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Conserved domains on  [gi|1236892066|ref|WP_095042828|]
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deoxynucleoside kinase [Candidatus Promineifilum breve]

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];
1-199 6.33e-56

Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];


:

Pssm-ID: 441037 [Multi-domain]  Cd Length: 205  Bit Score: 176.52  E-value: 6.33e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236892066   1 MSNVIAIVGNSGVGKTTLVEALRRARPLAVGLEQHAARPFQALMAADPPRYALANQIDYLLLRAEQERALRAGPTTGLID 80
Cdd:COG1428     2 KPRYIAVEGNIGAGKTTLARLLAEHLGAELLLEPVEDNPFLEDFYEDPKRWAFPLQLFFLLSRFKQLKDLRQFGGNVVSD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236892066  81 GGLDLDFHgFTRLFHRRGYLTDAEFDLCARLYRQLRALLGPPDLILHLIAPLPVVEARYAQRGRALEIAQRAD-LALMEE 159
Cdd:COG1428    82 RSIYKDAI-FAKLLHEMGTLSDREFDLYRQLFDNLTEDLPKPDLVIYLQASVDTLLERIKKRGRDYEQNIDLDyLERLNE 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1236892066 160 FVADWIASVRDMPVITVDASADDF-CGPDSILHLLDEIDRA 199
Cdd:COG1428   161 AYEEWFEHYDASPVLIIDTDELDFvNNPEDLELLLEQIEEK 201
 
Name Accession Description Interval E-value
Dck COG1428
Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];
1-199 6.33e-56

Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];


Pssm-ID: 441037 [Multi-domain]  Cd Length: 205  Bit Score: 176.52  E-value: 6.33e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236892066   1 MSNVIAIVGNSGVGKTTLVEALRRARPLAVGLEQHAARPFQALMAADPPRYALANQIDYLLLRAEQERALRAGPTTGLID 80
Cdd:COG1428     2 KPRYIAVEGNIGAGKTTLARLLAEHLGAELLLEPVEDNPFLEDFYEDPKRWAFPLQLFFLLSRFKQLKDLRQFGGNVVSD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236892066  81 GGLDLDFHgFTRLFHRRGYLTDAEFDLCARLYRQLRALLGPPDLILHLIAPLPVVEARYAQRGRALEIAQRAD-LALMEE 159
Cdd:COG1428    82 RSIYKDAI-FAKLLHEMGTLSDREFDLYRQLFDNLTEDLPKPDLVIYLQASVDTLLERIKKRGRDYEQNIDLDyLERLNE 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1236892066 160 FVADWIASVRDMPVITVDASADDF-CGPDSILHLLDEIDRA 199
Cdd:COG1428   161 AYEEWFEHYDASPVLIIDTDELDFvNNPEDLELLLEQIEEK 201
dNK pfam01712
Deoxynucleoside kinase; This family consists of various deoxynucleoside kinases cytidine EC:2. ...
 5-183 2.55e-19

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: 81.98  E-value: 2.55e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236892066   5 IAIVGNSGVGKTTLVEALRRARPLAVGLE--QHAARPFQALMAADPPRYALANQIDYLLLR-AEQERALRAGPTtGLIDG 81
Cdd:pfam01712   1 ISIEGNIGAGKSTLTKILSKRLGFKVFEEpvDRWTNPYLDKFYKDPSRWSFALQTYFLNSRfKQQLEAFFTGQV-VILER 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236892066  82 GLDLDFHGFTRLFHRRGYLTDAEFDLCARLYRQLRALLGPPDLILHLIAPLPVVEARYAQRGRALEIAQRAD-LALMEEF 160
Cdd:pfam01712  80 SIYSDRYIFAKMLYDKGTMSDEEYKTYKDLYDNMLLEFPKPDLIIYLKTSPETCLERIKKRGRTEEQNISLDyLERLHEK 159

                         170       180
                  ....*....|....*....|...
gi 1236892066 161 VADWIASVRDMPVITVDASADDF 183
Cdd:pfam01712 160 YEAWLKKLNLSPVLVIDGDELDF 182
dNK cd01673
Deoxyribonucleoside kinase (dNK) catalyzes the phosphorylation of deoxyribonucleosides to ...
 4-183 2.83e-19

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: 81.51  E-value: 2.83e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236892066   4 VIAIVGNSGVGKTTLVEALRRARPLAVGLEQHAAR----PFQALMAADPPRYALANQIDYLLLRAEQERALRAGPTTGli 79
Cdd:cd01673     1 VIVVEGNIGAGKSTLAKELAEHLGYEVVPEPVEPDvegnPFLEKFYEDPKRWAFPFQLYFLLSRLKQYKDALEHLSTG-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236892066  80 DGGLdLDFH-----GFTRLFHRRGYLTDAEFDlcarLYRQLRALL----GPPDLILHLIAPLPVVEARYAQRGRALEIA- 149
Cdd:cd01673    79 QGVI-LERSifsdrVFAEANLKEGGIMKTEYD----LYNELFDNLipelLPPDLVIYLDASPETCLKRIKKRGRPEEQGi 153

