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Conserved domains on  [gi|24647458|ref|NP_732147|]
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dihydrofolate reductase, isoform A [Drosophila melanogaster]

Protein Classification

dihydrofolate reductase( domain architecture ID 10082841)

dihydrofolate reductase (DHFR) is involved in the biosynthesis of deoxythymidine phosphate; it reduces 7,8-dihydrofolate to 5,6,7,8-tetrahydrofolate with NADPH as a cofactor

CATH:  3.40.430.10
EC:  1.5.1.3
SCOP:  4000755

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DHFR cd00209
Dihydrofolate reductase (DHFR). Reduces 7,8-dihydrofolate to 5,6,7,8-tetrahydrofolate with ...
4-179 7.12e-62

Dihydrofolate reductase (DHFR). Reduces 7,8-dihydrofolate to 5,6,7,8-tetrahydrofolate with NADPH as a cofactor. This is an essential step in the biosynthesis of deoxythymidine phosphate since 5,6,7,8-tetrahydrofolate is required to regenerate 5,10-methylenetetrahydrofolate which is then utilized by thymidylate synthase. Inhibition of DHFR interrupts thymidilate synthesis and DNA replication, inhibitors of DHFR (such as Methotrexate) are used in cancer chemotherapy. 5,6,7,8-tetrahydrofolate also is involved in glycine, serine, and threonine metabolism and aminoacyl-tRNA biosynthesis.


:

Pssm-ID: 238127 [Multi-domain]  Cd Length: 158  Bit Score: 188.50  E-value: 7.12e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647458   4 FNLIVAVCENFGIGIRGDLPWRIKSELKYFSRTTKRtsdptkqNAVVMGRKTYFGVPesKRPLPDRLNIVLSTTLQESDL 83
Cdd:cd00209   1 ISLIVAVDENGVIGKDNKLPWHLPEDLKHFKKTTTG-------NPVIMGRKTFESIP--RRPLPGRTNIVLSRQLDYQDA 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647458  84 PkGVLLCPNLETAMKILEeqNEVENIWIVGGSGVYEEAMasPRCHRLYITKIMQKFDCDTFFPAI-PDSFREVAPDsdmp 162
Cdd:cd00209  72 E-GVEVVHSLEEALELAE--NTVEEIFVIGGAEIYKQAL--PYADRLYLTRIHAEFEGDTFFPEIdESEWELVSEE---- 142
                       170
                ....*....|....*..
gi 24647458 163 lGVQEENGIKFEYKILE 179
Cdd:cd00209 143 -EVFEEDGYSYTFETYE 158
 
Name Accession Description Interval E-value
DHFR cd00209
Dihydrofolate reductase (DHFR). Reduces 7,8-dihydrofolate to 5,6,7,8-tetrahydrofolate with ...
4-179 7.12e-62

Dihydrofolate reductase (DHFR). Reduces 7,8-dihydrofolate to 5,6,7,8-tetrahydrofolate with NADPH as a cofactor. This is an essential step in the biosynthesis of deoxythymidine phosphate since 5,6,7,8-tetrahydrofolate is required to regenerate 5,10-methylenetetrahydrofolate which is then utilized by thymidylate synthase. Inhibition of DHFR interrupts thymidilate synthesis and DNA replication, inhibitors of DHFR (such as Methotrexate) are used in cancer chemotherapy. 5,6,7,8-tetrahydrofolate also is involved in glycine, serine, and threonine metabolism and aminoacyl-tRNA biosynthesis.


Pssm-ID: 238127 [Multi-domain]  Cd Length: 158  Bit Score: 188.50  E-value: 7.12e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647458   4 FNLIVAVCENFGIGIRGDLPWRIKSELKYFSRTTKRtsdptkqNAVVMGRKTYFGVPesKRPLPDRLNIVLSTTLQESDL 83
Cdd:cd00209   1 ISLIVAVDENGVIGKDNKLPWHLPEDLKHFKKTTTG-------NPVIMGRKTFESIP--RRPLPGRTNIVLSRQLDYQDA 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647458  84 PkGVLLCPNLETAMKILEeqNEVENIWIVGGSGVYEEAMasPRCHRLYITKIMQKFDCDTFFPAI-PDSFREVAPDsdmp 162
Cdd:cd00209  72 E-GVEVVHSLEEALELAE--NTVEEIFVIGGAEIYKQAL--PYADRLYLTRIHAEFEGDTFFPEIdESEWELVSEE---- 142
                       170
                ....*....|....*..
gi 24647458 163 lGVQEENGIKFEYKILE 179
Cdd:cd00209 143 -EVFEEDGYSYTFETYE 158
PTZ00164 PTZ00164
bifunctional dihydrofolate reductase-thymidylate synthase; Provisional
4-181 6.32e-61

