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Conserved domains on  [gi|17535647|ref|NP_496151|]
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Thymidylate kinase [Caenorhabditis elegans]

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 ...
6-202 4.76e-75

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: 225.76  E-value: 4.76e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535647    6 KRGLLIVFEGLDRSGKSTQAKRLVESINKKSTEsgdassspsAVLQAFPDRSSSIGKLIDQYLRKEIDMDEHALHLLFSA 85
Cdd:PLN02924  14 SRGALIVLEGLDRSGKSTQCAKLVSFLKGLGVA---------AELWRFPDRTTSVGQMISAYLSNKSQLDDRAIHLLFSA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535647   86 DRFSKNQMIRDNIAKGIDVICDRYCYSGVAYSLAKGLPEQWVRSSDVGLPKPDAVLFFDVSPEVAAQRGGFGEERLETAT 165
Cdd:PLN02924  85 NRWEKRSLMERKLKSGTTLVVDRYSYSGVAFSAAKGLDLEWCKAPEVGLPAPDLVLYLDISPEEAAERGGYGGERYEKLE 164
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 17535647  166 IQQKVAAVMPTLRDDAyWKTVNADGDLDSVEKNVFRI 202
Cdd:PLN02924 165 FQKKVAKRFQTLRDSS-WKIIDASQSIEEVEKKIREV 200
 
Name Accession Description Interval E-value
PLN02924 PLN02924
thymidylate kinase
6-202 4.76e-75

thymidylate kinase


Pssm-ID: 178512  Cd Length: 220  Bit Score: 225.76  E-value: 4.76e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535647    6 KRGLLIVFEGLDRSGKSTQAKRLVESINKKSTEsgdassspsAVLQAFPDRSSSIGKLIDQYLRKEIDMDEHALHLLFSA 85
Cdd:PLN02924  14 SRGALIVLEGLDRSGKSTQCAKLVSFLKGLGVA---------AELWRFPDRTTSVGQMISAYLSNKSQLDDRAIHLLFSA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535647   86 DRFSKNQMIRDNIAKGIDVICDRYCYSGVAYSLAKGLPEQWVRSSDVGLPKPDAVLFFDVSPEVAAQRGGFGEERLETAT 165
Cdd:PLN02924  85 NRWEKRSLMERKLKSGTTLVVDRYSYSGVAFSAAKGLDLEWCKAPEVGLPAPDLVLYLDISPEEAAERGGYGGERYEKLE 164
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 17535647  166 IQQKVAAVMPTLRDDAyWKTVNADGDLDSVEKNVFRI 202
Cdd:PLN02924 165 FQKKVAKRFQTLRDSS-WKIIDASQSIEEVEKKIREV 200
Tmk COG0125
Thymidylate kinase [Nucleotide transport and metabolism]; Thymidylate kinase is part of the ...
7-206 2.07e-43

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: 144.53  E-value: 2.07e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535647   7 RGLLIVFEGLDRSGKSTQAKRLVESINKKstesgdassSPSAVLQAFPdRSSSIGKLI-DQYLRKEIDMDEHALHLLFSA 85
Cdd:COG0125   2 KGKFIVFEGIDGSGKSTQIKLLAEYLEAR---------GYDVVLTREP-GGTPLGEAIrELLLGDNEDMSPRTELLLFAA 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535647  86 DRF-SKNQMIRDNIAKGIDVICDRYCYSGVAY-SLAKGLPEQWVR---SSDVGLPKPDAVLFFDVSPEVAAQR---GGFG 157
Cdd:COG0125  72 DRAqHVEEVIRPALAAGKIVICDRYVDSSLAYqGGGRGLDLEWIRqlnRFATGGLKPDLTILLDVPPEVALARaraRGGE 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 17535647 158 EERLETATI--QQKVAAVMPTL--RDDAYWKTVNADGDLDSVEKNVFRIYENL 206
Cdd:COG0125 152 LDRFESEDLefHERVREGYLELaaKEPERIVVIDASQSIEEVHAEIREALAEL 204
Thymidylate_kin pfam02223
Thymidylate kinase;
13-197 3.10e-37

