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Conserved domains on  [gi|38492611|pdb|1OE0|D]
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Chain D, Deoxyribonucleoside Kinase

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 ...
23-214 9.89e-64

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: 196.68  E-value: 9.89e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OE0_D       23 VLIEGNIGSGKTTYLNHFEKyKNDICLLTEPVEkwRNVNGVNLLELMYKDPKKWAMPFQSYVTLTMLQSHTAP----TNK 98
Cdd:cd01673   2 IVVEGNIGAGKSTLAKELAE-HLGYEVVPEPVE--PDVEGNPFLEKFYEDPKRWAFPFQLYFLLSRLKQYKDAlehlSTG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OE0_D       99 KLKIMERSIFSARYCFVENMRRNGSLEQgMYNTLEEWYKFIEESiHVQADLIIYLRTSPEVAYERIRQRARSEESCVPLK 178
Cdd:cd01673  79 QGVILERSIFSDRVFAEANLKEGGIMKT-EYDLYNELFDNLIPE-LLPPDLVIYLDASPETCLKRIKKRGRPEEQGIPLD 156
                       170       180       190
                ....*....|....*....|....*....|....*..
1OE0_D      179 YLQELHELHEDWLIHQRRpQSCKVLVLDAD-LNLENI 214
Cdd:cd01673 157 YLEDLHEAYEKWFLPQMY-EKAPVLIIDANeADIEYN 192
 
Name Accession Description Interval E-value
dNK cd01673
Deoxyribonucleoside kinase (dNK) catalyzes the phosphorylation of deoxyribonucleosides to ...
23-214 9.89e-64

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: 196.68  E-value: 9.89e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OE0_D       23 VLIEGNIGSGKTTYLNHFEKyKNDICLLTEPVEkwRNVNGVNLLELMYKDPKKWAMPFQSYVTLTMLQSHTAP----TNK 98
Cdd:cd01673   2 IVVEGNIGAGKSTLAKELAE-HLGYEVVPEPVE--PDVEGNPFLEKFYEDPKRWAFPFQLYFLLSRLKQYKDAlehlSTG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OE0_D       99 KLKIMERSIFSARYCFVENMRRNGSLEQgMYNTLEEWYKFIEESiHVQADLIIYLRTSPEVAYERIRQRARSEESCVPLK 178
Cdd:cd01673  79 QGVILERSIFSDRVFAEANLKEGGIMKT-EYDLYNELFDNLIPE-LLPPDLVIYLDASPETCLKRIKKRGRPEEQGIPLD 156
                       170       180       190
                ....*....|....*....|....*....|....*..
1OE0_D      179 YLQELHELHEDWLIHQRRpQSCKVLVLDAD-LNLENI 214
Cdd:cd01673 157 YLEDLHEAYEKWFLPQMY-EKAPVLIIDANeADIEYN 192
dNK pfam01712
Deoxynucleoside kinase; This family consists of various deoxynucleoside kinases cytidine EC:2. ...
25-208 2.52e-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: 172.89  E-value: 2.52e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OE0_D         25 IEGNIGSGKTTYLNHFEKYkNDICLLTEPVEKWRNvngvNLLELMYKDPKKWAMPFQSYVTLTMLQSHTAPTNKK-LKIM 103
Cdd:pfam01712   3 IEGNIGAGKSTLTKILSKR-LGFKVFEEPVDRWTN----PYLDKFYKDPSRWSFALQTYFLNSRFKQQLEAFFTGqVVIL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OE0_D        104 ERSIFSARYCFVENMRRNGSLEQGMYNTLEEWYKFIEESIHvQADLIIYLRTSPEVAYERIRQRARSEESCVPLKYLQEL 183
Cdd:pfam01712  78 ERSIYSDRYIFAKMLYDKGTMSDEEYKTYKDLYDNMLLEFP-KPDLIIYLKTSPETCLERIKKRGRTEEQNISLDYLERL 156
                         170       180
                  ....*....|....*....|....*
1OE0_D        184 HELHEDWLIHQrrpQSCKVLVLDAD 208
Cdd:pfam01712 157 HEKYEAWLKKL---NLSPVLVIDGD 178
Dck COG1428
Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];
25-208 1.08e-38

Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];


Pssm-ID: 441037 [Multi-domain]  Cd Length: 205  Bit Score: 132.99  E-value: 1.08e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OE0_D       25 IEGNIGSGKTTYLNHFEKYKNDICLLtEPVEkwRNvngvNLLELMYKDPKKWAMPFQSYVTLTMLQSHT-APTNKKLKIM 103
Cdd:COG1428   8 VEGNIGAGKTTLARLLAEHLGAELLL-EPVE--DN----PFLEDFYEDPKRWAFPLQLFFLLSRFKQLKdLRQFGGNVVS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OE0_D      104 ERSIFSARYcFVENMRRNGSLEQGMYNTLEEWYKFIEESIhVQADLIIYLRTSPEVAYERIRQRARSEESCVPLKYLQEL 183
Cdd:COG1428  81 DRSIYKDAI-FAKLLHEMGTLSDREFDLYRQLFDNLTEDL-PKPDLVIYLQASVDTLLERIKKRGRDYEQNIDLDYLERL 158
                       170       180
                ....*....|....*....|....*
1OE0_D      184 HELHEDWLIHQRRpqsCKVLVLDAD 208
Cdd:COG1428 159 NEAYEEWFEHYDA---SPVLIIDTD 180
PHA03132 PHA03132
thymidine kinase; Provisional
9-185 1.71e-10

thymidine kinase; Provisional


Pssm-ID: 222997 [Multi-domain]  Cd Length: 580  Bit Score: 60.16  E-value: 1.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OE0_D         9 RKGTKYAEGTQPFTVLIEGNIGSGKTTYLNHF-EKYKNDICLLTEPVEKWRNVNGvNLLELMYKDPKKW----------- 76
Cdd:PHA03132 246 PLLTEYVPYKPACFLFLEGVMGVGKTTLLNHMrGILGDNVLVFPEPMRYWTEVYS-NCLKEIYKLVKPGkhgktstsakl 324
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OE0_D        77 -------AMPFQSYVTLT-MLQSHTAPTNKKLK-----IMERSIFSARYCFVENMRRNGSLEQGMYNTLeeWYKFieeSI 143
Cdd:PHA03132 325 lacqmkfATPFRALATRTrRLVQPESVRRPVAPldnwvLFDRHLLSATVVFPLMHLRNGMLSFSHFIQL--LSTF---RA 399
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
1OE0_D       144 HVqADLIIYLRTSPEVAYERIRQRARSEESCVPLKYLQELHE 185
Cdd:PHA03132 400 HE-GDVIVLLKLNSEENLRRVKKRGRKEEKGINLTYLKELNW 440
DTMP_kinase TIGR00041
dTMP kinase; Function: phosphorylation of DTMP to form DTDP in both de novo and salvage ...
23-214 4.38e-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: 4.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OE0_D         23 VLIEGNIGSGKTTYLN----HFEKYKNDICLLTEP-----VEKWRNVNGVNLLELMykDPKKWAMPFQSYVTLtmlqsHT 93
Cdd:TIGR00041   6 IVIEGIDGAGKTTQANllkkLLQENGYDVLFTREPggtpiGEKIRELLLNENDEPL--TDKAEALLFAADRHE-----HL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OE0_D         94 ------APTNKKLKIMERSIFSarycfvenmrrnGSLEQGMYNTL-EEWYKFIEESI-HVQADLIIYLRTSPEVAYERIr 165
Cdd:TIGR00041  79 edkikpALAEGKLVISDRYVFS------------SIAYQGGARGIdEDLVLELNEDAlGDMPDLTIYLDIDPEVALERL- 145
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
1OE0_D        166 qRARSEESCVPLKYLQELHELHEDWLIHQRRPqsCKVLVLDADLNLENI 214
Cdd:TIGR00041 146 -RKRGELDREEFEKLDFFEKVRQRYLELADKE--KSIHVIDATNSVEEV 191
 
Name Accession Description Interval E-value
dNK cd01673
Deoxyribonucleoside kinase (dNK) catalyzes the phosphorylation of deoxyribonucleosides to ...
23-214 9.89e-64

