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Conserved domains on  [gi|1565696185|ref|WP_129045679|]
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deoxynucleoside kinase [Companilactobacillus metriopterae]

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];
1-210 5.46e-90

Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];


:

Pssm-ID: 441037 [Multi-domain]  Cd Length: 205  Bit Score: 262.80  E-value: 5.46e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565696185   1 MIVLSGTIGAGKSSLATLLSEHLGTEAFYEQVDDNPVLPLFYKDPKKYAFLLQIYFLNKRFDSIKQAM-SDDNNVLDRSI 79
Cdd:COG1428     5 YIAVEGNIGAGKTTLARLLAEHLGAELLLEPVEDNPFLEDFYEDPKRWAFPLQLFFLLSRFKQLKDLRqFGGNVVSDRSI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565696185  80 YEDSLFFHMNADMGRATSQEVQVYDDLLDNMMQELPyaadkkAPDLLVHIDVSYETMINRIQKRGRDYEQLEQDStlenY 159
Cdd:COG1428    85 YKDAIFAKLLHEMGTLSDREFDLYRQLFDNLTEDLP------KPDLVIYLQASVDTLLERIKKRGRDYEQNIDLD----Y 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1565696185 160 YKSLLKRYDGWYDNYDYSPKMKIDGDKFNFVENEDDLQSVLQQIDKELELR 210
Cdd:COG1428   155 LERLNEAYEEWFEHYDASPVLIIDTDELDFVNNPEDLELLLEQIEEKLKGR 205
 
Name Accession Description Interval E-value
Dck COG1428
Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];
1-210 5.46e-90

Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];


Pssm-ID: 441037 [Multi-domain]  Cd Length: 205  Bit Score: 262.80  E-value: 5.46e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565696185   1 MIVLSGTIGAGKSSLATLLSEHLGTEAFYEQVDDNPVLPLFYKDPKKYAFLLQIYFLNKRFDSIKQAM-SDDNNVLDRSI 79
Cdd:COG1428     5 YIAVEGNIGAGKTTLARLLAEHLGAELLLEPVEDNPFLEDFYEDPKRWAFPLQLFFLLSRFKQLKDLRqFGGNVVSDRSI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565696185  80 YEDSLFFHMNADMGRATSQEVQVYDDLLDNMMQELPyaadkkAPDLLVHIDVSYETMINRIQKRGRDYEQLEQDStlenY 159
Cdd:COG1428    85 YKDAIFAKLLHEMGTLSDREFDLYRQLFDNLTEDLP------KPDLVIYLQASVDTLLERIKKRGRDYEQNIDLD----Y 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1565696185 160 YKSLLKRYDGWYDNYDYSPKMKIDGDKFNFVENEDDLQSVLQQIDKELELR 210
Cdd:COG1428   155 LERLNEAYEEWFEHYDASPVLIIDTDELDFVNNPEDLELLLEQIEEKLKGR 205
dNK pfam01712
Deoxynucleoside kinase; This family consists of various deoxynucleoside kinases cytidine EC:2. ...
2-205 1.14e-69

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: 211.41  E-value: 1.14e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565696185   2 IVLSGTIGAGKSSLATLLSEHLGTEAFYEQVDD--NPVLPLFYKDPKKYAFLLQIYFLNKRFDSIKQAM-SDDNNVLDRS 78
Cdd:pfam01712   1 ISIEGNIGAGKSTLTKILSKRLGFKVFEEPVDRwtNPYLDKFYKDPSRWSFALQTYFLNSRFKQQLEAFfTGQVVILERS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565696185  79 IYED-SLFFHMNADMGRATSQEVQVYDDLLDNMMQELPyaadkkAPDLLVHIDVSYETMINRIQKRGRDYEQleqdSTLE 157
Cdd:pfam01712  81 IYSDrYIFAKMLYDKGTMSDEEYKTYKDLYDNMLLEFP------KPDLIIYLKTSPETCLERIKKRGRTEEQ----NISL 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1565696185 158 NYYKSLLKRYDGWYDNYDYSPKMKIDGDKFNFVENEDDLQSVLQQIDK 205
Cdd:pfam01712 151 DYLERLHEKYEAWLKKLNLSPVLVIDGDELDFVFFEEDREDVMNEVNE 198
dNK cd01673
Deoxyribonucleoside kinase (dNK) catalyzes the phosphorylation of deoxyribonucleosides to ...
2-193 1.35e-58