bifunctional dihydrofolate reductase-thymidylate synthase; Provisional


Pssm-ID: 240299 [Multi-domain]  Cd Length: 514  Bit Score: 196.82  E-value: 6.32e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647458    4 FNLIVAVCENFGIGIRGDLPWRIKSELKYFSRTTKRT------SDPTKQNAVVMGRKTYFGVPESKRPLPDRLNIVLSTT 77
Cdd:PTZ00164  10 FSIVVAVTLKRGIGIGNSLPWHIPEDMKFFSKITTYVreekyeKSPKKQNAVIMGRKTWESIPKKFRPLKNRINVVLSRT 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647458   78 LQESDLPKGVLLCPNLETAMKILEEQNEVENIWIVGGSGVYEEAMASPRCHRLYITKIMQKFDCDTFFPAIPDSFREVAP 157
Cdd:PTZ00164  90 LTEEEADPGVLVFGSLEDALRLLAEDLSIEKIFIIGGASVYREALSANLLDKIYLTRVNSEYECDVFFPKIPESFFIVAI 169
                        170       180
                 ....*....|....*....|....
gi 24647458  158 DSDmplgVQEENGIKFEYKILEKH 181
Cdd:PTZ00164 170 VSQ----TFSTNGTSYDFVIYEKK 189
DHFR_1 pfam00186
Dihydrofolate reductase;
3-180 4.59e-47

Dihydrofolate reductase;


Pssm-ID: 425512 [Multi-domain]  Cd Length: 159  Bit Score: 151.16  E-value: 4.59e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647458     3 RFNLIVAVCENFGIGIRGDLPWRIKSELKYFSRTtkrtsdpTKQNAVVMGRKTYfgvpES-KRPLPDRLNIVLSTtlQES 81
Cdd:pfam00186   1 MISLIAAMDENGVIGKDNDLPWHLPADLKHFKKL-------TTGKPVIMGRKTF----ESiGRPLPGRKNIVLTR--NPD 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647458    82 DLPKGVLLCPNLETAMKILEEQNEvenIWIVGGSGVYEEAMasPRCHRLYITKIMQKFDCDTFFPAI-PDSFREVA---P 157
Cdd:pfam00186  68 YKVDGVEVVHSLEEALALAAEAEE---IFIIGGAEIYAQAL--PLADRLYITEIDAEFDGDTFFPEIdPSEWQLVSreeH 142
                         170       180
                  ....*....|....*....|...
gi 24647458   158 DSDmplgvqEENGIKFEYKILEK 180
Cdd:pfam00186 143 EAD------EKNPYPYTFVTYER 159
FolA COG0262
Dihydrofolate reductase [Coenzyme transport and metabolism]; Dihydrofolate reductase is part ...
6-160 1.86e-30

Dihydrofolate reductase [Coenzyme transport and metabolism]; Dihydrofolate reductase is part of the Pathway/BioSystem: Folate biosynthesis


Pssm-ID: 440032 [Multi-domain]  Cd Length: 168  Bit Score: 108.79  E-value: 1.86e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647458   6 LIVAVCENFGIGIR-GDLPWRIKSE--LKYFSRTTKRTSdptkqnAVVMGRKTY--FGVPESKRPLPDRLNIVLSTTLQE 80
Cdd:COG0262   5 LIVAVSLDGVIGGPdGDLPWLFPDPedLAHFKELTAGAD------AVLMGRKTYesIAGYWPTRPLPGRPKIVLSRTLDE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647458  81 SDLPKGVLLCPNLETAMKILEEQNEvENIWIVGGSGVYEEAMASPRCHRLYITKIMQKF-DCDTFFPAI--PDSFREVAP 157
Cdd:COG0262  79 ADWEGVTVVSGDLEEALAALKAAGG-KDIWVIGGGELYRQLLPAGLVDELYLTVVPVVLgEGDRLFPELdaPSRLELVES 157

