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Conserved domains on  [gi|6016164|sp|O75715|]
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RecName: Full=Epididymal secretory glutathione peroxidase; AltName: Full=Epididymis-specific glutathione peroxidase-like protein; Short=EGLP; AltName: Full=Glutathione peroxidase 5; Short=GPx-5; Short=GSHPx-5; Flags: Precursor

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

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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 4.29e-65

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: 198.12  E-value: 4.29e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6016164   39 TIYDYEAIALNKNEyVSFKQYVGKHILFVNVATYCGLTAQYPELNALQEELKPYGLVVLGFPCNQFGKQEPGDNKEILPG 118
Cdd:cd00340   1 SIYDFSVKDIDGEP-VSLSKYKGKVLLIVNVASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6016164  119 LKYVRPgggfvPSFQLFEKGDVNGEKEQKVFSFLKHSCPHPSeilgtfksiswdpvkVHDIRWNFEKFLVGPDGIPVMRW 198
Cdd:cd00340  80 CETNYG-----VTFPMFAKIDVNGENAHPLYKYLKEEAPGLL---------------GKDIKWNFTKFLVDRDGEVVKRF 139
                       170
                ....*....|...
gi 6016164  199 SHRATVSSVKTDI 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 4.29e-65

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: 198.12  E-value: 4.29e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6016164   39 TIYDYEAIALNKNEyVSFKQYVGKHILFVNVATYCGLTAQYPELNALQEELKPYGLVVLGFPCNQFGKQEPGDNKEILPG 118
Cdd:cd00340   1 SIYDFSVKDIDGEP-VSLSKYKGKVLLIVNVASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6016164  119 LKYVRPgggfvPSFQLFEKGDVNGEKEQKVFSFLKHSCPHPSeilgtfksiswdpvkVHDIRWNFEKFLVGPDGIPVMRW 198
Cdd:cd00340  80 CETNYG-----VTFPMFAKIDVNGENAHPLYKYLKEEAPGLL---------------GKDIKWNFTKFLVDRDGEVVKRF 139
                       170
                ....*....|...
gi 6016164  199 SHRATVSSVKTDI 211
Cdd:cd00340 140 APTTDPEELEKDI 152
GSHPx pfam00255
Glutathione peroxidase;
40-153 2.39e-57

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 177.16  E-value: 2.39e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6016164     40 IYDYEAIALNKnEYVSFKQYVGKHILFVNVATYCGLTAQYPELNALQEELKPYGLVVLGFPCNQFGKQEPGDNKEIlpgl 119
Cdd:pfam00255   1 IYEFSAKDIDG-EPVPFDQYRGKVVLIVNVASKCGLTPQYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEI---- 75
                          90       100       110
                  ....*....|....*....|....*....|....
gi 6016164    120 KYVRPgGGFVPSFQLFEKGDVNGEKEQKVFSFLK 153
Cdd:pfam00255  76 KYFCP-GGYGVTFPLFSKIEVNGEKAHPVYKFLK 108
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
39-215 9.20e-51

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


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 162.17  E-value: 9.20e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6016164   39 TIYDYEAIALNKNEyVSFKQYVGKHILFVNVATYCGLTAQYPELNALQEELKPYGLVVLGFPCNQFGKQEPGDNKEILPG 118
Cdd:COG0386   3 SIYDFSVTTLDGEP-VSLSDYKGKVLLIVNTASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIAEF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6016164  119 --LKY-VrpgggfvpSFQLFEKGDVNGEKEQKVFSFLKHscpHPSEILGTFksiswdpvkvhDIRWNFEKFLVGPDGIPV 195
Cdd:COG0386  82 csLNYgV--------TFPMFAKIDVNGPNAHPLYKYLKE---EAPGLLGGG-----------DIKWNFTKFLIDRDGNVV 139
                       170       180
                ....*....|....*....|..
gi 6016164  196 MRWSHRATVSS--VKTDILAYL 215
Cdd:COG0386 140 ARFAPTTKPEDpeLEAAIEKLL 161
btuE PRK10606
putative glutathione peroxidase; Provisional
39-199 6.87e-36

