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Conserved domains on  [gi|157822271|ref|NP_001101296|]
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dolichol kinase [Rattus norvegicus]

Protein Classification

diacylglycerol/polyprenol kinase family protein( domain architecture ID 1903207)

diacylglycerol/polyprenol kinase family protein similar to mammalian dolichol kinase and plant phytol kinase

EC:  2.7.1.-
Gene Ontology:  GO:0016301|GO:0016310
PubMed:  2819898

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SEC59 super family cl46770
Dolichol kinase [Posttranslational modification, protein turnover, chaperones, Cell wall ...
331-522 1.54e-11

Dolichol kinase [Posttranslational modification, protein turnover, chaperones, Cell wall/membrane/envelope biogenesis];


The actual alignment was detected with superfamily member COG0170:

Pssm-ID: 439940  Cd Length: 190  Bit Score: 63.34  E-value: 1.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822271 331 PTITRKYFHfIVVATYIPGIIF---DRPLLYVAATVCLAVFIFLEYVRYFRIKPLghtLRSLLSLflDERDsgpLILTHI 407
Cdd:COG0170    5 KELSRKIIH-IGSGLVILLALYlfiGRWIALILLALLLVGYLIIELLRLRYPLIL---LSSILRE--VERK---PSLGTV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822271 408 YLLLGMSLPIWLIPRPCAqkgslggaralvpYAGVLAVGVGDTVASIFGSTMGEIRWP-GTKKTFEGTMTSIFAQIISVA 486
Cdd:COG0170   76 YFALGILILVLLFPPEIA-------------AAAILVLALGDGLAALVGKRFGKHKLPvGGGKSLEGSLAMFIVSFLILL 142
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 157822271 487 LILIFdsgvdLNYSYAWILGSISTvsLLEAYTTQID 522
Cdd:COG0170  143 LVLLL-----FSLLIALLIALVAT--LVEALSPKGD 171
 
Name Accession Description Interval E-value
SEC59 COG0170
Dolichol kinase [Posttranslational modification, protein turnover, chaperones, Cell wall ...
331-522 1.54e-11

Dolichol kinase [Posttranslational modification, protein turnover, chaperones, Cell wall/membrane/envelope biogenesis];


Pssm-ID: 439940  Cd Length: 190  Bit Score: 63.34  E-value: 1.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822271 331 PTITRKYFHfIVVATYIPGIIF---DRPLLYVAATVCLAVFIFLEYVRYFRIKPLghtLRSLLSLflDERDsgpLILTHI 407
Cdd:COG0170    5 KELSRKIIH-IGSGLVILLALYlfiGRWIALILLALLLVGYLIIELLRLRYPLIL---LSSILRE--VERK---PSLGTV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822271 408 YLLLGMSLPIWLIPRPCAqkgslggaralvpYAGVLAVGVGDTVASIFGSTMGEIRWP-GTKKTFEGTMTSIFAQIISVA 486
Cdd:COG0170   76 YFALGILILVLLFPPEIA-------------AAAILVLALGDGLAALVGKRFGKHKLPvGGGKSLEGSLAMFIVSFLILL 142
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 157822271 487 LILIFdsgvdLNYSYAWILGSISTvsLLEAYTTQID 522
Cdd:COG0170  143 LVLLL-----FSLLIALLIALVAT--LVEALSPKGD 171
 
Name Accession Description Interval E-value
SEC59 COG0170
Dolichol kinase [Posttranslational modification, protein turnover, chaperones, Cell wall ...
331-522 1.54e-11

Dolichol kinase [Posttranslational modification, protein turnover, chaperones, Cell wall/membrane/envelope biogenesis];


Pssm-ID: 439940  Cd Length: 190  Bit Score: 63.34  E-value: 1.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822271 331 PTITRKYFHfIVVATYIPGIIF---DRPLLYVAATVCLAVFIFLEYVRYFRIKPLghtLRSLLSLflDERDsgpLILTHI 407
Cdd:COG0170    5 KELSRKIIH-IGSGLVILLALYlfiGRWIALILLALLLVGYLIIELLRLRYPLIL---LSSILRE--VERK---PSLGTV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822271 408 YLLLGMSLPIWLIPRPCAqkgslggaralvpYAGVLAVGVGDTVASIFGSTMGEIRWP-GTKKTFEGTMTSIFAQIISVA 486
Cdd:COG0170   76 YFALGILILVLLFPPEIA-------------AAAILVLALGDGLAALVGKRFGKHKLPvGGGKSLEGSLAMFIVSFLILL 142
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 157822271 487 LILIFdsgvdLNYSYAWILGSISTvsLLEAYTTQID 522
Cdd:COG0170  143 LVLLL-----FSLLIALLIALVAT--LVEALSPKGD 171
 
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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