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Conserved domains on  [gi|1104688808|gb|APD76283|]
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dihydrofolate reductase [Anguillid herpesvirus 1]

Protein Classification

dihydrofolate reductase family protein( domain architecture ID 106942)

dihydrofolate reductase family protein; similar to Lacticaseibacillus rhamnosus dihydrofolate reductase which reduces dihydrofolic acid to tetrahydrofolic acid, using NADPH as electron donor

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DHFR super family cl17279
Dihydrofolate reductase (DHFR). Reduces 7,8-dihydrofolate to 5,6,7,8-tetrahydrofolate with ...
3-173 9.12e-34

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.


The actual alignment was detected with superfamily member pfam00186:

Pssm-ID: 473077 [Multi-domain]  Cd Length: 159  Bit Score: 118.80  E-value: 9.12e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104688808   3 LIVARNLNGAIGRGGRLLYKLPKDLQRFRDLTQDQIIVMGRKTFETLPRVLPRRRHVVLSKSApainihdpclqelatnr 82
Cdd:pfam00186   4 LIAAMDENGVIGKDNDLPWHLPADLKHFKKLTTGKPVIMGRKTFESIGRPLPGRKNIVLTRNP----------------- 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104688808  83 egvwirNWTVEQVRSLESLPRLLSPADKTrttcqinqikskdclysflpaqarvsgaeidktarSKLFIIGGAEVYNLFW 162
Cdd:pfam00186  67 ------DYKVDGVEVVHSLEEALALAAEA-----------------------------------EEIFIIGGAEIYAQAL 105
                         170
                  ....*....|.
gi 1104688808 163 KHCSVLHITKV 173
Cdd:pfam00186 106 PLADRLYITEI 116
 
Name Accession Description Interval E-value
DHFR_1 pfam00186
Dihydrofolate reductase;
3-173 9.12e-34

Dihydrofolate reductase;


Pssm-ID: 425512 [Multi-domain]  Cd Length: 159  Bit Score: 118.80  E-value: 9.12e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104688808   3 LIVARNLNGAIGRGGRLLYKLPKDLQRFRDLTQDQIIVMGRKTFETLPRVLPRRRHVVLSKSApainihdpclqelatnr 82
Cdd:pfam00186   4 LIAAMDENGVIGKDNDLPWHLPADLKHFKKLTTGKPVIMGRKTFESIGRPLPGRKNIVLTRNP----------------- 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104688808  83 egvwirNWTVEQVRSLESLPRLLSPADKTrttcqinqikskdclysflpaqarvsgaeidktarSKLFIIGGAEVYNLFW 162
Cdd:pfam00186  67 ------DYKVDGVEVVHSLEEALALAAEA-----------------------------------EEIFIIGGAEIYAQAL 105
                         170
                  ....*....|.
gi 1104688808 163 KHCSVLHITKV 173
Cdd:pfam00186 106 PLADRLYITEI 116
DHFR cd00209
Dihydrofolate reductase (DHFR). Reduces 7,8-dihydrofolate to 5,6,7,8-tetrahydrofolate with ...
3-173 4.93e-33

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: 116.85  E-value: 4.93e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104688808   3 LIVARNLNGAIGRGGRLLYKLPKDLQRFRDLTQDQIIVMGRKTFETLP-RVLPRRRHVVLSKSAPAINIHDpclqelatn 81
Cdd:cd00209     3 LIVAVDENGVIGKDNKLPWHLPEDLKHFKKTTTGNPVIMGRKTFESIPrRPLPGRTNIVLSRQLDYQDAEG--------- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104688808  82 regvwirnwtVEQVRSLESLPRLLSPADKtrttcqinqikskdclysflpaqarvsgaeidktarsKLFIIGGAEVYNLF 161
Cdd:cd00209    74 ----------VEVVHSLEEALELAENTVE-------------------------------------EIFVIGGAEIYKQA 106
                         170
                  ....*....|..
gi 1104688808 162 WKHCSVLHITKV 173
Cdd:cd00209   107 LPYADRLYLTRI 118
FolA COG0262
Dihydrofolate reductase [Coenzyme transport and metabolism]; Dihydrofolate reductase is part ...
3-173 5.85e-13

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: 64.49  E-value: 5.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104688808   3 LIVARNLNGAIG-RGGRL--LYKLPKDLQRFRDLTQD-QIIVMGRKTFETL-----PRVLPRRRHVVLSKSAPAInihdp 73
Cdd:COG0262     5 LIVAVSLDGVIGgPDGDLpwLFPDPEDLAHFKELTAGaDAVLMGRKTYESIagywpTRPLPGRPKIVLSRTLDEA----- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104688808  74 clqelatNREGVWIRNWTVEQVrsleslprllspadktrttcqINQIKSKDclysflpaqarvsGAEIdktarsklFIIG 153
Cdd:COG0262    80 -------DWEGVTVVSGDLEEA---------------------LAALKAAG-------------GKDI--------WVIG 110
                         170       180
                  ....*....|....*....|..
gi 1104688808 154 GAEVYNLFWKH--CSVLHITKV 173
Cdd:COG0262   111 GGELYRQLLPAglVDELYLTVV 132
PTZ00164 PTZ00164
bifunctional dihydrofolate reductase-thymidylate synthase; Provisional
3-196 1.36e-12