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: 182.81  E-value: 1.35e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565696185   2 IVLSGTIGAGKSSLATLLSEHLGTEAFYE----QVDDNPVLPLFYKDPKKYAFLLQIYFLNKRFDSIKQAMSDDNN---- 73
Cdd:cd01673     2 IVVEGNIGAGKSTLAKELAEHLGYEVVPEpvepDVEGNPFLEKFYEDPKRWAFPFQLYFLLSRLKQYKDALEHLSTgqgv 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565696185  74 VLDRSIYEDSLFFHMNADMGRATSQEVQVYDDLLDNMMQELPyaadkkAPDLLVHIDVSYETMINRIQKRGRDYEQleqd 153
Cdd:cd01673    82 ILERSIFSDRVFAEANLKEGGIMKTEYDLYNELFDNLIPELL------PPDLVIYLDASPETCLKRIKKRGRPEEQ---- 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1565696185 154 STLENYYKSLLKRYDGWYDN--YDYSPKMKIDGDKFNFVENE 193
Cdd:cd01673   152 GIPLDYLEDLHEAYEKWFLPqmYEKAPVLIIDANEADIEYNK 193
DTMP_kinase TIGR00041
dTMP kinase; Function: phosphorylation of DTMP to form DTDP in both de novo and salvage ...
2-166 2.47e-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: 37.73  E-value: 2.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565696185   2 IVLSGTIGAGKSSLATLLSEHLGTEAFY-------------------------EQVDDNPVLPLFYKDpkkyafllQIYF 56
Cdd:TIGR00041   6 IVIEGIDGAGKTTQANLLKKLLQENGYDvlftrepggtpigekirelllnendEPLTDKAEALLFAAD--------RHEH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565696185  57 LNkrfDSIKQAMSDDNNVL-DRSIYedslffhmnadmgraTSQEVQVYDDLLD-NMMQELPYAADKKAPDLLVHIDVSYE 134
Cdd:TIGR00041  78 LE---DKIKPALAEGKLVIsDRYVF---------------SSIAYQGGARGIDeDLVLELNEDALGDMPDLTIYLDIDPE 139
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1565696185 135 TMINRIQKRGR----DYEQLEQDSTLENYYKSLLKR 166
Cdd:TIGR00041 140 VALERLRKRGEldreEFEKLDFFEKVRQRYLELADK 175
 
Name Accession Description Interval E-value
Dck COG1428
Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];
1-210 5.46e-90

Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];


Pssm-ID: 441037 [Multi-domain]  Cd Length: 205  Bit Score: 262.80  E-value: 5.46e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565696185   1 MIVLSGTIGAGKSSLATLLSEHLGTEAFYEQVDDNPVLPLFYKDPKKYAFLLQIYFLNKRFDSIKQAM-SDDNNVLDRSI 79
Cdd:COG1428     5 YIAVEGNIGAGKTTLARLLAEHLGAELLLEPVEDNPFLEDFYEDPKRWAFPLQLFFLLSRFKQLKDLRqFGGNVVSDRSI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565696185  80 YEDSLFFHMNADMGRATSQEVQVYDDLLDNMMQELPyaadkkAPDLLVHIDVSYETMINRIQKRGRDYEQLEQDStlenY 159
Cdd:COG1428    85 YKDAIFAKLLHEMGTLSDREFDLYRQLFDNLTEDLP------KPDLVIYLQASVDTLLERIKKRGRDYEQNIDLD----Y 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1565696185 160 YKSLLKRYDGWYDNYDYSPKMKIDGDKFNFVENEDDLQSVLQQIDKELELR 210
Cdd:COG1428   155 LERLNEAYEEWFEHYDASPVLIIDTDELDFVNNPEDLELLLEQIEEKLKGR 205
dNK pfam01712
Deoxynucleoside kinase; This family consists of various deoxynucleoside kinases cytidine EC:2. ...
2-205 1.14e-69

