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Conserved domains on  [gi|488235898|ref|WP_002307106|]
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MULTISPECIES: diacylglycerol kinase family protein [Enterococcus]

Protein Classification

diacylglycerol/lipid kinase family protein( domain architecture ID 11446635)

diacylglycerol/lipid kinase family protein may catalyze the ATP-dependent phosphorylation of diacylglycerol and/or other lipids, and is involved in the phospholipid biosynthetic process

CATH:  3.40.50.10330
EC:  2.7.1.-
SCOP:  3001940

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
4-312 1.08e-61

Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, General function prediction only];


:

Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 198.15  E-value: 1.08e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488235898   4 HYHILINPSAGSGNGYKVAERILPVLKNKHIDYTLHYSEYKGHDAEIAETLAKETlipwieeeqktidtFPLLIIVGGDG 83
Cdd:COG1597    4 RALLIVNPASGRGRAARLLERLVAALRAAGLEVEVLETESPGDATELAREAAAEG--------------ADLVVAAGGDG 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488235898  84 TLHQVLDTFYQMEVefPVAYIPAGSGNDFARGADLPKNPKKGLQLILAAQsPEKVHIMAYEEKIsekkgiAVNNFGIGLD 163
Cdd:COG1597   70 TVNEVANGLAGTGP--PLGILPLGTGNDFARALGIPLDPEAALEALLTGR-TRRIDLGRVNGRY------FLNVAGIGFD 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488235898 164 AAIVHATNhsstkkRLNKYNLGSFSYLFSILRALFTQKGFPILVDAGGKQLSFsNAFLCTATKHPFFGGGIAIVPTADAS 243
Cdd:COG1597  141 AEVVERAN------RALKRRLGKLAYVLAALRALLRYRPFRLRIELDGEEIEG-EALLVAVGNGPYYGGGLRLAPDASLD 213
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488235898 244 KPVIDFVVVERINFFKILWLILLLIQKKQLKSKYFHHYTTNRLRIVSTTPQHGQEDGEEM-EKRPFDITI 312
Cdd:COG1597  214 DGLLDVVVVRPLSRLRLLRLLPRLLRGRHLRHPGVRYFRAREVEIESDRPLPVQLDGEPLgLATPLEFEV 283
 
Name Accession Description Interval E-value
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
4-312 1.08e-61

Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, General function prediction only];


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 198.15  E-value: 1.08e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488235898   4 HYHILINPSAGSGNGYKVAERILPVLKNKHIDYTLHYSEYKGHDAEIAETLAKETlipwieeeqktidtFPLLIIVGGDG 83
Cdd:COG1597    4 RALLIVNPASGRGRAARLLERLVAALRAAGLEVEVLETESPGDATELAREAAAEG--------------ADLVVAAGGDG 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488235898  84 TLHQVLDTFYQMEVefPVAYIPAGSGNDFARGADLPKNPKKGLQLILAAQsPEKVHIMAYEEKIsekkgiAVNNFGIGLD 163
Cdd:COG1597   70 TVNEVANGLAGTGP--PLGILPLGTGNDFARALGIPLDPEAALEALLTGR-TRRIDLGRVNGRY------FLNVAGIGFD 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488235898 164 AAIVHATNhsstkkRLNKYNLGSFSYLFSILRALFTQKGFPILVDAGGKQLSFsNAFLCTATKHPFFGGGIAIVPTADAS 243
Cdd:COG1597  141 AEVVERAN------RALKRRLGKLAYVLAALRALLRYRPFRLRIELDGEEIEG-EALLVAVGNGPYYGGGLRLAPDASLD 213
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488235898 244 KPVIDFVVVERINFFKILWLILLLIQKKQLKSKYFHHYTTNRLRIVSTTPQHGQEDGEEM-EKRPFDITI 312
Cdd:COG1597  214 DGLLDVVVVRPLSRLRLLRLLPRLLRGRHLRHPGVRYFRAREVEIESDRPLPVQLDGEPLgLATPLEFEV 283
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
4-134 2.29e-27

Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. The catalytic domain is assumed from the finding of bacterial homologs. YegS is the Escherichia coli protein in this family whose crystal structure reveals an active site in the inter-domain cleft formed by four conserved sequence motifs, revealing a novel metal-binding site. The residues of this site are conserved across the family.


