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Conserved domains on  [gi|1057506576|ref|WP_068805188|]
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MULTISPECIES: deoxynucleoside kinase [Pediococcus]

Protein Classification

deoxynucleoside kinase( domain architecture ID 10787652)

deoxynucleoside kinase catalyzes the phosphorylation of deoxyribonucleosides to yield the corresponding monophosphates

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Dck COG1428
Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];
1-209 9.47e-85

Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];


:

Pssm-ID: 441037 [Multi-domain]  Cd Length: 205  Bit Score: 249.70  E-value: 9.47e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057506576   1 MVIITAGMIGVGKTTLTGKIAKHYGSKAFYEPVGDNPVLPLYYSDQKSYGFLLQIYFLNKRFAMIKKAL-SDDNNVLDRS 79
Cdd:COG1428     4 RYIAVEGNIGAGKTTLARLLAEHLGAELLLEPVEDNPFLEDFYEDPKRWAFPLQLFFLLSRFKQLKDLRqFGGNVVSDRS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057506576  80 IYEDALFTRENNKEGNITDTEFGVYLNLLDNMMNELndlpkKAPDLMVYAETDFDTILYRIKKRGRDYEQFDNnpelEDY 159
Cdd:COG1428    84 IYKDAIFAKLLHEMGTLSDREFDLYRQLFDNLTEDL-----PKPDLVIYLQASVDTLLERIKKRGRDYEQNID----LDY 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1057506576 160 YLKMWAAYKEWYRDYDASPKLKIDLQKYDL-ENPKNVETVLGQIDTALAKI 209
Cdd:COG1428   155 LERLNEAYEEWFEHYDASPVLIIDTDELDFvNNPEDLELLLEQIEEKLKGR 205
 
Name Accession Description Interval E-value
Dck COG1428
Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];
1-209 9.47e-85

Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];


Pssm-ID: 441037 [Multi-domain]  Cd Length: 205  Bit Score: 249.70  E-value: 9.47e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057506576   1 MVIITAGMIGVGKTTLTGKIAKHYGSKAFYEPVGDNPVLPLYYSDQKSYGFLLQIYFLNKRFAMIKKAL-SDDNNVLDRS 79
Cdd:COG1428     4 RYIAVEGNIGAGKTTLARLLAEHLGAELLLEPVEDNPFLEDFYEDPKRWAFPLQLFFLLSRFKQLKDLRqFGGNVVSDRS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057506576  80 IYEDALFTRENNKEGNITDTEFGVYLNLLDNMMNELndlpkKAPDLMVYAETDFDTILYRIKKRGRDYEQFDNnpelEDY 159
Cdd:COG1428    84 IYKDAIFAKLLHEMGTLSDREFDLYRQLFDNLTEDL-----PKPDLVIYLQASVDTLLERIKKRGRDYEQNID----LDY 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1057506576 160 YLKMWAAYKEWYRDYDASPKLKIDLQKYDL-ENPKNVETVLGQIDTALAKI 209
Cdd:COG1428   155 LERLNEAYEEWFEHYDASPVLIIDTDELDFvNNPEDLELLLEQIEEKLKGR 205
dNK cd01673
Deoxyribonucleoside kinase (dNK) catalyzes the phosphorylation of deoxyribonucleosides to ...
2-193 2.01e-57

Deoxyribonucleoside kinase (dNK) catalyzes the phosphorylation of deoxyribonucleosides to yield corresponding monophosphates (dNMPs). This family consists of various deoxynucleoside kinases including deoxyribo- cytidine (EC 2.7.1.74), guanosine (EC 2.7.1.113), adenosine (EC 2.7.1.76), and thymidine (EC 2.7.1.21) kinases. They are key enzymes in the salvage of deoxyribonucleosides originating from extra- or intracellular breakdown of DNA.


