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Conserved domains on  [gi|1768712444|ref|XP_031326174|]
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glutathione peroxidase 1 [Camelus dromedarius]

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 ...
18-195 1.83e-72

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: 216.23  E-value: 1.83e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768712444  18 TVYTFSARPLaGGEPVSLGSLRGKVLLIENVASLUGTTvRDYTQLNELQRRLGPRGLVVLGFPCNQFGYQENAKNEEILN 97
Cdd:cd00340     1 SIYDFSVKDI-DGEPVSLSKYKGKVLLIVNVASKCGFT-PQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768712444  98 CLKYVRPgggfePNFMLFEKCDVNGSKAHPLFSFLREALPTPsddatalmtdpkfitwspvCRNDVSWNFEKFLVGPDGV 177
Cdd:cd00340    79 FCETNYG-----VTFPMFAKIDVNGENAHPLYKYLKEEAPGL-------------------LGKDIKWNFTKFLVDRDGE 134
                         170
                  ....*....|....*...
gi 1768712444 178 PVRRYSRRFLTIDIEPDI 195
Cdd:cd00340   135 VVKRFAPTTDPEELEKDI 152
 
Name Accession Description Interval E-value
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
18-195 1.83e-72

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: 216.23  E-value: 1.83e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768712444  18 TVYTFSARPLaGGEPVSLGSLRGKVLLIENVASLUGTTvRDYTQLNELQRRLGPRGLVVLGFPCNQFGYQENAKNEEILN 97
Cdd:cd00340     1 SIYDFSVKDI-DGEPVSLSKYKGKVLLIVNVASKCGFT-PQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768712444  98 CLKYVRPgggfePNFMLFEKCDVNGSKAHPLFSFLREALPTPsddatalmtdpkfitwspvCRNDVSWNFEKFLVGPDGV 177
Cdd:cd00340    79 FCETNYG-----VTFPMFAKIDVNGENAHPLYKYLKEEAPGL-------------------LGKDIKWNFTKFLVDRDGE 134
                         170
                  ....*....|....*...
gi 1768712444 178 PVRRYSRRFLTIDIEPDI 195
Cdd:cd00340   135 VVKRFAPTTDPEELEKDI 152
GSHPx pfam00255
Glutathione peroxidase;
19-133 4.31e-59

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 181.01  E-value: 4.31e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768712444  19 VYTFSARPLAGgEPVSLGSLRGKVLLIENVASLUGTTVrDYTQLNELQRRLGPRGLVVLGFPCNQFGYQENAKNEEIlnc 98
Cdd:pfam00255   1 IYEFSAKDIDG-EPVPFDQYRGKVVLIVNVASKCGLTP-QYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEI--- 75
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1768712444  99 lKYVRPgGGFEPNFMLFEKCDVNGSKAHPLFSFLR 133
Cdd:pfam00255  76 -KYFCP-GGYGVTFPLFSKIEVNGEKAHPVYKFLK 108
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
18-199 4.67e-55

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


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 172.18  E-value: 4.67e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768712444  18 TVYTFSARPLaGGEPVSLGSLRGKVLLIENVASLUGTTvRDYTQLNELQRRLGPRGLVVLGFPCNQFGYQENAKNEEILN 97
Cdd:COG0386     3 SIYDFSVTTL-DGEPVSLSDYKGKVLLIVNTASKCGFT-PQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768712444  98 -C-LKY-VrpgggfepNFMLFEKCDVNGSKAHPLFSFLREALPTPSDDatalmtdpkfitwspvcrNDVSWNFEKFLVGP 174
Cdd:COG0386    81 fCsLNYgV--------TFPMFAKIDVNGPNAHPLYKYLKEEAPGLLGG------------------GDIKWNFTKFLIDR 134
                         170       180
                  ....*....|....*....|....*..
gi 1768712444 175 DGVPVRRYSRRF--LTIDIEPDIEALL 199
Cdd:COG0386   135 DGNVVARFAPTTkpEDPELEAAIEKLL 161
PLN02412 PLN02412
probable glutathione peroxidase
16-201 2.31e-37

