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Conserved domains on  [gi|487657633|ref|WP_001749985|]
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MULTISPECIES: trimethoprim-resistant dihydrofolate reductase DfrA27 [Bacteria]

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 ...
3-155 5.95e-52

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: 162.31  E-value: 5.95e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487657633   3 ISLMAAKARNGVIGCGSDIPWNAKGEQLLFKAITYNQWLLVGRKTFEAMG--ALPNRKYAVVSRSGSVATNDDVVVFPSI 80
Cdd:cd00209    1 ISLIVAVDENGVIGKDNKLPWHLPEDLKHFKKTTTGNPVIMGRKTFESIPrrPLPGRTNIVLSRQLDYQDAEGVEVVHSL 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 487657633  81 EAAMRELKTLTNHVVVSGGGEIYKSLIAHADTLHISTIDSEPEGNVFFPEI-PKEFNVVFEQEFHSNINYRY--QIWQ 155
Cdd:cd00209   81 EEALELAENTVEEIFVIGGAEIYKQALPYADRLYLTRIHAEFEGDTFFPEIdESEWELVSEEEVFEEDGYSYtfETYE 158
 
Name Accession Description Interval E-value
DHFR cd00209
Dihydrofolate reductase (DHFR). Reduces 7,8-dihydrofolate to 5,6,7,8-tetrahydrofolate with ...
3-155 5.95e-52

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: 162.31  E-value: 5.95e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487657633   3 ISLMAAKARNGVIGCGSDIPWNAKGEQLLFKAITYNQWLLVGRKTFEAMG--ALPNRKYAVVSRSGSVATNDDVVVFPSI 80
Cdd:cd00209    1 ISLIVAVDENGVIGKDNKLPWHLPEDLKHFKKTTTGNPVIMGRKTFESIPrrPLPGRTNIVLSRQLDYQDAEGVEVVHSL 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 487657633  81 EAAMRELKTLTNHVVVSGGGEIYKSLIAHADTLHISTIDSEPEGNVFFPEI-PKEFNVVFEQEFHSNINYRY--QIWQ 155
Cdd:cd00209   81 EEALELAENTVEEIFVIGGAEIYKQALPYADRLYLTRIHAEFEGDTFFPEIdESEWELVSEEEVFEEDGYSYtfETYE 158
DHFR_1 pfam00186
Dihydrofolate reductase;
2-156 1.41e-46

Dihydrofolate reductase;


Pssm-ID: 425512 [Multi-domain]  Cd Length: 159  Bit Score: 148.85  E-value: 1.41e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487657633    2 KISLMAAKARNGVIGCGSDIPWNAKGEQLLFKAITYNQWLLVGRKTFEAMG-ALPNRKYAVVSRSGSvATNDDVVVFPSI 80
Cdd:pfam00186   1 MISLIAAMDENGVIGKDNDLPWHLPADLKHFKKLTTGKPVIMGRKTFESIGrPLPGRKNIVLTRNPD-YKVDGVEVVHSL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487657633   81 EAAMRELKTlTNHVVVSGGGEIYKSLIAHADTLHISTIDSEPEGNVFFPEI-PKEFNVVFEQEFHSN----INYRYQIWQ 155
Cdd:pfam00186  80 EEALALAAE-AEEIFIIGGAEIYAQALPLADRLYITEIDAEFDGDTFFPEIdPSEWQLVSREEHEADeknpYPYTFVTYE 158

                  .
gi 487657633  156 R 156
Cdd:pfam00186 159 R 159
FolA COG0262
Dihydrofolate reductase [Coenzyme transport and metabolism]; Dihydrofolate reductase is part ...
1-151 4.99e-26

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: 96.85  E-value: 4.99e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487657633   1 MKISLMAAKARNGVIG-CGSDIPWNAKGEQLL--FKAITYN-QWLLVGRKTFEAMGA------LPNRKYAVVSRSGSVAT 70
Cdd:COG0262    1 RKLILIVAVSLDGVIGgPDGDLPWLFPDPEDLahFKELTAGaDAVLMGRKTYESIAGywptrpLPGRPKIVLSRTLDEAD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487657633  71 NDDVVVFP-SIEAAMRELKTLT-NHVVVSGGGEIYKSLIAH--ADTLHISTIDSEP-EGNVFFPEI--PKEFNVVFEQEF 143
Cdd:COG0262   81 WEGVTVVSgDLEEALAALKAAGgKDIWVIGGGELYRQLLPAglVDELYLTVVPVVLgEGDRLFPELdaPSRLELVESEAD 160