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: 196.68  E-value: 9.89e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OE0_D       23 VLIEGNIGSGKTTYLNHFEKyKNDICLLTEPVEkwRNVNGVNLLELMYKDPKKWAMPFQSYVTLTMLQSHTAP----TNK 98
Cdd:cd01673   2 IVVEGNIGAGKSTLAKELAE-HLGYEVVPEPVE--PDVEGNPFLEKFYEDPKRWAFPFQLYFLLSRLKQYKDAlehlSTG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OE0_D       99 KLKIMERSIFSARYCFVENMRRNGSLEQgMYNTLEEWYKFIEESiHVQADLIIYLRTSPEVAYERIRQRARSEESCVPLK 178
Cdd:cd01673  79 QGVILERSIFSDRVFAEANLKEGGIMKT-EYDLYNELFDNLIPE-LLPPDLVIYLDASPETCLKRIKKRGRPEEQGIPLD 156
                       170       180       190
                ....*....|....*....|....*....|....*..
1OE0_D      179 YLQELHELHEDWLIHQRRpQSCKVLVLDAD-LNLENI 214
Cdd:cd01673 157 YLEDLHEAYEKWFLPQMY-EKAPVLIIDANeADIEYN 192
dNK pfam01712
Deoxynucleoside kinase; This family consists of various deoxynucleoside kinases cytidine EC:2. ...
25-208 2.52e-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: 172.89  E-value: 2.52e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OE0_D         25 IEGNIGSGKTTYLNHFEKYkNDICLLTEPVEKWRNvngvNLLELMYKDPKKWAMPFQSYVTLTMLQSHTAPTNKK-LKIM 103
Cdd:pfam01712   3 IEGNIGAGKSTLTKILSKR-LGFKVFEEPVDRWTN----PYLDKFYKDPSRWSFALQTYFLNSRFKQQLEAFFTGqVVIL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OE0_D        104 ERSIFSARYCFVENMRRNGSLEQGMYNTLEEWYKFIEESIHvQADLIIYLRTSPEVAYERIRQRARSEESCVPLKYLQEL 183
Cdd:pfam01712  78 ERSIYSDRYIFAKMLYDKGTMSDEEYKTYKDLYDNMLLEFP-KPDLIIYLKTSPETCLERIKKRGRTEEQNISLDYLERL 156
                         170       180
                  ....*....|....*....|....*
1OE0_D        184 HELHEDWLIHQrrpQSCKVLVLDAD 208
Cdd:pfam01712 157 HEKYEAWLKKL---NLSPVLVIDGD 178
Dck COG1428
Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];
25-208 1.08e-38

Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];


Pssm-ID: 441037 [Multi-domain]  Cd Length: 205  Bit Score: 132.99  E-value: 1.08e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OE0_D       25 IEGNIGSGKTTYLNHFEKYKNDICLLtEPVEkwRNvngvNLLELMYKDPKKWAMPFQSYVTLTMLQSHT-APTNKKLKIM 103
Cdd:COG1428   8 VEGNIGAGKTTLARLLAEHLGAELLL-EPVE--DN----PFLEDFYEDPKRWAFPLQLFFLLSRFKQLKdLRQFGGNVVS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OE0_D      104 ERSIFSARYcFVENMRRNGSLEQGMYNTLEEWYKFIEESIhVQADLIIYLRTSPEVAYERIRQRARSEESCVPLKYLQEL 183
Cdd:COG1428  81 DRSIYKDAI-FAKLLHEMGTLSDREFDLYRQLFDNLTEDL-PKPDLVIYLQASVDTLLERIKKRGRDYEQNIDLDYLERL 158
                       170       180
                ....*....|....*....|....*
1OE0_D      184 HELHEDWLIHQRRpqsCKVLVLDAD 208
Cdd:COG1428 159 NEAYEEWFEHYDA---SPVLIIDTD 180
NDUO42 cd02030
NADH:Ubiquinone oxioreductase, 42 kDa (NDUO42) is a family of proteins that are highly similar ...
25-227 1.74e-11

