NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1743359677|gb|KAA3546814|]
View 

trimethoprim-resistant dihydrofolate reductase DfrA17 [Escherichia coli]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 6.23e-51

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: 160.00  E-value: 6.23e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743359677   3 ISLISAVSENGVIGSGPDIPWSVKGEQLLFKALTYNQWLLVGRKTFDSMG--VLPNRKYAVVSKNGISSSNENVLVFPSI 80
Cdd:cd00209     1 ISLIVAVDENGVIGKDNKLPWHLPEDLKHFKKTTTGNPVIMGRKTFESIPrrPLPGRTNIVLSRQLDYQDAEGVEVVHSL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1743359677  81 ENALKELSKVTDHVYVSGGGQIYNSLIEKADIIHLSTVHVEVEGDIKFP-IMPENFNLVF--EQFFMSNINYTYQIWK 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 6.23e-51

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: 160.00  E-value: 6.23e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743359677   3 ISLISAVSENGVIGSGPDIPWSVKGEQLLFKALTYNQWLLVGRKTFDSMG--VLPNRKYAVVSKNGISSSNENVLVFPSI 80
Cdd:cd00209     1 ISLIVAVDENGVIGKDNKLPWHLPEDLKHFKKTTTGNPVIMGRKTFESIPrrPLPGRTNIVLSRQLDYQDAEGVEVVHSL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1743359677  81 ENALKELSKVTDHVYVSGGGQIYNSLIEKADIIHLSTVHVEVEGDIKFP-IMPENFNLVF--EQFFMSNINYTYQIWK 155
Cdd:cd00209    81 EEALELAENTVEEIFVIGGAEIYKQALPYADRLYLTRIHAEFEGDTFFPeIDESEWELVSeeEVFEEDGYSYTFETYE 158
DHFR_1 pfam00186
Dihydrofolate reductase;
2-156 9.73e-46

Dihydrofolate reductase;


Pssm-ID: 425512 [Multi-domain]  Cd Length: 159  Bit Score: 146.53  E-value: 9.73e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743359677   2 KISLISAVSENGVIGSGPDIPWSVKGEQLLFKALTYNQWLLVGRKTFDSMG-VLPNRKYAVVSKNgISSSNENVLVFPSI 80
Cdd:pfam00186   1 MISLIAAMDENGVIGKDNDLPWHLPADLKHFKKLTTGKPVIMGRKTFESIGrPLPGRKNIVLTRN-PDYKVDGVEVVHSL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743359677  81 ENALKELSKvTDHVYVSGGGQIYNSLIEKADIIHLSTVHVEVEGDIKFP-IMPENFNLVFEQFFMSN----INYTYQIWK 155
Cdd:pfam00186  80 EEALALAAE-AEEIFIIGGAEIYAQALPLADRLYITEIDAEFDGDTFFPeIDPSEWQLVSREEHEADeknpYPYTFVTYE 158

                  .
gi 1743359677 156 K 156
Cdd:pfam00186 159 R 159
FolA COG0262
Dihydrofolate reductase [Coenzyme transport and metabolism]; Dihydrofolate reductase is part ...
1-141 2.99e-25

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: 94.53  E-value: 2.99e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743359677   1 MKISLISAVSENGVIGS-GPDIPWSVKGEQLL--FKALTYN-QWLLVGRKTFDSMG------VLPNRKYAVVSKNGISSS 70
Cdd:COG0262     1 RKLILIVAVSLDGVIGGpDGDLPWLFPDPEDLahFKELTAGaDAVLMGRKTYESIAgywptrPLPGRPKIVLSRTLDEAD 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1743359677  71 NENV-LVFPSIENALKELSKVTD-HVYVSGGGQIYNSLIEK--ADIIHLSTVHVEV-EGDIKFP--IMPENFNLVFEQ 141
Cdd:COG0262    81 WEGVtVVSGDLEEALAALKAAGGkDIWVIGGGELYRQLLPAglVDELYLTVVPVVLgEGDRLFPelDAPSRLELVESE 158
PTZ00164 PTZ00164
bifunctional dihydrofolate reductase-thymidylate synthase; Provisional
3-156 9.29e-24

