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Conserved domains on  [gi|398366205|ref|NP_014956|]
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diacylglycerol kinase [Saccharomyces cerevisiae S288C]

Protein Classification

diacylglycerol/polyprenol kinase family protein( domain architecture ID 10000685)

diacylglycerol/polyprenol kinase family protein similar to yeast dolichol kinase SEC59 and CTP-dependent diacylglycerol kinase 1, as well as plant phytol kinase 1

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SEC59 COG0170
Dolichol kinase [Posttranslational modification, protein turnover, chaperones, Cell wall ...
71-281 3.37e-30

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


:

Pssm-ID: 439940  Cd Length: 190  Bit Score: 112.26  E-value: 3.37e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366205  71 KHEIPRKVFHSSIGFITLYLYTQGINYKNVLWPLIYAFIILFILDLIRLNWPFFNmlycrtVGALMRKKEIHTYNGVLWY 150
Cdd:COG0170    4 KKELSRKIIHIGSGLVILLALYLFIGRWIALILLALLLVGYLIIELLRLRYPLIL------LSSILREVERKPSLGTVYF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366205 151 ILGLIFSFNFFSKDVTLISLFLLSWSDTAAATIGRKYGHLTPKVARNKSLAGSIAAFTVGVITCWVFYGYFVPAysyvnk 230
Cdd:COG0170   78 ALGILILVLLFPPEIAAAAILVLALGDGLAALVGKRFGKHKLPVGGGKSLEGSLAMFIVSFLILLLVLLLFSLL------ 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 398366205 231 pgeiqwspetsrlslnmLSLLGGVVAALSEGIDLFNwDDNFTIPVLSSLFM 281
Cdd:COG0170  152 -----------------IALLIALVATLVEALSPKG-DDNLTIPLASALLL 184
 
Name Accession Description Interval E-value
SEC59 COG0170
Dolichol kinase [Posttranslational modification, protein turnover, chaperones, Cell wall ...
71-281 3.37e-30

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


Pssm-ID: 439940  Cd Length: 190  Bit Score: 112.26  E-value: 3.37e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366205  71 KHEIPRKVFHSSIGFITLYLYTQGINYKNVLWPLIYAFIILFILDLIRLNWPFFNmlycrtVGALMRKKEIHTYNGVLWY 150
Cdd:COG0170    4 KKELSRKIIHIGSGLVILLALYLFIGRWIALILLALLLVGYLIIELLRLRYPLIL------LSSILREVERKPSLGTVYF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366205 151 ILGLIFSFNFFSKDVTLISLFLLSWSDTAAATIGRKYGHLTPKVARNKSLAGSIAAFTVGVITCWVFYGYFVPAysyvnk 230
Cdd:COG0170   78 ALGILILVLLFPPEIAAAAILVLALGDGLAALVGKRFGKHKLPVGGGKSLEGSLAMFIVSFLILLLVLLLFSLL------ 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 398366205 231 pgeiqwspetsrlslnmLSLLGGVVAALSEGIDLFNwDDNFTIPVLSSLFM 281
Cdd:COG0170  152 -----------------IALLIALVATLVEALSPKG-DDNLTIPLASALLL 184
 
Name Accession Description Interval E-value
SEC59 COG0170
Dolichol kinase [Posttranslational modification, protein turnover, chaperones, Cell wall ...
71-281 3.37e-30

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


Pssm-ID: 439940  Cd Length: 190  Bit Score: 112.26  E-value: 3.37e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366205  71 KHEIPRKVFHSSIGFITLYLYTQGINYKNVLWPLIYAFIILFILDLIRLNWPFFNmlycrtVGALMRKKEIHTYNGVLWY 150
Cdd:COG0170    4 KKELSRKIIHIGSGLVILLALYLFIGRWIALILLALLLVGYLIIELLRLRYPLIL------LSSILREVERKPSLGTVYF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366205 151 ILGLIFSFNFFSKDVTLISLFLLSWSDTAAATIGRKYGHLTPKVARNKSLAGSIAAFTVGVITCWVFYGYFVPAysyvnk 230
Cdd:COG0170   78 ALGILILVLLFPPEIAAAAILVLALGDGLAALVGKRFGKHKLPVGGGKSLEGSLAMFIVSFLILLLVLLLFSLL------ 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 398366205 231 pgeiqwspetsrlslnmLSLLGGVVAALSEGIDLFNwDDNFTIPVLSSLFM 281
Cdd:COG0170  152 -----------------IALLIALVATLVEALSPKG-DDNLTIPLASALLL 184
 
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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