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Conserved domains on  [gi|32709481|gb|AAP86759|]
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thymidylate synthase, partial [Enterobacteria phage TuIa]

Protein Classification

thymidylate synthase( domain architecture ID 10447802)

thymidylate synthase catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product

CATH:  3.30.572.10
EC:  2.1.1.45
Gene Ontology:  GO:0008168|GO:0032259|GO:0016740|GO:0006231|GO:0004799
PubMed:  16178783|2223755|12084462|23611499
SCOP:  4001903

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Thymidylat_synt pfam00303
Thymidylate synthase; This is a family of proteins that are flavin-dependent thymidylate ...
 1-162 2.06e-83

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


:

Pssm-ID: 459753  Cd Length: 259  Bit Score: 246.18  E-value: 2.06e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32709481     1 QLVKTIDRIKALPNDRRQIVSAWNPAEIDQMALPPCHMFYQFNVRNGHLDLQWYQRSVDVFLGLPFNIASYAALTHIVAK 80
Cdd:pfam00303 111 QLAQVIDQLKNNPDSRRIIVSAWNPADLPKMALPPCHYLFQFYVDGGKLSCQLYQRSADVFLGVPFNIASYALLTHMIAQ 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32709481    81 MCNLIPGDLVFSGGNTHIYSNHVEQCKEVIRREPKELCSLEITWPSNFENWptkiqmdwvtgtmTHTDFVLKNYESHPAI 160
Cdd:pfam00303 191 VTGLEPGEFVHTIGDAHIYDNHVEQVKEQLTREPRPLPKLKINRKVSIFDF-------------TFEDFELEGYQPHPKI 257


                  ..
gi 32709481   161 KA 162
Cdd:pfam00303 258 KA 259
 
Name Accession Description Interval E-value
Thymidylat_synt pfam00303
Thymidylate synthase; This is a family of proteins that are flavin-dependent thymidylate ...
 1-162 2.06e-83

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


Pssm-ID: 459753  Cd Length: 259  Bit Score: 246.18  E-value: 2.06e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32709481     1 QLVKTIDRIKALPNDRRQIVSAWNPAEIDQMALPPCHMFYQFNVRNGHLDLQWYQRSVDVFLGLPFNIASYAALTHIVAK 80
Cdd:pfam00303 111 QLAQVIDQLKNNPDSRRIIVSAWNPADLPKMALPPCHYLFQFYVDGGKLSCQLYQRSADVFLGVPFNIASYALLTHMIAQ 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32709481    81 MCNLIPGDLVFSGGNTHIYSNHVEQCKEVIRREPKELCSLEITWPSNFENWptkiqmdwvtgtmTHTDFVLKNYESHPAI 160
Cdd:pfam00303 191 VTGLEPGEFVHTIGDAHIYDNHVEQVKEQLTREPRPLPKLKINRKVSIFDF-------------TFEDFELEGYQPHPKI 257


                  ..
gi 32709481   161 KA 162
Cdd:pfam00303 258 KA 259
ThyA COG0207
Thymidylate synthase [Nucleotide transport and metabolism]; Thymidylate synthase is part of ...
 1-166 3.50e-82

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


Pssm-ID: 439977  Cd Length: 264  Bit Score: 243.09  E-value: 3.50e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32709481   1 QLVKTIDRIKALPNDRRQIVSAWNPAEIDQMALPPCHMFYQFNVRNGHLDLQWYQRSVDVFLGLPFNIASYAALTHIVAK 80
Cdd:COG0207 111 QIAQVIDQLKTNPDSRRLIVSAWNPAELDEMALPPCHALFQFYVADGKLSCQLYQRSADVFLGVPFNIASYALLTHMVAQ 190

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32709481  81 MCNLIPGDLVFSGGNTHIYSNHVEQCKEVIRREPKELCSLEI-TWPSNFENwptkIQMDwvtgtmthtDFVLKNYESHPA 159
Cdd:COG0207 191 VTGLEPGEFVHTIGDAHIYLNHLEQVKEQLSREPRPLPKLKInPKVKSIFD----FTFE---------DFELEGYDPHPA 257