putative glutathione peroxidase; Provisional


Pssm-ID: 182585 [Multi-domain]  Cd Length: 183  Bit Score: 124.89  E-value: 6.87e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6016164    39 TIYDYEAIALNkNEYVSFKQYVGKHILFVNVATYCGLTAQYPELNALQEELKPYGLVVLGFPCNQFGKQEPGDNKEIlpg 118
Cdd:PRK10606   4 SILTTVVTTID-GEVTTLEKYAGNVLLIVNVASKCGLTPQYEQLENIQKAWADQGFVVLGFPCNQFLGQEPGSDEEI--- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6016164   119 LKYVRpgGGFVPSFQLFEKGDVNGEKEQKVFSFL-----KHSCPHPSEILGTFKSISWDPVKVHDIRWNFEKFLVGPDGI 193
Cdd:PRK10606  80 KTYCR--TTWGVTFPMFSKIEVNGEGRHPLYQKLiaaapTAVAPEESGFYARMVSKGRAPLYPDDILWNFEKFLVGRDGQ 157

                 ....*.
gi 6016164   194 PVMRWS 199
Cdd:PRK10606 158 VIQRFS 163
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
41-213 6.46e-29

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: 106.07  E-value: 6.46e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6016164     41 YDYEAIALnKNEYVSFKQYVGKHILFVNVATYCGLTAQ-YPELNALQEELKPYGLVVLGFPCNQFGKQEPGDNKEIlpgL 119
Cdd:TIGR02540   3 YSFEVKDA-RGRTVSLEKYRGKVSLVVNVASECGFTDQnYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEI---E 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6016164    120 KYVRPGGGFvpSFQLFEKGDVNGEKEQKVFSFLkhscphpseilgtFKSISWDPvkvhdiRWNFEKFLVGPDGIPVMRWS 199
Cdd:TIGR02540  79 SFARRNYGV--TFPMFSKIKILGSEAEPAFRFL-------------VDSSKKEP------RWNFWKYLVNPEGQVVKFWR 137
                         170
                  ....*....|....
gi 6016164    200 HRATVSSVKTDILA 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 4.29e-65

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: 198.12  E-value: 4.29e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6016164   39 TIYDYEAIALNKNEyVSFKQYVGKHILFVNVATYCGLTAQYPELNALQEELKPYGLVVLGFPCNQFGKQEPGDNKEILPG 118
Cdd:cd00340   1 SIYDFSVKDIDGEP-VSLSKYKGKVLLIVNVASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6016164  119 LKYVRPgggfvPSFQLFEKGDVNGEKEQKVFSFLKHSCPHPSeilgtfksiswdpvkVHDIRWNFEKFLVGPDGIPVMRW 198
Cdd:cd00340  80 CETNYG-----VTFPMFAKIDVNGENAHPLYKYLKEEAPGLL---------------GKDIKWNFTKFLVDRDGEVVKRF 139
                       170
                ....*....|...
gi 6016164  199 SHRATVSSVKTDI 211
Cdd:cd00340 140 APTTDPEELEKDI 152
GSHPx pfam00255
Glutathione peroxidase;
40-153 2.39e-57

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 177.16  E-value: 2.39e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6016164     40 IYDYEAIALNKnEYVSFKQYVGKHILFVNVATYCGLTAQYPELNALQEELKPYGLVVLGFPCNQFGKQEPGDNKEIlpgl 119
Cdd:pfam00255   1 IYEFSAKDIDG-EPVPFDQYRGKVVLIVNVASKCGLTPQYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEI---- 75
                          90       100       110
                  ....*....|....*....|....*....|....
gi 6016164    120 KYVRPgGGFVPSFQLFEKGDVNGEKEQKVFSFLK 153
Cdd:pfam00255  76 KYFCP-GGYGVTFPLFSKIEVNGEKAHPVYKFLK 108
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
39-215 9.20e-51

