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Conserved domains on  [gi|157785665|ref|NP_001099137|]
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thymidylate kinase isoform 1 [Mus musculus]

Protein Classification

nucleoside/nucleotide kinase family protein( domain architecture ID 106737)

nucleoside/nucleotide kinase family protein may catalyze the reversible phosphate group transfer from nucleoside triphosphates to nucleosides/nucleotides, nucleoside monophosphates, or sugars

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NK super family cl17190
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ...
5-211 2.23e-90

Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of enzymes that share structural similarity and are functionally related to the catalysis of the reversible phosphate group transfer from nucleoside triphosphates to nucleosides/nucleotides, nucleoside monophosphates, or sugars. Members of this family play a wide variety of essential roles in nucleotide metabolism, the biosynthesis of coenzymes and aromatic compounds, as well as the metabolism of sugar and sulfate.


The actual alignment was detected with superfamily member PLN02924:

Pssm-ID: 450170  Cd Length: 220  Bit Score: 264.28  E-value: 2.23e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157785665   5 RGALIVLEGVDRAGKTTQGLKLVTALCASGHRAELLRFPERSTEIGKLLNSYLEKKTELEDHSVHLLFSANRWEQVPLIK 84
Cdd:PLN02924  15 RGALIVLEGLDRSGKSTQCAKLVSFLKGLGVAAELWRFPDRTTSVGQMISAYLSNKSQLDDRAIHLLFSANRWEKRSLME 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157785665  85 AKLNQGVTLVLDRYAFSGVAFTGAKEnFSLDWCKQPDVGLPKPDLILFLQLQLLDAAARGEFGLERYETGTFQKQVLLCF 164
Cdd:PLN02924  95 RKLKSGTTLVVDRYSYSGVAFSAAKG-LDLEWCKAPEVGLPAPDLVLYLDISPEEAAERGGYGGERYEKLEFQKKVAKRF 173
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 157785665 165 QQLMEEKnlnWKVVDASKSIEEVHKEIRAHSEDAIRNA-AQRPLGELW 211
Cdd:PLN02924 174 QTLRDSS---WKIIDASQSIEEVEKKIREVVLDTVQRClAGKPLSRLW 218
 
Name Accession Description Interval E-value
PLN02924 PLN02924
thymidylate kinase
5-211 2.23e-90

thymidylate kinase


Pssm-ID: 178512  Cd Length: 220  Bit Score: 264.28  E-value: 2.23e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157785665   5 RGALIVLEGVDRAGKTTQGLKLVTALCASGHRAELLRFPERSTEIGKLLNSYLEKKTELEDHSVHLLFSANRWEQVPLIK 84
Cdd:PLN02924  15 RGALIVLEGLDRSGKSTQCAKLVSFLKGLGVAAELWRFPDRTTSVGQMISAYLSNKSQLDDRAIHLLFSANRWEKRSLME 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157785665  85 AKLNQGVTLVLDRYAFSGVAFTGAKEnFSLDWCKQPDVGLPKPDLILFLQLQLLDAAARGEFGLERYETGTFQKQVLLCF 164
Cdd:PLN02924  95 RKLKSGTTLVVDRYSYSGVAFSAAKG-LDLEWCKAPEVGLPAPDLVLYLDISPEEAAERGGYGGERYEKLEFQKKVAKRF 173
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 157785665 165 QQLMEEKnlnWKVVDASKSIEEVHKEIRAHSEDAIRNA-AQRPLGELW 211
Cdd:PLN02924 174 QTLRDSS---WKIIDASQSIEEVEKKIREVVLDTVQRClAGKPLSRLW 218
Thymidylate_kin pfam02223
Thymidylate kinase;
11-191 2.07e-50

Thymidylate kinase;


Pssm-ID: 396690  Cd Length: 184  Bit Score: 161.70  E-value: 2.07e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157785665   11 LEGVDRAGKTTQGLKLVTALCASGHRaELLRFPERSTEIGKLLNSYLEKKTELEDHSVHLLFSANR-WEQVPLIKAKLNQ 89
Cdd:pfam02223   1 IEGLDGAGKTTQAELLKERLKEQGIK-VVFTREPGGTPIGEKIRELLLRNEELSPLTEALLFAADRiQHLEQKIKPALKQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157785665   90 GVTLVLDRYAFSGVAFTGAKEN-FSLDWCKQPDVGlPKPDLILFLQLQLLDAAARGEFGLERYETG----TFQKQVLLCF 164
Cdd:pfam02223  80 GKTVIVDRYLFSGIAYQGAKGGdLDLVLSLNPDVP-GKPDLTFLLDVDPEVALKRLRRRGELEKTEfeqlDFLRKVRERY 158
                         170       180
                  ....*....|....*....|....*..
gi 157785665  165 QQLMEEKNlNWKVVDASKSIEEVHKEI 191
Cdd:pfam02223 159 LELAKFDE-RIKIIDASLSIEEVHEEI 184
DTMP_kinase TIGR00041
dTMP kinase; Function: phosphorylation of DTMP to form DTDP in both de novo and salvage ...
5-191 4.31e-36