                ....*..
gi 32709481 160 IKAKMAV 166
Cdd:COG0207 258 IKAPVAV 264
thyA PRK01827
thymidylate synthase; Reviewed
 1-166 2.34e-75

thymidylate synthase; Reviewed


Pssm-ID: 234984  Cd Length: 264  Bit Score: 225.80  E-value: 2.34e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32709481    1 QLVKTIDRIKALPNDRRQIVSAWNPAEIDQMALPPCHMFYQFNVRNGHLDLQWYQRSVDVFLGLPFNIASYAALTHIVAK 80
Cdd:PRK01827 111 QISKVIEQLKTNPDSRRLIVSAWNPGELDKMALPPCHALFQFYVADGKLSCQLYQRSADVFLGVPFNIASYALLTHMIAQ 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32709481   81 MCNLIPGDLVFSGGNTHIYSNHVEQCKEVIRREPKELCSLEITW-PSNFENwptkIQMDwvtgtmthtDFVLKNYESHPA 159
Cdd:PRK01827 191 QTGLKVGEFVHTIGDAHIYSNHLEQAREQLSREPRPLPKLVINPdIKSIFD----FEFE---------DFELEGYDPHPA 257


                 ....*..
gi 32709481  160 IKAKMAV 166
Cdd:PRK01827 258 IKAPVAV 264
thym_sym TIGR03284
thymidylate synthase; Members of this protein family are thymidylate synthase, an enzyme that ...
 1-166 1.05e-69

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: 212.69  E-value: 1.05e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32709481     1 QLVKTIDRIKALPNDRRQIVSAWNPAEIDQMALPPCHMFYQFNVRNGHLDLQWYQRSVDVFLGLPFNIASYAALTHIVAK 80
Cdd:TIGR03284 142 QIKNVIEMIKTNPDSRRLIVSAWNPEDVPTMALPPCHTLFQFYVADGKLSCQLYQRSADVFLGVPFNIASYALLTHLIAQ 221

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32709481    81 MCNLIPGDLVFSGGNTHIYSNHVEQCKEVIRREPKELCSLEItwpsnfeNWPTKIQMDWvtgtmTHTDFVLKNYESHPAI 160
Cdd:TIGR03284 222 ETGLEVGEFVHTLGDAHLYSNHLEQAKLQLTREPRPLPTLKL-------NPDKKDIFDF-----EYEDIEIEGYDPHPAI 289


                  ....*.
gi 32709481   161 KAKMAV 166
Cdd:TIGR03284 290 KAPVAV 295
TS_Pyrimidine_HMase cd00351
Thymidylate synthase and pyrimidine hydroxymethylase: Thymidylate synthase (TS) and ...
 1-107 7.87e-54

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: 169.38  E-value: 7.87e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32709481   1 QLVKTIDRIKALPNDRRQIVSAWNPAEIDQMALPPCHMFYQFNVRNGHLDLQWYQRSVDVFLGLPFNIASYAALTHIVAK 80
Cdd:cd00351 109 QIEKVIEKLKNNPDSRRAIISAWNPADLDLMALPPCHTLIQFYVRNGKLSLTLYQRSNDAFLGVPFNIASYALLTEMIAR 188

                        90       100
                ....*....|....*....|....*..
gi 32709481  81 MCNLIPGDLVFSGGNTHIYSNHVEQCK 107
Cdd:cd00351 189 VTGLEPGEFIHTIGDAHIYENHLEQVK 215
 
Name Accession Description Interval E-value
Thymidylat_synt pfam00303
Thymidylate synthase; This is a family of proteins that are flavin-dependent thymidylate ...
 1-162 2.06e-83

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


Pssm-ID: 459753  Cd Length: 259  Bit Score: 246.18  E-value: 2.06e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32709481     1 QLVKTIDRIKALPNDRRQIVSAWNPAEIDQMALPPCHMFYQFNVRNGHLDLQWYQRSVDVFLGLPFNIASYAALTHIVAK 80
Cdd:pfam00303 111 QLAQVIDQLKNNPDSRRIIVSAWNPADLPKMALPPCHYLFQFYVDGGKLSCQLYQRSADVFLGVPFNIASYALLTHMIAQ 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32709481    81 MCNLIPGDLVFSGGNTHIYSNHVEQCKEVIRREPKELCSLEITWPSNFENWptkiqmdwvtgtmTHTDFVLKNYESHPAI 160
Cdd:pfam00303 191 VTGLEPGEFVHTIGDAHIYDNHVEQVKEQLTREPRPLPKLKINRKVSIFDF-------------TFEDFELEGYQPHPKI 257


                  ..
gi 32709481   161 KA 162
Cdd:pfam00303 258 KA 259
ThyA COG0207
Thymidylate synthase [Nucleotide transport and metabolism]; Thymidylate synthase is part of ...
 1-166 3.50e-82

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


Pssm-ID: 439977  Cd Length: 264  Bit Score: 243.09  E-value: 3.50e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32709481   1 QLVKTIDRIKALPNDRRQIVSAWNPAEIDQMALPPCHMFYQFNVRNGHLDLQWYQRSVDVFLGLPFNIASYAALTHIVAK 80
Cdd:COG0207 111 QIAQVIDQLKTNPDSRRLIVSAWNPAELDEMALPPCHALFQFYVADGKLSCQLYQRSADVFLGVPFNIASYALLTHMVAQ 190