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: 211.41  E-value: 1.14e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565696185   2 IVLSGTIGAGKSSLATLLSEHLGTEAFYEQVDD--NPVLPLFYKDPKKYAFLLQIYFLNKRFDSIKQAM-SDDNNVLDRS 78
Cdd:pfam01712   1 ISIEGNIGAGKSTLTKILSKRLGFKVFEEPVDRwtNPYLDKFYKDPSRWSFALQTYFLNSRFKQQLEAFfTGQVVILERS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565696185  79 IYED-SLFFHMNADMGRATSQEVQVYDDLLDNMMQELPyaadkkAPDLLVHIDVSYETMINRIQKRGRDYEQleqdSTLE 157
Cdd:pfam01712  81 IYSDrYIFAKMLYDKGTMSDEEYKTYKDLYDNMLLEFP------KPDLIIYLKTSPETCLERIKKRGRTEEQ----NISL 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1565696185 158 NYYKSLLKRYDGWYDNYDYSPKMKIDGDKFNFVENEDDLQSVLQQIDK 205
Cdd:pfam01712 151 DYLERLHEKYEAWLKKLNLSPVLVIDGDELDFVFFEEDREDVMNEVNE 198
dNK cd01673
Deoxyribonucleoside kinase (dNK) catalyzes the phosphorylation of deoxyribonucleosides to ...
2-193 1.35e-58

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: 182.81  E-value: 1.35e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565696185   2 IVLSGTIGAGKSSLATLLSEHLGTEAFYE----QVDDNPVLPLFYKDPKKYAFLLQIYFLNKRFDSIKQAMSDDNN---- 73
Cdd:cd01673     2 IVVEGNIGAGKSTLAKELAEHLGYEVVPEpvepDVEGNPFLEKFYEDPKRWAFPFQLYFLLSRLKQYKDALEHLSTgqgv 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565696185  74 VLDRSIYEDSLFFHMNADMGRATSQEVQVYDDLLDNMMQELPyaadkkAPDLLVHIDVSYETMINRIQKRGRDYEQleqd 153
Cdd:cd01673    82 ILERSIFSDRVFAEANLKEGGIMKTEYDLYNELFDNLIPELL------PPDLVIYLDASPETCLKRIKKRGRPEEQ---- 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1565696185 154 STLENYYKSLLKRYDGWYDN--YDYSPKMKIDGDKFNFVENE 193
Cdd:cd01673   152 GIPLDYLEDLHEAYEKWFLPqmYEKAPVLIIDANEADIEYNK 193
NDUO42 cd02030
NADH:Ubiquinone oxioreductase, 42 kDa (NDUO42) is a family of proteins that are highly similar ...
2-170 4.95e-12

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: 62.76  E-value: 4.95e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565696185   2 IVLSGTIGAGKSSLATLLSEHLGTEAFYEqVDD-------------------NPVLPLFYKDPKKY---AFLLQIYFLNK 59
Cdd:cd02030     2 ITVDGNIASGKGKLAKELAEKLGMKYFPE-AGIhyldsttgdgkpldpafngNCSLEKFYDDPKSNdgnSYRLQSWMYSS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565696185  60 RFDSIKQAM-----SDDNNVLDRSIYEDSLFFHMNADMGRATSQEVQVYDDLLDNMMQE-LPyaadkkaPDLLVHIDVSY 133
Cdd:cd02030    81 RLLQYSDALehllsTGQGVVLERSPFSDFVFLEAMYKQGYIRKQCVDHYNEVKGNTIPElLP-------PHLVIYLDVPV 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1565696185 134 ETMINRIQKRGRDYEQ---LEQDSTLENYYK-SLLKRYDGW 170
Cdd:cd02030   154 PEVQKRIKKRGDPHEMkvtSAYLQDIENAYKkTFLPEISEH 194
AAA_18 pfam13238
AAA domain;
2-145 2.02e-03

