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Conserved domains on  [gi|489339956|ref|WP_003247138|]
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MULTISPECIES: deoxyguanosine kinase [Bacillus]

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];
5-206 5.01e-88

Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];


:

Pssm-ID: 441037 [Multi-domain]  Cd Length: 205  Bit Score: 257.79  E-value: 5.01e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339956   5 PFIAIEGPIGAGKTTLATMLSQKFGFPMINEIVEDNPYLDKFYDNIKEWSFQLEMFFLCHRYKQLEDTSdhflKKGQPVI 84
Cdd:COG1428    4 RYIAVEGNIGAGKTTLARLLAEHLGAELLLEPVEDNPFLEDFYEDPKRWAFPLQLFFLLSRFKQLKDLR----QFGGNVV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339956  85 ADYHIYKNVIFAER-----TLSPHQLEKYKKIYHLLTDDLPKPNFIIYIKASLPTLLHRIEKRGRPFEKKIETSYLEQLI 159
Cdd:COG1428   80 SDRSIYKDAIFAKLlhemgTLSDREFDLYRQLFDNLTEDLPKPDLVIYLQASVDTLLERIKKRGRDYEQNIDLDYLERLN 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 489339956 160 SDYEVAIKQLQEADpeltVLTVDGDSKDFVLNKSDFERIAAHVKELI 206
Cdd:COG1428  160 EAYEEWFEHYDASP----VLIIDTDELDFVNNPEDLELLLEQIEEKL 202
 
Name Accession Description Interval E-value
Dck COG1428
Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];
5-206 5.01e-88

Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];


Pssm-ID: 441037 [Multi-domain]  Cd Length: 205  Bit Score: 257.79  E-value: 5.01e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339956   5 PFIAIEGPIGAGKTTLATMLSQKFGFPMINEIVEDNPYLDKFYDNIKEWSFQLEMFFLCHRYKQLEDTSdhflKKGQPVI 84
Cdd:COG1428    4 RYIAVEGNIGAGKTTLARLLAEHLGAELLLEPVEDNPFLEDFYEDPKRWAFPLQLFFLLSRFKQLKDLR----QFGGNVV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339956  85 ADYHIYKNVIFAER-----TLSPHQLEKYKKIYHLLTDDLPKPNFIIYIKASLPTLLHRIEKRGRPFEKKIETSYLEQLI 159
Cdd:COG1428   80 SDRSIYKDAIFAKLlhemgTLSDREFDLYRQLFDNLTEDLPKPDLVIYLQASVDTLLERIKKRGRDYEQNIDLDYLERLN 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 489339956 160 SDYEVAIKQLQEADpeltVLTVDGDSKDFVLNKSDFERIAAHVKELI 206
Cdd:COG1428  160 EAYEEWFEHYDASP----VLIIDTDELDFVNNPEDLELLLEQIEEKL 202
dNK pfam01712
Deoxynucleoside kinase; This family consists of various deoxynucleoside kinases cytidine EC:2. ...
 7-207 1.50e-77

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: 231.05  E-value: 1.50e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339956    7 IAIEGPIGAGKTTLATMLSQKFGFPMINEIVED--NPYLDKFYDNIKEWSFQLEMFFLCHRYKQLEDtsdhFLKKGQPVI 84
Cdd:pfam01712   1 ISIEGNIGAGKSTLTKILSKRLGFKVFEEPVDRwtNPYLDKFYKDPSRWSFALQTYFLNSRFKQQLE----AFFTGQVVI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339956   85 ADYHIYKNV-IFAE-----RTLSPHQLEKYKKIYHLLTDDLPKPNFIIYIKASLPTLLHRIEKRGRPFEKKIETSYLEQL 158
Cdd:pfam01712  77 LERSIYSDRyIFAKmlydkGTMSDEEYKTYKDLYDNMLLEFPKPDLIIYLKTSPETCLERIKKRGRTEEQNISLDYLERL 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 489339956  159 ISDYEVAIKQLQEAdpelTVLTVDGDSKDFVLNKSDFERIAAHVKELIV 207
Cdd:pfam01712 157 HEKYEAWLKKLNLS----PVLVIDGDELDFVFFEEDREDVMNEVNEFVS 201
dNK cd01673
Deoxyribonucleoside kinase (dNK) catalyzes the phosphorylation of deoxyribonucleosides to ...
 6-192 1.40e-61

