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Conserved domains on  [gi|1063726786|ref|NP_001328947|]
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thymidylate synthase 2 [Arabidopsis thaliana]

Protein Classification

thymidylate synthase family protein( domain architecture ID 1000328)

thymidylate synthase family protein is involved in the biosynthesis of DNA precursors; it catalyzes alkylation of C5 of pyrimidine nucleotides

Gene Ontology:  GO:0004799|GO:0006231|GO:0016740
PubMed:  7969277|21876188|12704428|16511011|6996564

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTZ00164 super family cl36520
bifunctional dihydrofolate reductase-thymidylate synthase; Provisional
 61-397 1.80e-147

bifunctional dihydrofolate reductase-thymidylate synthase; Provisional


The actual alignment was detected with superfamily member PTZ00164:

Pssm-ID: 240299 [Multi-domain]  Cd Length: 514  Bit Score: 428.32  E-value: 1.80e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726786  61 KPQSTYQVVVAATKEMGIGKDGKLPWNLPTDLKFFKDLTLST------SDSAKKNAVVMGRKTWESIPKKYRPLSGRLNV 134
Cdd:PTZ00164    5 SSLKDFSIVVAVTLKRGIGIGNSLPWHIPEDMKFFSKITTYVreekyeKSPKKQNAVIMGRKTWESIPKKFRPLKNRINV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726786 135 VLSRSSGFDIANtENVVTCSSIDSALDLLAAPpfsLSIEKVFVIGGGDILREALNKPSCEAIHITEIDTSIDCDTFIPTV 214
Cdd:PTZ00164   85 VLSRTLTEEEAD-PGVLVFGSLEDALRLLAED---LSIEKIFIIGGASVYREALSANLLDKIYLTRVNSEYECDVFFPKI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726786 215 DTSAYQPWCSSFPICENGLRFSFTTHVRVKSSSA---GEASDESDGSKVLQVDWKKFSSVLPKMIFDRHEEYLYLNLVKE 291
Cdd:PTZ00164  161 PESFFIVAIVSQTFSTNGTSYDFVIYEKKNDDEEdllGKIFGQMKMTGRKKSPKEQLYKACPSLKIREHEEFQYLDLIAD 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726786 292 IISNGNLKDDRTGTGTLSKFGCQMKFNLRRNFPLLTTKRVFWRGVVEELLWFISGSTNAKVLQEKGIRIWDGNASRAYLD 371
Cdd:PTZ00164  241 IIKNGNVKEDRTGVGTISKFGYQMRFDLRESFPLLTTKKVFLRGIIEELLWFIRGETNGNLLLDKGVRIWEGNGSREFLD 320

                         330       340
                  ....*....|....*....|....*.
gi 1063726786 372 GIGLTEREEGDLGPVYGFQWRHFGAK 397
Cdd:PTZ00164  321 SRGLTHREENDLGPVYGFQWRHFGAE 346
 
Name Accession Description Interval E-value
PTZ00164 PTZ00164
bifunctional dihydrofolate reductase-thymidylate synthase; Provisional
 61-397 1.80e-147