probable glutathione peroxidase


Pssm-ID: 166053 [Multi-domain]  Cd Length: 167  Bit Score: 127.41  E-value: 2.31e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768712444  16 PRTVYTFSARPLaGGEPVSLGSLRGKVLLIENVASLUGTTVRDYTQLNELQRRLGPRGLVVLGFPCNQFGYQENAKNEEI 95
Cdd:PLN02412    6 PKSIYDFTVKDI-GGNDVSLNQYKGKVLLIVNVASKCGLTDSNYKELNVLYEKYKEQGFEILAFPCNQFLGQEPGSNEEI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768712444  96 LNCLKYVrpgggFEPNFMLFEKCDVNGSKAHPLFSFLREalptpsdDATALMTDPkfitwspvcrndVSWNFEKFLVGPD 175
Cdd:PLN02412   85 QQTVCTR-----FKAEFPIFDKVDVNGKNTAPLYKYLKA-------EKGGLFGDA------------IKWNFTKFLVSKE 140
                         170       180
                  ....*....|....*....|....*.
gi 1768712444 176 GVPVRRYSRRFLTIDIEPDIEALLSQ 201
Cdd:PLN02412  141 GKVVQRYAPTTSPLKIEKDIQNLLGQ 166
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
20-199 1.49e-31

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: 112.24  E-value: 1.49e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768712444  20 YTFSARPlAGGEPVSLGSLRGKVLLIENVASLUGTTVRDYTQLNELQRRLGPRGLVVLGFPCNQFGYQENAKNEEILNcl 99
Cdd:TIGR02540   3 YSFEVKD-ARGRTVSLEKYRGKVSLVVNVASECGFTDQNYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIES-- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768712444 100 kYVRPGGGFepNFMLFEKCDVNGSKAHPLFSFLREAlptpsddatalmtdpkfitwspvCRNDVSWNFEKFLVGPDGVPV 179
Cdd:TIGR02540  80 -FARRNYGV--TFPMFSKIKILGSEAEPAFRFLVDS-----------------------SKKEPRWNFWKYLVNPEGQVV 133
                         170       180
                  ....*....|....*....|
gi 1768712444 180 RRYSRRFLTIDIEPDIEALL 199
Cdd:TIGR02540 134 KFWRPEEPVEEIRPEITALV 153
 
Name Accession Description Interval E-value
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
18-195 1.83e-72

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: 216.23  E-value: 1.83e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768712444  18 TVYTFSARPLaGGEPVSLGSLRGKVLLIENVASLUGTTvRDYTQLNELQRRLGPRGLVVLGFPCNQFGYQENAKNEEILN 97
Cdd:cd00340     1 SIYDFSVKDI-DGEPVSLSKYKGKVLLIVNVASKCGFT-PQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768712444  98 CLKYVRPgggfePNFMLFEKCDVNGSKAHPLFSFLREALPTPsddatalmtdpkfitwspvCRNDVSWNFEKFLVGPDGV 177
Cdd:cd00340    79 FCETNYG-----VTFPMFAKIDVNGENAHPLYKYLKEEAPGL-------------------LGKDIKWNFTKFLVDRDGE 134
                         170
                  ....*....|....*...
gi 1768712444 178 PVRRYSRRFLTIDIEPDI 195
Cdd:cd00340   135 VVKRFAPTTDPEELEKDI 152
GSHPx pfam00255
Glutathione peroxidase;
19-133 4.31e-59

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 181.01  E-value: 4.31e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768712444  19 VYTFSARPLAGgEPVSLGSLRGKVLLIENVASLUGTTVrDYTQLNELQRRLGPRGLVVLGFPCNQFGYQENAKNEEIlnc 98
Cdd:pfam00255   1 IYEFSAKDIDG-EPVPFDQYRGKVVLIVNVASKCGLTP-QYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEI--- 75
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1768712444  99 lKYVRPgGGFEPNFMLFEKCDVNGSKAHPLFSFLR 133
Cdd:pfam00255  76 -KYFCP-GGYGVTFPLFSKIEVNGEKAHPVYKFLK 108
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
18-199 4.67e-55