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: 190.13  E-value: 1.40e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339956   6 FIAIEGPIGAGKTTLATMLSQKFGFPMINEI----VEDNPYLDKFYDNIKEWSFQLEMFFLCHRYKQLEDTSDHfLKKGQ 81
Cdd:cd01673    1 VIVVEGNIGAGKSTLAKELAEHLGYEVVPEPvepdVEGNPFLEKFYEDPKRWAFPFQLYFLLSRLKQYKDALEH-LSTGQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339956  82 PVIADYHIYKNVIFAERTLSPHQLEK-----YKKIYHLLTDDLPKPNFIIYIKASLPTLLHRIEKRGRPFEKKIETSYLE 156
Cdd:cd01673   80 GVILERSIFSDRVFAEANLKEGGIMKteydlYNELFDNLIPELLPPDLVIYLDASPETCLKRIKKRGRPEEQGIPLDYLE 159

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 489339956 157 QLISDYEVAIkqLQEADPELTVLTVDGDSKDFVLNK 192
Cdd:cd01673  160 DLHEAYEKWF--LPQMYEKAPVLIIDANEADIEYNK 193
PRK04182 PRK04182
cytidylate kinase; Provisional
 6-151 2.76e-06

cytidylate kinase; Provisional


Pssm-ID: 235244 [Multi-domain]  Cd Length: 180  Bit Score: 45.95  E-value: 2.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339956   6 FIAIEGPIGAGKTTLATMLSQKFGFPMIN--EIvednpyldkFYDNIKEWSFQLEMFflcHRYKQLEDTSDHFLKKGQPV 83
Cdd:PRK04182   2 IITISGPPGSGKTTVARLLAEKLGLKHVSagEI---------FRELAKERGMSLEEF---NKYAEEDPEIDKEIDRRQLE 69

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489339956  84 IADYHiyKNVIFAERtLSPHQLEKYkkiyhlltddlpkPNFIIYIKASLPTLLHRIEKR-GRPFEKKIE 151
Cdd:PRK04182  70 IAEKE--DNVVLEGR-LAGWMAKDY-------------ADLKIWLKAPLEVRAERIAEReGISVEEALE 122
DTMP_kinase TIGR00041
dTMP kinase; Function: phosphorylation of DTMP to form DTDP in both de novo and salvage ...
 6-186 5.17e-05

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: 42.35  E-value: 5.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339956    6 FIAIEGPIGAGKTTLATMLSQKF--------------GFPM---INEIVednpyldkFYDNIKEWSFQLEMF-FLCHRYK 67
Cdd:TIGR00041   5 FIVIEGIDGAGKTTQANLLKKLLqengydvlftrepgGTPIgekIRELL--------LNENDEPLTDKAEALlFAADRHE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339956   68 QLEDTSDHFLKKGQPVIADYHIYKNVIF--AERTLSPHQLekyKKIYHLLTDDlpKPNFIIYIKASLPTLLHRIEKRGrp 145
Cdd:TIGR00041  77 HLEDKIKPALAEGKLVISDRYVFSSIAYqgGARGIDEDLV---LELNEDALGD--MPDLTIYLDIDPEVALERLRKRG-- 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 489339956  146 fekKIETSYLEQLISDYEVAIKQLQEADPELTVLTVDGDSK 186
Cdd:TIGR00041 150 ---ELDREEFEKLDFFEKVRQRYLELADKEKSIHVIDATNS 187
 
Name Accession Description Interval E-value
Dck COG1428
Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];
5-206 5.01e-88

Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];


