPVMRW 198
Cdd:cd00340   80 CETNYG-----VTFPMFAKIDVNGENAHPLYKYLKEEAP---------------GLLGKDIKWNFTKFLVDRDGEVVKRF 139
                        170
                 ....*....|...
gi 157786758 199 FHQAPVSTVKSDI 211
Cdd:cd00340  140 APTTDPEELEKDI 152
GSHPx pfam00255
Glutathione peroxidase;
40-153 8.10e-52

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 162.91  E-value: 8.10e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786758   40 IYNYEALSLNGkERIPFKQYAGKHVLFVNVATYCGLTIQYPELNALQDDLKQFGLVILGFPCNQFGKQEPGDNTEIlpgl 119
Cdd:pfam00255   1 IYEFSAKDIDG-EPVPFDQYRGKVVLIVNVASKCGLTPQYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEI---- 75
                          90       100       110
                  ....*....|....*....|....*....|....
gi 157786758  120 KYVRPGkGFLPNFQLFAKGDVNGEKEQEIFTFLK 153
Cdd:pfam00255  76 KYFCPG-GYGVTFPLFSKIEVNGEKAHPVYKFLK 108
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
39-198 3.12e-49

Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid transport and metabolism];


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 157.93  E-value: 3.12e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786758  39 TIYNYEALSLNGKErIPFKQYAGKHVLFVNVATYCGLTIQYPELNALQDDLKQFGLVILGFPCNQFGKQEPGDNTEIlpg 118
Cdd:COG0386    3 SIYDFSVTTLDGEP-VSLSDYKGKVLLIVNTASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEI--- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786758 119 lkyvrpgKGFLPN-----FQLFAKGDVNGEKEQEIFTFLKRSCPHPSETvvtskhtfwepikvHDIRWNFEKFLVGPNGV 193
Cdd:COG0386   79 -------AEFCSLnygvtFPMFAKIDVNGPNAHPLYKYLKEEAPGLLGG--------------GDIKWNFTKFLIDRDGN 137

                 ....*
gi 157786758 194 PVMRW 198
Cdd:COG0386  138 VVARF 142
btuE PRK10606
putative glutathione peroxidase; Provisional
39-212 7.59e-35

putative glutathione peroxidase; Provisional


Pssm-ID: 182585 [Multi-domain]  Cd Length: 183  Bit Score: 122.19  E-value: 7.59e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786758  39 TIYNYEALSLNGkERIPFKQYAGKHVLFVNVATYCGLTIQYPELNALQDDLKQFGLVILGFPCNQFGKQEPGDNTEIlpg 118
Cdd:PRK10606   4 SILTTVVTTIDG-EVTTLEKYAGNVLLIVNVASKCGLTPQYEQLENIQKAWADQGFVVLGFPCNQFLGQEPGSDEEI--- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786758 119 LKYVRPGKGFlpNFQLFAKGDVNGEKEQEIFTFLKRSCPhpsETVVTSKHTFWE--------PIKVHDIRWNFEKFLVGP 190
Cdd:PRK10606  80 KTYCRTTWGV--TFPMFSKIEVNGEGRHPLYQKLIAAAP---TAVAPEESGFYArmvskgraPLYPDDILWNFEKFLVGR 154
                        170       180
                 ....*....|....*....|..
gi 157786758 191 NGVPVMRWfhqAPVSTVKSDIL 212
Cdd:PRK10606 155 DGQVIQRF---SPDMTPEDPIV 173
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
41-213 5.65e-25

putative glutathione peroxidase Gpx7; This model represents one of several families of known and probable glutathione peroxidases. This family is restricted to animals and designated GPX7.