Pssm-ID: 238836  Cd Length: 193  Bit Score: 180.12  E-value: 2.01e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057506576   2 VIITAGMIGVGKTTLTGKIAKHYGSKAFYEP----VGDNPVLPLYYSDQKSYGFLLQIYFLNKRFAMIKKALSDDNN--- 74
Cdd:cd01673     1 VIVVEGNIGAGKSTLAKELAEHLGYEVVPEPvepdVEGNPFLEKFYEDPKRWAFPFQLYFLLSRLKQYKDALEHLSTgqg 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057506576  75 -VLDRSIYEDALFTRENNKEGNITDTEFGVYLNLLDNMMNELndlpkKAPDLMVYAETDFDTILYRIKKRGRDYEQfdnn 153
Cdd:cd01673    81 vILERSIFSDRVFAEANLKEGGIMKTEYDLYNELFDNLIPEL-----LPPDLVIYLDASPETCLKRIKKRGRPEEQ---- 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1057506576 154 PELEDYYLKMWAAYKEWYRD--YDASPKLKIDLQKYDLENPK 193
Cdd:cd01673   152 GIPLDYLEDLHEAYEKWFLPqmYEKAPVLIIDANEADIEYNK 193
dNK pfam01712
Deoxynucleoside kinase; This family consists of various deoxynucleoside kinases cytidine EC:2. ...
3-204 3.07e-54

Deoxynucleoside kinase; This family consists of various deoxynucleoside kinases cytidine EC:2.7.1.74, guanosine EC:2.7.1.113, adenosine EC:2.7.1.76 and thymidine kinase EC:2.7.1.21 (which also phosphorylates deoxyuridine and deoxycytosine.) These enzymes catalyze the production of deoxynucleotide 5'-monophosphate from a deoxynucleoside. Using ATP and yielding ADP in the process.


Pssm-ID: 396326  Cd Length: 201  Bit Score: 172.12  E-value: 3.07e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057506576   3 IITAGMIGVGKTTLTGKIAKHYGSKAFYEPVGD--NPVLPLYYSDQKSYGFLLQIYFLNKRFAMIKKAL-SDDNNVLDRS 79
Cdd:pfam01712   1 ISIEGNIGAGKSTLTKILSKRLGFKVFEEPVDRwtNPYLDKFYKDPSRWSFALQTYFLNSRFKQQLEAFfTGQVVILERS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057506576  80 IYEDA-LFTRENNKEGNITDTEFGVYLNLLDNMMNELndlpkKAPDLMVYAETDFDTILYRIKKRGRDYEQfdnnPELED 158
Cdd:pfam01712  81 IYSDRyIFAKMLYDKGTMSDEEYKTYKDLYDNMLLEF-----PKPDLIIYLKTSPETCLERIKKRGRTEEQ----NISLD 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1057506576 159 YYLKMWAAYKEWYRDYDASPKLKIDLQKYDLENPKNV-ETVLGQIDT 204
Cdd:pfam01712 152 YLERLHEKYEAWLKKLNLSPVLVIDGDELDFVFFEEDrEDVMNEVNE 198
DTMP_kinase TIGR00041
dTMP kinase; Function: phosphorylation of DTMP to form DTDP in both de novo and salvage ...
1-181 3.20e-04

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: 40.04  E-value: 3.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057506576   1 MVIITAGMIGVGKTTLTGKIAKHY---GSKAFY--EPvGDNPV------LPLYYSD----QKSYGFLlqiyFLNKRF--- 62
Cdd:TIGR00041   4 MFIVIEGIDGAGKTTQANLLKKLLqenGYDVLFtrEP-GGTPIgekireLLLNENDepltDKAEALL----FAADRHehl 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057506576  63 -AMIKKALSDDNNVL-DRSIYEDALFtrenNKEGNITDTEFGVYLNLldnmmnelnDLPKKAPDLMVYAETDFDTILYRI 140
Cdd:TIGR00041  79 eDKIKPALAEGKLVIsDRYVFSSIAY----QGGARGIDEDLVLELNE---------DALGDMPDLTIYLDIDPEVALERL 145
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1057506576 141 KKRGR----DYEQFDNNPELEDYYLKMWAAYKEWYRdYDASPKLK 181
Cdd:TIGR00041 146 RKRGEldreEFEKLDFFEKVRQRYLELADKEKSIHV-IDATNSVE 189
 
Name Accession Description Interval E-value
Dck COG1428
Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];
1-209 9.47e-85

Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];