bifunctional dihydrofolate reductase-thymidylate synthase; Provisional


Pssm-ID: 240299 [Multi-domain]  Cd Length: 514  Bit Score: 66.23  E-value: 1.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104688808   3 LIVARNLNGAIGRGGRLLYKLPKDLQRFRDLT-------------QDQIIVMGRKTFETLP---RVLPRRRHVVLSKSap 66
Cdd:PTZ00164   12 IVVAVTLKRGIGIGNSLPWHIPEDMKFFSKITtyvreekyekspkKQNAVIMGRKTWESIPkkfRPLKNRINVVLSRT-- 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104688808  67 ainihdpcLQELATNrEGVWIrnwtveqVRSLESLPRLLspadktrttcqinqiKSKDCLYsflpaqarvsgaeidktar 146
Cdd:PTZ00164   90 --------LTEEEAD-PGVLV-------FGSLEDALRLL---------------AEDLSIE------------------- 119
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1104688808 147 sKLFIIGGAEVYN--LFWKHCSVLHITKvVASEPK-----PRHEEEDLVSWAVSDSQ 196
Cdd:PTZ00164  120 -KIFIIGGASVYReaLSANLLDKIYLTR-VNSEYEcdvffPKIPESFFIVAIVSQTF 174
dihyfolred_HdrA_Halo NF041386
dihydrofolate reductase HdrA;
1-64 2.30e-09

dihydrofolate reductase HdrA;


Pssm-ID: 469277 [Multi-domain]  Cd Length: 158  Bit Score: 54.58  E-value: 2.30e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1104688808   1 MELI----VARNlnGAIGRGGRLLY-KLPKDLQRFRDLTQDQIIVMGRKTFETLPRVLPRRRHVVLSKS 64
Cdd:NF041386    1 MELVsvaaVAEN--GVIGRDGELPWpSIPADKRQYRERVADDPVILGRRTFESMRDDLPGSAQIVLSRS 67
trim_DfrL NF041668
trimethoprim-resistant dihydrofolate reductase DfrL;
1-66 1.36e-03

trimethoprim-resistant dihydrofolate reductase DfrL;


Pssm-ID: 469550 [Multi-domain]  Cd Length: 176  Bit Score: 38.48  E-value: 1.36e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1104688808   1 MELIVARNLNGAIGRGGRLLYKLPKDLQRFRDLTQDQIIVMGRKTFETLP-RVLPRRRHVVLSKSAP 66
Cdd:NF041668    1 MGENIAEDCCGEIGKPGDLFVNAEDDMGHFGNSGDDDVNLMGDKKHEKIPtMDDKNRIGIKLTENIP 67
 
Name Accession Description Interval E-value
DHFR_1 pfam00186
Dihydrofolate reductase;
3-173 9.12e-34

Dihydrofolate reductase;


Pssm-ID: 425512 [Multi-domain]  Cd Length: 159  Bit Score: 118.80  E-value: 9.12e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104688808   3 LIVARNLNGAIGRGGRLLYKLPKDLQRFRDLTQDQIIVMGRKTFETLPRVLPRRRHVVLSKSApainihdpclqelatnr 82
Cdd:pfam00186   4 LIAAMDENGVIGKDNDLPWHLPADLKHFKKLTTGKPVIMGRKTFESIGRPLPGRKNIVLTRNP----------------- 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104688808  83 egvwirNWTVEQVRSLESLPRLLSPADKTrttcqinqikskdclysflpaqarvsgaeidktarSKLFIIGGAEVYNLFW 162
Cdd:pfam00186  67 ------DYKVDGVEVVHSLEEALALAAEA-----------------------------------EEIFIIGGAEIYAQAL 105
                         170
                  ....*....|.
gi 1104688808 163 KHCSVLHITKV 173
Cdd:pfam00186 106 PLADRLYITEI 116
DHFR cd00209
Dihydrofolate reductase (DHFR). Reduces 7,8-dihydrofolate to 5,6,7,8-tetrahydrofolate with ...
3-173 4.93e-33

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: 116.85  E-value: 4.93e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104688808   3 LIVARNLNGAIGRGGRLLYKLPKDLQRFRDLTQDQIIVMGRKTFETLP-RVLPRRRHVVLSKSAPAINIHDpclqelatn 81
Cdd:cd00209     3 LIVAVDENGVIGKDNKLPWHLPEDLKHFKKTTTGNPVIMGRKTFESIPrRPLPGRTNIVLSRQLDYQDAEG--------- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104688808  82 regvwirnwtVEQVRSLESLPRLLSPADKtrttcqinqikskdclysflpaqarvsgaeidktarsKLFIIGGAEVYNLF 161
Cdd:cd00209    74 ----------VEVVHSLEEALELAENTVE-------------------------------------EIFVIGGAEIYKQA 106
                         170
                  ....*....|..
gi 1104688808 162 WKHCSVLHITKV 173
Cdd:cd00209   107 LPYADRLYLTRI 118
FolA COG0262
Dihydrofolate reductase [Coenzyme transport and metabolism]; Dihydrofolate reductase is part ...
3-173 5.85e-13