Pssm-ID: 131592 [Multi-domain]  Cd Length: 153  Bit Score: 95.67  E-value: 5.65e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786758   41 YNYEALSLNGKErIPFKQYAGKHVLFVNVATYCGLTIQ-YPELNALQDDLKQFGLVILGFPCNQFGKQEPGDNTEIlpgL 119
Cdd:TIGR02540   3 YSFEVKDARGRT-VSLEKYRGKVSLVVNVASECGFTDQnYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEI---E 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786758  120 KYVRpgKGFLPNFQLFAKGDVNGEKEQEIFTFLkrscphpsetVVTSKHtfwEPikvhdiRWNFEKFLVGPNGVPVMRWF 199
Cdd:TIGR02540  79 SFAR--RNYGVTFPMFSKIKILGSEAEPAFRFL----------VDSSKK---EP------RWNFWKYLVNPEGQVVKFWR 137
                         170
                  ....*....|....
gi 157786758  200 HQAPVSTVKSDILA 213
Cdd:TIGR02540 138 PEEPVEEIRPEITA 151
 
Name Accession Description Interval E-value
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
39-211 3.82e-62

Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a variety of hydroperoxides including lipid peroxidases, using GSH as a specific electron donor substrate. GSH peroxidase contains one selenocysteine residue per subunit, which is involved in catalysis. Different isoenzymes are known in mammals,which are involved in protection against reactive oxygen species, redox regulation of many metabolic processes, peroxinitrite scavenging, and modulation of inflammatory processes.


Pssm-ID: 238207 [Multi-domain]  Cd Length: 152  Bit Score: 190.80  E-value: 3.82e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786758  39 TIYNYEALSLNGKErIPFKQYAGKHVLFVNVATYCGLTIQYPELNALQDDLKQFGLVILGFPCNQFGKQEPGDNTEILPG 118
Cdd:cd00340    1 SIYDFSVKDIDGEP-VSLSKYKGKVLLIVNVASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786758 119 LKYVRPgkgflPNFQLFAKGDVNGEKEQEIFTFLKRSCPhpsetvvtskhtfwePIKVHDIRWNFEKFLVGPNGVPVMRW 198
Cdd:cd00340   80 CETNYG-----VTFPMFAKIDVNGENAHPLYKYLKEEAP---------------GLLGKDIKWNFTKFLVDRDGEVVKRF 139
                        170
                 ....*....|...
gi 157786758 199 FHQAPVSTVKSDI 211
Cdd:cd00340  140 APTTDPEELEKDI 152
GSHPx pfam00255
Glutathione peroxidase;
40-153 8.10e-52

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 162.91  E-value: 8.10e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786758   40 IYNYEALSLNGkERIPFKQYAGKHVLFVNVATYCGLTIQYPELNALQDDLKQFGLVILGFPCNQFGKQEPGDNTEIlpgl 119
Cdd:pfam00255   1 IYEFSAKDIDG-EPVPFDQYRGKVVLIVNVASKCGLTPQYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEI---- 75
                          90       100       110
                  ....*....|....*....|....*....|....
gi 157786758  120 KYVRPGkGFLPNFQLFAKGDVNGEKEQEIFTFLK 153
Cdd:pfam00255  76 KYFCPG-GYGVTFPLFSKIEVNGEKAHPVYKFLK 108
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
39-198 3.12e-49

Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid transport and metabolism];


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 157.93  E-value: 3.12e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786758  39 TIYNYEALSLNGKErIPFKQYAGKHVLFVNVATYCGLTIQYPELNALQDDLKQFGLVILGFPCNQFGKQEPGDNTEIlpg 118
Cdd:COG0386    3 SIYDFSVTTLDGEP-VSLSDYKGKVLLIVNTASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEI--- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786758 119 lkyvrpgKGFLPN-----FQLFAKGDVNGEKEQEIFTFLKRSCPHPSETvvtskhtfwepikvHDIRWNFEKFLVGPNGV 193
Cdd:COG0386   79 -------AEFCSLnygvtFPMFAKIDVNGPNAHPLYKYLKEEAPGLLGG--------------GDIKWNFTKFLIDRDGN 137