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


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 172.18  E-value: 4.67e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768712444  18 TVYTFSARPLaGGEPVSLGSLRGKVLLIENVASLUGTTvRDYTQLNELQRRLGPRGLVVLGFPCNQFGYQENAKNEEILN 97
Cdd:COG0386     3 SIYDFSVTTL-DGEPVSLSDYKGKVLLIVNTASKCGFT-PQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768712444  98 -C-LKY-VrpgggfepNFMLFEKCDVNGSKAHPLFSFLREALPTPSDDatalmtdpkfitwspvcrNDVSWNFEKFLVGP 174
Cdd:COG0386    81 fCsLNYgV--------TFPMFAKIDVNGPNAHPLYKYLKEEAPGLLGG------------------GDIKWNFTKFLIDR 134
                         170       180
                  ....*....|....*....|....*..
gi 1768712444 175 DGVPVRRYSRRF--LTIDIEPDIEALL 199
Cdd:COG0386   135 DGNVVARFAPTTkpEDPELEAAIEKLL 161
PLN02412 PLN02412
probable glutathione peroxidase
16-201 2.31e-37

probable glutathione peroxidase


Pssm-ID: 166053 [Multi-domain]  Cd Length: 167  Bit Score: 127.41  E-value: 2.31e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768712444  16 PRTVYTFSARPLaGGEPVSLGSLRGKVLLIENVASLUGTTVRDYTQLNELQRRLGPRGLVVLGFPCNQFGYQENAKNEEI 95
Cdd:PLN02412    6 PKSIYDFTVKDI-GGNDVSLNQYKGKVLLIVNVASKCGLTDSNYKELNVLYEKYKEQGFEILAFPCNQFLGQEPGSNEEI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768712444  96 LNCLKYVrpgggFEPNFMLFEKCDVNGSKAHPLFSFLREalptpsdDATALMTDPkfitwspvcrndVSWNFEKFLVGPD 175
Cdd:PLN02412   85 QQTVCTR-----FKAEFPIFDKVDVNGKNTAPLYKYLKA-------EKGGLFGDA------------IKWNFTKFLVSKE 140
                         170       180
                  ....*....|....*....|....*.
gi 1768712444 176 GVPVRRYSRRFLTIDIEPDIEALLSQ 201
Cdd:PLN02412  141 GKVVQRYAPTTSPLKIEKDIQNLLGQ 166
PTZ00256 PTZ00256
glutathione peroxidase; Provisional
18-201 6.10e-37

glutathione peroxidase; Provisional


Pssm-ID: 173495 [Multi-domain]  Cd Length: 183  Bit Score: 126.80  E-value: 6.10e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768712444  18 TVYTFSARPLAGGEpVSLGSLRG-KVLLIENVASLUGTTVRDYTQLNELQRRLGPRGLVVLGFPCNQFGYQENAKNEEIL 96
Cdd:PTZ00256   19 SFFEFEAIDIDGQL-VQLSKFKGkKAIIVVNVACKCGLTSDHYTQLVELYKQYKSQGLEILAFPCNQFMEQEPWDEPEIK 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768712444  97 NclkYVRPggGFEPNFMLFEKCDVNGSKAHPLFSFLRealptpsddatalMTDPKFITWSPVCRnDVSWNFEKFLVGPDG 176
Cdd:PTZ00256   98 E---YVQK--KFNVDFPLFQKIEVNGENTHEIYKYLR-------------RNSELFQNNTNEAR-QIPWNFAKFLIDGQG 158
                         170       180
                  ....*....|....*....|....*
gi 1768712444 177 VPVRRYSRRFLTIDIEPDIEALLSQ 201
Cdd:PTZ00256  159 KVVKYFSPKVNPNEMIQDIEKLLNA 183
btuE PRK10606
putative glutathione peroxidase; Provisional
30-183 1.62e-34

putative glutathione peroxidase; Provisional


Pssm-ID: 182585 [Multi-domain]  Cd Length: 183  Bit Score: 120.65  E-value: 1.62e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768712444  30 GEPVSLGSLRGKVLLIENVASLUGTTvRDYTQLNELQRRLGPRGLVVLGFPCNQFGYQENAKNEEIlncLKYVRpgGGFE 109
Cdd:PRK10606   15 GEVTTLEKYAGNVLLIVNVASKCGLT-PQYEQLENIQKAWADQGFVVLGFPCNQFLGQEPGSDEEI---KTYCR--TTWG 88
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1768712444 110 PNFMLFEKCDVNGSKAHPLFSFLREALPTP-----SDDATALMTDPKfitwSPVCRNDVSWNFEKFLVGPDGVPVRRYS 183
Cdd:PRK10606   89 VTFPMFSKIEVNGEGRHPLYQKLIAAAPTAvapeeSGFYARMVSKGR----APLYPDDILWNFEKFLVGRDGQVIQRFS 163
PLN02399 PLN02399
phospholipid hydroperoxide glutathione peroxidase
17-200 6.78e-32