bifunctional dihydrofolate reductase-thymidylate synthase; Provisional


Pssm-ID: 240299 [Multi-domain]  Cd Length: 514  Bit Score: 428.32  E-value: 1.80e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726786  61 KPQSTYQVVVAATKEMGIGKDGKLPWNLPTDLKFFKDLTLST------SDSAKKNAVVMGRKTWESIPKKYRPLSGRLNV 134
Cdd:PTZ00164    5 SSLKDFSIVVAVTLKRGIGIGNSLPWHIPEDMKFFSKITTYVreekyeKSPKKQNAVIMGRKTWESIPKKFRPLKNRINV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726786 135 VLSRSSGFDIANtENVVTCSSIDSALDLLAAPpfsLSIEKVFVIGGGDILREALNKPSCEAIHITEIDTSIDCDTFIPTV 214
Cdd:PTZ00164   85 VLSRTLTEEEAD-PGVLVFGSLEDALRLLAED---LSIEKIFIIGGASVYREALSANLLDKIYLTRVNSEYECDVFFPKI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726786 215 DTSAYQPWCSSFPICENGLRFSFTTHVRVKSSSA---GEASDESDGSKVLQVDWKKFSSVLPKMIFDRHEEYLYLNLVKE 291
Cdd:PTZ00164  161 PESFFIVAIVSQTFSTNGTSYDFVIYEKKNDDEEdllGKIFGQMKMTGRKKSPKEQLYKACPSLKIREHEEFQYLDLIAD 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726786 292 IISNGNLKDDRTGTGTLSKFGCQMKFNLRRNFPLLTTKRVFWRGVVEELLWFISGSTNAKVLQEKGIRIWDGNASRAYLD 371
Cdd:PTZ00164  241 IIKNGNVKEDRTGVGTISKFGYQMRFDLRESFPLLTTKKVFLRGIIEELLWFIRGETNGNLLLDKGVRIWEGNGSREFLD 320

                         330       340
                  ....*....|....*....|....*.
gi 1063726786 372 GIGLTEREEGDLGPVYGFQWRHFGAK 397
Cdd:PTZ00164  321 SRGLTHREENDLGPVYGFQWRHFGAE 346
DHFR cd00209
Dihydrofolate reductase (DHFR). Reduces 7,8-dihydrofolate to 5,6,7,8-tetrahydrofolate with ...
 69-241 6.10e-60

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: 191.58  E-value: 6.10e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726786  69 VVAATKEMGIGKDGKLPWNLPTDLKFFKDLTlstsdsaKKNAVVMGRKTWESIPKkyRPLSGRLNVVLSRSSGFDIAntE 148
Cdd:cd00209     4 IVAVDENGVIGKDNKLPWHLPEDLKHFKKTT-------TGNPVIMGRKTFESIPR--RPLPGRTNIVLSRQLDYQDA--E 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726786 149 NVVTCSSIDSALDLLAappfsLSIEKVFVIGGGDILREALnkPSCEAIHITEIDTSIDCDTFIPTVDTSAYQPWCSSFPI 228
Cdd:cd00209    73 GVEVVHSLEEALELAE-----NTVEEIFVIGGAEIYKQAL--PYADRLYLTRIHAEFEGDTFFPEIDESEWELVSEEEVF 145

                         170
                  ....*....|...
gi 1063726786 229 CENGLRFSFTTHV 241
Cdd:cd00209   146 EEDGYSYTFETYE 158
Thymidylat_synt pfam00303
Thymidylate synthase; This is a family of proteins that are flavin-dependent thymidylate ...
 285-397 3.21e-59

Thymidylate synthase; This is a family of proteins that are flavin-dependent thymidylate synthases.


Pssm-ID: 459753  Cd Length: 259  Bit Score: 193.41  E-value: 3.21e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726786 285 YLNLVKEIISNGNLKDDRTGTGTLSKFGCQMKFNLRRN-FPLLTTKRVFWRGVVEELLWFISGSTNAKVLQEKGIRIWDg 363
Cdd:pfam00303   3 YLDLLRDILENGTEKEDRTGTGTLSVFGYQMRFDLSDGeFPLLTTKKVFWKSIIHELLWFLRGDTNIKYLQENGVHIWD- 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1063726786 364 nasrAYLDgiglterEEGDLGPVYGFQWRHFGAK 397
Cdd:pfam00303  82 ----EWAD-------ENGDLGPVYGFQWRHWGAP 104
ThyA COG0207
Thymidylate synthase [Nucleotide transport and metabolism]; Thymidylate synthase is part of ...
 285-394 2.44e-52

Thymidylate synthase [Nucleotide transport and metabolism]; Thymidylate synthase is part of the Pathway/BioSystem: Thymidylate biosynthesis


Pssm-ID: 439977  Cd Length: 264  Bit Score: 175.68  E-value: 2.44e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726786 285 YLNLVKEIISNGNLKDDRTGTGTLSKFGCQMKFNLRRNFPLLTTKRVFWRGVVEELLWFISGSTNAKVLQEKGIRIWDGN 364
Cdd:COG0207     4 YLDLLRHILEEGTWKEDRTGTGTLSVFGYQMRFDLSEGFPLLTTKKVHWKSIIHELLWFLRGDTNIRYLRENGVKIWDEW 83