                 ....*
gi 157786758 194 PVMRW 198
Cdd:COG0386  138 VVARF 142
btuE PRK10606
putative glutathione peroxidase; Provisional
39-212 7.59e-35

putative glutathione peroxidase; Provisional


Pssm-ID: 182585 [Multi-domain]  Cd Length: 183  Bit Score: 122.19  E-value: 7.59e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786758  39 TIYNYEALSLNGkERIPFKQYAGKHVLFVNVATYCGLTIQYPELNALQDDLKQFGLVILGFPCNQFGKQEPGDNTEIlpg 118
Cdd:PRK10606   4 SILTTVVTTIDG-EVTTLEKYAGNVLLIVNVASKCGLTPQYEQLENIQKAWADQGFVVLGFPCNQFLGQEPGSDEEI--- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786758 119 LKYVRPGKGFlpNFQLFAKGDVNGEKEQEIFTFLKRSCPhpsETVVTSKHTFWE--------PIKVHDIRWNFEKFLVGP 190
Cdd:PRK10606  80 KTYCRTTWGV--TFPMFSKIEVNGEGRHPLYQKLIAAAP---TAVAPEESGFYArmvskgraPLYPDDILWNFEKFLVGR 154
                        170       180
                 ....*....|....*....|..
gi 157786758 191 NGVPVMRWfhqAPVSTVKSDIL 212
Cdd:PRK10606 155 DGQVIQRF---SPDMTPEDPIV 173
PTZ00256 PTZ00256
glutathione peroxidase; Provisional
25-217 2.53e-34

glutathione peroxidase; Provisional


Pssm-ID: 173495 [Multi-domain]  Cd Length: 183  Bit Score: 120.63  E-value: 2.53e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786758  25 LEKMKMDCYKDVKGTIYNYEALSLNGKERiPFKQYAGKHV-LFVNVATYCGLTIQ-YPELNALQDDLKQFGLVILGFPCN 102
Cdd:PTZ00256   5 LFKKGLEQIQPPTKSFFEFEAIDIDGQLV-QLSKFKGKKAiIVVNVACKCGLTSDhYTQLVELYKQYKSQGLEILAFPCN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786758 103 QFGKQEPGDNTEIlpgLKYVRpgKGFLPNFQLFAKGDVNGEKEQEIFTFLKRSCP-HPSETVVTSKhtfwepikvhdIRW 181
Cdd:PTZ00256  84 QFMEQEPWDEPEI---KEYVQ--KKFNVDFPLFQKIEVNGENTHEIYKYLRRNSElFQNNTNEARQ-----------IPW 147
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 157786758 182 NFEKFLVGPNGVPVmRWFH--QAPVSTVKsDILAYLNQ 217
Cdd:PTZ00256 148 NFAKFLIDGQGKVV-KYFSpkVNPNEMIQ-DIEKLLNA 183
PLN02412 PLN02412
probable glutathione peroxidase
39-217 2.09e-27

probable glutathione peroxidase


Pssm-ID: 166053 [Multi-domain]  Cd Length: 167  Bit Score: 102.37  E-value: 2.09e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786758  39 TIYNYEALSLNGKErIPFKQYAGKHVLFVNVATYCGLT-IQYPELNALQDDLKQFGLVILGFPCNQFGKQEPGDNTEILP 117
Cdd:PLN02412   8 SIYDFTVKDIGGND-VSLNQYKGKVLLIVNVASKCGLTdSNYKELNVLYEKYKEQGFEILAFPCNQFLGQEPGSNEEIQQ 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786758 118 GLKYVrpgkgFLPNFQLFAKGDVNGEKEQEIFTFLKrscphpsetvvTSKHTFWepikVHDIRWNFEKFLVGPNGVPVMR 197
Cdd:PLN02412  87 TVCTR-----FKAEFPIFDKVDVNGKNTAPLYKYLK-----------AEKGGLF----GDAIKWNFTKFLVSKEGKVVQR 146
                        170       180
                 ....*....|....*....|
gi 157786758 198 WFHQAPVSTVKSDILAYLNQ 217
Cdd:PLN02412 147 YAPTTSPLKIEKDIQNLLGQ 166
PLN02399 PLN02399
phospholipid hydroperoxide glutathione peroxidase
39-198 2.33e-27