Pssm-ID: 425868 [Multi-domain]  Cd Length: 125  Bit Score: 103.43  E-value: 2.29e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488235898    4 HYHILINPSAGSGNGYKVAERILPVLKNKHIDYTLHYSEYKGHDAEIAETLAketlipwieeeqktIDTFPLLIIVGGDG 83
Cdd:pfam00781   1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVEVELVLTEGPGDALELAREAA--------------EDGYDRIVVAGGDG 66
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 488235898   84 TLHQVLDTFYQMEVEFPVAYIPAGSGNDFARGADLPKNPKKGLQLILAAQS 134
Cdd:pfam00781  67 TVNEVLNGLAGLATRPPLGIIPLGTGNDFARALGIPGDPEEALEAILKGQT 117
TIGR00147 TIGR00147
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ...
4-312 4.78e-26

lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been purified and shown to have phosphatidylglycerol kinase activity. The member from M. tuberculosis, Rv2252, has diacylglycerol kinase activity. BmrU from B. subtilis is in an operon with multidrug efflux transporter Bmr, but is uncharacterized. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 161732 [Multi-domain]  Cd Length: 293  Bit Score: 104.89  E-value: 4.78e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488235898    4 HYHILINPSAGSGNGYKVAERILPVLKNKHIDYTLHYSEYKGHDAEIAETLAKetlipwieeeqktiDTFPLLIIVGGDG 83
Cdd:TIGR00147   3 EAPAILNPTAGKSNDNKPLREVIMLLREEGMEIHVRVTWEKGDAARYVEEARK--------------FGVDTVIAGGGDG 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488235898   84 TLHQVLDTFYQMEVEFPVAYIPAGSGNDFARGADLPKNPKKGLQLILAAQSpEKVHIMAYeekisEKKGIAVNNFGIGLD 163
Cdd:TIGR00147  69 TINEVVNALIQLDDIPALGILPLGTANDFARSLGIPEDLDKAAKLVIAGDA-RAIDMGQV-----NKQYCFINMAGGGFG 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488235898  164 AAIVHATNhsstkKRLnKYNLGSFSYLFSILRALFTQKGFPILVDAGGKQLSFsNAFLCTATKHPFFGGGIAIVPTADAS 243
Cdd:TIGR00147 143 TEITTETP-----EKL-KAALGSLSYILSGLMRMDTLQPFRCEIRGEGEHWQG-EAVVFLVGNGRQAGGGQKLAPDASIN 215
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488235898  244 KPVIDFVVVERINFFKILWLILLLIQKKQLKSKYFHHYTTNRLRIVSTTPQHGQEDGEEMEKRPFDITI 312
Cdd:TIGR00147 216 DGLLDLRIFTNDNLLPALVLTLMSDEGKHTDNPNIIYGKASRIDIQTPHKITFNLDGEPLGGTPFHIEI 284
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
6-124 2.95e-14

Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. DAG can be produced from the hydrolysis of phosphatidylinositol 4,5-bisphosphate (PIP2) by a phosphoinositide-specific phospholipase C and by the degradation of phosphatidylcholine (PC) by a phospholipase C or the concerted actions of phospholipase D and phosphatidate phosphohydrolase. This domain is presumed to be the catalytic domain. Bacterial homologues areknown.


