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Conserved domains on  [gi|672050160|ref|XP_008761279|]
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deoxyguanosine kinase, mitochondrial isoform X4 [Rattus norvegicus]

Protein Classification

deoxynucleoside kinase( domain architecture ID 10484182)

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

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
dNK pfam01712
Deoxynucleoside kinase; This family consists of various deoxynucleoside kinases cytidine EC:2. ...
41-270 2.05e-76

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: 232.21  E-value: 2.05e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672050160   41 LCIEGNIAVGKSTFVKLLTKtHPEWQVATEPIATWQNvqaagtqkdstsrrlgNLLDMMYQEPARWSYTFQTLSFMSRLK 120
Cdd:pfam01712   1 ISIEGNIGAGKSTLTKILSK-RLGFKVFEEPVDRWTN----------------PYLDKFYKDPSRWSFALQTYFLNSRFK 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672050160  121 VQLEPTpgrllqADTSVRVFERSVYSDRYIFAKNLFENGSLSDVEWHIYQDWHSFLLQEFEDRlllHGFIYLQASPQVCM 200
Cdd:pfam01712  64 QQLEAF------FTGQVVILERSIYSDRYIFAKMLYDKGTMSDEEYKTYKDLYDNMLLEFPKP---DLIIYLKTSPETCL 134
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672050160  201 ERLCQRGREEEKGIELAYLKQLHGQHEDWFINkttklhfeaLRHVPVLVLNISE-DFSENAAKQEELMGQV 270
Cdd:pfam01712 135 ERIKKRGRTEEQNISLDYLERLHEKYEAWLKK---------LNLSPVLVIDGDElDFVFFEEDREDVMNEV 196
 
Name Accession Description Interval E-value
dNK pfam01712
Deoxynucleoside kinase; This family consists of various deoxynucleoside kinases cytidine EC:2. ...
41-270 2.05e-76

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: 232.21  E-value: 2.05e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672050160   41 LCIEGNIAVGKSTFVKLLTKtHPEWQVATEPIATWQNvqaagtqkdstsrrlgNLLDMMYQEPARWSYTFQTLSFMSRLK 120
Cdd:pfam01712   1 ISIEGNIGAGKSTLTKILSK-RLGFKVFEEPVDRWTN----------------PYLDKFYKDPSRWSFALQTYFLNSRFK 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672050160  121 VQLEPTpgrllqADTSVRVFERSVYSDRYIFAKNLFENGSLSDVEWHIYQDWHSFLLQEFEDRlllHGFIYLQASPQVCM 200
Cdd:pfam01712  64 QQLEAF------FTGQVVILERSIYSDRYIFAKMLYDKGTMSDEEYKTYKDLYDNMLLEFPKP---DLIIYLKTSPETCL 134
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672050160  201 ERLCQRGREEEKGIELAYLKQLHGQHEDWFINkttklhfeaLRHVPVLVLNISE-DFSENAAKQEELMGQV 270
Cdd:pfam01712 135 ERIKKRGRTEEQNISLDYLERLHEKYEAWLKK---------LNLSPVLVIDGDElDFVFFEEDREDVMNEV 196
dNK cd01673
Deoxyribonucleoside kinase (dNK) catalyzes the phosphorylation of deoxyribonucleosides to ...
40-259 2.51e-66

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: 205.92  E-value: 2.51e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672050160  40 RLCIEGNIAVGKSTFVKLLTKtHPEWQVATEPIATWQNVqaagtqkdstsrrlGNLLDMMYQEPARWSYTFQTLSFMSRL 119
Cdd:cd01673    1 VIVVEGNIGAGKSTLAKELAE-HLGYEVVPEPVEPDVEG--------------NPFLEKFYEDPKRWAFPFQLYFLLSRL 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672050160 120 KVQLEPTPGrllQADTSVRVFERSVYSDRYIFAKNLFENGsLSDVEWHIYQDWHSFLLQEFedrLLLHGFIYLQASPQVC 199
Cdd:cd01673   66 KQYKDALEH---LSTGQGVILERSIFSDRVFAEANLKEGG-IMKTEYDLYNELFDNLIPEL---LPPDLVIYLDASPETC 138
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672050160 200 MERLCQRGREEEKGIELAYLKQLHGQHEDWFINKTTKlhfealrHVPVLVLNISE-DFSEN 259
Cdd:cd01673  139 LKRIKKRGRPEEQGIPLDYLEDLHEAYEKWFLPQMYE-------KAPVLIIDANEaDIEYN 192
Dck COG1428
Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];
38-273 1.49e-51

Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];


