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Conserved domains on  [gi|446626072|ref|WP_000703418|]
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MULTISPECIES: trimethoprim-resistant dihydrofolate reductase DfrA7 [Gammaproteobacteria]

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 6.95e-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: 159.61  E-value: 6.95e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626072   3 ISLISATSENGVIGNGPDIPWSAKGEQLLFKALTYNQWLLVGRKTFDSMG--VLPNRKYAVVSRKGISSSNENVLVFPSI 80
Cdd:cd00209    1 ISLIVAVDENGVIGKDNKLPWHLPEDLKHFKKTTTGNPVIMGRKTFESIPrrPLPGRTNIVLSRQLDYQDAEGVEVVHSL 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446626072  81 EIALQELSKITDHLYVSGGGQIYNSLIEKADIIHLSTVHVEVEGDINFPKI-PENFNLVF--EQFFLSNINYTYQIWK 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 6.95e-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: 159.61  E-value: 6.95e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626072   3 ISLISATSENGVIGNGPDIPWSAKGEQLLFKALTYNQWLLVGRKTFDSMG--VLPNRKYAVVSRKGISSSNENVLVFPSI 80
Cdd:cd00209    1 ISLIVAVDENGVIGKDNKLPWHLPEDLKHFKKTTTGNPVIMGRKTFESIPrrPLPGRTNIVLSRQLDYQDAEGVEVVHSL 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446626072  81 EIALQELSKITDHLYVSGGGQIYNSLIEKADIIHLSTVHVEVEGDINFPKI-PENFNLVF--EQFFLSNINYTYQIWK 155
Cdd:cd00209   81 EEALELAENTVEEIFVIGGAEIYKQALPYADRLYLTRIHAEFEGDTFFPEIdESEWELVSeeEVFEEDGYSYTFETYE 158
DHFR_1 pfam00186
Dihydrofolate reductase;
2-156 1.08e-43

Dihydrofolate reductase;


Pssm-ID: 425512 [Multi-domain]  Cd Length: 159  Bit Score: 141.53  E-value: 1.08e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626072    2 KISLISATSENGVIGNGPDIPWSAKGEQLLFKALTYNQWLLVGRKTFDSMG-VLPNRKYAVVSRKgISSSNENVLVFPSI 80
Cdd:pfam00186   1 MISLIAAMDENGVIGKDNDLPWHLPADLKHFKKLTTGKPVIMGRKTFESIGrPLPGRKNIVLTRN-PDYKVDGVEVVHSL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626072   81 EIALQELSKiTDHLYVSGGGQIYNSLIEKADIIHLSTVHVEVEGDINFPKI-PENFNLVFEQFFLSN----INYTYQIWK 155
Cdd:pfam00186  80 EEALALAAE-AEEIFIIGGAEIYAQALPLADRLYITEIDAEFDGDTFFPEIdPSEWQLVSREEHEADeknpYPYTFVTYE 158

                  .
gi 446626072  156 K 156
Cdd:pfam00186 159 R 159
FolA COG0262
Dihydrofolate reductase [Coenzyme transport and metabolism]; Dihydrofolate reductase is part ...
1-141 1.21e-24

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: 92.99  E-value: 1.21e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626072   1 MKISLISATSENGVIGN-GPDIPWSAKGEQLL--FKALTYN-QWLLVGRKTFDSMG------VLPNRKYAVVSRKGISSS 70
Cdd:COG0262    1 RKLILIVAVSLDGVIGGpDGDLPWLFPDPEDLahFKELTAGaDAVLMGRKTYESIAgywptrPLPGRPKIVLSRTLDEAD 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446626072  71 NENV-LVFPSIEIALQELSKITD-HLYVSGGGQIYNSLIEK--ADIIHLSTVHVEV-EGDINFPKI--PENFNLVFEQ 141
Cdd:COG0262   81 WEGVtVVSGDLEEALAALKAAGGkDIWVIGGGELYRQLLPAglVDELYLTVVPVVLgEGDRLFPELdaPSRLELVESE 158
PTZ00164 PTZ00164
bifunctional dihydrofolate reductase-thymidylate synthase; Provisional
3-156 9.11e-24