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32709481  81 MCNLIPGDLVFSGGNTHIYSNHVEQCKEVIRREPKELCSLEI-TWPSNFENwptkIQMDwvtgtmthtDFVLKNYESHPA 159
Cdd:COG0207 191 VTGLEPGEFVHTIGDAHIYLNHLEQVKEQLSREPRPLPKLKInPKVKSIFD----FTFE---------DFELEGYDPHPA 257


                ....*..
gi 32709481 160 IKAKMAV 166
Cdd:COG0207 258 IKAPVAV 264
thyA PRK01827
thymidylate synthase; Reviewed
 1-166 2.34e-75

thymidylate synthase; Reviewed


Pssm-ID: 234984  Cd Length: 264  Bit Score: 225.80  E-value: 2.34e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32709481    1 QLVKTIDRIKALPNDRRQIVSAWNPAEIDQMALPPCHMFYQFNVRNGHLDLQWYQRSVDVFLGLPFNIASYAALTHIVAK 80
Cdd:PRK01827 111 QISKVIEQLKTNPDSRRLIVSAWNPGELDKMALPPCHALFQFYVADGKLSCQLYQRSADVFLGVPFNIASYALLTHMIAQ 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32709481   81 MCNLIPGDLVFSGGNTHIYSNHVEQCKEVIRREPKELCSLEITW-PSNFENwptkIQMDwvtgtmthtDFVLKNYESHPA 159
Cdd:PRK01827 191 QTGLKVGEFVHTIGDAHIYSNHLEQAREQLSREPRPLPKLVINPdIKSIFD----FEFE---------DFELEGYDPHPA 257


                 ....*..
gi 32709481  160 IKAKMAV 166
Cdd:PRK01827 258 IKAPVAV 264
thym_sym TIGR03284
thymidylate synthase; Members of this protein family are thymidylate synthase, an enzyme that ...
 1-166 1.05e-69

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: 212.69  E-value: 1.05e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32709481     1 QLVKTIDRIKALPNDRRQIVSAWNPAEIDQMALPPCHMFYQFNVRNGHLDLQWYQRSVDVFLGLPFNIASYAALTHIVAK 80
Cdd:TIGR03284 142 QIKNVIEMIKTNPDSRRLIVSAWNPEDVPTMALPPCHTLFQFYVADGKLSCQLYQRSADVFLGVPFNIASYALLTHLIAQ 221

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32709481    81 MCNLIPGDLVFSGGNTHIYSNHVEQCKEVIRREPKELCSLEItwpsnfeNWPTKIQMDWvtgtmTHTDFVLKNYESHPAI 160
Cdd:TIGR03284 222 ETGLEVGEFVHTLGDAHLYSNHLEQAKLQLTREPRPLPTLKL-------NPDKKDIFDF-----EYEDIEIEGYDPHPAI 289


                  ....*.
gi 32709481   161 KAKMAV 166
Cdd:TIGR03284 290 KAPVAV 295
PTZ00164 PTZ00164
bifunctional dihydrofolate reductase-thymidylate synthase; Provisional
 1-166 3.07e-60

bifunctional dihydrofolate reductase-thymidylate synthase; Provisional


Pssm-ID: 240299 [Multi-domain]  Cd Length: 514  Bit Score: 194.50  E-value: 3.07e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32709481    1 QLVKTIDRIKALPNDRRQIVSAWNPAEIDQMALPPCHMFYQFNVRNGHLDLQWYQRSVDVFLGLPFNIASYAALTHIVAK 80
Cdd:PTZ00164 361 QLKNIIETIKNNPDDRRLILTAWNPSALDQMALPPCHLLSQFYVNDGKLSCMMYQRSCDMGLGVPFNIASYALLTHMIAQ 440

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32709481   81 MCNLIPGDLVFSGGNTHIYSNHVEQCKEVIRREPKELCSLeitwpsNFENWPTKIQmDWvtgtmTHTDFVLKNYESHPAI 160
Cdd:PTZ00164 441 VCGLRPGEFVHFLGDAHVYSNHVDALKEQLERVPYPFPTL------KLKREVENIE-DF-----TIEDIEVIGYVPHPKI 508


                 ....*.
gi 32709481  161 KAKMAV 166
Cdd:PTZ00164 509 KMEMAV 514
TS_Pyrimidine_HMase cd00351
Thymidylate synthase and pyrimidine hydroxymethylase: Thymidylate synthase (TS) and ...
 1-107 7.87e-54