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: 61.60  E-value: 1.74e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OE0_D       25 IEGNIGSGKTT--------------------YLNHFEKYKNDIclltePVEKWRNVNgvnlLELMYKDPKKW---AMPFQ 81
Cdd:cd02030   4 VDGNIASGKGKlakelaeklgmkyfpeagihYLDSTTGDGKPL-----DPAFNGNCS----LEKFYDDPKSNdgnSYRLQ 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OE0_D       82 SYV-TLTMLQ-----SHTAPTNKKLkIMERSIFSaRYCFVENMRRNGSLEQGMYNTleewYKFI-EESI--HVQADLIIY 152
Cdd:cd02030  75 SWMySSRLLQysdalEHLLSTGQGV-VLERSPFS-DFVFLEAMYKQGYIRKQCVDH----YNEVkGNTIpeLLPPHLVIY 148
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1OE0_D      153 LRTSPEVAYERIRQRARSEESCVPLKYLQELHELHEDWLIHQRRpQSCKVLVLDAdlnlenigTEYQRSESSIFD 227
Cdd:cd02030 149 LDVPVPEVQKRIKKRGDPHEMKVTSAYLQDIENAYKKTFLPEIS-EHSEVLQYDW--------TEAGDTEKVVED 214
PHA03132 PHA03132
thymidine kinase; Provisional
9-185 1.71e-10

thymidine kinase; Provisional


Pssm-ID: 222997 [Multi-domain]  Cd Length: 580  Bit Score: 60.16  E-value: 1.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OE0_D         9 RKGTKYAEGTQPFTVLIEGNIGSGKTTYLNHF-EKYKNDICLLTEPVEKWRNVNGvNLLELMYKDPKKW----------- 76
Cdd:PHA03132 246 PLLTEYVPYKPACFLFLEGVMGVGKTTLLNHMrGILGDNVLVFPEPMRYWTEVYS-NCLKEIYKLVKPGkhgktstsakl 324
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OE0_D        77 -------AMPFQSYVTLT-MLQSHTAPTNKKLK-----IMERSIFSARYCFVENMRRNGSLEQGMYNTLeeWYKFieeSI 143
Cdd:PHA03132 325 lacqmkfATPFRALATRTrRLVQPESVRRPVAPldnwvLFDRHLLSATVVFPLMHLRNGMLSFSHFIQL--LSTF---RA 399
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
1OE0_D       144 HVqADLIIYLRTSPEVAYERIRQRARSEESCVPLKYLQELHE 185
Cdd:PHA03132 400 HE-GDVIVLLKLNSEENLRRVKKRGRKEEKGINLTYLKELNW 440
Tmk COG0125
Thymidylate kinase [Nucleotide transport and metabolism]; Thymidylate kinase is part of the ...
146-214 8.53e-05

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: 42.07  E-value: 8.53e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1OE0_D      146 QADLIIYLRTSPEVAYERIRQRARSEEscvplKYLQELHELHE------DWLIhQRRPQSCKvlVLDADLNLENI 214
Cdd:COG0125 127 KPDLTILLDVPPEVALARARARGGELD-----RFESEDLEFHErvregyLELA-AKEPERIV--VIDASQSIEEV 193
DTMP_kinase TIGR00041
dTMP kinase; Function: phosphorylation of DTMP to form DTDP in both de novo and salvage ...
23-214 4.38e-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: 4.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OE0_D         23 VLIEGNIGSGKTTYLN----HFEKYKNDICLLTEP-----VEKWRNVNGVNLLELMykDPKKWAMPFQSYVTLtmlqsHT 93
Cdd:TIGR00041   6 IVIEGIDGAGKTTQANllkkLLQENGYDVLFTREPggtpiGEKIRELLLNENDEPL--TDKAEALLFAADRHE-----HL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OE0_D         94 ------APTNKKLKIMERSIFSarycfvenmrrnGSLEQGMYNTL-EEWYKFIEESI-HVQADLIIYLRTSPEVAYERIr 165
Cdd:TIGR00041  79 edkikpALAEGKLVISDRYVFS------------SIAYQGGARGIdEDLVLELNEDAlGDMPDLTIYLDIDPEVALERL- 145
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
1OE0_D        166 qRARSEESCVPLKYLQELHELHEDWLIHQRRPqsCKVLVLDADLNLENI 214
Cdd:TIGR00041 146 -RKRGELDREEFEKLDFFEKVRQRYLELADKE--KSIHVIDATNSVEEV 191
TMPK cd01672
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the ...
25-214 6.41e-04