bifunctional dihydrofolate reductase-thymidylate synthase; Provisional


Pssm-ID: 240299 [Multi-domain]  Cd Length: 514  Bit Score: 95.89  E-value: 9.29e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743359677   3 ISLISAVSENGVIGSGPDIPWSVKGEQLLFKALTYN-------------QWLLVGRKTFDSMGV----LPNRKYAVVSKN 65
Cdd:PTZ00164   10 FSIVVAVTLKRGIGIGNSLPWHIPEDMKFFSKITTYvreekyekspkkqNAVIMGRKTWESIPKkfrpLKNRINVVLSRT 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743359677  66 GISSSN-ENVLVFPSIENALKELSKVTDH--VYVSGGGQIYNSLIE--KADIIHLSTVHVEVEGDIKFPIMPENF---NL 137
Cdd:PTZ00164   90 LTEEEAdPGVLVFGSLEDALRLLAEDLSIekIFIIGGASVYREALSanLLDKIYLTRVNSEYECDVFFPKIPESFfivAI 169
                         170
                  ....*....|....*....
gi 1743359677 138 VFEQFFMSNINYTYQIWKK 156
Cdd:PTZ00164  170 VSQTFSTNGTSYDFVIYEK 188
dihyfolred_HdrA_Halo NF041386
dihydrofolate reductase HdrA;
1-129 2.37e-18

dihydrofolate reductase HdrA;


Pssm-ID: 469277 [Multi-domain]  Cd Length: 158  Bit Score: 76.53  E-value: 2.37e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743359677   1 MKISLISAVSENGVIGSGPDIPW-SVKGEQLLFKALTYNQWLLVGRKTFDSM-GVLPNRKYAVVSKNGISSSNENVLVFP 78
Cdd:NF041386    1 MELVSVAAVAENGVIGRDGELPWpSIPADKRQYRERVADDPVILGRRTFESMrDDLPGSAQIVLSRSEREFDVETAHHAG 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1743359677  79 SIENALkELSKVTDH--VYVSGGGQIYNSLIEKADIIHLSTVHVEVEGDIKFP 129
Cdd:NF041386   81 GVDEAI-EIAESLGAerAYVLGGAAIYELFQPHVDRMVLSRVPGEYEGDAYYP 132
trim_DfrL NF041668
trimethoprim-resistant dihydrofolate reductase DfrL;
12-151 9.95e-09

trimethoprim-resistant dihydrofolate reductase DfrL;


Pssm-ID: 469550 [Multi-domain]  Cd Length: 176  Bit Score: 51.58  E-value: 9.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743359677  12 NGVIGSGPDIPWSVKGEQLLFKALTYNQWLLVGRKTFDSMGVLP----------NRKYAVVSKNGISSSNENVLvfpsie 81
Cdd:NF041668   10 CGEIGKPGDLFVNAEDDMGHFGNSGDDDVNLMGDKKHEKIPTMDdknrigikltENIPVRADGAIICHSKEDNK------ 83
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1743359677  82 NALKElSKVTDHVYVSGGGQIYNSLIEKADIIHLSTVHVEVEGDikfPIMPENFNLVFEQF----FMSNINYTY 151
Cdd:NF041668   84 NYLAD-GAIECHIHEDGGISAFEMFIDEPIHLHGGIIAEEFEGD---EVMIEHDTIIDECFdgadGMPDEDNKY 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 6.23e-51

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: 160.00  E-value: 6.23e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743359677   3 ISLISAVSENGVIGSGPDIPWSVKGEQLLFKALTYNQWLLVGRKTFDSMG--VLPNRKYAVVSKNGISSSNENVLVFPSI 80
Cdd:cd00209     1 ISLIVAVDENGVIGKDNKLPWHLPEDLKHFKKTTTGNPVIMGRKTFESIPrrPLPGRTNIVLSRQLDYQDAEGVEVVHSL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1743359677  81 ENALKELSKVTDHVYVSGGGQIYNSLIEKADIIHLSTVHVEVEGDIKFP-IMPENFNLVF--EQFFMSNINYTYQIWK 155
Cdd:cd00209    81 EEALELAENTVEEIFVIGGAEIYKQALPYADRLYLTRIHAEFEGDTFFPeIDESEWELVSeeEVFEEDGYSYTFETYE 158
DHFR_1 pfam00186
Dihydrofolate reductase;
2-156 9.73e-46