bifunctional dihydrofolate reductase-thymidylate synthase; Provisional


Pssm-ID: 240299 [Multi-domain]  Cd Length: 514  Bit Score: 95.89  E-value: 9.11e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626072   3 ISLISATSENGVIGNGPDIPWSAKGEQLLFKALTYN-------------QWLLVGRKTFDSMGV----LPNRKYAVVSRK 65
Cdd:PTZ00164  10 FSIVVAVTLKRGIGIGNSLPWHIPEDMKFFSKITTYvreekyekspkkqNAVIMGRKTWESIPKkfrpLKNRINVVLSRT 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626072  66 GISSSN-ENVLVFPSIEIALQELSKITDH--LYVSGGGQIYNSLIE--KADIIHLSTVHVEVEGDINFPKIPENF---NL 137
Cdd:PTZ00164  90 LTEEEAdPGVLVFGSLEDALRLLAEDLSIekIFIIGGASVYREALSanLLDKIYLTRVNSEYECDVFFPKIPESFfivAI 169
                        170
                 ....*....|....*....
gi 446626072 138 VFEQFFLSNINYTYQIWKK 156
Cdd:PTZ00164 170 VSQTFSTNGTSYDFVIYEK 188
dihyfolred_HdrA_Halo NF041386
dihydrofolate reductase HdrA;
1-129 1.78e-17

dihydrofolate reductase HdrA;


Pssm-ID: 469277 [Multi-domain]  Cd Length: 158  Bit Score: 74.22  E-value: 1.78e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626072   1 MKISLISATSENGVIGNGPDIPWS---AKGEQllFKALTYNQWLLVGRKTFDSM-GVLPNRKYAVVSRKGISSSNENVLV 76
Cdd:NF041386   1 MELVSVAAVAENGVIGRDGELPWPsipADKRQ--YRERVADDPVILGRRTFESMrDDLPGSAQIVLSRSEREFDVETAHH 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446626072  77 FPSIEIALQELSKI-TDHLYVSGGGQIYNSLIEKADIIHLSTVHVEVEGDINFP 129
Cdd:NF041386  79 AGGVDEAIEIAESLgAERAYVLGGAAIYELFQPHVDRMVLSRVPGEYEGDAYYP 132
trim_DfrL NF041668
trimethoprim-resistant dihydrofolate reductase DfrL;
12-151 4.02e-06

trimethoprim-resistant dihydrofolate reductase DfrL;


Pssm-ID: 469550 [Multi-domain]  Cd Length: 176  Bit Score: 44.65  E-value: 4.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626072  12 NGVIGNGPDIPWSAKGEQLLFKALTYNQWLLVGRKTFDSMGVLPNR-KYAVVSRKGISSSNENVLVFPSIEIALQELS-- 88
Cdd:NF041668  10 CGEIGKPGDLFVNAEDDMGHFGNSGDDDVNLMGDKKHEKIPTMDDKnRIGIKLTENIPVRADGAIICHSKEDNKNYLAdg 89
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446626072  89 KITDHLYVSGGGQIYNSLIEKADIIHLSTVHVEVEGDINFPKIPENFNLVFE-QFFLSNINYTY 151
Cdd:NF041668  90 AIECHIHEDGGISAFEMFIDEPIHLHGGIIAEEFEGDEVMIEHDTIIDECFDgADGMPDEDNKY 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 6.95e-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: 159.61  E-value: 6.95e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626072   3 ISLISATSENGVIGNGPDIPWSAKGEQLLFKALTYNQWLLVGRKTFDSMG--VLPNRKYAVVSRKGISSSNENVLVFPSI 80
Cdd:cd00209    1 ISLIVAVDENGVIGKDNKLPWHLPEDLKHFKKTTTGNPVIMGRKTFESIPrrPLPGRTNIVLSRQLDYQDAEGVEVVHSL 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446626072  81 EIALQELSKITDHLYVSGGGQIYNSLIEKADIIHLSTVHVEVEGDINFPKI-PENFNLVF--EQFFLSNINYTYQIWK 155
Cdd:cd00209   81 EEALELAENTVEEIFVIGGAEIYKQALPYADRLYLTRIHAEFEGDTFFPEIdESEWELVSeeEVFEEDGYSYTFETYE 158
DHFR_1 pfam00186
Dihydrofolate reductase;
2-156 1.08e-43

