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Protein Overview: gi|38492611, gi|...

General Information:
Name(s) found: gi|38492611 [NCBI NR]
gi|38492610 [NCBI NR]
gi|38492609 [NCBI NR]
gi|38492608 [NCBI NR]
gi|225733913 [NCBI NR]
gi|225733912 [NCBI NR]
gi|186972898 [NCBI NR]
gi|186972897 [NCBI NR]
gi|186972896 [NCBI NR]
gi|186972895 [NCBI NR]
gi|186972848 [NCBI NR]
gi|186972847 [NCBI NR]
gi|186972846 [NCBI NR]
gi|186972845 [NCBI NR]
gi|186972844 [NCBI NR]
gi|186972843 [NCBI NR]
gi|186972842 [NCBI NR]
gi|186972841 [NCBI NR]
gi|186972840 [NCBI NR]
gi|186972839 [NCBI NR]
gi|186972838 [NCBI NR]
gi|186972837 [NCBI NR]
gi|186972836 [NCBI NR]
gi|186972835 [NCBI NR]
gi|186972834 [NCBI NR]
gi|186972833 [NCBI NR]
gi|186972832 [NCBI NR]
gi|186972831 [NCBI NR]
gi|186972830 [NCBI NR]
gi|186972829 [NCBI NR]
gi|186972828 [NCBI NR]
gi|186972827 [NCBI NR]
gi|186972826 [NCBI NR]
gi|186972825 [NCBI NR]
gi|186972734 [NCBI NR]
gi|186972733 [NCBI NR]
gi|186972732 [NCBI NR]
gi|186972731 [NCBI NR]
gi|17942829 [NCBI NR]
gi|17942828 [NCBI NR]
Description(s) found:
Found 47 descriptions.
SHOW ALL
  • gi|38492611|pdb|1OE0|D Chain D, Crystal Structure Of Drosophila Deoxyribonucleoside Kinase In Complex With Dttp [NCBI NR]
  • gi|38492610|pdb|1OE0|C Chain C, Crystal Structure Of Drosophila Deoxyribonucleoside Kinase In Complex With Dttp [NCBI NR]
  • gi|38492609|pdb|1OE0|B Chain B, Crystal Structure Of Drosophila Deoxyribonucleoside Kinase In Complex With Dttp [NCBI NR]
  • gi|38492608|pdb|1OE0|A Chain A, Crystal Structure Of Drosophila Deoxyribonucleoside Kinase In Complex With Dttp [NCBI NR]
  • gi|225733913|pdb|2VPP|B Chain B, Drosophila Melanogaster Deoxyribonucleoside Kinase Successfully Activates Gemcitabine In Transduced Cancer Cell Lines [NCBI NR]
  • gi|225733912|pdb|2VPP|A Chain A, Drosophila Melanogaster Deoxyribonucleoside Kinase Successfully Activates Gemcitabine In Transduced Cancer Cell Lines [NCBI NR]
  • gi|186972898|pdb|2VQS|D Chain D, Structural Studies Of Nucleoside Analog And Feedback Inhibitor Binding To Drosophila Melanogaster Multisubstrate Deoxyribonucleoside Kinase [NCBI NR]
  • gi|186972897|pdb|2VQS|C Chain C, Structural Studies Of Nucleoside Analog And Feedback Inhibitor Binding To Drosophila Melanogaster Multisubstrate Deoxyribonucleoside Kinase [NCBI NR]
  • gi|186972896|pdb|2VQS|B Chain B, Structural Studies Of Nucleoside Analog And Feedback Inhibitor Binding To Drosophila Melanogaster Multisubstrate Deoxyribonucleoside Kinase [NCBI NR]
  • gi|186972895|pdb|2VQS|A Chain A, Structural Studies Of Nucleoside Analog And Feedback Inhibitor Binding To Drosophila Melanogaster Multisubstrate Deoxyribonucleoside Kinase [NCBI NR]