Pssm-ID: 441037 [Multi-domain]  Cd Length: 205  Bit Score: 249.70  E-value: 9.47e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057506576   1 MVIITAGMIGVGKTTLTGKIAKHYGSKAFYEPVGDNPVLPLYYSDQKSYGFLLQIYFLNKRFAMIKKAL-SDDNNVLDRS 79
Cdd:COG1428     4 RYIAVEGNIGAGKTTLARLLAEHLGAELLLEPVEDNPFLEDFYEDPKRWAFPLQLFFLLSRFKQLKDLRqFGGNVVSDRS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057506576  80 IYEDALFTRENNKEGNITDTEFGVYLNLLDNMMNELndlpkKAPDLMVYAETDFDTILYRIKKRGRDYEQFDNnpelEDY 159
Cdd:COG1428    84 IYKDAIFAKLLHEMGTLSDREFDLYRQLFDNLTEDL-----PKPDLVIYLQASVDTLLERIKKRGRDYEQNID----LDY 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1057506576 160 YLKMWAAYKEWYRDYDASPKLKIDLQKYDL-ENPKNVETVLGQIDTALAKI 209
Cdd:COG1428   155 LERLNEAYEEWFEHYDASPVLIIDTDELDFvNNPEDLELLLEQIEEKLKGR 205
dNK cd01673
Deoxyribonucleoside kinase (dNK) catalyzes the phosphorylation of deoxyribonucleosides to ...
2-193 2.01e-57

Deoxyribonucleoside kinase (dNK) catalyzes the phosphorylation of deoxyribonucleosides to yield corresponding monophosphates (dNMPs). This family consists of various deoxynucleoside kinases including deoxyribo- cytidine (EC 2.7.1.74), guanosine (EC 2.7.1.113), adenosine (EC 2.7.1.76), and thymidine (EC 2.7.1.21) kinases. They are key enzymes in the salvage of deoxyribonucleosides originating from extra- or intracellular breakdown of DNA.


Pssm-ID: 238836  Cd Length: 193  Bit Score: 180.12  E-value: 2.01e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057506576   2 VIITAGMIGVGKTTLTGKIAKHYGSKAFYEP----VGDNPVLPLYYSDQKSYGFLLQIYFLNKRFAMIKKALSDDNN--- 74
Cdd:cd01673     1 VIVVEGNIGAGKSTLAKELAEHLGYEVVPEPvepdVEGNPFLEKFYEDPKRWAFPFQLYFLLSRLKQYKDALEHLSTgqg 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057506576  75 -VLDRSIYEDALFTRENNKEGNITDTEFGVYLNLLDNMMNELndlpkKAPDLMVYAETDFDTILYRIKKRGRDYEQfdnn 153
Cdd:cd01673    81 vILERSIFSDRVFAEANLKEGGIMKTEYDLYNELFDNLIPEL-----LPPDLVIYLDASPETCLKRIKKRGRPEEQ---- 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1057506576 154 PELEDYYLKMWAAYKEWYRD--YDASPKLKIDLQKYDLENPK 193
Cdd:cd01673   152 GIPLDYLEDLHEAYEKWFLPqmYEKAPVLIIDANEADIEYNK 193
dNK pfam01712
Deoxynucleoside kinase; This family consists of various deoxynucleoside kinases cytidine EC:2. ...
3-204 3.07e-54

Deoxynucleoside kinase; This family consists of various deoxynucleoside kinases cytidine EC:2.7.1.74, guanosine EC:2.7.1.113, adenosine EC:2.7.1.76 and thymidine kinase EC:2.7.1.21 (which also phosphorylates deoxyuridine and deoxycytosine.) These enzymes catalyze the production of deoxynucleotide 5'-monophosphate from a deoxynucleoside. Using ATP and yielding ADP in the process.


Pssm-ID: 396326  Cd Length: 201  Bit Score: 172.12  E-value: 3.07e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057506576   3 IITAGMIGVGKTTLTGKIAKHYGSKAFYEPVGD--NPVLPLYYSDQKSYGFLLQIYFLNKRFAMIKKAL-SDDNNVLDRS 79
Cdd:pfam01712   1 ISIEGNIGAGKSTLTKILSKRLGFKVFEEPVDRwtNPYLDKFYKDPSRWSFALQTYFLNSRFKQQLEAFfTGQVVILERS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057506576  80 IYEDA-LFTRENNKEGNITDTEFGVYLNLLDNMMNELndlpkKAPDLMVYAETDFDTILYRIKKRGRDYEQfdnnPELED 158
Cdd:pfam01712  81 IYSDRyIFAKMLYDKGTMSDEEYKTYKDLYDNMLLEF-----PKPDLIIYLKTSPETCLERIKKRGRTEEQ----NISLD 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1057506576 159 YYLKMWAAYKEWYRDYDASPKLKIDLQKYDLENPKNV-ETVLGQIDT 204
Cdd:pfam01712 152 YLERLHEKYEAWLKKLNLSPVLVIDGDELDFVFFEEDrEDVMNEVNE 198
NDUO42 cd02030
NADH:Ubiquinone oxioreductase, 42 kDa (NDUO42) is a family of proteins that are highly similar ...
2-203 7.42e-10