Pssm-ID: 441037 [Multi-domain]  Cd Length: 205  Bit Score: 257.79  E-value: 5.01e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339956   5 PFIAIEGPIGAGKTTLATMLSQKFGFPMINEIVEDNPYLDKFYDNIKEWSFQLEMFFLCHRYKQLEDTSdhflKKGQPVI 84
Cdd:COG1428    4 RYIAVEGNIGAGKTTLARLLAEHLGAELLLEPVEDNPFLEDFYEDPKRWAFPLQLFFLLSRFKQLKDLR----QFGGNVV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339956  85 ADYHIYKNVIFAER-----TLSPHQLEKYKKIYHLLTDDLPKPNFIIYIKASLPTLLHRIEKRGRPFEKKIETSYLEQLI 159
Cdd:COG1428   80 SDRSIYKDAIFAKLlhemgTLSDREFDLYRQLFDNLTEDLPKPDLVIYLQASVDTLLERIKKRGRDYEQNIDLDYLERLN 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 489339956 160 SDYEVAIKQLQEADpeltVLTVDGDSKDFVLNKSDFERIAAHVKELI 206
Cdd:COG1428  160 EAYEEWFEHYDASP----VLIIDTDELDFVNNPEDLELLLEQIEEKL 202
dNK pfam01712
Deoxynucleoside kinase; This family consists of various deoxynucleoside kinases cytidine EC:2. ...
 7-207 1.50e-77

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: 231.05  E-value: 1.50e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339956    7 IAIEGPIGAGKTTLATMLSQKFGFPMINEIVED--NPYLDKFYDNIKEWSFQLEMFFLCHRYKQLEDtsdhFLKKGQPVI 84
Cdd:pfam01712   1 ISIEGNIGAGKSTLTKILSKRLGFKVFEEPVDRwtNPYLDKFYKDPSRWSFALQTYFLNSRFKQQLE----AFFTGQVVI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339956   85 ADYHIYKNV-IFAE-----RTLSPHQLEKYKKIYHLLTDDLPKPNFIIYIKASLPTLLHRIEKRGRPFEKKIETSYLEQL 158
Cdd:pfam01712  77 LERSIYSDRyIFAKmlydkGTMSDEEYKTYKDLYDNMLLEFPKPDLIIYLKTSPETCLERIKKRGRTEEQNISLDYLERL 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 489339956  159 ISDYEVAIKQLQEAdpelTVLTVDGDSKDFVLNKSDFERIAAHVKELIV 207
Cdd:pfam01712 157 HEKYEAWLKKLNLS----PVLVIDGDELDFVFFEEDREDVMNEVNEFVS 201
dNK cd01673
Deoxyribonucleoside kinase (dNK) catalyzes the phosphorylation of deoxyribonucleosides to ...
 6-192 1.40e-61

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: 190.13  E-value: 1.40e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339956   6 FIAIEGPIGAGKTTLATMLSQKFGFPMINEI----VEDNPYLDKFYDNIKEWSFQLEMFFLCHRYKQLEDTSDHfLKKGQ 81
Cdd:cd01673    1 VIVVEGNIGAGKSTLAKELAEHLGYEVVPEPvepdVEGNPFLEKFYEDPKRWAFPFQLYFLLSRLKQYKDALEH-LSTGQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339956  82 PVIADYHIYKNVIFAERTLSPHQLEK-----YKKIYHLLTDDLPKPNFIIYIKASLPTLLHRIEKRGRPFEKKIETSYLE 156
Cdd:cd01673   80 GVILERSIFSDRVFAEANLKEGGIMKteydlYNELFDNLIPELLPPDLVIYLDASPETCLKRIKKRGRPEEQGIPLDYLE 159

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 489339956 157 QLISDYEVAIkqLQEADPELTVLTVDGDSKDFVLNK 192
Cdd:cd01673  160 DLHEAYEKWF--LPQMYEKAPVLIIDANEADIEYNK 193
NDUO42 cd02030
NADH:Ubiquinone oxioreductase, 42 kDa (NDUO42) is a family of proteins that are highly similar ...
 7-199 6.07e-21