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1236892066 150 QRADLALMEEFVADWIASVRDM--PVITVDASADDF 183
Cdd:cd01673   154 PLDYLEDLHEAYEKWFLPQMYEkaPVLIIDANEADI 189
mobB TIGR00176
molybdopterin-guanine dinucleotide biosynthesis protein MobB; This molybdenum cofactor ...
 4-41 7.70e-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: 35.82  E-value: 7.70e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1236892066   4 VIAIVGNSGVGKTTLVEAL---RRARPLAVGLEQHAARPFQ 41
Cdd:TIGR00176   1 VLQIVGPKNSGKTTLIERLvkaLKARGYRVATIKHDHHDFD 41
 
Name Accession Description Interval E-value
Dck COG1428
Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];
1-199 6.33e-56

Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];


Pssm-ID: 441037 [Multi-domain]  Cd Length: 205  Bit Score: 176.52  E-value: 6.33e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236892066   1 MSNVIAIVGNSGVGKTTLVEALRRARPLAVGLEQHAARPFQALMAADPPRYALANQIDYLLLRAEQERALRAGPTTGLID 80
Cdd:COG1428     2 KPRYIAVEGNIGAGKTTLARLLAEHLGAELLLEPVEDNPFLEDFYEDPKRWAFPLQLFFLLSRFKQLKDLRQFGGNVVSD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236892066  81 GGLDLDFHgFTRLFHRRGYLTDAEFDLCARLYRQLRALLGPPDLILHLIAPLPVVEARYAQRGRALEIAQRAD-LALMEE 159
Cdd:COG1428    82 RSIYKDAI-FAKLLHEMGTLSDREFDLYRQLFDNLTEDLPKPDLVIYLQASVDTLLERIKKRGRDYEQNIDLDyLERLNE 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1236892066 160 FVADWIASVRDMPVITVDASADDF-CGPDSILHLLDEIDRA 199
Cdd:COG1428   161 AYEEWFEHYDASPVLIIDTDELDFvNNPEDLELLLEQIEEK 201
dNK pfam01712
Deoxynucleoside kinase; This family consists of various deoxynucleoside kinases cytidine EC:2. ...
 5-183 2.55e-19

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: 81.98  E-value: 2.55e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236892066   5 IAIVGNSGVGKTTLVEALRRARPLAVGLE--QHAARPFQALMAADPPRYALANQIDYLLLR-AEQERALRAGPTtGLIDG 81
Cdd:pfam01712   1 ISIEGNIGAGKSTLTKILSKRLGFKVFEEpvDRWTNPYLDKFYKDPSRWSFALQTYFLNSRfKQQLEAFFTGQV-VILER 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236892066  82 GLDLDFHGFTRLFHRRGYLTDAEFDLCARLYRQLRALLGPPDLILHLIAPLPVVEARYAQRGRALEIAQRAD-LALMEEF 160
Cdd:pfam01712  80 SIYSDRYIFAKMLYDKGTMSDEEYKTYKDLYDNMLLEFPKPDLIIYLKTSPETCLERIKKRGRTEEQNISLDyLERLHEK 159

                         170       180
                  ....*....|....*....|...
gi 1236892066 161 VADWIASVRDMPVITVDASADDF 183
Cdd:pfam01712 160 YEAWLKKLNLSPVLVIDGDELDF 182
dNK cd01673
Deoxyribonucleoside kinase (dNK) catalyzes the phosphorylation of deoxyribonucleosides to ...
 4-183 2.83e-19

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: 81.51  E-value: 2.83e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236892066   4 VIAIVGNSGVGKTTLVEALRRARPLAVGLEQHAAR----PFQALMAADPPRYALANQIDYLLLRAEQERALRAGPTTGli 79
Cdd:cd01673     1 VIVVEGNIGAGKSTLAKELAEHLGYEVVPEPVEPDvegnPFLEKFYEDPKRWAFPFQLYFLLSRLKQYKDALEHLSTG-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236892066  80 DGGLdLDFH-----GFTRLFHRRGYLTDAEFDlcarLYRQLRALL----GPPDLILHLIAPLPVVEARYAQRGRALEIA- 149
Cdd:cd01673    79 QGVI-LERSifsdrVFAEANLKEGGIMKTEYD----LYNELFDNLipelLPPDLVIYLDASPETCLKRIKKRGRPEEQGi 153

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1236892066 150 QRADLALMEEFVADWIASVRDM--PVITVDASADDF 183
Cdd:cd01673   154 PLDYLEDLHEAYEKWFLPQMYEkaPVLIIDANEADI 189
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
 4-162 4.17e-06

AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the AAA superfamily. Many of the proteins in this family are just short fragments so there is no Walker B motif.