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: 169.38  E-value: 7.87e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32709481   1 QLVKTIDRIKALPNDRRQIVSAWNPAEIDQMALPPCHMFYQFNVRNGHLDLQWYQRSVDVFLGLPFNIASYAALTHIVAK 80
Cdd:cd00351 109 QIEKVIEKLKNNPDSRRAIISAWNPADLDLMALPPCHTLIQFYVRNGKLSLTLYQRSNDAFLGVPFNIASYALLTEMIAR 188

                        90       100
                ....*....|....*....|....*..
gi 32709481  81 MCNLIPGDLVFSGGNTHIYSNHVEQCK 107
Cdd:cd00351 189 VTGLEPGEFIHTIGDAHIYENHLEQVK 215
thyA PRK13821
thymidylate synthase; Provisional
 1-166 2.53e-36

thymidylate synthase; Provisional


Pssm-ID: 184347  Cd Length: 323  Bit Score: 127.57  E-value: 2.53e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32709481    1 QLVKTIDRIKALPNDRRQIVSAWNPAEIDQMALPPCHMFYQF--NVRNGHLDLQWYQRSVDVFLGLPFNIASYAALTHIV 78
Cdd:PRK13821 157 QLRQCLDTIMNNPGSRRILFHGWNPAVLDEIALPACHLLYQFlpNVETREISLCLYIRSNDVGLGTPFNLTEGAALLSLV 236

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32709481   79 AKMCNLIPGDLVFSGGNTHIYSNHVEQCKEVIRREPKELCSLEITwpsnfENWPT-----KIQMDWVTgTMTHTDFVLKN 153
Cdd:PRK13821 237 GRLTGYTPRWFTYFIGDAHIYENQLDMLQEQLTREPYESPRLVIS-----DRVPEyaktgVYEPEWLE-KIEPSDFSLVG 310

                        170
                 ....*....|...
gi 32709481  154 YESHPAIKAKMAV 166
Cdd:PRK13821 311 YRHHEPLTAPMAV 323
thy_syn_methano TIGR03283
thymidylate synthase, methanogen type; Thymidylate synthase makes dTMP for DNA synthesis, and ...
 1-99 1.92e-12

thymidylate synthase, methanogen type; Thymidylate synthase makes dTMP for DNA synthesis, and is among the most widely distributed of all enzymes. Members of this protein family are encoded within a completed genome sequence if and only if that species is one of the methanogenenic archaea. In these species, tetrahydromethanopterin replaces tetrahydrofolate, The member from Methanobacterium thermoautotrophicum was shown to behave as a thymidylate synthase based on similar side reactions (the exchange of a characteristic proton with water), although the full reaction was not reconstituted. Partial sequence data showed no similarity to known thymidylate synthases simply because the region sequenced was from a distinctive N-terminal region not found in other thymidylate synthases. Members of this protein family appear, therefore, to a novel, tetrahydromethanopterin-dependent thymidylate synthase. [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism]


Pssm-ID: 132326  Cd Length: 199  Bit Score: 62.07  E-value: 1.92e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32709481     1 QLVKTIDRIKALPNDRRQIVSAWNPAEIDQMALPPCHMFYQFNVRNGHLDLQWYQRSVDVFLGLPFNIASYAALTHIVAK 80
Cdd:TIGR03283  94 QIDYIIERLNQSPNSRRAIAITWDPPQDIKVDEVPCLQLVQFLIRDNKLYLTAFFRSNDVGGAWVANAIGLRRLQEYVAE 173

                          90
                  ....*....|....*....
gi 32709481    81 MCNLIPGDLVFSGGNTHIY 99
Cdd:TIGR03283 174 KVGVEPGTLTTHAISAHIY 192
thyA PRK00956
thymidylate synthase; Provisional
 1-111 2.25e-12

thymidylate synthase; Provisional


Pssm-ID: 179181  Cd Length: 208  Bit Score: 62.31  E-value: 2.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32709481    1 QLVKTIDRIKALPNDRRQIVSAWNPaEIDQ-MALPPCHMFYQFNVRNGHLDLQWYQRSVDVFLGLPFNIASYAALTHIVA 79
Cdd:PRK00956  97 QIDYIIEKLKENKNSRRATAVTWNP-YIDTkVDEVPCLQLVDFLIRDGKLYLTVLFRSNDAGGAFHANAIGLIKLGEYVA 175

                         90       100       110
                 ....*....|....*....|....*....|..
gi 32709481   80 KMCNLIPGDLVFSGGNTHIYSNHVEQCKEVIR 111
Cdd:PRK00956 176 EKVGVELGTYTHHSVSAHIYERDWDYLEKIFK 207
 
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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