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: 86.64  E-value: 6.07e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339956   7 IAIEGPIGAGKTTLATMLSQKFG---FPMINEIVED---------------NPYLDKFYDNIK---EWSFQLEMFFLCHR 65
Cdd:cd02030    2 ITVDGNIASGKGKLAKELAEKLGmkyFPEAGIHYLDsttgdgkpldpafngNCSLEKFYDDPKsndGNSYRLQSWMYSSR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339956  66 YKQLEDTSDHFLKKGQPVIADYHIYKNVIFAE-----RTLSPHQLEKYKKIYHLLTDDLPKPNFIIYIKASLPTLLHRIE 140
Cdd:cd02030   82 LLQYSDALEHLLSTGQGVVLERSPFSDFVFLEamykqGYIRKQCVDHYNEVKGNTIPELLPPHLVIYLDVPVPEVQKRIK 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489339956 141 KRGRPFEKKIETSYLEqlisDYEVAIKQ--LQEADPELTVLTVD----GDSKDFVlnkSDFERIA 199
Cdd:cd02030  162 KRGDPHEMKVTSAYLQ----DIENAYKKtfLPEISEHSEVLQYDwteaGDTEKVV---EDIEYLK 219
Tmk COG0125
Thymidylate kinase [Nucleotide transport and metabolism]; Thymidylate kinase is part of the ...
 6-206 6.37e-09

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: 53.62  E-value: 6.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339956   6 FIAIEGPIGAGKTTLATMLSQKF----------GFP-------MINEIVEDNPyldkfydniKEWSFQLE-MFFLCHRYK 67
Cdd:COG0125    5 FIVFEGIDGSGKSTQIKLLAEYLeargydvvltREPggtplgeAIRELLLGDN---------EDMSPRTElLLFAADRAQ 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339956  68 QLEDTSDHFLKKGQPVIADYHIYKNVIF--AERTLSPHQLEkykKIYHLLTDDlPKPNFIIYIKASLPTLLHRIEKRGRP 145
Cdd:COG0125   76 HVEEVIRPALAAGKIVICDRYVDSSLAYqgGGRGLDLEWIR---QLNRFATGG-LKPDLTILLDVPPEVALARARARGGE 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489339956 146 FEkKIETSYLEQLISDYEvAIKQLQEADPElTVLTVDGD-SKDFVlnksdFERIAAHVKELI 206
Cdd:COG0125  152 LD-RFESEDLEFHERVRE-GYLELAAKEPE-RIVVIDASqSIEEV-----HAEIREALAELL 205
AAA_18 pfam13238
AAA domain;
7-158 2.15e-08

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 50.89  E-value: 2.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339956    7 IAIEGPIGAGKTTLATMLSQKFGF-PMINEIVEDNPYLDkfyDNIKEWSFQLEMfflchRYKQLEDTSDHFLKkgqpvIA 85
Cdd:pfam13238   1 ILITGTPGVGKTTLAKELSKRLGFgDNVRDLALENGLVL---GDDPETRESKRL-----DEDKLDRLLDLLEE-----NA 67

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489339956   86 DYHIYKNVIFaERTLSPHQLEKYKKIyhlltddlpkpnFIIYIKASLPTLLHRIEKRGRPFEKKIETSYLEQL 158
Cdd:pfam13238  68 ALEEGGNLII-DGHLAELEPERAKDL------------VGIVLRASPEELLERLEKRGYEEAKIKENEEAEIL 127
TMPK cd01672
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the ...
 6-204 3.37e-07

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: 48.80  E-value: 3.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339956   6 FIAIEGPIGAGKTTLATMLSQKF---GFPM----------INEIVEDNpYLDKFYDNIkEWSFQLEMFFLCHRykqledt 72
Cdd:cd01672    2 FIVFEGIDGAGKTTLIELLAERLearGYEVvltrepggtpIGEAIREL-LLDPEDEKM-DPRAELLLFAADRA------- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339956  73 sDHF-------LKKGQPVIADYHIYKNVIFAE--RTLSPhqlEKYKKIYHLLTDDLpKPNFIIYIKASLPTLLHRIEKRG 143
Cdd:cd01672   73 -QHVeevikpaLARGKIVLSDRFVDSSLAYQGagRGLGE---ALIEALNDLATGGL-KPDLTILLDIDPEVGLARIEARG 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489339956 144 R--PFEKKIEtSYLEQLISDYEvaikQLQEADPElTVLTVDG-DSKDFVLNKsdferIAAHVKE 204
Cdd:cd01672  148 RddRDEQEGL-EFHERVREGYL----ELAAQEPE-RIIVIDAsQPLEEVLAE-----ILKAILE 200
CMPK cd02020
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ...
 7-59 6.66e-07