  • gi|186972848|pdb|2VP9|H Chain H, Structural Studies Of Nucleoside Analog And Feedback Inhibitor Binding To Drosophila Melanogaster Multisubstrate Deoxyribonucleoside Kinase [NCBI NR]
  • gi|186972847|pdb|2VP9|G Chain G, Structural Studies Of Nucleoside Analog And Feedback Inhibitor Binding To Drosophila Melanogaster Multisubstrate Deoxyribonucleoside Kinase [NCBI NR]
  • gi|186972846|pdb|2VP9|F Chain F, Structural Studies Of Nucleoside Analog And Feedback Inhibitor Binding To Drosophila Melanogaster Multisubstrate Deoxyribonucleoside Kinase [NCBI NR]
  • gi|186972845|pdb|2VP9|E Chain E, Structural Studies Of Nucleoside Analog And Feedback Inhibitor Binding To Drosophila Melanogaster Multisubstrate Deoxyribonucleoside Kinase [NCBI NR]
  • gi|186972844|pdb|2VP9|D Chain D, Structural Studies Of Nucleoside Analog And Feedback Inhibitor Binding To Drosophila Melanogaster Multisubstrate Deoxyribonucleoside Kinase [NCBI NR]
  • gi|186972843|pdb|2VP9|C Chain C, Structural Studies Of Nucleoside Analog And Feedback Inhibitor Binding To Drosophila Melanogaster Multisubstrate Deoxyribonucleoside Kinase [NCBI NR]
  • gi|186972842|pdb|2VP9|B Chain B, Structural Studies Of Nucleoside Analog And Feedback Inhibitor Binding To Drosophila Melanogaster Multisubstrate Deoxyribonucleoside Kinase [NCBI NR]
  • gi|186972841|pdb|2VP9|A Chain A, Structural Studies Of Nucleoside Analog And Feedback Inhibitor Binding To Drosophila Melanogaster Multisubstrate Deoxyribonucleoside Kinase [NCBI NR]
  • gi|186972840|pdb|2VP6|H Chain H, Structural Studies Of Nucleoside Analog And Feedback Inhibitor Binding To Drosophila Melanogaster Multisubstrate Deoxyribonucleoside Kinase [NCBI NR]
  • gi|186972839|pdb|2VP6|G Chain G, Structural Studies Of Nucleoside Analog And Feedback Inhibitor Binding To Drosophila Melanogaster Multisubstrate Deoxyribonucleoside Kinase [NCBI NR]
  • gi|186972838|pdb|2VP6|F Chain F, Structural Studies Of Nucleoside Analog And Feedback Inhibitor Binding To Drosophila Melanogaster Multisubstrate Deoxyribonucleoside Kinase [NCBI NR]
  • gi|186972837|pdb|2VP6|E Chain E, Structural Studies Of Nucleoside Analog And Feedback Inhibitor Binding To Drosophila Melanogaster Multisubstrate Deoxyribonucleoside Kinase [NCBI NR]
  • gi|186972836|pdb|2VP6|D Chain D, Structural Studies Of Nucleoside Analog And Feedback Inhibitor Binding To Drosophila Melanogaster Multisubstrate Deoxyribonucleoside Kinase [NCBI NR]
  • gi|186972835|pdb|2VP6|C Chain C, Structural Studies Of Nucleoside Analog And Feedback Inhibitor Binding To Drosophila Melanogaster Multisubstrate Deoxyribonucleoside Kinase [NCBI NR]
  • gi|186972834|pdb|2VP6|B Chain B, Structural Studies Of Nucleoside Analog And Feedback Inhibitor Binding To Drosophila Melanogaster Multisubstrate Deoxyribonucleoside Kinase [NCBI NR]