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 37.02  E-value: 2.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565696185   2 IVLSGTIGAGKSSLATLLSEHLGTEAFYEQVDDNPVLPlfykdpkkyafllqIYFLNKRFDSIKQAMSDDNNVLDrsiye 81
Cdd:pfam13238   1 ILITGTPGVGKTTLAKELSKRLGFGDNVRDLALENGLV--------------LGDDPETRESKRLDEDKLDRLLD----- 61
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1565696185  82 dslFFHMNADMGRAtsqEVQVYDDLLDNMmqELPYAADKKapdlLVHIDVSYETMINRIQKRGR 145
Cdd:pfam13238  62 ---LLEENAALEEG---GNLIIDGHLAEL--EPERAKDLV----GIVLRASPEELLERLEKRGY 113
AAA_28 pfam13521
AAA domain;
2-79 2.08e-03

AAA domain;


Pssm-ID: 433278 [Multi-domain]  Cd Length: 164  Bit Score: 37.63  E-value: 2.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565696185   2 IVLSGTIGAGKSSLATLLSEHLGTEAFYE---------QVDDNPVLPLFYkDPKkyafLLQIYFLNKRFDSIKQAmsDDN 72
Cdd:pfam13521   2 IVITGGPSTGKTTLAEALAARFGYPVVPEaareileelGADGGDALPWVE-DLL----AFARGVLEAQLEDEAAA--AAN 74

                  ....*....
gi 1565696185  73 NVL--DRSI 79
Cdd:pfam13521  75 DLLffDRGP 83
DTMP_kinase TIGR00041
dTMP kinase; Function: phosphorylation of DTMP to form DTDP in both de novo and salvage ...
2-166 2.47e-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: 37.73  E-value: 2.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565696185   2 IVLSGTIGAGKSSLATLLSEHLGTEAFY-------------------------EQVDDNPVLPLFYKDpkkyafllQIYF 56
Cdd:TIGR00041   6 IVIEGIDGAGKTTQANLLKKLLQENGYDvlftrepggtpigekirelllnendEPLTDKAEALLFAAD--------RHEH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565696185  57 LNkrfDSIKQAMSDDNNVL-DRSIYedslffhmnadmgraTSQEVQVYDDLLD-NMMQELPYAADKKAPDLLVHIDVSYE 134
Cdd:TIGR00041  78 LE---DKIKPALAEGKLVIsDRYVF---------------SSIAYQGGARGIDeDLVLELNEDALGDMPDLTIYLDIDPE 139
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1565696185 135 TMINRIQKRGR----DYEQLEQDSTLENYYKSLLKR 166
Cdd:TIGR00041 140 VALERLRKRGEldreEFEKLDFFEKVRQRYLELADK 175
Fap7 COG1936
Broad-specificity NMP kinase [Nucleotide transport and metabolism];
1-26 3.40e-03

Broad-specificity NMP kinase [Nucleotide transport and metabolism];


Pssm-ID: 441539 [Multi-domain]  Cd Length: 173  Bit Score: 37.10  E-value: 3.40e-03
                          10        20
                  ....*....|....*....|....*.
gi 1565696185   1 MIVLSGTIGAGKSSLATLLSEHLGTE 26
Cdd:COG1936     2 RIAITGTPGTGKTTVAKLLAERLGLE 27
CMPK cd02020
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ...
2-24 4.86e-03

Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.


Pssm-ID: 238978 [Multi-domain]  Cd Length: 147  Bit Score: 36.31  E-value: 4.86e-03
                          10        20
                  ....*....|....*....|...
gi 1565696185   2 IVLSGTIGAGKSSLATLLSEHLG 24
Cdd:cd02020     2 IAIDGPAGSGKSTVAKLLAKKLG 24
 
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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