                ...
gi 24647458 158 DSD 160
Cdd:COG0262 158 EAD 160
dihyfolred_HdrA_Halo NF041386
dihydrofolate reductase HdrA;
9-147 3.07e-11

dihydrofolate reductase HdrA;


Pssm-ID: 469277 [Multi-domain]  Cd Length: 158  Bit Score: 58.43  E-value: 3.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647458    9 AVCENFGIGIRGDLPWRIKSELKYFSRttKRTSDPTkqnaVVMGRKTYfgvpESKRP-LPDRLNIVLSTTLQESDLPKgV 87
Cdd:NF041386   8 AVAENGVIGRDGELPWPSIPADKRQYR--ERVADDP----VILGRRTF----ESMRDdLPGSAQIVLSRSEREFDVET-A 76
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647458   88 LLCPNLETAMKILEEQnEVENIWIVGGSGVYEeaMASPRCHRLYITKIMQKFDCDTFFPA 147
Cdd:NF041386  77 HHAGGVDEAIEIAESL-GAERAYVLGGAAIYE--LFQPHVDRMVLSRVPGEYEGDAYYPE 133
trim_DfrL NF041668
trimethoprim-resistant dihydrofolate reductase DfrL;
16-152 1.46e-07

trimethoprim-resistant dihydrofolate reductase DfrL;


Pssm-ID: 469550 [Multi-domain]  Cd Length: 176  Bit Score: 48.88  E-value: 1.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647458   16 IGIRGDLPWRIKSELKYFsrttkrtSDPTKQNAVVMGRKTYFGVPesKRPLPDRLNIVLSTTLqeSDLPKGVLLCPNLET 95
Cdd:NF041668  30 FGNSGDDDVNLMGDKKHE-------KIPTMDDKNRIGIKLTENIP--VRADGAIICHSKEDNK--NYLADGAIECHIHED 98
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 24647458   96 AMKILEEQNEVENIWIVGgsGVYEEAMASPRCHRLYITKIMQKFDCDTFFPAIPDSF 152
Cdd:NF041668  99 GGISAFEMFIDEPIHLHG--GIIAEEFEGDEVMIEHDTIIDECFDGADGMPDEDNKY 153
 
Name Accession Description Interval E-value
DHFR cd00209
Dihydrofolate reductase (DHFR). Reduces 7,8-dihydrofolate to 5,6,7,8-tetrahydrofolate with ...
4-179 7.12e-62

Dihydrofolate reductase (DHFR). Reduces 7,8-dihydrofolate to 5,6,7,8-tetrahydrofolate with NADPH as a cofactor. This is an essential step in the biosynthesis of deoxythymidine phosphate since 5,6,7,8-tetrahydrofolate is required to regenerate 5,10-methylenetetrahydrofolate which is then utilized by thymidylate synthase. Inhibition of DHFR interrupts thymidilate synthesis and DNA replication, inhibitors of DHFR (such as Methotrexate) are used in cancer chemotherapy. 5,6,7,8-tetrahydrofolate also is involved in glycine, serine, and threonine metabolism and aminoacyl-tRNA biosynthesis.


Pssm-ID: 238127 [Multi-domain]  Cd Length: 158  Bit Score: 188.50  E-value: 7.12e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647458   4 FNLIVAVCENFGIGIRGDLPWRIKSELKYFSRTTKRtsdptkqNAVVMGRKTYFGVPesKRPLPDRLNIVLSTTLQESDL 83
Cdd:cd00209   1 ISLIVAVDENGVIGKDNKLPWHLPEDLKHFKKTTTG-------NPVIMGRKTFESIP--RRPLPGRTNIVLSRQLDYQDA 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647458  84 PkGVLLCPNLETAMKILEeqNEVENIWIVGGSGVYEEAMasPRCHRLYITKIMQKFDCDTFFPAI-PDSFREVAPDsdmp 162
Cdd:cd00209  72 E-GVEVVHSLEEALELAE--NTVEEIFVIGGAEIYKQAL--PYADRLYLTRIHAEFEGDTFFPEIdESEWELVSEE---- 142
                       170
                ....*....|....*..
gi 24647458 163 lGVQEENGIKFEYKILE 179
Cdd:cd00209 143 -EVFEEDGYSYTFETYE 158
PTZ00164 PTZ00164
bifunctional dihydrofolate reductase-thymidylate synthase; Provisional
4-181 6.32e-61

