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Conserved domains on  [gi|446998995|ref|WP_001076251|]
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dTMP kinase [Escherichia coli]

Protein Classification

dTMP kinase( domain architecture ID 10109302)

dTMP (thymidylate) kinase catalyzes the reversible phosphorylation of deoxythymidine monophosphate (dTMP) to deoxythymidine diphosphate (dTDP) using ATP as a phosphoryl donor

CATH:  3.40.50.300
EC:  2.7.4.9
Gene Ontology:  GO:0005524|GO:0004798|GO:0006233|GO:0016310|GO:0006235
PubMed:  8631667
SCOP:  4004030

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TMPK cd01672
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the ...
 15-234 8.11e-25

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: 96.95  E-value: 8.11e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998995  15 RVIAIVGCDGSGKSTLTASLVNELAARmptehiylgqssgrigewisQLPVI------GAPFGRYLRSKAAHVHEKPSTP 88
Cdd:cd01672    1 MFIVFEGIDGAGKTTLIELLAERLEAR--------------------GYEVVltrepgGTPIGEAIRELLLDPEDEKMDP 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998995  89 PGNitalvIYLLSCWRAYKFRKMLCKS-QQGYLLITDRYPQVEVPGFRFDGPqlakttGGNGWIKMLRQRELKLYQwmas 167
Cdd:cd01672   61 RAE-----LLLFAADRAQHVEEVIKPAlARGKIVLSDRFVDSSLAYQGAGRG------LGEALIEALNDLATGGLK---- 125

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446998995 168 ylPVLLIRLGIDEQTAFSRKPDHQL--------AALQEKIAVTPQLTFN--GAKILELDGRQPADEIMQASLRAIHA 234
Cdd:cd01672  126 --PDLTILLDIDPEVGLARIEARGRddrdeqegLEFHERVREGYLELAAqePERIIVIDASQPLEEVLAEILKAILE 200
 
Name Accession Description Interval E-value
TMPK cd01672
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the ...
 15-234 8.11e-25

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: 96.95  E-value: 8.11e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998995  15 RVIAIVGCDGSGKSTLTASLVNELAARmptehiylgqssgrigewisQLPVI------GAPFGRYLRSKAAHVHEKPSTP 88
Cdd:cd01672    1 MFIVFEGIDGAGKTTLIELLAERLEAR--------------------GYEVVltrepgGTPIGEAIRELLLDPEDEKMDP 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998995  89 PGNitalvIYLLSCWRAYKFRKMLCKS-QQGYLLITDRYPQVEVPGFRFDGPqlakttGGNGWIKMLRQRELKLYQwmas 167
Cdd:cd01672   61 RAE-----LLLFAADRAQHVEEVIKPAlARGKIVLSDRFVDSSLAYQGAGRG------LGEALIEALNDLATGGLK---- 125

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446998995 168 ylPVLLIRLGIDEQTAFSRKPDHQL--------AALQEKIAVTPQLTFN--GAKILELDGRQPADEIMQASLRAIHA 234
Cdd:cd01672  126 --PDLTILLDIDPEVGLARIEARGRddrdeqegLEFHERVREGYLELAAqePERIIVIDASQPLEEVLAEILKAILE 200
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 11-44 3.13e-05

Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 440337 [Multi-domain]  Cd Length: 206  Bit Score: 43.29  E-value: 3.13e-05
                         10        20        30
                 ....*....|....*....|....*....|....
gi 446998995  11 STPVRVIAIVGCDGSGKSTLTASLVNELAARMPT 44
Cdd:COG0572    4 SGKPRIIGIAGPSGSGKTTFARRLAEQLGADKVV 37
PRK07933 PRK07933
dTMP kinase;
15-80 8.13e-04

dTMP kinase;


Pssm-ID: 236133  Cd Length: 213  Bit Score: 39.19  E-value: 8.13e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446998995  15 RVIAIVGCDGSGKSTLTASLVNELAARmptehiylGQSSGRIGewisqlpvigapFGRYLRSKAAH 80
Cdd:PRK07933   1 MLIAIEGVDGAGKRTLTEALRAALEAR--------GRSVATLA------------FPRYGRSVHAD 46
MobB pfam03205
Molybdopterin guanine dinucleotide synthesis protein B; This protein contains a P-loop.
 16-41 3.43e-03

Molybdopterin guanine dinucleotide synthesis protein B; This protein contains a P-loop.