  • gi|186972833|pdb|2VP6|A Chain A, Structural Studies Of Nucleoside Analog And Feedback Inhibitor Binding To Drosophila Melanogaster Multisubstrate Deoxyribonucleoside Kinase [NCBI NR]
  • gi|186972832|pdb|2VP5|B Chain B, Structural Studies Of Nucleoside Analog And Feedback Inhibitor Binding To Drosophila Melanogaster Multisubstrate Deoxyribonucleoside Kinase [NCBI NR]
  • gi|186972831|pdb|2VP5|A Chain A, Structural Studies Of Nucleoside Analog And Feedback Inhibitor Binding To Drosophila Melanogaster Multisubstrate Deoxyribonucleoside Kinase [NCBI NR]
  • gi|186972830|pdb|2VP4|D Chain D, Structural Studies Of Nucleoside Analog And Feedback Inhibitor Binding To Drosophila Melanogaster Multisubstrate Deoxyribonucleoside Kinase [NCBI NR]
  • gi|186972829|pdb|2VP4|C Chain C, Structural Studies Of Nucleoside Analog And Feedback Inhibitor Binding To Drosophila Melanogaster Multisubstrate Deoxyribonucleoside Kinase [NCBI NR]
  • gi|186972828|pdb|2VP4|B Chain B, Structural Studies Of Nucleoside Analog And Feedback Inhibitor Binding To Drosophila Melanogaster Multisubstrate Deoxyribonucleoside Kinase [NCBI NR]
  • gi|186972827|pdb|2VP4|A Chain A, Structural Studies Of Nucleoside Analog And Feedback Inhibitor Binding To Drosophila Melanogaster Multisubstrate Deoxyribonucleoside Kinase [NCBI NR]
  • gi|186972826|pdb|2VP2|B Chain B, Structural Studies Of Nucleoside Analog And Feedback Inhibitor Binding To Drosophila Melanogaster Multisubstrate Deoxyribonucleoside Kinase [NCBI NR]
  • gi|186972825|pdb|2VP2|A Chain A, Structural Studies Of Nucleoside Analog And Feedback Inhibitor Binding To Drosophila Melanogaster Multisubstrate Deoxyribonucleoside Kinase [NCBI NR]
  • gi|186972734|pdb|2JJ8|D Chain D, Structural Studies Of Nucleoside Analog And Feedback Inhibitor Binding To Drosophila Melanogaster Multisubstrate Deoxyribonucleoside Kinase [NCBI NR]
  • gi|186972733|pdb|2JJ8|C Chain C, Structural Studies Of Nucleoside Analog And Feedback Inhibitor Binding To Drosophila Melanogaster Multisubstrate Deoxyribonucleoside Kinase [NCBI NR]
  • gi|186972732|pdb|2JJ8|B Chain B, Structural Studies Of Nucleoside Analog And Feedback Inhibitor Binding To Drosophila Melanogaster Multisubstrate Deoxyribonucleoside Kinase [NCBI NR]
  • gi|186972731|pdb|2JJ8|A Chain A, Structural Studies Of Nucleoside Analog And Feedback Inhibitor Binding To Drosophila Melanogaster Multisubstrate Deoxyribonucleoside Kinase [NCBI NR]
  • gi|17942829|pdb|1J90|B Chain B, Crystal Structure Of Drosophila Deoxyribonucleoside Kinase [NCBI NR]
  • gi|17942828|pdb|1J90|A Chain A, Crystal Structure Of Drosophila Deoxyribonucleoside Kinase [NCBI NR]
    • Organism: Drosophila melanogaster
    Length: 230 amino acids