                          90       100       110
                  ....*....|....*....|....*....|
gi 1063726786 365 AsrayldgiglteREEGDLGPVYGFQWRHF 394
Cdd:COG0207    84 A------------DENGDLGPVYGKQWRSW 101
thym_sym TIGR03284
thymidylate synthase; Members of this protein family are thymidylate synthase, an enzyme that ...
 285-398 5.98e-38

thymidylate synthase; Members of this protein family are thymidylate synthase, an enzyme that produces dTMP from dUMP. In prokaryotes, its gene usually is found close to that for dihydrofolate reductase, and in some systems the two enzymes are found as a fusion protein. This model excludes a set of related proteins (TIGR03283) that appears to replace this family in archaeal methanogens, where tetrahydrofolate is replaced by tetrahydromethanopterin. [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism]


Pssm-ID: 213790 [Multi-domain]  Cd Length: 295  Bit Score: 138.73  E-value: 5.98e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726786 285 YLNLVKEIISNGNLKDDRTGTGTLSKFGCQMKFNLRRNFPLLTTKRVFWRGVVEELLWFISGSTNAKVLQEKGIRIWDGN 364
Cdd:TIGR03284   2 YLDLLRDILENGHQKGDRTGTGTISVFGYQMRFDLSKGFPLLTTKKVPFRLIASELLWFLKGDTNIRYLLDHNVNIWDEW 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1063726786 365 ASRAYL-----DGIGLTE----------------REEGDLGPVYGFQWRHFGAKS 398
Cdd:TIGR03284  82 AFERWVksddyNGPDMTDfghraqddpeeddefaDKYGDLGPVYGKQWRSWATPD 136
dihyfolred_HdrA_Halo NF041386
dihydrofolate reductase HdrA;
68-220 1.28e-13

dihydrofolate reductase HdrA;


Pssm-ID: 469277 [Multi-domain]  Cd Length: 158  Bit Score: 68.06  E-value: 1.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726786  68 VVVAATKEMG-IGKDGKLPWN-LPTDLKFFKDltlSTSDSakknAVVMGRKTWESIpkkYRPLSGRLNVVLSRS-SGFDI 144
Cdd:NF041386    4 VSVAAVAENGvIGRDGELPWPsIPADKRQYRE---RVADD----PVILGRRTFESM---RDDLPGSAQIVLSRSeREFDV 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063726786 145 antENVVTCSSIDSALDLLAappfSLSIEKVFVIGGGDILreALNKPSCEAIHITEIDTSIDCDTFIPTVDTSAYQ 220
Cdd:NF041386   74 ---ETAHHAGGVDEAIEIAE----SLGAERAYVLGGAAIY--ELFQPHVDRMVLSRVPGEYEGDAYYPEWDEDEWE 140
trim_DfrL NF041668
trimethoprim-resistant dihydrofolate reductase DfrL;
78-215 8.53e-11

trimethoprim-resistant dihydrofolate reductase DfrL;


Pssm-ID: 469550 [Multi-domain]  Cd Length: 176  Bit Score: 60.44  E-value: 8.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726786  78 IGKDGKLPWNLPTDLKFFKDLTLST----------SDSAKKNAVVMGRKTWESIPkkYRPLSGRLNVVLSRSSGFdiaNT 147
Cdd:NF041668   13 IGKPGDLFVNAEDDMGHFGNSGDDDvnlmgdkkheKIPTMDDKNRIGIKLTENIP--VRADGAIICHSKEDNKNY---LA 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063726786 148 ENVVTCSSIDSALDLLaappFSLSIEKVFVIGGGdILREALNKPSCEAIHITEIDTSIDCDTFIPTVD 215
Cdd:NF041668   88 DGAIECHIHEDGGISA----FEMFIDEPIHLHGG-IIAEEFEGDEVMIEHDTIIDECFDGADGMPDED 150
 