Pssm-ID: 427196 [Multi-domain]  Cd Length: 133  Bit Score: 36.76  E-value: 3.43e-03
                          10        20
                  ....*....|....*....|....*.
gi 446998995   16 VIAIVGCDGSGKSTLTASLVNELAAR 41
Cdd:pfam03205   1 ILGIVGWSGSGKTTLLEKLIPELKAR 26
DTMP_kinase TIGR00041
dTMP kinase; Function: phosphorylation of DTMP to form DTDP in both de novo and salvage ...
 17-126 3.73e-03

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: 37.34  E-value: 3.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998995   17 IAIVGCDGSGKSTLTASLVNELAARMPTEHIYLGQSSGRIGEWIsqlpvigapfgrylRSKAAHVHEKPSTPpgnitALV 96
Cdd:TIGR00041   6 IVIEGIDGAGKTTQANLLKKLLQENGYDVLFTREPGGTPIGEKI--------------RELLLNENDEPLTD-----KAE 66

                          90       100       110
                  ....*....|....*....|....*....|.
gi 446998995   97 IYLLSCWRAYKFR-KMLCKSQQGYLLITDRY 126
Cdd:TIGR00041  67 ALLFAADRHEHLEdKIKPALAEGKLVISDRY 97
 
Name Accession Description Interval E-value
TMPK cd01672
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the ...
 15-234 8.11e-25

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: 96.95  E-value: 8.11e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998995  15 RVIAIVGCDGSGKSTLTASLVNELAARmptehiylgqssgrigewisQLPVI------GAPFGRYLRSKAAHVHEKPSTP 88
Cdd:cd01672    1 MFIVFEGIDGAGKTTLIELLAERLEAR--------------------GYEVVltrepgGTPIGEAIRELLLDPEDEKMDP 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998995  89 PGNitalvIYLLSCWRAYKFRKMLCKS-QQGYLLITDRYPQVEVPGFRFDGPqlakttGGNGWIKMLRQRELKLYQwmas 167
Cdd:cd01672   61 RAE-----LLLFAADRAQHVEEVIKPAlARGKIVLSDRFVDSSLAYQGAGRG------LGEALIEALNDLATGGLK---- 125

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446998995 168 ylPVLLIRLGIDEQTAFSRKPDHQL--------AALQEKIAVTPQLTFN--GAKILELDGRQPADEIMQASLRAIHA 234
Cdd:cd01672  126 --PDLTILLDIDPEVGLARIEARGRddrdeqegLEFHERVREGYLELAAqePERIIVIDASQPLEEVLAEILKAILE 200
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 11-44 3.13e-05

Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 440337 [Multi-domain]  Cd Length: 206  Bit Score: 43.29  E-value: 3.13e-05
                         10        20        30
                 ....*....|....*....|....*....|....
gi 446998995  11 STPVRVIAIVGCDGSGKSTLTASLVNELAARMPT 44
Cdd:COG0572    4 SGKPRIIGIAGPSGSGKTTFARRLAEQLGADKVV 37
PRK07933 PRK07933
dTMP kinase;
15-80 8.13e-04

dTMP kinase;


Pssm-ID: 236133  Cd Length: 213  Bit Score: 39.19  E-value: 8.13e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446998995  15 RVIAIVGCDGSGKSTLTASLVNELAARmptehiylGQSSGRIGewisqlpvigapFGRYLRSKAAH 80
Cdd:PRK07933   1 MLIAIEGVDGAGKRTLTEALRAALEAR--------GRSVATLA------------FPRYGRSVHAD 46
Tmk COG0125
Thymidylate kinase [Nucleotide transport and metabolism]; Thymidylate kinase is part of the ...
 17-126 3.22e-03

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: 37.44  E-value: 3.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998995  17 IAIVGCDGSGKSTLTASLVNELAARmptehiylgqssGRigewisqlPVI------GAPFGRYLRSKAAHVHEKPStppg 90
Cdd:COG0125    6 IVFEGIDGSGKSTQIKLLAEYLEAR------------GY--------DVVltrepgGTPLGEAIRELLLGDNEDMS---- 61

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 446998995  91 NITALVIYLLScwRAYKFRKMLCKS-QQGYLLITDRY 126
Cdd:COG0125   62 PRTELLLFAAD--RAQHVEEVIRPAlAAGKIVICDRY 96
MobB pfam03205
Molybdopterin guanine dinucleotide synthesis protein B; This protein contains a P-loop.
 16-41 3.43e-03

Molybdopterin guanine dinucleotide synthesis protein B; This protein contains a P-loop.