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: 64.49  E-value: 5.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104688808   3 LIVARNLNGAIG-RGGRL--LYKLPKDLQRFRDLTQD-QIIVMGRKTFETL-----PRVLPRRRHVVLSKSAPAInihdp 73
Cdd:COG0262     5 LIVAVSLDGVIGgPDGDLpwLFPDPEDLAHFKELTAGaDAVLMGRKTYESIagywpTRPLPGRPKIVLSRTLDEA----- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104688808  74 clqelatNREGVWIRNWTVEQVrsleslprllspadktrttcqINQIKSKDclysflpaqarvsGAEIdktarsklFIIG 153
Cdd:COG0262    80 -------DWEGVTVVSGDLEEA---------------------LAALKAAG-------------GKDI--------WVIG 110
                         170       180
                  ....*....|....*....|..
gi 1104688808 154 GAEVYNLFWKH--CSVLHITKV 173
Cdd:COG0262   111 GGELYRQLLPAglVDELYLTVV 132
PTZ00164 PTZ00164
bifunctional dihydrofolate reductase-thymidylate synthase; Provisional
3-196 1.36e-12

bifunctional dihydrofolate reductase-thymidylate synthase; Provisional


Pssm-ID: 240299 [Multi-domain]  Cd Length: 514  Bit Score: 66.23  E-value: 1.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104688808   3 LIVARNLNGAIGRGGRLLYKLPKDLQRFRDLT-------------QDQIIVMGRKTFETLP---RVLPRRRHVVLSKSap 66
Cdd:PTZ00164   12 IVVAVTLKRGIGIGNSLPWHIPEDMKFFSKITtyvreekyekspkKQNAVIMGRKTWESIPkkfRPLKNRINVVLSRT-- 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104688808  67 ainihdpcLQELATNrEGVWIrnwtveqVRSLESLPRLLspadktrttcqinqiKSKDCLYsflpaqarvsgaeidktar 146
Cdd:PTZ00164   90 --------LTEEEAD-PGVLV-------FGSLEDALRLL---------------AEDLSIE------------------- 119
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1104688808 147 sKLFIIGGAEVYN--LFWKHCSVLHITKvVASEPK-----PRHEEEDLVSWAVSDSQ 196
Cdd:PTZ00164  120 -KIFIIGGASVYReaLSANLLDKIYLTR-VNSEYEcdvffPKIPESFFIVAIVSQTF 174
dihyfolred_HdrA_Halo NF041386
dihydrofolate reductase HdrA;
1-64 2.30e-09

dihydrofolate reductase HdrA;


Pssm-ID: 469277 [Multi-domain]  Cd Length: 158  Bit Score: 54.58  E-value: 2.30e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1104688808   1 MELI----VARNlnGAIGRGGRLLY-KLPKDLQRFRDLTQDQIIVMGRKTFETLPRVLPRRRHVVLSKS 64
Cdd:NF041386    1 MELVsvaaVAEN--GVIGRDGELPWpSIPADKRQYRERVADDPVILGRRTFESMRDDLPGSAQIVLSRS 67
folA PRK10769
type 3 dihydrofolate reductase;
3-62 5.42e-07

type 3 dihydrofolate reductase;


Pssm-ID: 182714 [Multi-domain]  Cd Length: 159  Bit Score: 47.81  E-value: 5.42e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104688808   3 LIVARNLNGAIGRGGRLLYKLPKDLQRFRDLTQDQIIVMGRKTFETLPRVLPRRRHVVLS 62
Cdd:PRK10769    4 LIAALAVDRVIGMENAMPWNLPADLAWFKRNTLNKPVIMGRHTWESIGRPLPGRKNIVIS 63
scpA PRK00478
segregation and condensation protein ScpA;
1-63 1.10e-03

segregation and condensation protein ScpA;


Pssm-ID: 234776 [Multi-domain]  Cd Length: 505  Bit Score: 39.53  E-value: 1.10e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1104688808   1 MELIVARNLNGAIGRGGRLLYKLPKDLQRFRDLTQDQIIVMGRKTFETLPRVLPRRRHVVLSK 63
Cdd:PRK00478    2 IKLIWCEDLNFGIAKNNQIPWKIDEELNHFHQTTTNHTIVMGYNTFQAMNKILANQANIVISK 64
trim_DfrL NF041668
trimethoprim-resistant dihydrofolate reductase DfrL;
1-66 1.36e-03

trimethoprim-resistant dihydrofolate reductase DfrL;


Pssm-ID: 469550 [Multi-domain]  Cd Length: 176  Bit Score: 38.48  E-value: 1.36e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1104688808   1 MELIVARNLNGAIGRGGRLLYKLPKDLQRFRDLTQDQIIVMGRKTFETLP-RVLPRRRHVVLSKSAP 66
Cdd:NF041668    1 MGENIAEDCCGEIGKPGDLFVNAEDDMGHFGNSGDDDVNLMGDKKHEKIPtMDDKNRIGIKLTENIP 67
 
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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