                 ....*...
gi 487657633 144 HSNINYRY 151
Cdd:COG0262  161 SGFVHLTY 168
folA PRK10769
type 3 dihydrofolate reductase;
3-156 7.33e-25

type 3 dihydrofolate reductase;


Pssm-ID: 182714 [Multi-domain]  Cd Length: 159  Bit Score: 93.65  E-value: 7.33e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487657633   3 ISLMAAKARNGVIGCGSDIPWNAKGEQLLFKAITYNQWLLVGRKTFEAMG-ALPNRKYAVVSRSGsvATNDDVVVFPSIE 81
Cdd:PRK10769   2 ISLIAALAVDRVIGMENAMPWNLPADLAWFKRNTLNKPVIMGRHTWESIGrPLPGRKNIVISSQP--GTDDRVTWVKSVD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487657633  82 AAMrELKTLTNHVVVSGGGEIYKSLIAHADTLHISTIDSEPEGNVFFPEI-PKEFNVVFeQEFH-----SNINYRYQIWQ 155
Cdd:PRK10769  80 EAL-AAAGDVPEIMVIGGGRVYEQFLPKAQRLYLTHIDAEVEGDTHFPDYePDEWESVF-SEFHdadeqNSHSYCFEILE 157

                 .
gi 487657633 156 R 156
Cdd:PRK10769 158 R 158
dihyfolred_HdrA_Halo NF041386
dihydrofolate reductase HdrA;
1-156 5.47e-16

dihydrofolate reductase HdrA;


Pssm-ID: 469277 [Multi-domain]  Cd Length: 158  Bit Score: 70.37  E-value: 5.47e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487657633   1 MKISLMAAKARNGVIGCGSDIPWN---AKGEQllFKAITYNQWLLVGRKTFEAMGA-LPNRKYAVVSRSGSVATNDDVVV 76
Cdd:NF041386   1 MELVSVAAVAENGVIGRDGELPWPsipADKRQ--YRERVADDPVILGRRTFESMRDdLPGSAQIVLSRSEREFDVETAHH 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487657633  77 FPSIEAAMRELKTL-TNHVVVSGGGEIYKSLIAHADTLHISTIDSEPEGNVFFPEI-PKEFNVVFEQEFHsniNYRYQIW 154
Cdd:NF041386  79 AGGVDEAIEIAESLgAERAYVLGGAAIYELFQPHVDRMVLSRVPGEYEGDAYYPEWdEDEWELVEETEYD---GFTLEEW 155

                 ..
gi 487657633 155 QR 156
Cdd:NF041386 156 VR 157
trim_DfrL NF041668
trimethoprim-resistant dihydrofolate reductase DfrL;
12-151 2.59e-06

trimethoprim-resistant dihydrofolate reductase DfrL;


Pssm-ID: 469550 [Multi-domain]  Cd Length: 176  Bit Score: 45.03  E-value: 2.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487657633  12 NGVIGCGSDIPWNAKGEQLLFKAITYNQWLLVGRKTFEAMGALP--NRKYAVVSRSGSVATnDDVVVFPSIEAAMRELK- 88
Cdd:NF041668  10 CGEIGKPGDLFVNAEDDMGHFGNSGDDDVNLMGDKKHEKIPTMDdkNRIGIKLTENIPVRA-DGAIICHSKEDNKNYLAd 88
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 487657633  89 -TLTNHVVVSGGGEIYKSLIAHADTLHISTIDSEPEGNVFFPEIPKEFNVVFE-QEFHSNINYRY 151
Cdd:NF041668  89 gAIECHIHEDGGISAFEMFIDEPIHLHGGIIAEEFEGDEVMIEHDTIIDECFDgADGMPDEDNKY 153
 
Name Accession Description Interval E-value
DHFR cd00209
Dihydrofolate reductase (DHFR). Reduces 7,8-dihydrofolate to 5,6,7,8-tetrahydrofolate with ...
3-155 5.95e-52