Pssm-ID: 214487 [Multi-domain]  Cd Length: 124  Bit Score: 68.09  E-value: 2.95e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488235898     6 HILINPSAGSGNGYKVAERILPVLkNKHIDYTLhysEYKGHDAEIaetlaketlipwieEEQKTIDTFPLLIIVGGDGTL 85
Cdd:smart00046   1 LVFVNPKSGGGKGEKLLRKFRLLL-NPRQVFDL---TKKGPAVAL--------------VIFRDVPDFNRVLVCGGDGTV 62
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 488235898    86 HQVLDTFYQMEV---EFPVAYIPAGSGNDFARGADLPKNPKK 124
Cdd:smart00046  63 GWVLNALDKRELplpEPPVAVLPLGTGNDLARSLGWGGGYDG 104
PRK11914 PRK11914
diacylglycerol kinase; Reviewed
7-252 3.51e-13

diacylglycerol kinase; Reviewed


Pssm-ID: 237021 [Multi-domain]  Cd Length: 306  Bit Score: 69.04  E-value: 3.51e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488235898   7 ILINPSAGSGNGYKVAERILPVLKNKHIDYTlhysEYKGHDAEIAETLAKETLipwieeeQKTIDTfplLIIVGGDGTLH 86
Cdd:PRK11914  13 VLTNPLSGHGAAPHAAERAIARLHHRGVDVV----EIVGTDAHDARHLVAAAL-------AKGTDA---LVVVGGDGVIS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488235898  87 QVLDTFYQMEVefPVAYIPAGSGNDFARGADLP-KNPKKGLQLILAAQSpEKVHImayeEKISEKKGiAVNNFGI----G 161
Cdd:PRK11914  79 NALQVLAGTDI--PLGIIPAGTGNDHAREFGIPtGDPEAAADVIVDGWT-ETVDL----GRIQDDDG-IVKWFGTvaatG 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488235898 162 LDAAIVHATNHSSTKKRLNKYNLGSFSYLfSILRALftqkGFPILVDaGGKQLSfSNAFLCTATKHPFFGGGIAIVPTAD 241
Cdd:PRK11914 151 FDSLVTDRANRMRWPHGRMRYNLAMLAEL-SKLRPL----PFRLVLD-GTEEIV-TDLTLAAFGNTRSYGGGMLICPNAD 223
                        250
                 ....*....|.
gi 488235898 242 ASKPVIDFVVV 252
Cdd:PRK11914 224 HTDGLLDITMV 234
 
Name Accession Description Interval E-value
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
4-312 1.08e-61

Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, General function prediction only];


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 198.15  E-value: 1.08e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488235898   4 HYHILINPSAGSGNGYKVAERILPVLKNKHIDYTLHYSEYKGHDAEIAETLAKETlipwieeeqktidtFPLLIIVGGDG 83
Cdd:COG1597    4 RALLIVNPASGRGRAARLLERLVAALRAAGLEVEVLETESPGDATELAREAAAEG--------------ADLVVAAGGDG 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488235898  84 TLHQVLDTFYQMEVefPVAYIPAGSGNDFARGADLPKNPKKGLQLILAAQsPEKVHIMAYEEKIsekkgiAVNNFGIGLD 163
Cdd:COG1597   70 TVNEVANGLAGTGP--PLGILPLGTGNDFARALGIPLDPEAALEALLTGR-TRRIDLGRVNGRY------FLNVAGIGFD 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488235898 164 AAIVHATNhsstkkRLNKYNLGSFSYLFSILRALFTQKGFPILVDAGGKQLSFsNAFLCTATKHPFFGGGIAIVPTADAS 243
Cdd:COG1597  141 AEVVERAN------RALKRRLGKLAYVLAALRALLRYRPFRLRIELDGEEIEG-EALLVAVGNGPYYGGGLRLAPDASLD 213
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488235898 244 KPVIDFVVVERINFFKILWLILLLIQKKQLKSKYFHHYTTNRLRIVSTTPQHGQEDGEEM-EKRPFDITI 312
Cdd:COG1597  214 DGLLDVVVVRPLSRLRLLRLLPRLLRGRHLRHPGVRYFRAREVEIESDRPLPVQLDGEPLgLATPLEFEV 283
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
4-134 2.29e-27

Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. The catalytic domain is assumed from the finding of bacterial homologs. YegS is the Escherichia coli protein in this family whose crystal structure reveals an active site in the inter-domain cleft formed by four conserved sequence motifs, revealing a novel metal-binding site. The residues of this site are conserved across the family.