Pssm-ID: 441037 [Multi-domain]  Cd Length: 205  Bit Score: 168.81  E-value: 1.49e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672050160  38 PRRLCIEGNIAVGKSTFVKLLTKtHPEWQVATEPIAtwQNvqaagtqkdstsrrlgNLLDMMYQEPARWSYTFQtLSF-M 116
Cdd:COG1428    3 PRYIAVEGNIGAGKTTLARLLAE-HLGAELLLEPVE--DN----------------PFLEDFYEDPKRWAFPLQ-LFFlL 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672050160 117 SRLKvQLEptpgRLLQADTSVrVFERSVYSDRyIFAKNLFENGSLSDVEWHIYQDWHSFLLQEFE--DrlllhGFIYLQA 194
Cdd:COG1428   63 SRFK-QLK----DLRQFGGNV-VSDRSIYKDA-IFAKLLHEMGTLSDREFDLYRQLFDNLTEDLPkpD-----LVIYLQA 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672050160 195 SPQVCMERLCQRGREEEKGIELAYLKQLHGQHEDWFINKTtklhfealrHVPVLVLNISE-DFSENAAKQEELMGQVSRA 273
Cdd:COG1428  131 SVDTLLERIKKRGRDYEQNIDLDYLERLNEAYEEWFEHYD---------ASPVLIIDTDElDFVNNPEDLELLLEQIEEK 201
PHA03132 PHA03132
thymidine kinase; Provisional
44-224 4.12e-09

thymidine kinase; Provisional


Pssm-ID: 222997 [Multi-domain]  Cd Length: 580  Bit Score: 57.47  E-value: 4.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672050160  44 EGNIAVGKSTFVKLLTKTHPEwQVAT--EPIATWQNVqaagtqkdstsrrLGNLLDMMYQ-----EPARWSYTFQTLS-- 114
Cdd:PHA03132 263 EGVMGVGKTTLLNHMRGILGD-NVLVfpEPMRYWTEV-------------YSNCLKEIYKlvkpgKHGKTSTSAKLLAcq 328
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672050160 115 --FMSRLKVQLEPTpGRLLQADTSVR---------VFERSVYSDRYIFAKNLFENGSLSDVewHIYQDWHSFLLQEFEDR 183
Cdd:PHA03132 329 mkFATPFRALATRT-RRLVQPESVRRpvapldnwvLFDRHLLSATVVFPLMHLRNGMLSFS--HFIQLLSTFRAHEGDVI 405
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 672050160 184 LLLhgfiylQASPQVCMERLCQRGREEEKGIELAYLKQLHG 224
Cdd:PHA03132 406 VLL------KLNSEENLRRVKKRGRKEEKGINLTYLKELNW 440
 
Name Accession Description Interval E-value
dNK pfam01712
Deoxynucleoside kinase; This family consists of various deoxynucleoside kinases cytidine EC:2. ...
41-270 2.05e-76

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: 232.21  E-value: 2.05e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672050160   41 LCIEGNIAVGKSTFVKLLTKtHPEWQVATEPIATWQNvqaagtqkdstsrrlgNLLDMMYQEPARWSYTFQTLSFMSRLK 120
Cdd:pfam01712   1 ISIEGNIGAGKSTLTKILSK-RLGFKVFEEPVDRWTN----------------PYLDKFYKDPSRWSFALQTYFLNSRFK 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672050160  121 VQLEPTpgrllqADTSVRVFERSVYSDRYIFAKNLFENGSLSDVEWHIYQDWHSFLLQEFEDRlllHGFIYLQASPQVCM 200
Cdd:pfam01712  64 QQLEAF------FTGQVVILERSIYSDRYIFAKMLYDKGTMSDEEYKTYKDLYDNMLLEFPKP---DLIIYLKTSPETCL 134
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672050160  201 ERLCQRGREEEKGIELAYLKQLHGQHEDWFINkttklhfeaLRHVPVLVLNISE-DFSENAAKQEELMGQV 270
Cdd:pfam01712 135 ERIKKRGRTEEQNISLDYLERLHEKYEAWLKK---------LNLSPVLVIDGDElDFVFFEEDREDVMNEV 196
dNK cd01673
Deoxyribonucleoside kinase (dNK) catalyzes the phosphorylation of deoxyribonucleosides to ...
40-259 2.51e-66

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: 205.92  E-value: 2.51e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672050160  40 RLCIEGNIAVGKSTFVKLLTKtHPEWQVATEPIATWQNVqaagtqkdstsrrlGNLLDMMYQEPARWSYTFQTLSFMSRL 119
Cdd:cd01673    1 VIVVEGNIGAGKSTLAKELAE-HLGYEVVPEPVEPDVEG--------------NPFLEKFYEDPKRWAFPFQLYFLLSRL 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672050160 120 KVQLEPTPGrllQADTSVRVFERSVYSDRYIFAKNLFENGsLSDVEWHIYQDWHSFLLQEFedrLLLHGFIYLQASPQVC 199
Cdd:cd01673   66 KQYKDALEH---LSTGQGVILERSIFSDRVFAEANLKEGG-IMKTEYDLYNELFDNLIPEL---LPPDLVIYLDASPETC 138
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672050160 200 MERLCQRGREEEKGIELAYLKQLHGQHEDWFINKTTKlhfealrHVPVLVLNISE-DFSEN 259
Cdd:cd01673  139 LKRIKKRGRPEEQGIPLDYLEDLHEAYEKWFLPQMYE-------KAPVLIIDANEaDIEYN 192
Dck COG1428
Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];
38-273 1.49e-51

Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];


Pssm-ID: 441037 [Multi-domain]  Cd Length: 205  Bit Score: 168.81  E-value: 1.49e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672050160  38 PRRLCIEGNIAVGKSTFVKLLTKtHPEWQVATEPIAtwQNvqaagtqkdstsrrlgNLLDMMYQEPARWSYTFQtLSF-M 116
Cdd:COG1428    3 PRYIAVEGNIGAGKTTLARLLAE-HLGAELLLEPVE--DN----------------PFLEDFYEDPKRWAFPLQ-LFFlL 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672050160 117 SRLKvQLEptpgRLLQADTSVrVFERSVYSDRyIFAKNLFENGSLSDVEWHIYQDWHSFLLQEFE--DrlllhGFIYLQA 194
Cdd:COG1428   63 SRFK-QLK----DLRQFGGNV-VSDRSIYKDA-IFAKLLHEMGTLSDREFDLYRQLFDNLTEDLPkpD-----LVIYLQA 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672050160 195 SPQVCMERLCQRGREEEKGIELAYLKQLHGQHEDWFINKTtklhfealrHVPVLVLNISE-DFSENAAKQEELMGQVSRA 273
Cdd:COG1428  131 SVDTLLERIKKRGRDYEQNIDLDYLERLNEAYEEWFEHYD---------ASPVLIIDTDElDFVNNPEDLELLLEQIEEK 201
NDUO42 cd02030
NADH:Ubiquinone oxioreductase, 42 kDa (NDUO42) is a family of proteins that are highly similar ...
41-231 4.71e-13

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: 67.00  E-value: 4.71e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672050160  41 LCIEGNIAVGKSTFVKLLT-----KTHPEWQVaTEPIATwqnvqaAGTQKDSTSRRLGNL-LDMMYQEPARW---SYTFQ 111
Cdd:cd02030    2 ITVDGNIASGKGKLAKELAeklgmKYFPEAGI-HYLDST------TGDGKPLDPAFNGNCsLEKFYDDPKSNdgnSYRLQ 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672050160 112 TLSFMSRLkVQLEPTPGRLLQADTSVrVFERSVYSDrYIFAKNLFENGSLSdvewHIYQDWHSFLLQEFEDRLLL-HGFI 190
Cdd:cd02030   75 SWMYSSRL-LQYSDALEHLLSTGQGV-VLERSPFSD-FVFLEAMYKQGYIR----KQCVDHYNEVKGNTIPELLPpHLVI 147
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 672050160 191 YLQASPQVCMERLCQRGREEEKGIELAYLKQLHGQHEDWFI 231
Cdd:cd02030  148 YLDVPVPEVQKRIKKRGDPHEMKVTSAYLQDIENAYKKTFL 188
PHA03132 PHA03132
thymidine kinase; Provisional
44-224 4.12e-09

thymidine kinase; Provisional


Pssm-ID: 222997 [Multi-domain]  Cd Length: 580  Bit Score: 57.47  E-value: 4.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672050160  44 EGNIAVGKSTFVKLLTKTHPEwQVAT--EPIATWQNVqaagtqkdstsrrLGNLLDMMYQ-----EPARWSYTFQTLS-- 114
Cdd:PHA03132 263 EGVMGVGKTTLLNHMRGILGD-NVLVfpEPMRYWTEV-------------YSNCLKEIYKlvkpgKHGKTSTSAKLLAcq 328
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672050160 115 --FMSRLKVQLEPTpGRLLQADTSVR---------VFERSVYSDRYIFAKNLFENGSLSDVewHIYQDWHSFLLQEFEDR 183
Cdd:PHA03132 329 mkFATPFRALATRT-RRLVQPESVRRpvapldnwvLFDRHLLSATVVFPLMHLRNGMLSFS--HFIQLLSTFRAHEGDVI 405
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 672050160 184 LLLhgfiylQASPQVCMERLCQRGREEEKGIELAYLKQLHG 224
Cdd:PHA03132 406 VLL------KLNSEENLRRVKKRGRKEEKGINLTYLKELNW 440
AAA_18 pfam13238
AAA domain;
147-215 4.40e-05

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 42.42  E-value: 4.40e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 672050160  147 DRYIFAKNLFENGSLSDVEWHIYQDWHsfLLQEFEDRLLLHGFIYLQASPQVCMERLCQRGREEEKGIE 215
Cdd:pfam13238  54 DKLDRLLDLLEENAALEEGGNLIIDGH--LAELEPERAKDLVGIVLRASPEELLERLEKRGYEEAKIKE 120
 
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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