Dihydrofolate reductase;


Pssm-ID: 425512 [Multi-domain]  Cd Length: 159  Bit Score: 146.53  E-value: 9.73e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743359677   2 KISLISAVSENGVIGSGPDIPWSVKGEQLLFKALTYNQWLLVGRKTFDSMG-VLPNRKYAVVSKNgISSSNENVLVFPSI 80
Cdd:pfam00186   1 MISLIAAMDENGVIGKDNDLPWHLPADLKHFKKLTTGKPVIMGRKTFESIGrPLPGRKNIVLTRN-PDYKVDGVEVVHSL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743359677  81 ENALKELSKvTDHVYVSGGGQIYNSLIEKADIIHLSTVHVEVEGDIKFP-IMPENFNLVFEQFFMSN----INYTYQIWK 155
Cdd:pfam00186  80 EEALALAAE-AEEIFIIGGAEIYAQALPLADRLYITEIDAEFDGDTFFPeIDPSEWQLVSREEHEADeknpYPYTFVTYE 158

                  .
gi 1743359677 156 K 156
Cdd:pfam00186 159 R 159
FolA COG0262
Dihydrofolate reductase [Coenzyme transport and metabolism]; Dihydrofolate reductase is part ...
1-141 2.99e-25

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: 94.53  E-value: 2.99e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743359677   1 MKISLISAVSENGVIGS-GPDIPWSVKGEQLL--FKALTYN-QWLLVGRKTFDSMG------VLPNRKYAVVSKNGISSS 70
Cdd:COG0262     1 RKLILIVAVSLDGVIGGpDGDLPWLFPDPEDLahFKELTAGaDAVLMGRKTYESIAgywptrPLPGRPKIVLSRTLDEAD 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1743359677  71 NENV-LVFPSIENALKELSKVTD-HVYVSGGGQIYNSLIEK--ADIIHLSTVHVEV-EGDIKFP--IMPENFNLVFEQ 141
Cdd:COG0262    81 WEGVtVVSGDLEEALAALKAAGGkDIWVIGGGELYRQLLPAglVDELYLTVVPVVLgEGDRLFPelDAPSRLELVESE 158
PTZ00164 PTZ00164
bifunctional dihydrofolate reductase-thymidylate synthase; Provisional
3-156 9.29e-24

bifunctional dihydrofolate reductase-thymidylate synthase; Provisional


Pssm-ID: 240299 [Multi-domain]  Cd Length: 514  Bit Score: 95.89  E-value: 9.29e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743359677   3 ISLISAVSENGVIGSGPDIPWSVKGEQLLFKALTYN-------------QWLLVGRKTFDSMGV----LPNRKYAVVSKN 65
Cdd:PTZ00164   10 FSIVVAVTLKRGIGIGNSLPWHIPEDMKFFSKITTYvreekyekspkkqNAVIMGRKTWESIPKkfrpLKNRINVVLSRT 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743359677  66 GISSSN-ENVLVFPSIENALKELSKVTDH--VYVSGGGQIYNSLIE--KADIIHLSTVHVEVEGDIKFPIMPENF---NL 137
Cdd:PTZ00164   90 LTEEEAdPGVLVFGSLEDALRLLAEDLSIekIFIIGGASVYREALSanLLDKIYLTRVNSEYECDVFFPKIPESFfivAI 169
                         170
                  ....*....|....*....
gi 1743359677 138 VFEQFFMSNINYTYQIWKK 156
Cdd:PTZ00164  170 VSQTFSTNGTSYDFVIYEK 188
folA PRK10769
type 3 dihydrofolate reductase;
3-142 2.59e-23

type 3 dihydrofolate reductase;