    Gene Ontology:
    Cellular Component: NONE FOUND
    Biological Process: NONE FOUND
    Molecular Function: NONE FOUND


    Sequence:
    Sequence:
    [PDR BLAST]
    [ProtParam] 
          1          11         21         31         41         51         
      |          |          |          |          |          |          
    1 MAEAASCARK GTKYAEGTQP FTVLIEGNIG SGKTTYLNHF EKYKNDICLL TEPVEKWRNV  60
   61 NGVNLLELMY KDPKKWAMPF QSYVTLTMLQ SHTAPTNKKL KIMERSIFSA RYCFVENMRR 120
  121 NGSLEQGMYN TLEEWYKFIE ESIHVQADLI IYLRTSPEVA YERIRQRARS EESCVPLKYL 180
  181 QELHELHEDW LIHQRRPQSC KVLVLDADLN LENIGTEYQR SESSIFDAIS

    Protein Complex Data

    No complex found for this protein.

    Mass Spectrometry Data

    No mass spectrometry results found for this protein.

    Yeast Two-Hybrid Data

    The following interactions contain this protein:

    NOT SHOWING SINGLE HITS. [ Show Single Hits ]

    [View our yeast two-hybrid interpretation guidelines.]

    No yeast two-hybrid interactions found for this protein.

    Microscopy / Localization Data

    New Feature: Upload Your Own Microscopy Data

    No microscopy data found in the PDR for this protein.

    Protein Structure Data


    [What does the above image mean?]
    [View Top Sequence Alignments] [Show Ginzu Version Information]

    Domains predicted:

    #   Region(s) Method Confidence Match Description
    1 View Details [1..230] PSI-BLAST 43.0 Deoxyribonucleoside kinase

    Functions predicted (by domain):

    # Gene Ontology predictions
    1
    Term Confidence Notes
  • nucleobase, nucleoside, nucleotide kinase activity
    		•  3.66392587433723 bayes_pls_golite062009
  • nucleotide kinase activity
    		•  2.24094813695083 bayes_pls_golite062009
  • phosphotransferase activity, phosphate group as acceptor
    		•  1.96697952975573 bayes_pls_golite062009
  • ribonucleotide binding
    		•  1.53142082854758 bayes_pls_golite062009
  • purine nucleotide binding
    		•  1.52938239070386 bayes_pls_golite062009
  • purine ribonucleotide binding
    		•  1.52887308780164 bayes_pls_golite062009
  • nucleotide binding
    		•  1.52746968836881 bayes_pls_golite062009
  • binding
    		•  1.46714820387895 bayes_pls_golite062009
  • adenylate kinase activity
    		•  1.27088333982087 bayes_pls_golite062009
  • ATP binding
    		•  1.23942044024113 bayes_pls_golite062009
  • adenyl ribonucleotide binding
    		•  1.21044170258803 bayes_pls_golite062009
  • adenyl nucleotide binding
    		•  1.19481945569892 bayes_pls_golite062009
  • kinase activity
    		•  1.11120928120082 bayes_pls_golite062009
  • hydrogen ion transmembrane transporter activity
    		•  1.00388614309685 bayes_pls_golite062009
  • catalytic activity
    		•  1.00104173493322 bayes_pls_golite062009
  • transferase activity, transferring phosphorus-containing groups
    		•  0.908046791062776 bayes_pls_golite062009
  • hydrogen ion transporting ATP synthase activity, rotational mechanism
    		•  0.872487338145151 bayes_pls_golite062009
  • monovalent inorganic cation transmembrane transporter activity
    		•  0.854269100162193 bayes_pls_golite062009
  • CTP synthase activity
    		•  0.554689818807922 bayes_pls_golite062009
  • nucleic acid binding
    		•  0.503971340374059 bayes_pls_golite062009
  • inorganic cation transmembrane transporter activity
    		•  0.450562042301179 bayes_pls_golite062009
  • phosphotransferase activity, alcohol group as acceptor
    		•  0.421921195209539 bayes_pls_golite062009
  • hydrolase activity
    		•  0.420858111948277 bayes_pls_golite062009
  • protein binding
    		•  0.232442551591362 bayes_pls_golite062009
  • transferase activity
    		•  0.175269600441384 bayes_pls_golite062009
  • DNA binding
    		•  0.111331583742205 bayes_pls_golite062009
  • protein kinase activity
    		•  0.0646123847220056 bayes_pls_golite062009


    Reference: Drew K, et al. (2011) The proteome folding project: Proteome-scale prediction of structure and function. Genome Res. 2011 Sep 16


    Philius Transmembrane Prediction:

    Protein predicted to be: GLOBULAR (No transmembrane regions or signal peptide)
    Confidence of classification: 0.99

    Source: Reynolds et al. (2008)

    YRC Informatics Platform - Version 3.0
    Created and Maintained by: Michael Riffle