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: 162.31  E-value: 5.95e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487657633   3 ISLMAAKARNGVIGCGSDIPWNAKGEQLLFKAITYNQWLLVGRKTFEAMG--ALPNRKYAVVSRSGSVATNDDVVVFPSI 80
Cdd:cd00209    1 ISLIVAVDENGVIGKDNKLPWHLPEDLKHFKKTTTGNPVIMGRKTFESIPrrPLPGRTNIVLSRQLDYQDAEGVEVVHSL 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 487657633  81 EAAMRELKTLTNHVVVSGGGEIYKSLIAHADTLHISTIDSEPEGNVFFPEI-PKEFNVVFEQEFHSNINYRY--QIWQ 155
Cdd:cd00209   81 EEALELAENTVEEIFVIGGAEIYKQALPYADRLYLTRIHAEFEGDTFFPEIdESEWELVSEEEVFEEDGYSYtfETYE 158
DHFR_1 pfam00186
Dihydrofolate reductase;
2-156 1.41e-46

Dihydrofolate reductase;


Pssm-ID: 425512 [Multi-domain]  Cd Length: 159  Bit Score: 148.85  E-value: 1.41e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487657633    2 KISLMAAKARNGVIGCGSDIPWNAKGEQLLFKAITYNQWLLVGRKTFEAMG-ALPNRKYAVVSRSGSvATNDDVVVFPSI 80
Cdd:pfam00186   1 MISLIAAMDENGVIGKDNDLPWHLPADLKHFKKLTTGKPVIMGRKTFESIGrPLPGRKNIVLTRNPD-YKVDGVEVVHSL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487657633   81 EAAMRELKTlTNHVVVSGGGEIYKSLIAHADTLHISTIDSEPEGNVFFPEI-PKEFNVVFEQEFHSN----INYRYQIWQ 155
Cdd:pfam00186  80 EEALALAAE-AEEIFIIGGAEIYAQALPLADRLYITEIDAEFDGDTFFPEIdPSEWQLVSREEHEADeknpYPYTFVTYE 158

                  .
gi 487657633  156 R 156
Cdd:pfam00186 159 R 159
FolA COG0262
Dihydrofolate reductase [Coenzyme transport and metabolism]; Dihydrofolate reductase is part ...
1-151 4.99e-26

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: 96.85  E-value: 4.99e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487657633   1 MKISLMAAKARNGVIG-CGSDIPWNAKGEQLL--FKAITYN-QWLLVGRKTFEAMGA------LPNRKYAVVSRSGSVAT 70
Cdd:COG0262    1 RKLILIVAVSLDGVIGgPDGDLPWLFPDPEDLahFKELTAGaDAVLMGRKTYESIAGywptrpLPGRPKIVLSRTLDEAD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487657633  71 NDDVVVFP-SIEAAMRELKTLT-NHVVVSGGGEIYKSLIAH--ADTLHISTIDSEP-EGNVFFPEI--PKEFNVVFEQEF 143
Cdd:COG0262   81 WEGVTVVSgDLEEALAALKAAGgKDIWVIGGGELYRQLLPAglVDELYLTVVPVVLgEGDRLFPELdaPSRLELVESEAD 160

                 ....*...
gi 487657633 144 HSNINYRY 151
Cdd:COG0262  161 SGFVHLTY 168
folA PRK10769
type 3 dihydrofolate reductase;
3-156 7.33e-25

type 3 dihydrofolate reductase;


Pssm-ID: 182714 [Multi-domain]  Cd Length: 159  Bit Score: 93.65  E-value: 7.33e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487657633   3 ISLMAAKARNGVIGCGSDIPWNAKGEQLLFKAITYNQWLLVGRKTFEAMG-ALPNRKYAVVSRSGsvATNDDVVVFPSIE 81
Cdd:PRK10769   2 ISLIAALAVDRVIGMENAMPWNLPADLAWFKRNTLNKPVIMGRHTWESIGrPLPGRKNIVISSQP--GTDDRVTWVKSVD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487657633  82 AAMrELKTLTNHVVVSGGGEIYKSLIAHADTLHISTIDSEPEGNVFFPEI-PKEFNVVFeQEFH-----SNINYRYQIWQ 155
Cdd:PRK10769  80 EAL-AAAGDVPEIMVIGGGRVYEQFLPKAQRLYLTHIDAEVEGDTHFPDYePDEWESVF-SEFHdadeqNSHSYCFEILE 157