Thymidylate kinase;


Pssm-ID: 396690  Cd Length: 184  Bit Score: 128.19  E-value: 3.10e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535647    13 FEGLDRSGKSTQAKRLVESINKKStesgdassspSAVLQAFPDRSSSIGKLIDQYLRKEIDMDEHALHLLFSADRFsknQ 92
Cdd:pfam02223   1 IEGLDGAGKTTQAELLKERLKEQG----------IKVVFTREPGGTPIGEKIRELLLRNEELSPLTEALLFAADRI---Q 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535647    93 MIRDNI----AKGIDVICDRYCYSGVAYSLAKGLPEQWVRS-SDVGLPKPDAVLFFDVSPEVAAQRGGFGEER----LET 163
Cdd:pfam02223  68 HLEQKIkpalKQGKTVIVDRYLFSGIAYQGAKGGDLDLVLSlNPDVPGKPDLTFLLDVDPEVALKRLRRRGELekteFEQ 147
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 17535647   164 ATIQQKVAAVMPTL-RDDAYWKTVNADGDLDSVEK 197
Cdd:pfam02223 148 LDFLRKVRERYLELaKFDERIKIIDASLSIEEVHE 182
DTMP_kinase TIGR00041
dTMP kinase; Function: phosphorylation of DTMP to form DTDP in both de novo and salvage ...
7-172 9.18e-32

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: 114.38  E-value: 9.18e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535647     7 RGLLIVFEGLDRSGKSTQAKRLVESINKKSTesgdassspsAVLQAFPDRSSSIGKLIDQYLRKEID--MDEHALHLLFS 84
Cdd:TIGR00041   2 RGMFIVIEGIDGAGKTTQANLLKKLLQENGY----------DVLFTREPGGTPIGEKIRELLLNENDepLTDKAEALLFA 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535647    85 ADRfskNQMIRDNI----AKGIDVICDRYCYSGVAYS-LAKGLPEQWVRS--SDVGLPKPDAVLFFDVSPEVAAQR-GGF 156
Cdd:TIGR00041  72 ADR---HEHLEDKIkpalAEGKLVISDRYVFSSIAYQgGARGIDEDLVLElnEDALGDMPDLTIYLDIDPEVALERlRKR 148
                         170
                  ....*....|....*....
gi 17535647   157 GE---ERLETATIQQKVAA 172
Cdd:TIGR00041 149 GEldrEEFEKLDFFEKVRQ 167
TMPK cd01672
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the ...
9-202 4.38e-27

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: 102.35  E-value: 4.38e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535647   9 LLIVFEGLDRSGKSTQAKRLVESINKKSTEsgdassspsAVLQAFPDrSSSIGKLIDQYL--RKEIDMDEHALHLLFSAD 86
Cdd:cd01672   1 MFIVFEGIDGAGKTTLIELLAERLEARGYE---------VVLTREPG-GTPIGEAIRELLldPEDEKMDPRAELLLFAAD 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535647  87 R---FSknQMIRDNIAKGIDVICDRYCYSGVAYSLA-KGLPE---QWVRSSDVGLPKPDAVLFFDVSPEVAAQR----GG 155
Cdd:cd01672  71 RaqhVE--EVIKPALARGKIVLSDRFVDSSLAYQGAgRGLGEaliEALNDLATGGLKPDLTILLDIDPEVGLARiearGR 148
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 17535647 156 FGEERLETATIQQKVAAVMPTL--RDDAYWKTVNADGDLDSVEKNVFRI 202
Cdd:cd01672 149 DDRDEQEGLEFHERVREGYLELaaQEPERIIVIDASQPLEEVLAEILKA 197
 
