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Conserved domains on  [gi|755510922|ref|XP_011248064|]
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thymidylate synthase isoform X1 [Mus musculus]

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 ...
 5-161 2.08e-119

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


:

Pssm-ID: 459753  Cd Length: 259  Bit Score: 337.08  E-value: 2.08e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755510922    5 YSGQGVDQLQKVIDTIKTNPDDRRIIMCAWNPKDLPLMALPPCHALCQFYVVNGELSCQLYQRSGDMGLGVPFNIASYAL 84
Cdd:pfam00303 104 PDGGGIDQLAQVIDQLKNNPDSRRIIVSAWNPADLPKMALPPCHYLFQFYVDGGKLSCQLYQRSADVFLGVPFNIASYAL 183

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755510922   85 LTYMIAHITGLQPGDFVHTLGDAHIYLNHIEPLKIQLQREPRPFPKLKILRKVeTIDDFKVEDFQIEGYNPHPTIKM 161
Cdd:pfam00303 184 LTHMIAQVTGLEPGEFVHTIGDAHIYDNHVEQVKEQLTREPRPLPKLKINRKV-SIFDFTFEDFELEGYQPHPKIKA 259
 
Name Accession Description Interval E-value
Thymidylat_synt pfam00303
Thymidylate synthase; This is a family of proteins that are flavin-dependent thymidylate ...
 5-161 2.08e-119

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


Pssm-ID: 459753  Cd Length: 259  Bit Score: 337.08  E-value: 2.08e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755510922    5 YSGQGVDQLQKVIDTIKTNPDDRRIIMCAWNPKDLPLMALPPCHALCQFYVVNGELSCQLYQRSGDMGLGVPFNIASYAL 84
Cdd:pfam00303 104 PDGGGIDQLAQVIDQLKNNPDSRRIIVSAWNPADLPKMALPPCHYLFQFYVDGGKLSCQLYQRSADVFLGVPFNIASYAL 183

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755510922   85 LTYMIAHITGLQPGDFVHTLGDAHIYLNHIEPLKIQLQREPRPFPKLKILRKVeTIDDFKVEDFQIEGYNPHPTIKM 161
Cdd:pfam00303 184 LTHMIAQVTGLEPGEFVHTIGDAHIYDNHVEQVKEQLTREPRPLPKLKINRKV-SIFDFTFEDFELEGYQPHPKIKA 259
PTZ00164 PTZ00164
bifunctional dihydrofolate reductase-thymidylate synthase; Provisional
 1-165 7.57e-119

bifunctional dihydrofolate reductase-thymidylate synthase; Provisional


Pssm-ID: 240299 [Multi-domain]  Cd Length: 514  Bit Score: 345.12  E-value: 7.57e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755510922   1 MDSDYSGQGVDQLQKVIDTIKTNPDDRRIIMCAWNPKDLPLMALPPCHALCQFYVVNGELSCQLYQRSGDMGLGVPFNIA 80
Cdd:PTZ00164 350 MHDDYTGQGVDQLKNIIETIKNNPDDRRLILTAWNPSALDQMALPPCHLLSQFYVNDGKLSCMMYQRSCDMGLGVPFNIA 429

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755510922  81 SYALLTYMIAHITGLQPGDFVHTLGDAHIYLNHIEPLKIQLQREPRPFPKLKILRKVETIDDFKVEDFQIEGYNPHPTIK 160
Cdd:PTZ00164 430 SYALLTHMIAQVCGLRPGEFVHFLGDAHVYSNHVDALKEQLERVPYPFPTLKLKREVENIEDFTIEDIEVIGYVPHPKIK 509


                 ....*
gi 755510922 161 MEMAV 165
Cdd:PTZ00164 510 MEMAV 514
ThyA COG0207
Thymidylate synthase [Nucleotide transport and metabolism]; Thymidylate synthase is part of ...
 7-165 3.89e-116

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


Pssm-ID: 439977  Cd Length: 264  Bit Score: 328.99  E-value: 3.89e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755510922   7 GQGVDQLQKVIDTIKTNPDDRRIIMCAWNPKDLPLMALPPCHALCQFYVVNGELSCQLYQRSGDMGLGVPFNIASYALLT 86
Cdd:COG0207  106 GGTIDQIAQVIDQLKTNPDSRRLIVSAWNPAELDEMALPPCHALFQFYVADGKLSCQLYQRSADVFLGVPFNIASYALLT 185