Name Accession Description Interval E-value
PTZ00164 PTZ00164
bifunctional dihydrofolate reductase-thymidylate synthase; Provisional
 61-397 1.80e-147

bifunctional dihydrofolate reductase-thymidylate synthase; Provisional


Pssm-ID: 240299 [Multi-domain]  Cd Length: 514  Bit Score: 428.32  E-value: 1.80e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726786  61 KPQSTYQVVVAATKEMGIGKDGKLPWNLPTDLKFFKDLTLST------SDSAKKNAVVMGRKTWESIPKKYRPLSGRLNV 134
Cdd:PTZ00164    5 SSLKDFSIVVAVTLKRGIGIGNSLPWHIPEDMKFFSKITTYVreekyeKSPKKQNAVIMGRKTWESIPKKFRPLKNRINV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726786 135 VLSRSSGFDIANtENVVTCSSIDSALDLLAAPpfsLSIEKVFVIGGGDILREALNKPSCEAIHITEIDTSIDCDTFIPTV 214
Cdd:PTZ00164   85 VLSRTLTEEEAD-PGVLVFGSLEDALRLLAED---LSIEKIFIIGGASVYREALSANLLDKIYLTRVNSEYECDVFFPKI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726786 215 DTSAYQPWCSSFPICENGLRFSFTTHVRVKSSSA---GEASDESDGSKVLQVDWKKFSSVLPKMIFDRHEEYLYLNLVKE 291
Cdd:PTZ00164  161 PESFFIVAIVSQTFSTNGTSYDFVIYEKKNDDEEdllGKIFGQMKMTGRKKSPKEQLYKACPSLKIREHEEFQYLDLIAD 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726786 292 IISNGNLKDDRTGTGTLSKFGCQMKFNLRRNFPLLTTKRVFWRGVVEELLWFISGSTNAKVLQEKGIRIWDGNASRAYLD 371
Cdd:PTZ00164  241 IIKNGNVKEDRTGVGTISKFGYQMRFDLRESFPLLTTKKVFLRGIIEELLWFIRGETNGNLLLDKGVRIWEGNGSREFLD 320

                         330       340
                  ....*....|....*....|....*.
gi 1063726786 372 GIGLTEREEGDLGPVYGFQWRHFGAK 397
Cdd:PTZ00164  321 SRGLTHREENDLGPVYGFQWRHFGAE 346
DHFR cd00209
Dihydrofolate reductase (DHFR). Reduces 7,8-dihydrofolate to 5,6,7,8-tetrahydrofolate with ...
 69-241 6.10e-60

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: 191.58  E-value: 6.10e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726786  69 VVAATKEMGIGKDGKLPWNLPTDLKFFKDLTlstsdsaKKNAVVMGRKTWESIPKkyRPLSGRLNVVLSRSSGFDIAntE 148
Cdd:cd00209     4 IVAVDENGVIGKDNKLPWHLPEDLKHFKKTT-------TGNPVIMGRKTFESIPR--RPLPGRTNIVLSRQLDYQDA--E 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726786 149 NVVTCSSIDSALDLLAappfsLSIEKVFVIGGGDILREALnkPSCEAIHITEIDTSIDCDTFIPTVDTSAYQPWCSSFPI 228
Cdd:cd00209    73 GVEVVHSLEEALELAE-----NTVEEIFVIGGAEIYKQAL--PYADRLYLTRIHAEFEGDTFFPEIDESEWELVSEEEVF 145

                         170
                  ....*....|...
gi 1063726786 229 CENGLRFSFTTHV 241
Cdd:cd00209   146 EEDGYSYTFETYE 158
Thymidylat_synt pfam00303
Thymidylate synthase; This is a family of proteins that are flavin-dependent thymidylate ...
 285-397 3.21e-59

Thymidylate synthase; This is a family of proteins that are flavin-dependent thymidylate synthases.