Name Accession Description Interval E-value
PLN02924 PLN02924
thymidylate kinase
6-202 4.76e-75

thymidylate kinase


Pssm-ID: 178512  Cd Length: 220  Bit Score: 225.76  E-value: 4.76e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535647    6 KRGLLIVFEGLDRSGKSTQAKRLVESINKKSTEsgdassspsAVLQAFPDRSSSIGKLIDQYLRKEIDMDEHALHLLFSA 85
Cdd:PLN02924  14 SRGALIVLEGLDRSGKSTQCAKLVSFLKGLGVA---------AELWRFPDRTTSVGQMISAYLSNKSQLDDRAIHLLFSA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535647   86 DRFSKNQMIRDNIAKGIDVICDRYCYSGVAYSLAKGLPEQWVRSSDVGLPKPDAVLFFDVSPEVAAQRGGFGEERLETAT 165
Cdd:PLN02924  85 NRWEKRSLMERKLKSGTTLVVDRYSYSGVAFSAAKGLDLEWCKAPEVGLPAPDLVLYLDISPEEAAERGGYGGERYEKLE 164
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 17535647  166 IQQKVAAVMPTLRDDAyWKTVNADGDLDSVEKNVFRI 202
Cdd:PLN02924 165 FQKKVAKRFQTLRDSS-WKIIDASQSIEEVEKKIREV 200
Tmk COG0125
Thymidylate kinase [Nucleotide transport and metabolism]; Thymidylate kinase is part of the ...
7-206 2.07e-43

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: 144.53  E-value: 2.07e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535647   7 RGLLIVFEGLDRSGKSTQAKRLVESINKKstesgdassSPSAVLQAFPdRSSSIGKLI-DQYLRKEIDMDEHALHLLFSA 85
Cdd:COG0125   2 KGKFIVFEGIDGSGKSTQIKLLAEYLEAR---------GYDVVLTREP-GGTPLGEAIrELLLGDNEDMSPRTELLLFAA 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535647  86 DRF-SKNQMIRDNIAKGIDVICDRYCYSGVAY-SLAKGLPEQWVR---SSDVGLPKPDAVLFFDVSPEVAAQR---GGFG 157
Cdd:COG0125  72 DRAqHVEEVIRPALAAGKIVICDRYVDSSLAYqGGGRGLDLEWIRqlnRFATGGLKPDLTILLDVPPEVALARaraRGGE 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 17535647 158 EERLETATI--QQKVAAVMPTL--RDDAYWKTVNADGDLDSVEKNVFRIYENL 206
Cdd:COG0125 152 LDRFESEDLefHERVREGYLELaaKEPERIVVIDASQSIEEVHAEIREALAEL 204
Thymidylate_kin pfam02223
Thymidylate kinase;
13-197 3.10e-37

Thymidylate kinase;


Pssm-ID: 396690  Cd Length: 184  Bit Score: 128.19  E-value: 3.10e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535647    13 FEGLDRSGKSTQAKRLVESINKKStesgdassspSAVLQAFPDRSSSIGKLIDQYLRKEIDMDEHALHLLFSADRFsknQ 92
Cdd:pfam02223   1 IEGLDGAGKTTQAELLKERLKEQG----------IKVVFTREPGGTPIGEKIRELLLRNEELSPLTEALLFAADRI---Q 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535647    93 MIRDNI----AKGIDVICDRYCYSGVAYSLAKGLPEQWVRS-SDVGLPKPDAVLFFDVSPEVAAQRGGFGEER----LET 163
Cdd:pfam02223  68 HLEQKIkpalKQGKTVIVDRYLFSGIAYQGAKGGDLDLVLSlNPDVPGKPDLTFLLDVDPEVALKRLRRRGELekteFEQ 147
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 17535647   164 ATIQQKVAAVMPTL-RDDAYWKTVNADGDLDSVEK 197
Cdd:pfam02223 148 LDFLRKVRERYLELaKFDERIKIIDASLSIEEVHE 182
DTMP_kinase TIGR00041
dTMP kinase; Function: phosphorylation of DTMP to form DTDP in both de novo and salvage ...
7-172 9.18e-32