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755510922  87 YMIAHITGLQPGDFVHTLGDAHIYLNHIEPLKIQLQREPRPFPKLKILRKVETIDDFKVEDFQIEGYNPHPTIKMEMAV 165
Cdd:COG0207  186 HMVAQVTGLEPGEFVHTIGDAHIYLNHLEQVKEQLSREPRPLPKLKINPKVKSIFDFTFEDFELEGYDPHPAIKAPVAV 264
thym_sym TIGR03284
thymidylate synthase; Members of this protein family are thymidylate synthase, an enzyme that ...
 6-165 7.46e-100

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: 289.34  E-value: 7.46e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755510922    6 SGQGVDQLQKVIDTIKTNPDDRRIIMCAWNPKDLPLMALPPCHALCQFYVVNGELSCQLYQRSGDMGLGVPFNIASYALL 85
Cdd:TIGR03284 136 DGETIDQIKNVIEMIKTNPDSRRLIVSAWNPEDVPTMALPPCHTLFQFYVADGKLSCQLYQRSADVFLGVPFNIASYALL 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755510922   86 TYMIAHITGLQPGDFVHTLGDAHIYLNHIEPLKIQLQREPRPFPKLKILRKVETIDDFKVEDFQIEGYNPHPTIKMEMAV 165
Cdd:TIGR03284 216 THLIAQETGLEVGEFVHTLGDAHLYSNHLEQAKLQLTREPRPLPTLKLNPDKKDIFDFEYEDIEIEGYDPHPAIKAPVAV 295
TS_Pyrimidine_HMase cd00351
Thymidylate synthase and pyrimidine hydroxymethylase: Thymidylate synthase (TS) and ...
 4-118 2.83e-74

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: 221.38  E-value: 2.83e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755510922   4 DYSGQGVDQLQKVIDTIKTNPDDRRIIMCAWNPKDLPLMALPPCHALCQFYVVNGELSCQLYQRSGDMGLGVPFNIASYA 83
Cdd:cd00351  101 GAPGQGVDQIEKVIEKLKNNPDSRRAIISAWNPADLDLMALPPCHTLIQFYVRNGKLSLTLYQRSNDAFLGVPFNIASYA 180

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 755510922  84 LLTYMIAHITGLQPGDFVHTLGDAHIYLNHIEPLK 118
Cdd:cd00351  181 LLTEMIARVTGLEPGEFIHTIGDAHIYENHLEQVK 215
 
Name Accession Description Interval E-value
Thymidylat_synt pfam00303
Thymidylate synthase; This is a family of proteins that are flavin-dependent thymidylate ...
 5-161 2.08e-119

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


Pssm-ID: 459753  Cd Length: 259  Bit Score: 337.08  E-value: 2.08e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755510922    5 YSGQGVDQLQKVIDTIKTNPDDRRIIMCAWNPKDLPLMALPPCHALCQFYVVNGELSCQLYQRSGDMGLGVPFNIASYAL 84
Cdd:pfam00303 104 PDGGGIDQLAQVIDQLKNNPDSRRIIVSAWNPADLPKMALPPCHYLFQFYVDGGKLSCQLYQRSADVFLGVPFNIASYAL 183

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755510922   85 LTYMIAHITGLQPGDFVHTLGDAHIYLNHIEPLKIQLQREPRPFPKLKILRKVeTIDDFKVEDFQIEGYNPHPTIKM 161
Cdd:pfam00303 184 LTHMIAQVTGLEPGEFVHTIGDAHIYDNHVEQVKEQLTREPRPLPKLKINRKV-SIFDFTFEDFELEGYQPHPKIKA 259
PTZ00164 PTZ00164
bifunctional dihydrofolate reductase-thymidylate synthase; Provisional
 1-165 7.57e-119

bifunctional dihydrofolate reductase-thymidylate synthase; Provisional


Pssm-ID: 240299 [Multi-domain]  Cd Length: 514  Bit Score: 345.12  E-value: 7.57e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755510922   1 MDSDYSGQGVDQLQKVIDTIKTNPDDRRIIMCAWNPKDLPLMALPPCHALCQFYVVNGELSCQLYQRSGDMGLGVPFNIA 80
Cdd:PTZ00164 350 MHDDYTGQGVDQLKNIIETIKNNPDDRRLILTAWNPSALDQMALPPCHLLSQFYVNDGKLSCMMYQRSCDMGLGVPFNIA 429