                 .
gi 487657633 156 R 156
Cdd:PRK10769 158 R 158
PTZ00164 PTZ00164
bifunctional dihydrofolate reductase-thymidylate synthase; Provisional
3-156 1.85e-22

bifunctional dihydrofolate reductase-thymidylate synthase; Provisional


Pssm-ID: 240299 [Multi-domain]  Cd Length: 514  Bit Score: 92.43  E-value: 1.85e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487657633   3 ISLMAAKARNGVIGCGSDIPWNAKGEQLLFKAITYN-------------QWLLVGRKTFEAMGA----LPNRKYAVVSRS 65
Cdd:PTZ00164  10 FSIVVAVTLKRGIGIGNSLPWHIPEDMKFFSKITTYvreekyekspkkqNAVIMGRKTWESIPKkfrpLKNRINVVLSRT 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487657633  66 GSVATNDD-VVVFPSIEAAMRELKTLTNH--VVVSGGGEIYKSLIAH--ADTLHISTIDSEPEGNVFFPEIPKEFNVVFE 140
Cdd:PTZ00164  90 LTEEEADPgVLVFGSLEDALRLLAEDLSIekIFIIGGASVYREALSAnlLDKIYLTRVNSEYECDVFFPKIPESFFIVAI 169
                        170
                 ....*....|....*....
gi 487657633 141 --QEFHSN-INYRYQIWQR 156
Cdd:PTZ00164 170 vsQTFSTNgTSYDFVIYEK 188
dihyfolred_HdrA_Halo NF041386
dihydrofolate reductase HdrA;
1-156 5.47e-16

dihydrofolate reductase HdrA;


Pssm-ID: 469277 [Multi-domain]  Cd Length: 158  Bit Score: 70.37  E-value: 5.47e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487657633   1 MKISLMAAKARNGVIGCGSDIPWN---AKGEQllFKAITYNQWLLVGRKTFEAMGA-LPNRKYAVVSRSGSVATNDDVVV 76
Cdd:NF041386   1 MELVSVAAVAENGVIGRDGELPWPsipADKRQ--YRERVADDPVILGRRTFESMRDdLPGSAQIVLSRSEREFDVETAHH 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487657633  77 FPSIEAAMRELKTL-TNHVVVSGGGEIYKSLIAHADTLHISTIDSEPEGNVFFPEI-PKEFNVVFEQEFHsniNYRYQIW 154
Cdd:NF041386  79 AGGVDEAIEIAESLgAERAYVLGGAAIYELFQPHVDRMVLSRVPGEYEGDAYYPEWdEDEWELVEETEYD---GFTLEEW 155

                 ..
gi 487657633 155 QR 156
Cdd:NF041386 156 VR 157
scpA PRK00478
segregation and condensation protein ScpA;
3-156 2.36e-10

segregation and condensation protein ScpA;


Pssm-ID: 234776 [Multi-domain]  Cd Length: 505  Bit Score: 57.63  E-value: 2.36e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487657633   3 ISLMAAKARNGVIGCGSDIPWNAKGEQLLFKAITYNQWLLVGRKTFEAMGA-LPNRKYAVVSRS--GSVATNDDVVVFPS 79
Cdd:PRK00478   2 IKLIWCEDLNFGIAKNNQIPWKIDEELNHFHQTTTNHTIVMGYNTFQAMNKiLANQANIVISKKhqRELKNNNELFVFND 81
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 487657633  80 IEAAMRELktLTNHVVVSGGGEIYKSLIAHADTLHISTIDSEPEGNVFFPEIPKEFNVVFEQEFHsniNYRYQIWQR 156
Cdd:PRK00478  82 LKKLLIDF--SNVDLFIIGGKKTIEQFIKYADQLIISKLNADYKCDLFVNLNYDDFSLVQTKEYD---QFVVEYWEK 153
trim_DfrL NF041668
trimethoprim-resistant dihydrofolate reductase DfrL;
12-151 2.59e-06

trimethoprim-resistant dihydrofolate reductase DfrL;


Pssm-ID: 469550 [Multi-domain]  Cd Length: 176  Bit Score: 45.03  E-value: 2.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487657633  12 NGVIGCGSDIPWNAKGEQLLFKAITYNQWLLVGRKTFEAMGALP--NRKYAVVSRSGSVATnDDVVVFPSIEAAMRELK- 88
Cdd:NF041668  10 CGEIGKPGDLFVNAEDDMGHFGNSGDDDVNLMGDKKHEKIPTMDdkNRIGIKLTENIPVRA-DGAIICHSKEDNKNYLAd 88
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 487657633  89 -TLTNHVVVSGGGEIYKSLIAHADTLHISTIDSEPEGNVFFPEIPKEFNVVFE-QEFHSNINYRY 151
Cdd:NF041668  89 gAIECHIHEDGGISAFEMFIDEPIHLHGGIIAEEFEGDEVMIEHDTIIDECFDgADGMPDEDNKY 153
 
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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