NADH:Ubiquinone oxioreductase, 42 kDa (NDUO42) is a family of proteins that are highly similar to deoxyribonucleoside kinases (dNK). Members of this family have been identified as one of the subunits of NADH:Ubiquinone oxioreductase (complex I), a multi-protein complex located in the inner mitochondrial membrane. The main function of the complex is to transport electrons from NADH to ubiquinone, which is accompanied by the translocation of protons from the mitochondrial matrix to the inter membrane space.


Pssm-ID: 238988  Cd Length: 219  Bit Score: 56.60  E-value: 7.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057506576   2 VIITAGMIGVGKTTLTGKIAKHYGSKAFYEPV--------GD----------NPVLPLYYSDQKSYGFL---LQIYFLNK 60
Cdd:cd02030     1 VITVDGNIASGKGKLAKELAEKLGMKYFPEAGihyldsttGDgkpldpafngNCSLEKFYDDPKSNDGNsyrLQSWMYSS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057506576  61 RFAMIKKAL-----SDDNNVLDRSIYEDALFTRENNKEGNITDTEFGVYLNLLDNMMNELndLPkkaPDLMVYAETDFDT 135
Cdd:cd02030    81 RLLQYSDALehllsTGQGVVLERSPFSDFVFLEAMYKQGYIRKQCVDHYNEVKGNTIPEL--LP---PHLVIYLDVPVPE 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1057506576 136 ILYRIKKRGRDYEQfdnnpELEDYYLK-MWAAYKEWYRdydasPKL--KIDLQKYDLENPKNVETVLGQID 203
Cdd:cd02030   156 VQKRIKKRGDPHEM-----KVTSAYLQdIENAYKKTFL-----PEIseHSEVLQYDWTEAGDTEKVVEDIE 216
AAA_17 pfam13207
AAA domain;
7-148 1.84e-04

AAA domain;


Pssm-ID: 463810 [Multi-domain]  Cd Length: 136  Bit Score: 40.30  E-value: 1.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057506576   7 GMIGVGKTTLTGKIAKHYGSKAFYEpvGDnpvlpLYYSDQKSYGfllqiyfLNKRFAMIKKALSDDNNVLDRSIYEDAlf 86
Cdd:pfam13207   2 GVPGSGKTTQLKKLAEKLGFPHISA--GD-----LLREEAKERG-------LVEDRDEMRKLPLEPQKELQKLAAERI-- 65
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1057506576  87 tRENNKEGNI-------TDTEFGVYLNLLDNMMNELNdlpkkaPDLMVYAETDFDTILYRIKK---RGRDYE 148
Cdd:pfam13207  66 -AEEAGEGGVivdghprIKTPAGYLPGLPVEVLRELK------PDAIILLEADPEEILERRLKdrtRGRDDD 130
DTMP_kinase TIGR00041
dTMP kinase; Function: phosphorylation of DTMP to form DTDP in both de novo and salvage ...
1-181 3.20e-04

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: 40.04  E-value: 3.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057506576   1 MVIITAGMIGVGKTTLTGKIAKHY---GSKAFY--EPvGDNPV------LPLYYSD----QKSYGFLlqiyFLNKRF--- 62
Cdd:TIGR00041   4 MFIVIEGIDGAGKTTQANLLKKLLqenGYDVLFtrEP-GGTPIgekireLLLNENDepltDKAEALL----FAADRHehl 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057506576  63 -AMIKKALSDDNNVL-DRSIYEDALFtrenNKEGNITDTEFGVYLNLldnmmnelnDLPKKAPDLMVYAETDFDTILYRI 140
Cdd:TIGR00041  79 eDKIKPALAEGKLVIsDRYVFSSIAY----QGGARGIDEDLVLELNE---------DALGDMPDLTIYLDIDPEVALERL 145
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1057506576 141 KKRGR----DYEQFDNNPELEDYYLKMWAAYKEWYRdYDASPKLK 181
Cdd:TIGR00041 146 RKRGEldreEFEKLDFFEKVRQRYLELADKEKSIHV-IDATNSVE 189
 
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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