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755510922  81 SYALLTYMIAHITGLQPGDFVHTLGDAHIYLNHIEPLKIQLQREPRPFPKLKILRKVETIDDFKVEDFQIEGYNPHPTIK 160
Cdd:PTZ00164 430 SYALLTHMIAQVCGLRPGEFVHFLGDAHVYSNHVDALKEQLERVPYPFPTLKLKREVENIEDFTIEDIEVIGYVPHPKIK 509


                 ....*
gi 755510922 161 MEMAV 165
Cdd:PTZ00164 510 MEMAV 514
ThyA COG0207
Thymidylate synthase [Nucleotide transport and metabolism]; Thymidylate synthase is part of ...
 7-165 3.89e-116

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


Pssm-ID: 439977  Cd Length: 264  Bit Score: 328.99  E-value: 3.89e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755510922   7 GQGVDQLQKVIDTIKTNPDDRRIIMCAWNPKDLPLMALPPCHALCQFYVVNGELSCQLYQRSGDMGLGVPFNIASYALLT 86
Cdd:COG0207  106 GGTIDQIAQVIDQLKTNPDSRRLIVSAWNPAELDEMALPPCHALFQFYVADGKLSCQLYQRSADVFLGVPFNIASYALLT 185

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755510922  87 YMIAHITGLQPGDFVHTLGDAHIYLNHIEPLKIQLQREPRPFPKLKILRKVETIDDFKVEDFQIEGYNPHPTIKMEMAV 165
Cdd:COG0207  186 HMVAQVTGLEPGEFVHTIGDAHIYLNHLEQVKEQLSREPRPLPKLKINPKVKSIFDFTFEDFELEGYDPHPAIKAPVAV 264
thyA PRK01827
thymidylate synthase; Reviewed
 4-165 4.09e-105

thymidylate synthase; Reviewed


Pssm-ID: 234984  Cd Length: 264  Bit Score: 301.30  E-value: 4.09e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755510922   4 DYSGQGVDQLQKVIDTIKTNPDDRRIIMCAWNPKDLPLMALPPCHALCQFYVVNGELSCQLYQRSGDMGLGVPFNIASYA 83
Cdd:PRK01827 103 TPDGRHIDQISKVIEQLKTNPDSRRLIVSAWNPGELDKMALPPCHALFQFYVADGKLSCQLYQRSADVFLGVPFNIASYA 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755510922  84 LLTYMIAHITGLQPGDFVHTLGDAHIYLNHIEPLKIQLQREPRPFPKLKILRKVETIDDFKVEDFQIEGYNPHPTIKMEM 163
Cdd:PRK01827 183 LLTHMIAQQTGLKVGEFVHTIGDAHIYSNHLEQAREQLSREPRPLPKLVINPDIKSIFDFEFEDFELEGYDPHPAIKAPV 262


                 ..
gi 755510922 164 AV 165
Cdd:PRK01827 263 AV 264
thym_sym TIGR03284
thymidylate synthase; Members of this protein family are thymidylate synthase, an enzyme that ...
 6-165 7.46e-100

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: 289.34  E-value: 7.46e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755510922    6 SGQGVDQLQKVIDTIKTNPDDRRIIMCAWNPKDLPLMALPPCHALCQFYVVNGELSCQLYQRSGDMGLGVPFNIASYALL 85
Cdd:TIGR03284 136 DGETIDQIKNVIEMIKTNPDSRRLIVSAWNPEDVPTMALPPCHTLFQFYVADGKLSCQLYQRSADVFLGVPFNIASYALL 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755510922   86 TYMIAHITGLQPGDFVHTLGDAHIYLNHIEPLKIQLQREPRPFPKLKILRKVETIDDFKVEDFQIEGYNPHPTIKMEMAV 165
Cdd:TIGR03284 216 THLIAQETGLEVGEFVHTLGDAHLYSNHLEQAKLQLTREPRPLPTLKLNPDKKDIFDFEYEDIEIEGYDPHPAIKAPVAV 295
TS_Pyrimidine_HMase cd00351
Thymidylate synthase and pyrimidine hydroxymethylase: Thymidylate synthase (TS) and ...
 4-118 2.83e-74