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: 114.38  E-value: 9.18e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535647     7 RGLLIVFEGLDRSGKSTQAKRLVESINKKSTesgdassspsAVLQAFPDRSSSIGKLIDQYLRKEID--MDEHALHLLFS 84
Cdd:TIGR00041   2 RGMFIVIEGIDGAGKTTQANLLKKLLQENGY----------DVLFTREPGGTPIGEKIRELLLNENDepLTDKAEALLFA 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535647    85 ADRfskNQMIRDNI----AKGIDVICDRYCYSGVAYS-LAKGLPEQWVRS--SDVGLPKPDAVLFFDVSPEVAAQR-GGF 156
Cdd:TIGR00041  72 ADR---HEHLEDKIkpalAEGKLVISDRYVFSSIAYQgGARGIDEDLVLElnEDALGDMPDLTIYLDIDPEVALERlRKR 148
                         170
                  ....*....|....*....
gi 17535647   157 GE---ERLETATIQQKVAA 172
Cdd:TIGR00041 149 GEldrEEFEKLDFFEKVRQ 167
TMPK cd01672
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the ...
9-202 4.38e-27

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: 102.35  E-value: 4.38e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535647   9 LLIVFEGLDRSGKSTQAKRLVESINKKSTEsgdassspsAVLQAFPDrSSSIGKLIDQYL--RKEIDMDEHALHLLFSAD 86
Cdd:cd01672   1 MFIVFEGIDGAGKTTLIELLAERLEARGYE---------VVLTREPG-GTPIGEAIRELLldPEDEKMDPRAELLLFAAD 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535647  87 R---FSknQMIRDNIAKGIDVICDRYCYSGVAYSLA-KGLPE---QWVRSSDVGLPKPDAVLFFDVSPEVAAQR----GG 155
Cdd:cd01672  71 RaqhVE--EVIKPALARGKIVLSDRFVDSSLAYQGAgRGLGEaliEALNDLATGGLKPDLTILLDIDPEVGLARiearGR 148
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 17535647 156 FGEERLETATIQQKVAAVMPTL--RDDAYWKTVNADGDLDSVEKNVFRI 202
Cdd:cd01672 149 DDRDEQEGLEFHERVREGYLELaaQEPERIIVIDASQPLEEVLAEILKA 197
PRK07933 PRK07933
dTMP kinase;
9-200 4.36e-16

dTMP kinase;


Pssm-ID: 236133  Cd Length: 213  Bit Score: 73.47  E-value: 4.36e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535647    9 LLIVFEGLDRSGKSTQAKRLVESInkkstesgDASSSPSAVLqAFPDRSSSI-GKLIDQYLRKEI-DMDE--HALHLLFS 84
Cdd:PRK07933   1 MLIAIEGVDGAGKRTLTEALRAAL--------EARGRSVATL-AFPRYGRSVhADLAAEALHGRHgDLADsvYAMATLFA 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535647   85 ADRFSknqmIRDNIAKGID----VICDRYCYSGVAYSLAK------GLPEQWVRSSDV---GLPKPDAVLFFDVSPEVAA 151
Cdd:PRK07933  72 LDRAG----ARDELAGLLAahdvVILDRYVASNAAYSAARlhqdadGEAVAWVAELEFgrlGLPVPDLQVLLDVPVELAA 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17535647  152 QRGGFGEE--------RLET-ATIQQKVAAVMPTLRDDAY---WKTVNADGDLDSVEKNVF 200
Cdd:PRK07933 148 ERARRRAAqdadrardAYERdDGLQQRTGAVYAELAAQGWggpWLVVDPDVDPAALAARLA 208
 
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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