Pssm-ID: 459753  Cd Length: 259  Bit Score: 193.41  E-value: 3.21e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726786 285 YLNLVKEIISNGNLKDDRTGTGTLSKFGCQMKFNLRRN-FPLLTTKRVFWRGVVEELLWFISGSTNAKVLQEKGIRIWDg 363
Cdd:pfam00303   3 YLDLLRDILENGTEKEDRTGTGTLSVFGYQMRFDLSDGeFPLLTTKKVFWKSIIHELLWFLRGDTNIKYLQENGVHIWD- 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1063726786 364 nasrAYLDgiglterEEGDLGPVYGFQWRHFGAK 397
Cdd:pfam00303  82 ----EWAD-------ENGDLGPVYGFQWRHWGAP 104
ThyA COG0207
Thymidylate synthase [Nucleotide transport and metabolism]; Thymidylate synthase is part of ...
 285-394 2.44e-52

Thymidylate synthase [Nucleotide transport and metabolism]; Thymidylate synthase is part of the Pathway/BioSystem: Thymidylate biosynthesis


Pssm-ID: 439977  Cd Length: 264  Bit Score: 175.68  E-value: 2.44e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726786 285 YLNLVKEIISNGNLKDDRTGTGTLSKFGCQMKFNLRRNFPLLTTKRVFWRGVVEELLWFISGSTNAKVLQEKGIRIWDGN 364
Cdd:COG0207     4 YLDLLRHILEEGTWKEDRTGTGTLSVFGYQMRFDLSEGFPLLTTKKVHWKSIIHELLWFLRGDTNIRYLRENGVKIWDEW 83

                          90       100       110
                  ....*....|....*....|....*....|
gi 1063726786 365 AsrayldgiglteREEGDLGPVYGFQWRHF 394
Cdd:COG0207    84 A------------DENGDLGPVYGKQWRSW 101
DHFR_1 pfam00186
Dihydrofolate reductase;
69-242 3.18e-49

Dihydrofolate reductase;


Pssm-ID: 425512 [Multi-domain]  Cd Length: 159  Bit Score: 163.87  E-value: 3.18e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726786  69 VVAATKEMGIGKDGKLPWNLPTDLKFFKDLTLStsdsakkNAVVMGRKTWESIPkkyRPLSGRLNVVLSRSSGFDIantE 148
Cdd:pfam00186   5 IAAMDENGVIGKDNDLPWHLPADLKHFKKLTTG-------KPVIMGRKTFESIG---RPLPGRKNIVLTRNPDYKV---D 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726786 149 NVVTCSSIDSALDLLAAPpfslsiEKVFVIGGGDILREALnkPSCEAIHITEIDTSIDCDTFIPTVDTSAYQ-PWCSSFP 227
Cdd:pfam00186  72 GVEVVHSLEEALALAAEA------EEIFIIGGAEIYAQAL--PLADRLYITEIDAEFDGDTFFPEIDPSEWQlVSREEHE 143

                         170
                  ....*....|....*.
gi 1063726786 228 ICE-NGLRFSFTTHVR 242
Cdd:pfam00186 144 ADEkNPYPYTFVTYER 159
thyA PRK01827
thymidylate synthase; Reviewed
 285-399 2.48e-48

thymidylate synthase; Reviewed


Pssm-ID: 234984  Cd Length: 264  Bit Score: 165.32  E-value: 2.48e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726786 285 YLNLVKEIISNGNLKDDRTGTGTLSKFGCQMKFNLRRNFPLLTTKRVFWRGVVEELLWFISGSTNAKVLQEKGIRIWDGN 364
Cdd:PRK01827    4 YLDLLRKILDEGTKKNDRTGTGTLSVFGAQMRFDLSKGFPLLTTKKVHFKSIIHELLWFLRGDTNIAYLQENGVHIWDEW 83

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1063726786 365 AsrayldgiglteREEGDLGPVYGFQWRHFGAKSV 399
Cdd:PRK01827   84 A------------DENGDLGPVYGKQWRSWPTPDG 106
TS_Pyrimidine_HMase cd00351
Thymidylate synthase and pyrimidine hydroxymethylase: Thymidylate synthase (TS) and ...
 285-397 1.34e-44