Dihydrofolate reductase;


Pssm-ID: 425512 [Multi-domain]  Cd Length: 159  Bit Score: 141.53  E-value: 1.08e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626072    2 KISLISATSENGVIGNGPDIPWSAKGEQLLFKALTYNQWLLVGRKTFDSMG-VLPNRKYAVVSRKgISSSNENVLVFPSI 80
Cdd:pfam00186   1 MISLIAAMDENGVIGKDNDLPWHLPADLKHFKKLTTGKPVIMGRKTFESIGrPLPGRKNIVLTRN-PDYKVDGVEVVHSL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626072   81 EIALQELSKiTDHLYVSGGGQIYNSLIEKADIIHLSTVHVEVEGDINFPKI-PENFNLVFEQFFLSN----INYTYQIWK 155
Cdd:pfam00186  80 EEALALAAE-AEEIFIIGGAEIYAQALPLADRLYITEIDAEFDGDTFFPEIdPSEWQLVSREEHEADeknpYPYTFVTYE 158

                  .
gi 446626072  156 K 156
Cdd:pfam00186 159 R 159
FolA COG0262
Dihydrofolate reductase [Coenzyme transport and metabolism]; Dihydrofolate reductase is part ...
1-141 1.21e-24

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: 92.99  E-value: 1.21e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626072   1 MKISLISATSENGVIGN-GPDIPWSAKGEQLL--FKALTYN-QWLLVGRKTFDSMG------VLPNRKYAVVSRKGISSS 70
Cdd:COG0262    1 RKLILIVAVSLDGVIGGpDGDLPWLFPDPEDLahFKELTAGaDAVLMGRKTYESIAgywptrPLPGRPKIVLSRTLDEAD 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446626072  71 NENV-LVFPSIEIALQELSKITD-HLYVSGGGQIYNSLIEK--ADIIHLSTVHVEV-EGDINFPKI--PENFNLVFEQ 141
Cdd:COG0262   81 WEGVtVVSGDLEEALAALKAAGGkDIWVIGGGELYRQLLPAglVDELYLTVVPVVLgEGDRLFPELdaPSRLELVESE 158
PTZ00164 PTZ00164
bifunctional dihydrofolate reductase-thymidylate synthase; Provisional
3-156 9.11e-24

bifunctional dihydrofolate reductase-thymidylate synthase; Provisional


Pssm-ID: 240299 [Multi-domain]  Cd Length: 514  Bit Score: 95.89  E-value: 9.11e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626072   3 ISLISATSENGVIGNGPDIPWSAKGEQLLFKALTYN-------------QWLLVGRKTFDSMGV----LPNRKYAVVSRK 65
Cdd:PTZ00164  10 FSIVVAVTLKRGIGIGNSLPWHIPEDMKFFSKITTYvreekyekspkkqNAVIMGRKTWESIPKkfrpLKNRINVVLSRT 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626072  66 GISSSN-ENVLVFPSIEIALQELSKITDH--LYVSGGGQIYNSLIE--KADIIHLSTVHVEVEGDINFPKIPENF---NL 137
Cdd:PTZ00164  90 LTEEEAdPGVLVFGSLEDALRLLAEDLSIekIFIIGGASVYREALSanLLDKIYLTRVNSEYECDVFFPKIPESFfivAI 169
                        170
                 ....*....|....*....
gi 446626072 138 VFEQFFLSNINYTYQIWKK 156
Cdd:PTZ00164 170 VSQTFSTNGTSYDFVIYEK 188
folA PRK10769
type 3 dihydrofolate reductase;
3-142 1.26e-22

type 3 dihydrofolate reductase;