Pssm-ID: 427196 [Multi-domain]  Cd Length: 133  Bit Score: 36.76  E-value: 3.43e-03
                          10        20
                  ....*....|....*....|....*.
gi 446998995   16 VIAIVGCDGSGKSTLTASLVNELAAR 41
Cdd:pfam03205   1 ILGIVGWSGSGKTTLLEKLIPELKAR 26
DTMP_kinase TIGR00041
dTMP kinase; Function: phosphorylation of DTMP to form DTDP in both de novo and salvage ...
 17-126 3.73e-03

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: 37.34  E-value: 3.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998995   17 IAIVGCDGSGKSTLTASLVNELAARMPTEHIYLGQSSGRIGEWIsqlpvigapfgrylRSKAAHVHEKPSTPpgnitALV 96
Cdd:TIGR00041   6 IVIEGIDGAGKTTQANLLKKLLQENGYDVLFTREPGGTPIGEKI--------------RELLLNENDEPLTD-----KAE 66

                          90       100       110
                  ....*....|....*....|....*....|.
gi 446998995   97 IYLLSCWRAYKFR-KMLCKSQQGYLLITDRY 126
Cdd:TIGR00041  67 ALLFAADRHEHLEdKIKPALAEGKLVISDRY 97
PRK13894 PRK13894
conjugal transfer ATPase TrbB; Provisional
 15-56 3.90e-03

conjugal transfer ATPase TrbB; Provisional


Pssm-ID: 184377  Cd Length: 319  Bit Score: 37.80  E-value: 3.90e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 446998995  15 RVIAIVGCDGSGKSTLTASLVNELAARMPTEHIYLGQSSGRI 56
Cdd:PRK13894 149 RNILVIGGTGSGKTTLVNAIINEMVIQDPTERVFIIEDTGEI 190
mobB TIGR00176
molybdopterin-guanine dinucleotide biosynthesis protein MobB; This molybdenum cofactor ...
 16-41 4.31e-03

molybdopterin-guanine dinucleotide biosynthesis protein MobB; This molybdenum cofactor biosynthesis enzyme is similar to the urease accessory protein UreG and to the hydrogenase accessory protein HypB, both GTP hydrolases involved in loading nickel into the metallocenters of their respective target enzymes. [Biosynthesis of cofactors, prosthetic groups, and carriers, Molybdopterin]


Pssm-ID: 272943 [Multi-domain]  Cd Length: 155  Bit Score: 36.59  E-value: 4.31e-03
                          10        20
                  ....*....|....*....|....*.
gi 446998995   16 VIAIVGCDGSGKSTLTASLVNELAAR 41
Cdd:TIGR00176   1 VLQIVGPKNSGKTTLIERLVKALKAR 26
MobB COG1763
Molybdopterin-guanine dinucleotide biosynthesis protein [Coenzyme transport and metabolism]; ...
 14-41 4.46e-03

Molybdopterin-guanine dinucleotide biosynthesis protein [Coenzyme transport and metabolism]; Molybdopterin-guanine dinucleotide biosynthesis protein is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 441369 [Multi-domain]  Cd Length: 162  Bit Score: 36.70  E-value: 4.46e-03
                         10        20
                 ....*....|....*....|....*...
gi 446998995  14 VRVIAIVGCDGSGKSTLTASLVNELAAR 41
Cdd:COG1763    1 MPVLGIVGYSGSGKTTLLEKLIPELKAR 28
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 17-41 6.88e-03

CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 36.68  E-value: 6.88e-03
                         10        20
                 ....*....|....*....|....*
gi 446998995  17 IAIVGCDGSGKSTLTASLVNELAAR 41
Cdd:COG3640    3 IAVAGKGGVGKTTLSALLARYLAEK 27
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 15-41 8.85e-03

SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal recognition particle, MinD, and BioD), consists of signal recognition particle (SRP) GTPases, the assemblage of MinD-like ATPases, which are involved in protein localization, chromosome partitioning, and membrane transport, and a group of metabolic enzymes with kinase or related phosphate transferase activity. Functionally, proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion.


Pssm-ID: 349751 [Multi-domain]  Cd Length: 107  Bit Score: 35.10  E-value: 8.85e-03
                         10        20
                 ....*....|....*....|....*...
gi 446998995  15 RVIAIVGCD-GSGKSTLTASLVNELAAR 41
Cdd:cd01983    1 RVIAVTGGKgGVGKTTLAAALAVALAAK 28
Grc3 COG1341
Polynucleotide 5'-kinase, involved in rRNA processing [Translation, ribosomal structure and ...
 9-83 9.10e-03

Polynucleotide 5'-kinase, involved in rRNA processing [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440952  Cd Length: 353  Bit Score: 36.54  E-value: 9.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998995   9 INSTPVRVIAIVGCDGSGKSTLTASLVNELAARmpteHIYL-------GQSS---------GRIGEWISQLPVIGAPFGR 72
Cdd:COG1341   30 ILSSGPGRIMVLGPVDSGKSTLTTLLANKLLAE----GLKVaiidadvGQSDlgppttvslGLVREPVLSLSELKAEKLR 105

                         90
                 ....*....|.
gi 446998995  73 YLRSKAAHVHE 83
Cdd:COG1341  106 FVGSISPSGHL 116
 
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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