Thymidylate synthase and pyrimidine hydroxymethylase: Thymidylate synthase (TS) and deoxycytidylate hydroxymethylase (dCMP-HMase) are homologs that catalyze analogous alkylation of C5 of pyrimidine nucleotides. Both enzymes are involved in the biosynthesis of DNA precursors and are active as homodimers. However, they exhibit distinct pyrimidine base specificities and differ in the details of their catalyzed reactions. TS is biologically ubiquitous and catalyzes the conversion of dUMP and methylene-tetrahydrofolate (CH2THF) to dTMP and dihydrofolate (DHF). It also acts as a regulator of its own expression by binding and inactivating its own RNA. Due to its key role in the de novo pathway for thymidylate synthesis and, hence, DNA synthesis, it is one of the most conserved enzymes across species and phyla. TS is a well-recognized target for anticancer chemotherapy, as well as a valuable new target against infectious diseases. Interestingly, in several protozoa, a single polypeptide chain codes for both, dihydrofolate reductase (DHFR) and thymidylate synthase (TS), forming a bifunctional enzyme (DHFR-TS), possibly through gene fusion at a single evolutionary point. DHFR-TS is also active as a dimer. Virus encoded dCMP-HMase catalyzes the reversible conversion of dCMP and CH2THF to hydroxymethyl-dCMP and THF. This family also includes dUMP hydroxymethylase, which is encoded by several bacteriophages that infect Bacillus subtilis, for their own protection against the host restriction system, and contain hydroxymethyl-dUMP instead of dTMP in their DNA.


Pssm-ID: 238211  Cd Length: 215  Bit Score: 153.97  E-value: 1.34e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726786 285 YLNLVKEIISNGNLK-DDRTGTGTLSKFGCQMKFNLRRNFPLLTTKRVFWRGVVEELLWFISGSTNAKVLQEKGIRIWDG 363
Cdd:cd00351     2 YLDLWRKILEEGYRKtDDRTGTGTRSLFGAQLRFDLSEGFPLLTTKKVPWKSAIEELLWFLRGDTNAERLKEYGVSIWDE 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1063726786 364 NASrayldgiglterEEGDLGPVYGFQWRHFGAK 397
Cdd:cd00351    82 WAS------------KEGDLGYTYGFQWRHWGAP 103
thym_sym TIGR03284
thymidylate synthase; Members of this protein family are thymidylate synthase, an enzyme that ...
 285-398 5.98e-38

thymidylate synthase; Members of this protein family are thymidylate synthase, an enzyme that produces dTMP from dUMP. In prokaryotes, its gene usually is found close to that for dihydrofolate reductase, and in some systems the two enzymes are found as a fusion protein. This model excludes a set of related proteins (TIGR03283) that appears to replace this family in archaeal methanogens, where tetrahydrofolate is replaced by tetrahydromethanopterin. [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism]


Pssm-ID: 213790 [Multi-domain]  Cd Length: 295  Bit Score: 138.73  E-value: 5.98e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726786 285 YLNLVKEIISNGNLKDDRTGTGTLSKFGCQMKFNLRRNFPLLTTKRVFWRGVVEELLWFISGSTNAKVLQEKGIRIWDGN 364
Cdd:TIGR03284   2 YLDLLRDILENGHQKGDRTGTGTISVFGYQMRFDLSKGFPLLTTKKVPFRLIASELLWFLKGDTNIRYLLDHNVNIWDEW 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1063726786 365 ASRAYL-----DGIGLTE----------------REEGDLGPVYGFQWRHFGAKS 398
Cdd:TIGR03284  82 AFERWVksddyNGPDMTDfghraqddpeeddefaDKYGDLGPVYGKQWRSWATPD 136
folA PRK10769
type 3 dihydrofolate reductase;
78-226 3.80e-26

type 3 dihydrofolate reductase;