Pssm-ID: 182714 [Multi-domain]  Cd Length: 159  Bit Score: 87.87  E-value: 1.26e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626072   3 ISLISATSENGVIGNGPDIPWSAKGEQLLFKALTYNQWLLVGRKTFDSMG-VLPNRKYAVVSRKgiSSSNENVLVFPSIE 81
Cdd:PRK10769   2 ISLIAALAVDRVIGMENAMPWNLPADLAWFKRNTLNKPVIMGRHTWESIGrPLPGRKNIVISSQ--PGTDDRVTWVKSVD 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446626072  82 IALQELSKItDHLYVSGGGQIYNSLIEKADIIHLSTVHVEVEGDINFPKI-PENFNLVFEQF 142
Cdd:PRK10769  80 EALAAAGDV-PEIMVIGGGRVYEQFLPKAQRLYLTHIDAEVEGDTHFPDYePDEWESVFSEF 140
dihyfolred_HdrA_Halo NF041386
dihydrofolate reductase HdrA;
1-129 1.78e-17

dihydrofolate reductase HdrA;


Pssm-ID: 469277 [Multi-domain]  Cd Length: 158  Bit Score: 74.22  E-value: 1.78e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626072   1 MKISLISATSENGVIGNGPDIPWS---AKGEQllFKALTYNQWLLVGRKTFDSM-GVLPNRKYAVVSRKGISSSNENVLV 76
Cdd:NF041386   1 MELVSVAAVAENGVIGRDGELPWPsipADKRQ--YRERVADDPVILGRRTFESMrDDLPGSAQIVLSRSEREFDVETAHH 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446626072  77 FPSIEIALQELSKI-TDHLYVSGGGQIYNSLIEKADIIHLSTVHVEVEGDINFP 129
Cdd:NF041386  79 AGGVDEAIEIAESLgAERAYVLGGAAIYELFQPHVDRMVLSRVPGEYEGDAYYP 132
scpA PRK00478
segregation and condensation protein ScpA;
3-156 1.75e-09

segregation and condensation protein ScpA;


Pssm-ID: 234776 [Multi-domain]  Cd Length: 505  Bit Score: 54.94  E-value: 1.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626072   3 ISLISATSENGVIGNGPDIPWSAKGEQLLFKALTYNQWLLVGRKTFDSMG-VLPNRKYAVVSRKGIS--SSNENVLVFPS 79
Cdd:PRK00478   2 IKLIWCEDLNFGIAKNNQIPWKIDEELNHFHQTTTNHTIVMGYNTFQAMNkILANQANIVISKKHQRelKNNNELFVFND 81
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446626072  80 IEIALQELSkITDhLYVSGGGQIYNSLIEKADIIHLSTVHVEVEGDINFPKIPENFNLVFEQFFlsnINYTYQIWKK 156
Cdd:PRK00478  82 LKKLLIDFS-NVD-LFIIGGKKTIEQFIKYADQLIISKLNADYKCDLFVNLNYDDFSLVQTKEY---DQFVVEYWEK 153
trim_DfrL NF041668
trimethoprim-resistant dihydrofolate reductase DfrL;
12-151 4.02e-06

trimethoprim-resistant dihydrofolate reductase DfrL;


Pssm-ID: 469550 [Multi-domain]  Cd Length: 176  Bit Score: 44.65  E-value: 4.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626072  12 NGVIGNGPDIPWSAKGEQLLFKALTYNQWLLVGRKTFDSMGVLPNR-KYAVVSRKGISSSNENVLVFPSIEIALQELS-- 88
Cdd:NF041668  10 CGEIGKPGDLFVNAEDDMGHFGNSGDDDVNLMGDKKHEKIPTMDDKnRIGIKLTENIPVRADGAIICHSKEDNKNYLAdg 89
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446626072  89 KITDHLYVSGGGQIYNSLIEKADIIHLSTVHVEVEGDINFPKIPENFNLVFE-QFFLSNINYTY 151
Cdd:NF041668  90 AIECHIHEDGGISAFEMFIDEPIHLHGGIIAEEFEGDEVMIEHDTIIDECFDgADGMPDEDNKY 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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