Pssm-ID: 182714 [Multi-domain]  Cd Length: 159  Bit Score: 89.41  E-value: 2.59e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743359677   3 ISLISAVSENGVIGSGPDIPWSVKGEQLLFKALTYNQWLLVGRKTFDSMG-VLPNRKYAVVSKNgiSSSNENVLVFPSIE 81
Cdd:PRK10769    2 ISLIAALAVDRVIGMENAMPWNLPADLAWFKRNTLNKPVIMGRHTWESIGrPLPGRKNIVISSQ--PGTDDRVTWVKSVD 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1743359677  82 NALKELSKVtDHVYVSGGGQIYNSLIEKADIIHLSTVHVEVEGDIKFP-IMPENFNLVFEQF 142
Cdd:PRK10769   80 EALAAAGDV-PEIMVIGGGRVYEQFLPKAQRLYLTHIDAEVEGDTHFPdYEPDEWESVFSEF 140
dihyfolred_HdrA_Halo NF041386
dihydrofolate reductase HdrA;
1-129 2.37e-18

dihydrofolate reductase HdrA;


Pssm-ID: 469277 [Multi-domain]  Cd Length: 158  Bit Score: 76.53  E-value: 2.37e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743359677   1 MKISLISAVSENGVIGSGPDIPW-SVKGEQLLFKALTYNQWLLVGRKTFDSM-GVLPNRKYAVVSKNGISSSNENVLVFP 78
Cdd:NF041386    1 MELVSVAAVAENGVIGRDGELPWpSIPADKRQYRERVADDPVILGRRTFESMrDDLPGSAQIVLSRSEREFDVETAHHAG 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1743359677  79 SIENALkELSKVTDH--VYVSGGGQIYNSLIEKADIIHLSTVHVEVEGDIKFP 129
Cdd:NF041386   81 GVDEAI-EIAESLGAerAYVLGGAAIYELFQPHVDRMVLSRVPGEYEGDAYYP 132
scpA PRK00478
segregation and condensation protein ScpA;
3-156 1.49e-10

segregation and condensation protein ScpA;


Pssm-ID: 234776 [Multi-domain]  Cd Length: 505  Bit Score: 58.02  E-value: 1.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743359677   3 ISLISAVSENGVIGSGPDIPWSVKGEQLLFKALTYNQWLLVGRKTFDSMG-VLPNRKYAVVSKNGIS--SSNENVLVFPS 79
Cdd:PRK00478    2 IKLIWCEDLNFGIAKNNQIPWKIDEELNHFHQTTTNHTIVMGYNTFQAMNkILANQANIVISKKHQRelKNNNELFVFND 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1743359677  80 IENALKELSKVTdhVYVSGGGQIYNSLIEKADIIHLSTVHVEVEGDIKFPIMPENFNLVFEQFFMsniNYTYQIWKK 156
Cdd:PRK00478   82 LKKLLIDFSNVD--LFIIGGKKTIEQFIKYADQLIISKLNADYKCDLFVNLNYDDFSLVQTKEYD---QFVVEYWEK 153
trim_DfrL NF041668
trimethoprim-resistant dihydrofolate reductase DfrL;
12-151 9.95e-09

trimethoprim-resistant dihydrofolate reductase DfrL;


Pssm-ID: 469550 [Multi-domain]  Cd Length: 176  Bit Score: 51.58  E-value: 9.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743359677  12 NGVIGSGPDIPWSVKGEQLLFKALTYNQWLLVGRKTFDSMGVLP----------NRKYAVVSKNGISSSNENVLvfpsie 81
Cdd:NF041668   10 CGEIGKPGDLFVNAEDDMGHFGNSGDDDVNLMGDKKHEKIPTMDdknrigikltENIPVRADGAIICHSKEDNK------ 83
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1743359677  82 NALKElSKVTDHVYVSGGGQIYNSLIEKADIIHLSTVHVEVEGDikfPIMPENFNLVFEQF----FMSNINYTY 151
Cdd:NF041668   84 NYLAD-GAIECHIHEDGGISAFEMFIDEPIHLHGGIIAEEFEGD---EVMIEHDTIIDECFdgadGMPDEDNKY 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH