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Conserved domains on  [gi|47077006|dbj|BAD18437|]
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unnamed protein product [Homo sapiens]

Protein Classification

deoxynucleoside kinase( domain architecture ID 10109324)

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

CATH:  3.40.50.300
EC:  2.7.1.-
Gene Ontology:  GO:0019136|GO:0005524
SCOP:  4004030

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
dNK cd01673
Deoxyribonucleoside kinase (dNK) catalyzes the phosphorylation of deoxyribonucleosides to ...
199-390 4.05e-65

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: 209.39  E-value: 4.05e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47077006 199 FCVEGNISVGKTTFLQRIANetielRDLVEVVPEPISkwqdVGPDHFNILDAFYAEPQRYAYTFQNYVFVTRVMQERESS 278
Cdd:cd01673   2 IVVEGNIGAGKSTLAKELAE-----HLGYEVVPEPVE----PDVEGNPFLEKFYEDPKRWAFPFQLYFLLSRLKQYKDAL 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47077006 279 AGI--KPLRLMERSVFSDRMVFVRAVHEANWMNgMEISIYDSWFDPVVSSLPglIPDGFIYLRASPDTCHKRMMLRKRTE 356
Cdd:cd01673  73 EHLstGQGVILERSIFSDRVFAEANLKEGGIMK-TEYDLYNELFDNLIPELL--PPDLVIYLDASPETCLKRIKKRGRPE 149
                       170       180       190
                ....*....|....*....|....*....|....
gi 47077006 357 EGGVSLDYLCDLHEKHESWLFPSQSGNHGVLSVN 390
Cdd:cd01673 150 EQGIPLDYLEDLHEAYEKWFLPQMYEKAPVLIID 183
 
Name Accession Description Interval E-value
dNK cd01673
Deoxyribonucleoside kinase (dNK) catalyzes the phosphorylation of deoxyribonucleosides to ...
199-390 4.05e-65

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: 209.39  E-value: 4.05e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47077006 199 FCVEGNISVGKTTFLQRIANetielRDLVEVVPEPISkwqdVGPDHFNILDAFYAEPQRYAYTFQNYVFVTRVMQERESS 278
Cdd:cd01673   2 IVVEGNIGAGKSTLAKELAE-----HLGYEVVPEPVE----PDVEGNPFLEKFYEDPKRWAFPFQLYFLLSRLKQYKDAL 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47077006 279 AGI--KPLRLMERSVFSDRMVFVRAVHEANWMNgMEISIYDSWFDPVVSSLPglIPDGFIYLRASPDTCHKRMMLRKRTE 356
Cdd:cd01673  73 EHLstGQGVILERSIFSDRVFAEANLKEGGIMK-TEYDLYNELFDNLIPELL--PPDLVIYLDASPETCLKRIKKRGRPE 149
                       170       180       190
                ....*....|....*....|....*....|....
gi 47077006 357 EGGVSLDYLCDLHEKHESWLFPSQSGNHGVLSVN 390
Cdd:cd01673 150 EQGIPLDYLEDLHEAYEKWFLPQMYEKAPVLIID 183
dNK pfam01712
Deoxynucleoside kinase; This family consists of various deoxynucleoside kinases cytidine EC:2. ...
199-453 3.44e-51

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: 173.27  E-value: 3.44e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47077006   199 FCVEGNISVGKTTFLQRIANETielrdLVEVVPEPISKWQDvgpdhfNILDAFYAEPQRYAYTFQNYVFVTRVMQERESS 278
Cdd:pfam01712   1 ISIEGNIGAGKSTLTKILSKRL-----GFKVFEEPVDRWTN------PYLDKFYKDPSRWSFALQTYFLNSRFKQQLEAF 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47077006   279 AgIKPLRLMERSVFSDRMVFVRAVHEANWMNGMEISIYDSWFDPVVSSLPGliPDGFIYLRASPDTCHKRMMLRKRTEEG 358
Cdd:pfam01712  70 F-TGQVVILERSIYSDRYIFAKMLYDKGTMSDEEYKTYKDLYDNMLLEFPK--PDLIIYLKTSPETCLERIKKRGRTEEQ 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47077006   359 GVSLDYLCDLHEKHESWLfpsqsgnhgvlsvnqlphhidnslhpdirdrvfylegghmhSSIQKVPALVLDCEpNIDFSK 438
Cdd:pfam01712 147 NISLDYLERLHEKYEAWL-----------------------------------------KKLNLSPVLVIDGD-ELDFVF 184
                         250
                  ....*....|....*
gi 47077006   439 DIEAKRQYARQVAEF 453
Cdd:pfam01712 185 FEEDREDVMNEVNEF 199
Dck COG1428
Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];
201-453 2.42e-34

Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];


Pssm-ID: 441037 [Multi-domain]  Cd Length: 205  Bit Score: 128.37  E-value: 2.42e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47077006 201 VEGNISVGKTTFLQRIANetielrDL-VEVVPEPiskwqdvgPDHFNILDAFYAEPQRYAYTFQNYVFVTRVMQERESSA 279
Cdd:COG1428   8 VEGNIGAGKTTLARLLAE------HLgAELLLEP--------VEDNPFLEDFYEDPKRWAFPLQLFFLLSRFKQLKDLRQ 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47077006 280 GiKPLRLMERSVFSDRmVFVRAVHEANWMNGMEISIYDSWFDPVVSSLPGliPDGFIYLRASPDTCHKRMMLRKRTEEGG 359
Cdd:COG1428  74 F-GGNVVSDRSIYKDA-IFAKLLHEMGTLSDREFDLYRQLFDNLTEDLPK--PDLVIYLQASVDTLLERIKKRGRDYEQN 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47077006 360 VSLDYLCDLHEKHESWLfpsqsgnhgvlsvnqlpHHIDNSlhpdirdrvfylegghmhssiqkvPALVLDCEpNIDFSKD 439
Cdd:COG1428 150 IDLDYLERLNEAYEEWF-----------------EHYDAS------------------------PVLIIDTD-ELDFVNN 187
                       250
                ....*....|....
gi 47077006 440 IEAKRQYARQVAEF 453
Cdd:COG1428 188 PEDLELLLEQIEEK 201
 
Name Accession Description Interval E-value
dNK cd01673
Deoxyribonucleoside kinase (dNK) catalyzes the phosphorylation of deoxyribonucleosides to ...
199-390 4.05e-65

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: 209.39  E-value: 4.05e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47077006 199 FCVEGNISVGKTTFLQRIANetielRDLVEVVPEPISkwqdVGPDHFNILDAFYAEPQRYAYTFQNYVFVTRVMQERESS 278
Cdd:cd01673   2 IVVEGNIGAGKSTLAKELAE-----HLGYEVVPEPVE----PDVEGNPFLEKFYEDPKRWAFPFQLYFLLSRLKQYKDAL 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47077006 279 AGI--KPLRLMERSVFSDRMVFVRAVHEANWMNgMEISIYDSWFDPVVSSLPglIPDGFIYLRASPDTCHKRMMLRKRTE 356
Cdd:cd01673  73 EHLstGQGVILERSIFSDRVFAEANLKEGGIMK-TEYDLYNELFDNLIPELL--PPDLVIYLDASPETCLKRIKKRGRPE 149
                       170       180       190
                ....*....|....*....|....*....|....
gi 47077006 357 EGGVSLDYLCDLHEKHESWLFPSQSGNHGVLSVN 390
Cdd:cd01673 150 EQGIPLDYLEDLHEAYEKWFLPQMYEKAPVLIID 183
dNK pfam01712
Deoxynucleoside kinase; This family consists of various deoxynucleoside kinases cytidine EC:2. ...
199-453 3.44e-51

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: 173.27  E-value: 3.44e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47077006   199 FCVEGNISVGKTTFLQRIANETielrdLVEVVPEPISKWQDvgpdhfNILDAFYAEPQRYAYTFQNYVFVTRVMQERESS 278
Cdd:pfam01712   1 ISIEGNIGAGKSTLTKILSKRL-----GFKVFEEPVDRWTN------PYLDKFYKDPSRWSFALQTYFLNSRFKQQLEAF 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47077006   279 AgIKPLRLMERSVFSDRMVFVRAVHEANWMNGMEISIYDSWFDPVVSSLPGliPDGFIYLRASPDTCHKRMMLRKRTEEG 358
Cdd:pfam01712  70 F-TGQVVILERSIYSDRYIFAKMLYDKGTMSDEEYKTYKDLYDNMLLEFPK--PDLIIYLKTSPETCLERIKKRGRTEEQ 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47077006   359 GVSLDYLCDLHEKHESWLfpsqsgnhgvlsvnqlphhidnslhpdirdrvfylegghmhSSIQKVPALVLDCEpNIDFSK 438
Cdd:pfam01712 147 NISLDYLERLHEKYEAWL-----------------------------------------KKLNLSPVLVIDGD-ELDFVF 184
                         250
                  ....*....|....*
gi 47077006   439 DIEAKRQYARQVAEF 453
Cdd:pfam01712 185 FEEDREDVMNEVNEF 199
Dck COG1428
Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];
201-453 2.42e-34

Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];


Pssm-ID: 441037 [Multi-domain]  Cd Length: 205  Bit Score: 128.37  E-value: 2.42e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47077006 201 VEGNISVGKTTFLQRIANetielrDL-VEVVPEPiskwqdvgPDHFNILDAFYAEPQRYAYTFQNYVFVTRVMQERESSA 279
Cdd:COG1428   8 VEGNIGAGKTTLARLLAE------HLgAELLLEP--------VEDNPFLEDFYEDPKRWAFPLQLFFLLSRFKQLKDLRQ 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47077006 280 GiKPLRLMERSVFSDRmVFVRAVHEANWMNGMEISIYDSWFDPVVSSLPGliPDGFIYLRASPDTCHKRMMLRKRTEEGG 359
Cdd:COG1428  74 F-GGNVVSDRSIYKDA-IFAKLLHEMGTLSDREFDLYRQLFDNLTEDLPK--PDLVIYLQASVDTLLERIKKRGRDYEQN 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47077006 360 VSLDYLCDLHEKHESWLfpsqsgnhgvlsvnqlpHHIDNSlhpdirdrvfylegghmhssiqkvPALVLDCEpNIDFSKD 439
Cdd:COG1428 150 IDLDYLERLNEAYEEWF-----------------EHYDAS------------------------PVLIIDTD-ELDFVNN 187
                       250
                ....*....|....
gi 47077006 440 IEAKRQYARQVAEF 453
Cdd:COG1428 188 PEDLELLLEQIEEK 201
NDUO42 cd02030
NADH:Ubiquinone oxioreductase, 42 kDa (NDUO42) is a family of proteins that are highly similar ...
199-387 1.32e-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: 61.22  E-value: 1.32e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47077006 199 FCVEGNISVGKTTFLQRIANEtielrdL-VEVVPEPISKWQDVGPDHFNILDA----------FYAEPQRY---AYTFQN 264
Cdd:cd02030   2 ITVDGNIASGKGKLAKELAEK------LgMKYFPEAGIHYLDSTTGDGKPLDPafngncslekFYDDPKSNdgnSYRLQS 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47077006 265 YVFVTRVMQERESSA-------GIkplrLMERSVFSDrMVFVRAVHEANWMNGMEISIYDswfDPVVSSLPGLIPDGF-I 336
Cdd:cd02030  76 WMYSSRLLQYSDALEhllstgqGV----VLERSPFSD-FVFLEAMYKQGYIRKQCVDHYN---EVKGNTIPELLPPHLvI 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 47077006 337 YLRASPDTCHKRMMLRKRTEEGGVSLDYLCDLHEKHESWLFPSQSGNHGVL 387
Cdd:cd02030 148 YLDVPVPEVQKRIKKRGDPHEMKVTSAYLQDIENAYKKTFLPEISEHSEVL 198
 
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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