dTMP kinase; Function: phosphorylation of DTMP to form DTDP in both de novo and salvage pathways of DTTP synthesis. Catalytic activity: ATP + thymidine 5'-phosphate = ADP + thymidine 5'-diphosphate. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]


Pssm-ID: 161676  Cd Length: 195  Bit Score: 125.17  E-value: 4.31e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157785665    5 RGALIVLEGVDRAGKTTQgLKLVTALCASGHRAELLRFPERSTEIGKLLNSYL--EKKTELEDHSVHLLFSANR-WEQVP 81
Cdd:TIGR00041   2 RGMFIVIEGIDGAGKTTQ-ANLLKKLLQENGYDVLFTREPGGTPIGEKIRELLlnENDEPLTDKAEALLFAADRhEHLED 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157785665   82 LIKAKLNQGVTLVLDRYAFSGVAFTGAKENFSLD--WCKQPDVGLPKPDLILFLQLQLLDA----AARGEFGLERYETGT 155
Cdd:TIGR00041  81 KIKPALAEGKLVISDRYVFSSIAYQGGARGIDEDlvLELNEDALGDMPDLTIYLDIDPEVAlerlRKRGELDREEFEKLD 160
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 157785665  156 FQKQVLLCFQQLMEEKNlNWKVVDASKSIEEVHKEI 191
Cdd:TIGR00041 161 FFEKVRQRYLELADKEK-SIHVIDATNSVEEVEQDI 195
Tmk COG0125
Thymidylate kinase [Nucleotide transport and metabolism]; Thymidylate kinase is part of the ...
5-194 6.47e-34

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


Pssm-ID: 439895 [Multi-domain]  Cd Length: 206  Bit Score: 119.88  E-value: 6.47e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157785665   5 RGALIVLEGVDRAGKTTQGLKLVTALCASGHRAELLRFPeRSTEIGKLL-NSYLEKKTELEDHSVHLLFSANRWEQV-PL 82
Cdd:COG0125    2 KGKFIVFEGIDGSGKSTQIKLLAEYLEARGYDVVLTREP-GGTPLGEAIrELLLGDNEDMSPRTELLLFAADRAQHVeEV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157785665  83 IKAKLNQGVTLVLDRYAFSGVAFTGAKENFSLDWCKQ---PDVGLPKPDLILFLQLQLLDAAAR---GEFGLERYETGT- 155
Cdd:COG0125   81 IRPALAAGKIVICDRYVDSSLAYQGGGRGLDLEWIRQlnrFATGGLKPDLTILLDVPPEVALARaraRGGELDRFESEDl 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 157785665 156 -FQKQVLLCFQQLMEEKNLNWKVVDASKSIEEVHKEIRAH 194
Cdd:COG0125  161 eFHERVREGYLELAAKEPERIVVIDASQSIEEVHAEIREA 200
TMPK cd01672
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the ...
8-194 1.27e-23

Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the phosphorylation of thymidine monophosphate (TMP) to thymidine diphosphate (TDP) utilizing ATP as its preferred phophoryl donor. TMPK represents the rate-limiting step in either de novo or salvage biosynthesis of thymidine triphosphate (TTP).