phospholipid hydroperoxide glutathione peroxidase


Pssm-ID: 178021 [Multi-domain]  Cd Length: 236  Bit Score: 115.38  E-value: 6.78e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768712444  17 RTVYTFSARPLAGGEpVSLGSLRGKVLLIENVASLUGTTVRDYTQLNELQRRLGPRGLVVLGFPCNQFGYQENAKNEEIL 96
Cdd:PLN02399   77 KSVHDFTVKDIDGKD-VALSKFKGKVLLIVNVASKCGLTSSNYSELSHLYEKYKTQGFEILAFPCNQFGGQEPGSNPEIK 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768712444  97 N--CLKyvrpgggFEPNFMLFEKCDVNGSKAHPLFSFLREalptpsdDATALMTDPkfitwspvcrndVSWNFEKFLVGP 174
Cdd:PLN02399  156 QfaCTR-------FKAEFPIFDKVDVNGPSTAPVYQFLKS-------NAGGFLGDL------------IKWNFEKFLVDK 209
                         170       180
                  ....*....|....*....|....*.
gi 1768712444 175 DGVPVRRYSRRFLTIDIEPDIEALLS 200
Cdd:PLN02399  210 NGKVVERYPPTTSPFQIEKDIQKLLA 235
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
20-199 1.49e-31

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: 112.24  E-value: 1.49e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768712444  20 YTFSARPlAGGEPVSLGSLRGKVLLIENVASLUGTTVRDYTQLNELQRRLGPRGLVVLGFPCNQFGYQENAKNEEILNcl 99
Cdd:TIGR02540   3 YSFEVKD-ARGRTVSLEKYRGKVSLVVNVASECGFTDQNYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIES-- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768712444 100 kYVRPGGGFepNFMLFEKCDVNGSKAHPLFSFLREAlptpsddatalmtdpkfitwspvCRNDVSWNFEKFLVGPDGVPV 179
Cdd:TIGR02540  80 -FARRNYGV--TFPMFSKIKILGSEAEPAFRFLVDS-----------------------SKKEPRWNFWKYLVNPEGQVV 133
                         170       180
                  ....*....|....*....|
gi 1768712444 180 RRYSRRFLTIDIEPDIEALL 199
Cdd:TIGR02540 134 KFWRPEEPVEEIRPEITALV 153
PTZ00056 PTZ00056
glutathione peroxidase; Provisional
17-199 5.36e-31

glutathione peroxidase; Provisional


Pssm-ID: 240248 [Multi-domain]  Cd Length: 199  Bit Score: 112.25  E-value: 5.36e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768712444  17 RTVYTFSARPLAGgEPVSLGSLRGKVLLIENVASLUGTTVRDYTQLNELQRRLGPRGLVVLGFPCNQFGYQENAKNEEIL 96
Cdd:PTZ00056   17 KSIYDYTVKTLEG-TTVPMSSLKNKVLMITNSASKCGLTKKHVDQMNRLHSVFNPLGLEILAFPTSQFLNQEFPNTKDIR 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768712444  97 NCLKyvrpggGFEPNFMLFEKCDVNGSKAHPLFSFLREALPTPSDDATALmtdpkfitwspvcrNDVSWNFEKFLVGPDG 176
Cdd:PTZ00056   96 KFND------KNKIKYNFFEPIEVNGENTHELFKFLKANCDSMHDENGTL--------------KAIGWNFGKFLVNKSG 155
                         170       180
                  ....*....|....*....|...
gi 1768712444 177 VPVRRYSRRFLTIDIEPDIEALL 199
Cdd:PTZ00056  156 NVVAYFSPRTEPLELEKKIAELL 178
 
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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