bifunctional dihydrofolate reductase-thymidylate synthase; Provisional


Pssm-ID: 240299 [Multi-domain]  Cd Length: 514  Bit Score: 196.82  E-value: 6.32e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647458    4 FNLIVAVCENFGIGIRGDLPWRIKSELKYFSRTTKRT------SDPTKQNAVVMGRKTYFGVPESKRPLPDRLNIVLSTT 77
Cdd:PTZ00164  10 FSIVVAVTLKRGIGIGNSLPWHIPEDMKFFSKITTYVreekyeKSPKKQNAVIMGRKTWESIPKKFRPLKNRINVVLSRT 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647458   78 LQESDLPKGVLLCPNLETAMKILEEQNEVENIWIVGGSGVYEEAMASPRCHRLYITKIMQKFDCDTFFPAIPDSFREVAP 157
Cdd:PTZ00164  90 LTEEEADPGVLVFGSLEDALRLLAEDLSIEKIFIIGGASVYREALSANLLDKIYLTRVNSEYECDVFFPKIPESFFIVAI 169
                        170       180
                 ....*....|....*....|....
gi 24647458  158 DSDmplgVQEENGIKFEYKILEKH 181
Cdd:PTZ00164 170 VSQ----TFSTNGTSYDFVIYEKK 189
DHFR_1 pfam00186
Dihydrofolate reductase;
3-180 4.59e-47

Dihydrofolate reductase;


Pssm-ID: 425512 [Multi-domain]  Cd Length: 159  Bit Score: 151.16  E-value: 4.59e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647458     3 RFNLIVAVCENFGIGIRGDLPWRIKSELKYFSRTtkrtsdpTKQNAVVMGRKTYfgvpES-KRPLPDRLNIVLSTtlQES 81
Cdd:pfam00186   1 MISLIAAMDENGVIGKDNDLPWHLPADLKHFKKL-------TTGKPVIMGRKTF----ESiGRPLPGRKNIVLTR--NPD 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647458    82 DLPKGVLLCPNLETAMKILEEQNEvenIWIVGGSGVYEEAMasPRCHRLYITKIMQKFDCDTFFPAI-PDSFREVA---P 157
Cdd:pfam00186  68 YKVDGVEVVHSLEEALALAAEAEE---IFIIGGAEIYAQAL--PLADRLYITEIDAEFDGDTFFPEIdPSEWQLVSreeH 142
                         170       180
                  ....*....|....*....|...
gi 24647458   158 DSDmplgvqEENGIKFEYKILEK 180
Cdd:pfam00186 143 EAD------EKNPYPYTFVTYER 159
FolA COG0262
Dihydrofolate reductase [Coenzyme transport and metabolism]; Dihydrofolate reductase is part ...
6-160 1.86e-30

Dihydrofolate reductase [Coenzyme transport and metabolism]; Dihydrofolate reductase is part of the Pathway/BioSystem: Folate biosynthesis


Pssm-ID: 440032 [Multi-domain]  Cd Length: 168  Bit Score: 108.79  E-value: 1.86e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647458   6 LIVAVCENFGIGIR-GDLPWRIKSE--LKYFSRTTKRTSdptkqnAVVMGRKTY--FGVPESKRPLPDRLNIVLSTTLQE 80
Cdd:COG0262   5 LIVAVSLDGVIGGPdGDLPWLFPDPedLAHFKELTAGAD------AVLMGRKTYesIAGYWPTRPLPGRPKIVLSRTLDE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647458  81 SDLPKGVLLCPNLETAMKILEEQNEvENIWIVGGSGVYEEAMASPRCHRLYITKIMQKF-DCDTFFPAI--PDSFREVAP 157
Cdd:COG0262  79 ADWEGVTVVSGDLEEALAALKAAGG-KDIWVIGGGELYRQLLPAGLVDELYLTVVPVVLgEGDRLFPELdaPSRLELVES 157

                ...
gi 24647458 158 DSD 160
Cdd:COG0262 158 EAD 160
folA PRK10769
type 3 dihydrofolate reductase;
6-180 1.14e-20

type 3 dihydrofolate reductase;