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


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 162.17  E-value: 9.20e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6016164   39 TIYDYEAIALNKNEyVSFKQYVGKHILFVNVATYCGLTAQYPELNALQEELKPYGLVVLGFPCNQFGKQEPGDNKEILPG 118
Cdd:COG0386   3 SIYDFSVTTLDGEP-VSLSDYKGKVLLIVNTASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIAEF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6016164  119 --LKY-VrpgggfvpSFQLFEKGDVNGEKEQKVFSFLKHscpHPSEILGTFksiswdpvkvhDIRWNFEKFLVGPDGIPV 195
Cdd:COG0386  82 csLNYgV--------TFPMFAKIDVNGPNAHPLYKYLKE---EAPGLLGGG-----------DIKWNFTKFLIDRDGNVV 139
                       170       180
                ....*....|....*....|..
gi 6016164  196 MRWSHRATVSS--VKTDILAYL 215
Cdd:COG0386 140 ARFAPTTKPEDpeLEAAIEKLL 161
btuE PRK10606
putative glutathione peroxidase; Provisional
39-199 6.87e-36

putative glutathione peroxidase; Provisional


Pssm-ID: 182585 [Multi-domain]  Cd Length: 183  Bit Score: 124.89  E-value: 6.87e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6016164    39 TIYDYEAIALNkNEYVSFKQYVGKHILFVNVATYCGLTAQYPELNALQEELKPYGLVVLGFPCNQFGKQEPGDNKEIlpg 118
Cdd:PRK10606   4 SILTTVVTTID-GEVTTLEKYAGNVLLIVNVASKCGLTPQYEQLENIQKAWADQGFVVLGFPCNQFLGQEPGSDEEI--- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6016164   119 LKYVRpgGGFVPSFQLFEKGDVNGEKEQKVFSFL-----KHSCPHPSEILGTFKSISWDPVKVHDIRWNFEKFLVGPDGI 193
Cdd:PRK10606  80 KTYCR--TTWGVTFPMFSKIEVNGEGRHPLYQKLiaaapTAVAPEESGFYARMVSKGRAPLYPDDILWNFEKFLVGRDGQ 157

                 ....*.
gi 6016164   194 PVMRWS 199
Cdd:PRK10606 158 VIQRFS 163
PLN02412 PLN02412
probable glutathione peroxidase
39-217 5.43e-34

probable glutathione peroxidase


Pssm-ID: 166053 [Multi-domain]  Cd Length: 167  Bit Score: 119.32  E-value: 5.43e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6016164    39 TIYDYEAIALNKNEyVSFKQYVGKHILFVNVATYCGLT-AQYPELNALQEELKPYGLVVLGFPCNQFGKQEPGDNKEILP 117
Cdd:PLN02412   8 SIYDFTVKDIGGND-VSLNQYKGKVLLIVNVASKCGLTdSNYKELNVLYEKYKEQGFEILAFPCNQFLGQEPGSNEEIQQ 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6016164   118 GLKYVrpgggFVPSFQLFEKGDVNGEKEQKVFSFLKhscphpSEILGTFksiswdpvkVHDIRWNFEKFLVGPDGIPVMR 197
Cdd:PLN02412  87 TVCTR-----FKAEFPIFDKVDVNGKNTAPLYKYLK------AEKGGLF---------GDAIKWNFTKFLVSKEGKVVQR 146
                        170       180
                 ....*....|....*....|
gi 6016164   198 WSHRATVSSVKTDILAYLKQ 217
Cdd:PLN02412 147 YAPTTSPLKIEKDIQNLLGQ 166
PTZ00256 PTZ00256
glutathione peroxidase; Provisional
34-217 8.19e-34