Pssm-ID: 238835  Cd Length: 200  Bit Score: 93.10  E-value: 1.27e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157785665   8 LIVLEGVDRAGKTTQGLKLVTALCASGHRAELLRFPeRSTEIGKLLNSYLEKKTELEDHSVH--LLFSANRWE-QVPLIK 84
Cdd:cd01672    2 FIVFEGIDGAGKTTLIELLAERLEARGYEVVLTREP-GGTPIGEAIRELLLDPEDEKMDPRAelLLFAADRAQhVEEVIK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157785665  85 AKLNQGVTLVLDRYAFSGVAFTGAKENFSLDWCKQPD---VGLPKPDL----ILFLQLQLLDAAARGEFGLERYETGTFQ 157
Cdd:cd01672   81 PALARGKIVLSDRFVDSSLAYQGAGRGLGEALIEALNdlaTGGLKPDLtillDIDPEVGLARIEARGRDDRDEQEGLEFH 160
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 157785665 158 KQVLLCFQQLMEEKNLNWKVVDASKSIEEVHKEIRAH 194
Cdd:cd01672  161 ERVREGYLELAAQEPERIIVIDASQPLEEVLAEILKA 197
 
Name Accession Description Interval E-value
PLN02924 PLN02924
thymidylate kinase
5-211 2.23e-90

thymidylate kinase


Pssm-ID: 178512  Cd Length: 220  Bit Score: 264.28  E-value: 2.23e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157785665   5 RGALIVLEGVDRAGKTTQGLKLVTALCASGHRAELLRFPERSTEIGKLLNSYLEKKTELEDHSVHLLFSANRWEQVPLIK 84
Cdd:PLN02924  15 RGALIVLEGLDRSGKSTQCAKLVSFLKGLGVAAELWRFPDRTTSVGQMISAYLSNKSQLDDRAIHLLFSANRWEKRSLME 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157785665  85 AKLNQGVTLVLDRYAFSGVAFTGAKEnFSLDWCKQPDVGLPKPDLILFLQLQLLDAAARGEFGLERYETGTFQKQVLLCF 164
Cdd:PLN02924  95 RKLKSGTTLVVDRYSYSGVAFSAAKG-LDLEWCKAPEVGLPAPDLVLYLDISPEEAAERGGYGGERYEKLEFQKKVAKRF 173
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 157785665 165 QQLMEEKnlnWKVVDASKSIEEVHKEIRAHSEDAIRNA-AQRPLGELW 211
Cdd:PLN02924 174 QTLRDSS---WKIIDASQSIEEVEKKIREVVLDTVQRClAGKPLSRLW 218
Thymidylate_kin pfam02223
Thymidylate kinase;
11-191 2.07e-50

Thymidylate kinase;


Pssm-ID: 396690  Cd Length: 184  Bit Score: 161.70  E-value: 2.07e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157785665   11 LEGVDRAGKTTQGLKLVTALCASGHRaELLRFPERSTEIGKLLNSYLEKKTELEDHSVHLLFSANR-WEQVPLIKAKLNQ 89
Cdd:pfam02223   1 IEGLDGAGKTTQAELLKERLKEQGIK-VVFTREPGGTPIGEKIRELLLRNEELSPLTEALLFAADRiQHLEQKIKPALKQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157785665   90 GVTLVLDRYAFSGVAFTGAKEN-FSLDWCKQPDVGlPKPDLILFLQLQLLDAAARGEFGLERYETG----TFQKQVLLCF 164
Cdd:pfam02223  80 GKTVIVDRYLFSGIAYQGAKGGdLDLVLSLNPDVP-GKPDLTFLLDVDPEVALKRLRRRGELEKTEfeqlDFLRKVRERY 158
                         170       180
                  ....*....|....*....|....*..
gi 157785665  165 QQLMEEKNlNWKVVDASKSIEEVHKEI 191
Cdd:pfam02223 159 LELAKFDE-RIKIIDASLSIEEVHEEI 184
DTMP_kinase TIGR00041
dTMP kinase; Function: phosphorylation of DTMP to form DTDP in both de novo and salvage ...
5-191 4.31e-36

dTMP kinase; Function: phosphorylation of DTMP to form DTDP in both de novo and salvage pathways of DTTP synthesis. Catalytic activity: ATP + thymidine 5'-phosphate = ADP + thymidine 5'-diphosphate. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]