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: 47.10  E-value: 6.66e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489339956   7 IAIEGPIGAGKTTLATMLSQKFGFPMIN-------------EIVEDNPYLDKFYDNIkewsfQLEM 59
Cdd:cd02020    2 IAIDGPAGSGKSTVAKLLAKKLGLPYLDtggirteevgklaSEVAAIPEVRKALDER-----QREL 62
PRK04182 PRK04182
cytidylate kinase; Provisional
 6-151 2.76e-06

cytidylate kinase; Provisional


Pssm-ID: 235244 [Multi-domain]  Cd Length: 180  Bit Score: 45.95  E-value: 2.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339956   6 FIAIEGPIGAGKTTLATMLSQKFGFPMIN--EIvednpyldkFYDNIKEWSFQLEMFflcHRYKQLEDTSDHFLKKGQPV 83
Cdd:PRK04182   2 IITISGPPGSGKTTVARLLAEKLGLKHVSagEI---------FRELAKERGMSLEEF---NKYAEEDPEIDKEIDRRQLE 69

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489339956  84 IADYHiyKNVIFAERtLSPHQLEKYkkiyhlltddlpkPNFIIYIKASLPTLLHRIEKR-GRPFEKKIE 151
Cdd:PRK04182  70 IAEKE--DNVVLEGR-LAGWMAKDY-------------ADLKIWLKAPLEVRAERIAEReGISVEEALE 122
Thymidylate_kin pfam02223
Thymidylate kinase;
9-182 2.01e-05

Thymidylate kinase;


Pssm-ID: 396690  Cd Length: 184  Bit Score: 43.44  E-value: 2.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339956    9 IEGPIGAGKTTLATMLSQK---------FGFP--------MINEIVEDNpyldkfydniKEWSFQLE-MFFLCHRYKQLE 70
Cdd:pfam02223   1 IEGLDGAGKTTQAELLKERlkeqgikvvFTREpggtpigeKIRELLLRN----------EELSPLTEaLLFAADRIQHLE 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339956   71 DTSDHFLKKGQPVIADYHIYKNVIFAERTLSPHQLekykkIYHLLTDDLPKPNFIIYIKASLPTLLHRIEKRGrPFEKKI 150
Cdd:pfam02223  71 QKIKPALKQGKTVIVDRYLFSGIAYQGAKGGDLDL-----VLSLNPDVPGKPDLTFLLDVDPEVALKRLRRRG-ELEKTE 144

                         170       180       190
                  ....*....|....*....|....*....|..
gi 489339956  151 EtsylEQLISDYEVAIKQLQEADPELTVLTVD 182
Cdd:pfam02223 145 F----EQLDFLRKVRERYLELAKFDERIKIID 172
DTMP_kinase TIGR00041
dTMP kinase; Function: phosphorylation of DTMP to form DTDP in both de novo and salvage ...
 6-186 5.17e-05

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: 42.35  E-value: 5.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339956    6 FIAIEGPIGAGKTTLATMLSQKF--------------GFPM---INEIVednpyldkFYDNIKEWSFQLEMF-FLCHRYK 67
Cdd:TIGR00041   5 FIVIEGIDGAGKTTQANLLKKLLqengydvlftrepgGTPIgekIRELL--------LNENDEPLTDKAEALlFAADRHE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339956   68 QLEDTSDHFLKKGQPVIADYHIYKNVIF--AERTLSPHQLekyKKIYHLLTDDlpKPNFIIYIKASLPTLLHRIEKRGrp 145
Cdd:TIGR00041  77 HLEDKIKPALAEGKLVISDRYVFSSIAYqgGARGIDEDLV---LELNEDALGD--MPDLTIYLDIDPEVALERLRKRG-- 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 489339956  146 fekKIETSYLEQLISDYEVAIKQLQEADPELTVLTVDGDSK 186
Cdd:TIGR00041 150 ---ELDREEFEKLDFFEKVRQRYLELADKEKSIHVIDATNS 187
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 1-173 1.97e-04

Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 440337 [Multi-domain]  Cd Length: 206  Bit Score: 40.59  E-value: 1.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339956   1 MNTAPFIAIEGPIGAGKTTLATMLSQKFGFPMINEIVEDNPYLDKF-----------YDNIKEWSFQLemfflchRYKQL 69
Cdd:COG0572    4 SGKPRIIGIAGPSGSGKTTFARRLAEQLGADKVVVISLDDYYKDREhlpldergkpnFDHPEAFDLDL-------LNEHL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339956  70 EDtsdhfLKKGQPViaDYHIYKnviFAERTLS--PHQLEKyKKIY-----HLLTDDLPKP--NFIIYIKASLPTLLHR-- 138
Cdd:COG0572   77 EP-----LKAGESV--ELPVYD---FATGTRSgeTVKVEP-ADVIivegiHALNDELLRDllDLKIYVDADTDVRLIRri 145

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 489339956 139 ---IEKRGRPFEKKIEtSYLEQLISDYEVAIKQLQE-AD 173
Cdd:COG0572  146 vrdGEERGRTAESVIE-QYWATVRPGHEQYIEPTKEyAD 183
Fap7 COG1936
Broad-specificity NMP kinase [Nucleotide transport and metabolism];
6-46 2.32e-04

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


Pssm-ID: 441539 [Multi-domain]  Cd Length: 173  Bit Score: 40.18  E-value: 2.32e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 489339956   6 FIAIEGPIGAGKTTLATMLSQKFGFPMI--NEIVEDNPYLDKF 46
Cdd:COG1936    2 RIAITGTPGTGKTTVAKLLAERLGLEVIhlNDLVKEEGLYTEV 44
AAA_17 pfam13207
AAA domain;
11-145 3.98e-04

AAA domain;


Pssm-ID: 463810 [Multi-domain]  Cd Length: 136  Bit Score: 39.14  E-value: 3.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339956   11 GPIGAGKTTLATMLSQKFGFPMIN-------EIVEDNpyLDKFYDNIKEwsfqlemfflchryKQLEDTsDHFLKKGQPV 83
Cdd:pfam13207   2 GVPGSGKTTQLKKLAEKLGFPHISagdllreEAKERG--LVEDRDEMRK--------------LPLEPQ-KELQKLAAER 64

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489339956   84 IADYHIYKNVIFAE--RTLSPH-QLEKYKKIyhlLTDDLpKPNFIIYIKASLPTLLHRIEK---RGRP 145
Cdd:pfam13207  65 IAEEAGEGGVIVDGhpRIKTPAgYLPGLPVE---VLREL-KPDAIILLEADPEEILERRLKdrtRGRD 128
Cytidylate_kin pfam02224
Cytidylate kinase; Cytidylate kinase EC:2.7.4.14 catalyzes the phosphorylation of cytidine 5 ...
 7-34 4.37e-04

Cytidylate kinase; Cytidylate kinase EC:2.7.4.14 catalyzes the phosphorylation of cytidine 5'-monophosphate (dCMP) to cytidine 5'-diphosphate (dCDP) in the presence of ATP or GTP.


Pssm-ID: 280401 [Multi-domain]  Cd Length: 211  Bit Score: 39.59  E-value: 4.37e-04
                          10        20
                  ....*....|....*....|....*...
gi 489339956    7 IAIEGPIGAGKTTLATMLSQKFGFPMIN 34
Cdd:pfam02224   1 IAIDGPSGSGKSTVARILARKLGYKYLD 28
Cmk COG0283
Cytidylate kinase [Nucleotide transport and metabolism];
7-44 6.57e-04

Cytidylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 440052 [Multi-domain]  Cd Length: 220  Bit Score: 39.24  E-value: 6.57e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 489339956   7 IAIEGPIGAGKTTLATMLSQKFGFpmineivednPYLD 44
Cdd:COG0283    3 IAIDGPAGSGKSTVAKALAKRLGY----------HYLD 30
CmkB COG1102
Cytidylate kinase [Nucleotide transport and metabolism];
6-148 7.30e-04

Cytidylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 440719 [Multi-domain]  Cd Length: 188  Bit Score: 39.04  E-value: 7.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339956   6 FIAIEGPIGAGKTTLATMLSQKFGFPMIN-EIV-----EDNPYLDKF--YDNIKEWSFQLEMFflchrykqLEDTSDHFL 77
Cdd:COG1102    2 VITISREPGSGGTTIAKRLAEKLGLPLYDgEILreaakERGLSEEEFekLDEKAPSLLYRDTA--------EEDEIDRAL 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489339956  78 KKgqpVIADYHIYKNVIFAERtLSPHQLEKYKKIYHlltddlpkpnfiIYIKASLPTLLHRIEKR-GRPFEK 148
Cdd:COG1102   74 DK---VIRELARKGNCVIVGR-LADWILRDRPNVLK------------VFLTAPLEVRVKRIAEReGISEEE 129
AAA_28 pfam13521
AAA domain;
6-74 1.09e-03

AAA domain;


Pssm-ID: 433278 [Multi-domain]  Cd Length: 164  Bit Score: 38.01  E-value: 1.09e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489339956    6 FIAIEGPIGAGKTTLATMLSQKFGFPMINE----IVEDNpylDKFYDNIKEWSFQLEMF---FLCHRYKQLEDTSD 74
Cdd:pfam13521   1 RIVITGGPSTGKTTLAEALAARFGYPVVPEaareILEEL---GADGGDALPWVEDLLAFargVLEAQLEDEAAAAA 73
Adk COG0563
Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or ...
 1-33 2.16e-03

Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or related kinase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 440329 [Multi-domain]  Cd Length: 212  Bit Score: 37.80  E-value: 2.16e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 489339956   1 MNtapfIAIEGPIGAGKTTLATMLSQKFGFPMI 33
Cdd:COG0563    1 MR----IILLGPPGAGKGTQAKRLAEKYGIPHI 29
PRK13477 PRK13477
bifunctional pantoate--beta-alanine ligase/(d)CMP kinase;
1-30 2.38e-03

bifunctional pantoate--beta-alanine ligase/(d)CMP kinase;


Pssm-ID: 237393 [Multi-domain]  Cd Length: 512  Bit Score: 38.32  E-value: 2.38e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 489339956   1 MNTAPFIAIEGPIGAGKTTLATMLSQKFGF 30
Cdd:PRK13477 281 MKRQPIIAIDGPAGAGKSTVTRAVAKKLGL 310
UMPK cd02023
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ...
 6-44 2.62e-03

Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or uridine-cytidine kinase (UCK), catalyzes the reversible phosphoryl transfer from ATP to uridine or cytidine to yield UMP or CMP. In the primidine nucleotide-salvage pathway, this enzyme combined with nucleoside diphosphate kinases further phosphorylates UMP and CMP to form UTP and CTP. This kinase also catalyzes the phosphorylation of several cytotoxic ribonucleoside analogs such as 5-flurrouridine and cyclopentenyl-cytidine.


Pssm-ID: 238981 [Multi-domain]  Cd Length: 198  Bit Score: 37.53  E-value: 2.62e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 489339956   6 FIAIEGPIGAGKTTLATMLSQKFGFPMINEIVEDNPYLD 44
Cdd:cd02023    1 IIGIAGGSGSGKTTVAEEIIEQLGNPKVVIISQDSYYKD 39
NK cd02019
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ...
 7-38 2.95e-03

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.