Pssm-ID: 463952 [Multi-domain]  Cd Length: 143  Bit Score: 44.99  E-value: 4.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236892066   4 VIAIVGNSGVGKTTLVEALRRARPlAVGLEQHAARpfQALMAADPPR---YALANQIDYLLLRAEQERALRAGpttglid 80
Cdd:pfam13671   1 LILLVGLPGSGKSTLARRLLEELG-AVRLSSDDER--KRLFGEGRPSisyYTDATDRTYERLHELARIALRAG------- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236892066  81 ggldldfhgftrlfhrRGYLTDAEF-DLCAR-LYRQLRALLGPPDLILHLIAPLPVVEARYAQRGRALEIAQRADLALME 158
Cdd:pfam13671  71 ----------------RPVILDATNlRRDERaRLLALAREYGVPVRIVVFEAPEEVLRERLAARARAGGDPSDVPEEVLD 134


                  ....
gi 1236892066 159 EFVA 162
Cdd:pfam13671 135 RQKA 138
MobB pfam03205
Molybdopterin guanine dinucleotide synthesis protein B; This protein contains a P-loop.
 4-41 4.41e-04

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


Pssm-ID: 427196 [Multi-domain]  Cd Length: 133  Bit Score: 39.07  E-value: 4.41e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1236892066   4 VIAIVGNSGVGKTTLVEAL---RRARPLAVGLEQHAARPFQ 41
Cdd:pfam03205   1 ILGIVGWSGSGKTTLLEKLipeLKARGLRVGTIKHAHHGFD 41
MobB COG1763
Molybdopterin-guanine dinucleotide biosynthesis protein [Coenzyme transport and metabolism]; ...
 4-22 1.93e-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: 37.47  E-value: 1.93e-03
                          10
                  ....*....|....*....
gi 1236892066   4 VIAIVGNSGVGKTTLVEAL 22
Cdd:COG1763     3 VLGIVGYSGSGKTTLLEKL 21
AAA_23 pfam13476
AAA domain;
2-25 2.89e-03

AAA domain;


Pssm-ID: 463890 [Multi-domain]  Cd Length: 190  Bit Score: 37.48  E-value: 2.89e-03
                          10        20
                  ....*....|....*....|....
gi 1236892066   2 SNVIAIVGNSGVGKTTLVEALRRA 25
Cdd:pfam13476  18 KGLTLITGPNGSGKTTILDAIKLA 41
EF-G_bact cd04170
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ...
 5-22 3.30e-03

Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.


Pssm-ID: 206733 [Multi-domain]  Cd Length: 268  Bit Score: 37.57  E-value: 3.30e-03
                          10
                  ....*....|....*...
gi 1236892066   5 IAIVGNSGVGKTTLVEAL 22
Cdd:cd04170     2 IALVGHSGSGKTTLAEAL 19
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
4-182 4.23e-03

Predicted kinase, contains AAA domain [General function prediction only];


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 36.43  E-value: 4.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236892066   4 VIAIVGNSGVGKTTLVEALRRARPlAVGLEQHAARpfQALMAADPP---RYALANQIDYLLLRAEQERALRAGPTTgLID 80
Cdd:COG0645     1 LILVCGLPGSGKSTLARALAERLG-AVRLRSDVVR--KRLFGAGLApleRSPEATARTYARLLALARELLAAGRSV-ILD 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236892066  81 GgldldfhGFTRLFHRrgyltdaefdlcaRLYRQLRALLGPPDLILHLIAPLPVVEARYAQRGRALEI--AQRADLALME 158
Cdd:COG0645    77 A-------TFLRRAQR-------------EAFRALAEEAGAPFVLIWLDAPEEVLRERLEARNAEGGDsdATWEVLERQL 136

                         170       180
                  ....*....|....*....|....
gi 1236892066 159 EFVADWIASvrDMPVITVDASADD 182
Cdd:COG0645   137 AFEEPLTED--EGFLLVVDTSGLE 158
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
5-24 5.74e-03

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 36.11  E-value: 5.74e-03
                          10        20
                  ....*....|....*....|
gi 1236892066   5 IAIVGNSGVGKTTLVEALRR 24
Cdd:COG1100     6 IVVVGTGGVGKTSLVNRLVG 25
AAA_28 pfam13521
AAA domain;
5-80 7.69e-03

AAA domain;


Pssm-ID: 433278 [Multi-domain]  Cd Length: 164  Bit Score: 35.70  E-value: 7.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236892066   5 IAIVGNSGVGKTTLVEAL-RRARPLAVG------LEQHAARPFQALMAADPPryaLANQIDYLLLRAEQERALRAGPT-- 75
Cdd:pfam13521   2 IVITGGPSTGKTTLAEALaARFGYPVVPeaareiLEELGADGGDALPWVEDL---LAFARGVLEAQLEDEAAAAANDLlf 78


                  ....*..
gi 1236892066  76 --TGLID 80
Cdd:pfam13521  79 fdRGPLD 85
mobB TIGR00176
molybdopterin-guanine dinucleotide biosynthesis protein MobB; This molybdenum cofactor ...
 4-41 7.70e-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: 35.82  E-value: 7.70e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1236892066   4 VIAIVGNSGVGKTTLVEAL---RRARPLAVGLEQHAARPFQ 41
Cdd:TIGR00176   1 VLQIVGPKNSGKTTLIERLvkaLKARGYRVATIKHDHHDFD 41
 
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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