Pssm-ID: 182714 [Multi-domain]  Cd Length: 159  Bit Score: 102.90  E-value: 3.80e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726786  78 IGKDGKLPWNLPTDLKFFKDLTLSTSdsakknaVVMGRKTWESIPkkyRPLSGRLNVVLSRSSGFDiantENVVTCSSID 157
Cdd:PRK10769   14 IGMENAMPWNLPADLAWFKRNTLNKP-------VIMGRHTWESIG---RPLPGRKNIVISSQPGTD----DRVTWVKSVD 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063726786 158 SALDLLAappfslSIEKVFVIGGGDILREALnkPSCEAIHITEIDTSIDCDTFIPTvdtsaYQP--WCSSF 226
Cdd:PRK10769   80 EALAAAG------DVPEIMVIGGGRVYEQFL--PKAQRLYLTHIDAEVEGDTHFPD-----YEPdeWESVF 137
FolA COG0262
Dihydrofolate reductase [Coenzyme transport and metabolism]; Dihydrofolate reductase is part ...
 79-216 6.43e-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: 97.23  E-value: 6.43e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726786  79 GKDGKLPWNLPT--DLKFFKDLTLSTSdsakknAVVMGRKTWESIPKKY--RPLSGRLNVVLSRSSgfDIANTENV-VTC 153
Cdd:COG0262    17 GPDGDLPWLFPDpeDLAHFKELTAGAD------AVLMGRKTYESIAGYWptRPLPGRPKIVLSRTL--DEADWEGVtVVS 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063726786 154 SSIDSALDLLAAPPFslsiEKVFVIGGGDILREALNKPSCEAIHITEIDTSI-DCDTFIPTVDT 216
Cdd:COG0262    89 GDLEEALAALKAAGG----KDIWVIGGGELYRQLLPAGLVDELYLTVVPVVLgEGDRLFPELDA 148
thyA PRK13821
thymidylate synthase; Provisional
 285-396 1.09e-21

thymidylate synthase; Provisional


Pssm-ID: 184347  Cd Length: 323  Bit Score: 94.83  E-value: 1.09e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726786 285 YLNLVKEIISNGNLKDDRTGTGTLSKFGCQMKFNLRRNFPLLTTKRVFWRGVVEELLWFISGSTNAKVLQEKGIRIWDGN 364
Cdd:PRK13821    4 YLDLVRTILDTGTWQENRTGIRTISIPGAMLRFDLQQGFPAVTTKKLAFKSAIGELVGFLRASRSAADFRALGCKVWDQN 83

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1063726786 365 ASR-------AYLDGigltereEGDLGPVYGFQWRHFGA 396
Cdd:PRK13821   84 ANEnaqwlanPYRQG-------VDDLGDVYGVQWRQWPG 115
dihyfolred_HdrA_Halo NF041386
dihydrofolate reductase HdrA;
68-220 1.28e-13

dihydrofolate reductase HdrA;


Pssm-ID: 469277 [Multi-domain]  Cd Length: 158  Bit Score: 68.06  E-value: 1.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726786  68 VVVAATKEMG-IGKDGKLPWN-LPTDLKFFKDltlSTSDSakknAVVMGRKTWESIpkkYRPLSGRLNVVLSRS-SGFDI 144
Cdd:NF041386    4 VSVAAVAENGvIGRDGELPWPsIPADKRQYRE---RVADD----PVILGRRTFESM---RDDLPGSAQIVLSRSeREFDV 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063726786 145 antENVVTCSSIDSALDLLAappfSLSIEKVFVIGGGDILreALNKPSCEAIHITEIDTSIDCDTFIPTVDTSAYQ 220
Cdd:NF041386   74 ---ETAHHAGGVDEAIEIAE----SLGAERAYVLGGAAIY--ELFQPHVDRMVLSRVPGEYEGDAYYPEWDEDEWE 140
trim_DfrL NF041668
trimethoprim-resistant dihydrofolate reductase DfrL;
78-215 8.53e-11

trimethoprim-resistant dihydrofolate reductase DfrL;