Pssm-ID: 238977 [Multi-domain]  Cd Length: 69  Bit Score: 35.00  E-value: 2.95e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 489339956   7 IAIEGPIGAGKTTLATMLSQKFGFPMINEIVE 38
Cdd:cd02019    2 IAITGGSGSGKSTVAKKLAEQLGGRSVVVLDE 33
PRK06547 PRK06547
hypothetical protein; Provisional
 4-47 3.63e-03

hypothetical protein; Provisional


Pssm-ID: 235825  Cd Length: 172  Bit Score: 36.64  E-value: 3.63e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 489339956   4 APFIAIEGPIGAGKTTLATMLSQKFGFpminEIVednpYLDKFY 47
Cdd:PRK06547  15 MITVLIDGRSGSGKTTLAGALAARTGF----QLV----HLDDLY 50
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 1-44 4.75e-03

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 36.68  E-value: 4.75e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 489339956   1 MNTAPF-IAIEGPIGAGKTTLATMLSQKFGFPMINEIVEDNPYLD 44
Cdd:PRK05480   2 MMKKPIiIGIAGGSGSGKTTVASTIYEELGDESIAVIPQDSYYKD 46
ADK cd01428
Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine ...
 7-143 4.98e-03

Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine triphosphates (ATP) to adenosine monophosphates (AMP) and to yield adenosine diphosphates (ADP). This enzyme is required for the biosynthesis of ADP and is essential for homeostasis of adenosine phosphates.


Pssm-ID: 238713 [Multi-domain]  Cd Length: 194  Bit Score: 36.45  E-value: 4.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339956   7 IAIEGPIGAGKTTLATMLSQKFGFPMI-------NEIVEDNPYLDKFYDNIKEWSF---QLEMFFLCHRYKQlEDTSDHF 76
Cdd:cd01428    2 ILLLGPPGSGKGTQAERLAKKYGLPHIstgdllrEEIASGTELGKKAKEYIDSGKLvpdEIVIKLLKERLKK-PDCKKGF 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489339956  77 LKKGQPviadyhiyknvifaeRTLSphQLEKYKKIyhllTDDLPKPNFIIYIKASLPTLLHRIEKRG 143
Cdd:cd01428   81 ILDGFP---------------RTVD--QAEALDEL----LDEGIKPDKVIELDVPDEVLIERILGRR 126
TIGR00152 TIGR00152
dephospho-CoA kinase; This model produces scores in the range of 0-25 bits against adenylate, ...
 7-34 6.37e-03

dephospho-CoA kinase; This model produces scores in the range of 0-25 bits against adenylate, guanylate, uridine, and thymidylate kinases. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]


Pssm-ID: 272931  Cd Length: 190  Bit Score: 36.21  E-value: 6.37e-03
                          10        20
                  ....*....|....*....|....*...
gi 489339956    7 IAIEGPIGAGKTTLATMLSQKFGFPMIN 34
Cdd:TIGR00152   2 IALTGGIGSGKSTVLQYLADKYHFPVID 29
SK cd00464
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ...
 7-158 7.39e-03

Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic pathway which converts erythrose-4-phosphate to chorismic acid, found in bacteria, fungi and plants. Chorismic acid is a important intermediate in the synthesis of aromatic compounds, such as aromatic amino acids, p-aminobenzoic acid, folate and ubiquinone. Shikimate kinase catalyses the phosphorylation of the 3-hydroxyl group of shikimic acid using ATP.


Pssm-ID: 238260 [Multi-domain]  Cd Length: 154  Bit Score: 35.61  E-value: 7.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339956   7 IAIEGPIGAGKTTLATMLSQKFGFPMI---NEIVEdnpyldKFYDNIKEwsfqlemFFlchrykqLEDTSDHFLKKGQPV 83
Cdd:cd00464    2 IVLIGMMGAGKTTVGRLLAKALGLPFVdldELIEQ------RAGMSIPE-------IF-------AEEGEEGFRELEREV 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339956  84 IADYHIYKNVIFAerT-----LSPHQLEKYKkiyhlltddlpKPNFIIYIKASLPTLLHRIEKRG-RPFEKKIETSYLEQ 157
Cdd:cd00464   62 LLLLLTKENAVIA--TgggavLREENRRLLL-----------ENGIVVWLDASPEELLERLARDKtRPLLQDEDPERLRE 128


                 .
gi 489339956 158 L 158
Cdd:cd00464  129 L 129
 
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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