glutathione peroxidase; Provisional


Pssm-ID: 173495 [Multi-domain]  Cd Length: 183  Bit Score: 119.48  E-value: 8.19e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6016164    34 KDEKGTIYDYEAIALNKNEyVSFKQYVGKH-ILFVNVATYCGLTAQ-YPELNALQEELKPYGLVVLGFPCNQFGKQEPGD 111
Cdd:PTZ00256  14 QPPTKSFFEFEAIDIDGQL-VQLSKFKGKKaIIVVNVACKCGLTSDhYTQLVELYKQYKSQGLEILAFPCNQFMEQEPWD 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6016164   112 NKEIlpgLKYVRPggGFVPSFQLFEKGDVNGEKEQKVFSFLKHScphpSEILGTFKSiswdpvKVHDIRWNFEKFLVGPD 191
Cdd:PTZ00256  93 EPEI---KEYVQK--KFNVDFPLFQKIEVNGENTHEIYKYLRRN----SELFQNNTN------EARQIPWNFAKFLIDGQ 157
                        170       180
                 ....*....|....*....|....*.
gi 6016164   192 GIPVMRWSHRATVSSVKTDILAYLKQ 217
Cdd:PTZ00256 158 GKVVKYFSPKVNPNEMIQDIEKLLNA 183
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
41-213 6.46e-29

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: 106.07  E-value: 6.46e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6016164     41 YDYEAIALnKNEYVSFKQYVGKHILFVNVATYCGLTAQ-YPELNALQEELKPYGLVVLGFPCNQFGKQEPGDNKEIlpgL 119
Cdd:TIGR02540   3 YSFEVKDA-RGRTVSLEKYRGKVSLVVNVASECGFTDQnYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEI---E 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6016164    120 KYVRPGGGFvpSFQLFEKGDVNGEKEQKVFSFLkhscphpseilgtFKSISWDPvkvhdiRWNFEKFLVGPDGIPVMRWS 199
Cdd:TIGR02540  79 SFARRNYGV--TFPMFSKIKILGSEAEPAFRFL-------------VDSSKKEP------RWNFWKYLVNPEGQVVKFWR 137
                         170
                  ....*....|....
gi 6016164    200 HRATVSSVKTDILA 213
Cdd:TIGR02540 138 PEEPVEEIRPEITA 151
PLN02399 PLN02399
phospholipid hydroperoxide glutathione peroxidase
39-215 8.92e-29

phospholipid hydroperoxide glutathione peroxidase


Pssm-ID: 178021 [Multi-domain]  Cd Length: 236  Bit Score: 108.06  E-value: 8.92e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6016164    39 TIYDYEAIALNKNEyVSFKQYVGKHILFVNVATYCGLTA-QYPELNALQEELKPYGLVVLGFPCNQFGKQEPGDNKEIlP 117
Cdd:PLN02399  78 SVHDFTVKDIDGKD-VALSKFKGKVLLIVNVASKCGLTSsNYSELSHLYEKYKTQGFEILAFPCNQFGGQEPGSNPEI-K 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6016164   118 GLKYVRpgggFVPSFQLFEKGDVNGEKEQKVFSFLKHSCphpSEILGTFksiswdpvkvhdIRWNFEKFLVGPDGIPVMR 197
Cdd:PLN02399 156 QFACTR----FKAEFPIFDKVDVNGPSTAPVYQFLKSNA---GGFLGDL------------IKWNFEKFLVDKNGKVVER 216
                        170
                 ....*....|....*...
gi 6016164   198 WSHRATVSSVKTDILAYL 215
Cdd:PLN02399 217 YPPTTSPFQIEKDIQKLL 234
PTZ00056 PTZ00056
glutathione peroxidase; Provisional
39-192 1.72e-20

glutathione peroxidase; Provisional


Pssm-ID: 240248 [Multi-domain]  Cd Length: 199  Bit Score: 85.29  E-value: 1.72e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6016164    39 TIYDYEAIALNKNEYvSFKQYVGKHILFVNVATYCGLTAQY-PELNALQEELKPYGLVVLGFPCNQFGKQEPGDNKEIlp 117
Cdd:PTZ00056  18 SIYDYTVKTLEGTTV-PMSSLKNKVLMITNSASKCGLTKKHvDQMNRLHSVFNPLGLEILAFPTSQFLNQEFPNTKDI-- 94
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6016164   118 glkyVRPGGGFVPSFQLFEKGDVNGEKEQKVFSFLKHSCPHPSEILGTFKSISwdpvkvhdirWNFEKFLVGPDG 192
Cdd:PTZ00056  95 ----RKFNDKNKIKYNFFEPIEVNGENTHELFKFLKANCDSMHDENGTLKAIG----------WNFGKFLVNKSG 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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