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: 39.56  E-value: 6.41e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OE0_D       25 IEGNIGSGKTTYLN----HFEKYKNDICLLTEPvekwrnvNGVNL---LELMYKDPKKWAMpfqSYVTLTMLQS-----H 92
Cdd:cd01672   5 FEGIDGAGKTTLIEllaeRLEARGYEVVLTREP-------GGTPIgeaIRELLLDPEDEKM---DPRAELLLFAadraqH 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OE0_D       93 ------TAPTNKKLKIMERSIFSAR-YcfvenmrrngsleQGM-YNTLEEWYKFIEESIH--VQADLIIYLRTSPEVAYE 162
Cdd:cd01672  75 veevikPALARGKIVLSDRFVDSSLaY-------------QGAgRGLGEALIEALNDLATggLKPDLTILLDIDPEVGLA 141
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
1OE0_D      163 RIRQR-ARSEESCVPLKYLQELHELHEDwlIHQRRPQscKVLVLDADLNLENI 214
Cdd:cd01672 142 RIEARgRDDRDEQEGLEFHERVREGYLE--LAAQEPE--RIIVIDASQPLEEV 190
Thymidylate_kin pfam02223
Thymidylate kinase;
25-214 2.04e-03

Thymidylate kinase;


Pssm-ID: 396690  Cd Length: 184  Bit Score: 37.67  E-value: 2.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OE0_D         25 IEGNIGSGKTTYLNHF-EKYKN---DICLLTEP-----VEKWRNvngvnLLELMYK-DPKKWAMPFQSYVTLTMLQSHtA 94
Cdd:pfam02223   1 IEGLDGAGKTTQAELLkERLKEqgiKVVFTREPggtpiGEKIRE-----LLLRNEElSPLTEALLFAADRIQHLEQKI-K 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OE0_D         95 PTNKKLK--IMERSIFSarycfvenmrrnGSLEQGMYNTLEEWYKFIEESIHVQADLIIYLRTSPEVAYERIRQRARSEE 172
Cdd:pfam02223  75 PALKQGKtvIVDRYLFS------------GIAYQGAKGGDLDLVLSLNPDVPGKPDLTFLLDVDPEVALKRLRRRGELEK 142
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
1OE0_D        173 SCV-PLKYLQELHELHEDwLIHQRrpqsCKVLVLDADLNLENI 214
Cdd:pfam02223 143 TEFeQLDFLRKVRERYLE-LAKFD----ERIKIIDASLSIEEV 180
PHA03138 PHA03138
thymidine kinase; Provisional
23-62 2.12e-03

thymidine kinase; Provisional


Pssm-ID: 165410  Cd Length: 340  Bit Score: 38.42  E-value: 2.12e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
1OE0_D        23 VLIEGNIGSGKTT----YLNHFEKYKNDICLLTEPVEKWRNVNG 62
Cdd:PHA03138  15 IYLDGAFGIGKTTaaeaFLHGFAINPNRIFFIGEPLMYWRNLAG 58
NK cd02019
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ...
22-52 3.10e-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: 35.39  E-value: 3.10e-03
                        10        20        30
                ....*....|....*....|....*....|...
1OE0_D       22 TVLIEGNIGSGKTTYLNHFEK--YKNDICLLTE 52
Cdd:cd02019   1 IIAITGGSGSGKSTVAKKLAEqlGGRSVVVLDE 33
Fap7 COG1936
Broad-specificity NMP kinase [Nucleotide transport and metabolism];
144-172 4.85e-03

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


Pssm-ID: 441539 [Multi-domain]  Cd Length: 173  Bit Score: 36.72  E-value: 4.85e-03
                        10        20
                ....*....|....*....|....*....
1OE0_D      144 HVQADLIIYLRTSPEVAYERIRQRARSEE 172
Cdd:COG1936  79 LVDVDRVIVLRCNPEVLEERLEERGYSEE 107
 
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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