Pssm-ID: 161676  Cd Length: 195  Bit Score: 125.17  E-value: 4.31e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157785665    5 RGALIVLEGVDRAGKTTQgLKLVTALCASGHRAELLRFPERSTEIGKLLNSYL--EKKTELEDHSVHLLFSANR-WEQVP 81
Cdd:TIGR00041   2 RGMFIVIEGIDGAGKTTQ-ANLLKKLLQENGYDVLFTREPGGTPIGEKIRELLlnENDEPLTDKAEALLFAADRhEHLED 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157785665   82 LIKAKLNQGVTLVLDRYAFSGVAFTGAKENFSLD--WCKQPDVGLPKPDLILFLQLQLLDA----AARGEFGLERYETGT 155
Cdd:TIGR00041  81 KIKPALAEGKLVISDRYVFSSIAYQGGARGIDEDlvLELNEDALGDMPDLTIYLDIDPEVAlerlRKRGELDREEFEKLD 160
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 157785665  156 FQKQVLLCFQQLMEEKNlNWKVVDASKSIEEVHKEI 191
Cdd:TIGR00041 161 FFEKVRQRYLELADKEK-SIHVIDATNSVEEVEQDI 195
Tmk COG0125
Thymidylate kinase [Nucleotide transport and metabolism]; Thymidylate kinase is part of the ...
5-194 6.47e-34

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


Pssm-ID: 439895 [Multi-domain]  Cd Length: 206  Bit Score: 119.88  E-value: 6.47e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157785665   5 RGALIVLEGVDRAGKTTQGLKLVTALCASGHRAELLRFPeRSTEIGKLL-NSYLEKKTELEDHSVHLLFSANRWEQV-PL 82
Cdd:COG0125    2 KGKFIVFEGIDGSGKSTQIKLLAEYLEARGYDVVLTREP-GGTPLGEAIrELLLGDNEDMSPRTELLLFAADRAQHVeEV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157785665  83 IKAKLNQGVTLVLDRYAFSGVAFTGAKENFSLDWCKQ---PDVGLPKPDLILFLQLQLLDAAAR---GEFGLERYETGT- 155
Cdd:COG0125   81 IRPALAAGKIVICDRYVDSSLAYQGGGRGLDLEWIRQlnrFATGGLKPDLTILLDVPPEVALARaraRGGELDRFESEDl 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 157785665 156 -FQKQVLLCFQQLMEEKNLNWKVVDASKSIEEVHKEIRAH 194
Cdd:COG0125  161 eFHERVREGYLELAAKEPERIVVIDASQSIEEVHAEIREA 200
TMPK cd01672
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the ...
8-194 1.27e-23

Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the phosphorylation of thymidine monophosphate (TMP) to thymidine diphosphate (TDP) utilizing ATP as its preferred phophoryl donor. TMPK represents the rate-limiting step in either de novo or salvage biosynthesis of thymidine triphosphate (TTP).


Pssm-ID: 238835  Cd Length: 200  Bit Score: 93.10  E-value: 1.27e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157785665   8 LIVLEGVDRAGKTTQGLKLVTALCASGHRAELLRFPeRSTEIGKLLNSYLEKKTELEDHSVH--LLFSANRWE-QVPLIK 84
Cdd:cd01672    2 FIVFEGIDGAGKTTLIELLAERLEARGYEVVLTREP-GGTPIGEAIRELLLDPEDEKMDPRAelLLFAADRAQhVEEVIK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157785665  85 AKLNQGVTLVLDRYAFSGVAFTGAKENFSLDWCKQPD---VGLPKPDL----ILFLQLQLLDAAARGEFGLERYETGTFQ 157
Cdd:cd01672   81 PALARGKIVLSDRFVDSSLAYQGAGRGLGEALIEALNdlaTGGLKPDLtillDIDPEVGLARIEARGRDDRDEQEGLEFH 160
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 157785665 158 KQVLLCFQQLMEEKNLNWKVVDASKSIEEVHKEIRAH 194
Cdd:cd01672  161 ERVREGYLELAAQEPERIIVIDASQPLEEVLAEILKA 197
PRK07933 PRK07933
dTMP kinase;
8-128 2.72e-08

dTMP kinase;


Pssm-ID: 236133  Cd Length: 213  Bit Score: 51.90  E-value: 2.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157785665   8 LIVLEGVDRAGKTTQGLKLVTALCASGHRAELLRFPERSTEI-GKLLNSYLekKTELED--HSVH---LLFSANRWEQVP 81
Cdd:PRK07933   2 LIAIEGVDGAGKRTLTEALRAALEARGRSVATLAFPRYGRSVhADLAAEAL--HGRHGDlaDSVYamaTLFALDRAGARD 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 157785665  82 LIKAKLNQGVTLVLDRYAFSGVAFTGAK-----ENFSLDWCKQPDV---GLPKPD 128
Cdd:PRK07933  80 ELAGLLAAHDVVILDRYVASNAAYSAARlhqdaDGEAVAWVAELEFgrlGLPVPD 134
 
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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