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: 221.38  E-value: 2.83e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755510922   4 DYSGQGVDQLQKVIDTIKTNPDDRRIIMCAWNPKDLPLMALPPCHALCQFYVVNGELSCQLYQRSGDMGLGVPFNIASYA 83
Cdd:cd00351  101 GAPGQGVDQIEKVIEKLKNNPDSRRAIISAWNPADLDLMALPPCHTLIQFYVRNGKLSLTLYQRSNDAFLGVPFNIASYA 180

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 755510922  84 LLTYMIAHITGLQPGDFVHTLGDAHIYLNHIEPLK 118
Cdd:cd00351  181 LLTEMIARVTGLEPGEFIHTIGDAHIYENHLEQVK 215
thyA PRK13821
thymidylate synthase; Provisional
 8-165 7.63e-47

thymidylate synthase; Provisional


Pssm-ID: 184347  Cd Length: 323  Bit Score: 154.92  E-value: 7.63e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755510922   8 QGVDQLQKVIDTIKTNPDDRRIIMCAWNPKDLPLMALPPCHALCQFY--VVNGELSCQLYQRSGDMGLGVPFNIASYALL 85
Cdd:PRK13821 153 KAIDQLRQCLDTIMNNPGSRRILFHGWNPAVLDEIALPACHLLYQFLpnVETREISLCLYIRSNDVGLGTPFNLTEGAAL 232

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755510922  86 TYMIAHITGLQPGDFVHTLGDAHIYLNHIEPLKIQLQREPRPFPKLKIlrkVETIDDF------------KVE--DFQIE 151
Cdd:PRK13821 233 LSLVGRLTGYTPRWFTYFIGDAHIYENQLDMLQEQLTREPYESPRLVI---SDRVPEYaktgvyepewleKIEpsDFSLV 309

                        170
                 ....*....|....
gi 755510922 152 GYNPHPTIKMEMAV 165
Cdd:PRK13821 310 GYRHHEPLTAPMAV 323
thy_syn_methano TIGR03283
thymidylate synthase, methanogen type; Thymidylate synthase makes dTMP for DNA synthesis, and ...
 9-110 1.01e-15

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: 70.93  E-value: 1.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755510922    9 GVDQLQKVIDTIKTNPDDRRIIMCAWNPKDLPLMALPPCHALCQFYVVNGELSCQLYQRSGDMGLGVPFNIASYALLTYM 88
Cdd:TIGR03283  91 GIDQIDYIIERLNQSPNSRRAIAITWDPPQDIKVDEVPCLQLVQFLIRDNKLYLTAFFRSNDVGGAWVANAIGLRRLQEY 170

                          90       100
                  ....*....|....*....|..
gi 755510922   89 IAHITGLQPGDFVHTLGDAHIY 110
Cdd:TIGR03283 171 VAEKVGVEPGTLTTHAISAHIY 192
thyA PRK00956
thymidylate synthase; Provisional
 10-110 2.00e-12

thymidylate synthase; Provisional


Pssm-ID: 179181  Cd Length: 208  Bit Score: 62.31  E-value: 2.00e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755510922  10 VDQLQKVIDTIKTNPDDRRIIMCAWNPK-DLPLMALPpCHALCQFYVVNGELSCQLYQRSGDMGLGVPFNIASYALLTYM 88
Cdd:PRK00956  95 VDQIDYIIEKLKENKNSRRATAVTWNPYiDTKVDEVP-CLQLVDFLIRDGKLYLTVLFRSNDAGGAFHANAIGLIKLGEY 173

                         90       100
                 ....*....|....*....|..
gi 755510922  89 IAHITGLQPGDFVHTLGDAHIY 110
Cdd:PRK00956 174 VAEKVGVELGTYTHHSVSAHIY 195
 
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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