Pssm-ID: 469550 [Multi-domain]  Cd Length: 176  Bit Score: 60.44  E-value: 8.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726786  78 IGKDGKLPWNLPTDLKFFKDLTLST----------SDSAKKNAVVMGRKTWESIPkkYRPLSGRLNVVLSRSSGFdiaNT 147
Cdd:NF041668   13 IGKPGDLFVNAEDDMGHFGNSGDDDvnlmgdkkheKIPTMDDKNRIGIKLTENIP--VRADGAIICHSKEDNKNY---LA 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063726786 148 ENVVTCSSIDSALDLLaappFSLSIEKVFVIGGGdILREALNKPSCEAIHITEIDTSIDCDTFIPTVD 215
Cdd:NF041668   88 DGAIECHIHEDGGISA----FEMFIDEPIHLHGG-IIAEEFEGDEVMIEHDTIIDECFDGADGMPDED 150
PLN02366 PLN02366
spermidine synthase
 174-202 1.70e-04

spermidine synthase


Pssm-ID: 215208 [Multi-domain]  Cd Length: 308  Bit Score: 43.10  E-value: 1.70e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1063726786 174 KVFVIGGGD--ILREALNKPSCEAIHITEID 202
Cdd:PLN02366   94 KVLVVGGGDggVLREIARHSSVEQIDICEID 124
scpA PRK00478
segregation and condensation protein ScpA;
74-211 2.94e-04

segregation and condensation protein ScpA;


Pssm-ID: 234776 [Multi-domain]  Cd Length: 505  Bit Score: 42.99  E-value: 2.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726786  74 KEMGIGKDGKLPWNLPTDLKFFKDLTLStsdsakkNAVVMGRKTWESIPKKYRPLSgrlNVVLSRSSGFDIANTENVVTC 153
Cdd:PRK00478   10 LNFGIAKNNQIPWKIDEELNHFHQTTTN-------HTIVMGYNTFQAMNKILANQA---NIVISKKHQRELKNNNELFVF 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1063726786 154 SSIDSALdllaappFSLSIEKVFVIGGGDILREALNKpsCEAIHITEIDTSIDCDTFI 211
Cdd:PRK00478   80 NDLKKLL-------IDFSNVDLFIIGGKKTIEQFIKY--ADQLIISKLNADYKCDLFV 128
Spermine_synth pfam01564
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ...
 173-221 4.63e-04

Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family includes spermidine synthase that catalyzes the fifth (last) step in the biosynthesis of spermidine from arginine, and spermine synthase.


Pssm-ID: 396237 [Multi-domain]  Cd Length: 183  Bit Score: 40.77  E-value: 4.63e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1063726786 173 EKVFVIGGGD--ILREALNKPSCEAIHITEIDTS-ID-CDTFIPTVDTSAYQP 221
Cdd:pfam01564  20 KKVLIIGGGDggVLREVVKHPSVEKITLVDIDEKvIDfSKKFLPSLAIGFQDP 72
PRK00811 PRK00811
polyamine aminopropyltransferase;
162-219 5.75e-04

polyamine aminopropyltransferase;


Pssm-ID: 234843 [Multi-domain]  Cd Length: 283  Bit Score: 41.30  E-value: 5.75e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063726786 162 LLAAPpfslSIEKVFVIGGGD--ILREALNKPSCEAIHITEID-TSID-CDTFIPTVDTSAY 219
Cdd:PRK00811   71 LFAHP----NPKRVLIIGGGDggTLREVLKHPSVEKITLVEIDeRVVEvCRKYLPEIAGGAY 128
COG4262 COG4262
Predicted spermidine synthase with an N-terminal membrane domain [General function prediction ...
 154-205 2.37e-03

Predicted spermidine synthase with an N-terminal membrane domain [General function prediction only];


Pssm-ID: 443404 [Multi-domain]  Cd Length: 426  Bit Score: 39.85  E-value: 2.37e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1063726786 154 SSIDSAL--DLLAAPPFSLS--IEKVFVIGGGD--ILREALNKPSCEAIHITEIDTSI 205
Cdd:COG4262   265 SSLDEYRyhEALVHPPMAAHprPRRVLVLGGGDglAAREVLKYPDVESVTLVDLDPEV 322
 
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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