Pssm-ID: 182714 [Multi-domain]  Cd Length: 159  Bit Score: 83.64  E-value: 1.14e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647458    6 LIVAVCENFGIGIRGDLPWRIKSELKYFSRTTkrTSDPtkqnaVVMGRKTYfgvpES-KRPLPDRLNIVLSTTLQESDlp 84
Cdd:PRK10769   4 LIAALAVDRVIGMENAMPWNLPADLAWFKRNT--LNKP-----VIMGRHTW----ESiGRPLPGRKNIVISSQPGTDD-- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647458   85 kGVLLCPNLETAmkiLEEQNEVENIWIVGGSGVYEEAMasPRCHRLYITKIMQKFDCDTFFPAI-PDSFREVAP---DSD 160
Cdd:PRK10769  71 -RVTWVKSVDEA---LAAAGDVPEIMVIGGGRVYEQFL--PKAQRLYLTHIDAEVEGDTHFPDYePDEWESVFSefhDAD 144
                        170       180
                 ....*....|....*....|
gi 24647458  161 mplgvqEENGIKFEYKILEK 180
Cdd:PRK10769 145 ------EQNSHSYCFEILER 158
dihyfolred_HdrA_Halo NF041386
dihydrofolate reductase HdrA;
9-147 3.07e-11

dihydrofolate reductase HdrA;


Pssm-ID: 469277 [Multi-domain]  Cd Length: 158  Bit Score: 58.43  E-value: 3.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647458    9 AVCENFGIGIRGDLPWRIKSELKYFSRttKRTSDPTkqnaVVMGRKTYfgvpESKRP-LPDRLNIVLSTTLQESDLPKgV 87
Cdd:NF041386   8 AVAENGVIGRDGELPWPSIPADKRQYR--ERVADDP----VILGRRTF----ESMRDdLPGSAQIVLSRSEREFDVET-A 76
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647458   88 LLCPNLETAMKILEEQnEVENIWIVGGSGVYEeaMASPRCHRLYITKIMQKFDCDTFFPA 147
Cdd:NF041386  77 HHAGGVDEAIEIAESL-GAERAYVLGGAAIYE--LFQPHVDRMVLSRVPGEYEGDAYYPE 133
trim_DfrL NF041668
trimethoprim-resistant dihydrofolate reductase DfrL;
16-152 1.46e-07

trimethoprim-resistant dihydrofolate reductase DfrL;


Pssm-ID: 469550 [Multi-domain]  Cd Length: 176  Bit Score: 48.88  E-value: 1.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647458   16 IGIRGDLPWRIKSELKYFsrttkrtSDPTKQNAVVMGRKTYFGVPesKRPLPDRLNIVLSTTLqeSDLPKGVLLCPNLET 95
Cdd:NF041668  30 FGNSGDDDVNLMGDKKHE-------KIPTMDDKNRIGIKLTENIP--VRADGAIICHSKEDNK--NYLADGAIECHIHED 98
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 24647458   96 AMKILEEQNEVENIWIVGgsGVYEEAMASPRCHRLYITKIMQKFDCDTFFPAIPDSF 152
Cdd:NF041668  99 GGISAFEMFIDEPIHLHG--GIIAEEFEGDEVMIEHDTIIDECFDGADGMPDEDNKY 153
scpA PRK00478
segregation and condensation protein ScpA;
13-152 6.61e-07

segregation and condensation protein ScpA;


Pssm-ID: 234776 [Multi-domain]  Cd Length: 505  Bit Score: 48.39  E-value: 6.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647458   13 NFGIGIRGDLPWRIKSELKYFSRTtkrtsdpTKQNAVVMGRKTYFgvpESKRPLPDRLNIVLSTTLQESDLPKGVLLCPN 92
Cdd:PRK00478  11 NFGIAKNNQIPWKIDEELNHFHQT-------TTNHTIVMGYNTFQ---AMNKILANQANIVISKKHQRELKNNNELFVFN 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647458   93 letAMKILEEQNEVENIWIVGGSGVYEEAMAspRCHRLYITKIMQKFDCDTFFPAIPDSF 152
Cdd:PRK00478  81 ---DLKKLLIDFSNVDLFIIGGKKTIEQFIK--YADQLIISKLNADYKCDLFVNLNYDDF 135
 
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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