phospholipid hydroperoxide glutathione peroxidase


Pssm-ID: 178021 [Multi-domain]  Cd Length: 236  Bit Score: 104.21  E-value: 2.33e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786758  39 TIYNYEALSLNGKErIPFKQYAGKHVLFVNVATYCGLTI-QYPELNALQDDLKQFGLVILGFPCNQFGKQEPGDNTEIlP 117
Cdd:PLN02399  78 SVHDFTVKDIDGKD-VALSKFKGKVLLIVNVASKCGLTSsNYSELSHLYEKYKTQGFEILAFPCNQFGGQEPGSNPEI-K 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786758 118 GLKYVRpgkgFLPNFQLFAKGDVNGEKEQEIFTFLKrscphpsetvvTSKHTFWEPIkvhdIRWNFEKFLVGPNGVPVMR 197
Cdd:PLN02399 156 QFACTR----FKAEFPIFDKVDVNGPSTAPVYQFLK-----------SNAGGFLGDL----IKWNFEKFLVDKNGKVVER 216

                 .
gi 157786758 198 W 198
Cdd:PLN02399 217 Y 217
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
41-213 5.65e-25

putative glutathione peroxidase Gpx7; This model represents one of several families of known and probable glutathione peroxidases. This family is restricted to animals and designated GPX7.


Pssm-ID: 131592 [Multi-domain]  Cd Length: 153  Bit Score: 95.67  E-value: 5.65e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786758   41 YNYEALSLNGKErIPFKQYAGKHVLFVNVATYCGLTIQ-YPELNALQDDLKQFGLVILGFPCNQFGKQEPGDNTEIlpgL 119
Cdd:TIGR02540   3 YSFEVKDARGRT-VSLEKYRGKVSLVVNVASECGFTDQnYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEI---E 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786758  120 KYVRpgKGFLPNFQLFAKGDVNGEKEQEIFTFLkrscphpsetVVTSKHtfwEPikvhdiRWNFEKFLVGPNGVPVMRWF 199
Cdd:TIGR02540  79 SFAR--RNYGVTFPMFSKIKILGSEAEPAFRFL----------VDSSKK---EP------RWNFWKYLVNPEGQVVKFWR 137
                         170
                  ....*....|....
gi 157786758  200 HQAPVSTVKSDILA 213
Cdd:TIGR02540 138 PEEPVEEIRPEITA 151
PTZ00056 PTZ00056
glutathione peroxidase; Provisional
39-192 5.15e-21

glutathione peroxidase; Provisional


Pssm-ID: 240248 [Multi-domain]  Cd Length: 199  Bit Score: 86.45  E-value: 5.15e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786758  39 TIYNYEALSLNGkERIPFKQYAGKHVLFVNVATYCGLTIQY-PELNALQDDLKQFGLVILGFPCNQFGKQEPGDNTEIlp 117
Cdd:PTZ00056  18 SIYDYTVKTLEG-TTVPMSSLKNKVLMITNSASKCGLTKKHvDQMNRLHSVFNPLGLEILAFPTSQFLNQEFPNTKDI-- 94
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157786758 118 gLKYVRPGKgflPNFQLFAKGDVNGEKEQEIFTFLKRSCPhpsetvvtSKHTfwEPIKVHDIRWNFEKFLVGPNG 192
Cdd:PTZ00056  95 -RKFNDKNK---IKYNFFEPIEVNGENTHELFKFLKANCD--------SMHD--ENGTLKAIGWNFGKFLVNKSG 155
 
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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