Pssm-ID: 425868 [Multi-domain]  Cd Length: 125  Bit Score: 103.43  E-value: 2.29e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488235898    4 HYHILINPSAGSGNGYKVAERILPVLKNKHIDYTLHYSEYKGHDAEIAETLAketlipwieeeqktIDTFPLLIIVGGDG 83
Cdd:pfam00781   1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVEVELVLTEGPGDALELAREAA--------------EDGYDRIVVAGGDG 66
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 488235898   84 TLHQVLDTFYQMEVEFPVAYIPAGSGNDFARGADLPKNPKKGLQLILAAQS 134
Cdd:pfam00781  67 TVNEVLNGLAGLATRPPLGIIPLGTGNDFARALGIPGDPEEALEAILKGQT 117
TIGR00147 TIGR00147
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ...
4-312 4.78e-26

lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been purified and shown to have phosphatidylglycerol kinase activity. The member from M. tuberculosis, Rv2252, has diacylglycerol kinase activity. BmrU from B. subtilis is in an operon with multidrug efflux transporter Bmr, but is uncharacterized. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 161732 [Multi-domain]  Cd Length: 293  Bit Score: 104.89  E-value: 4.78e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488235898    4 HYHILINPSAGSGNGYKVAERILPVLKNKHIDYTLHYSEYKGHDAEIAETLAKetlipwieeeqktiDTFPLLIIVGGDG 83
Cdd:TIGR00147   3 EAPAILNPTAGKSNDNKPLREVIMLLREEGMEIHVRVTWEKGDAARYVEEARK--------------FGVDTVIAGGGDG 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488235898   84 TLHQVLDTFYQMEVEFPVAYIPAGSGNDFARGADLPKNPKKGLQLILAAQSpEKVHIMAYeekisEKKGIAVNNFGIGLD 163
Cdd:TIGR00147  69 TINEVVNALIQLDDIPALGILPLGTANDFARSLGIPEDLDKAAKLVIAGDA-RAIDMGQV-----NKQYCFINMAGGGFG 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488235898  164 AAIVHATNhsstkKRLnKYNLGSFSYLFSILRALFTQKGFPILVDAGGKQLSFsNAFLCTATKHPFFGGGIAIVPTADAS 243
Cdd:TIGR00147 143 TEITTETP-----EKL-KAALGSLSYILSGLMRMDTLQPFRCEIRGEGEHWQG-EAVVFLVGNGRQAGGGQKLAPDASIN 215
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488235898  244 KPVIDFVVVERINFFKILWLILLLIQKKQLKSKYFHHYTTNRLRIVSTTPQHGQEDGEEMEKRPFDITI 312
Cdd:TIGR00147 216 DGLLDLRIFTNDNLLPALVLTLMSDEGKHTDNPNIIYGKASRIDIQTPHKITFNLDGEPLGGTPFHIEI 284
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
6-124 2.95e-14

Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. DAG can be produced from the hydrolysis of phosphatidylinositol 4,5-bisphosphate (PIP2) by a phosphoinositide-specific phospholipase C and by the degradation of phosphatidylcholine (PC) by a phospholipase C or the concerted actions of phospholipase D and phosphatidate phosphohydrolase. This domain is presumed to be the catalytic domain. Bacterial homologues areknown.


Pssm-ID: 214487 [Multi-domain]  Cd Length: 124  Bit Score: 68.09  E-value: 2.95e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488235898     6 HILINPSAGSGNGYKVAERILPVLkNKHIDYTLhysEYKGHDAEIaetlaketlipwieEEQKTIDTFPLLIIVGGDGTL 85
Cdd:smart00046   1 LVFVNPKSGGGKGEKLLRKFRLLL-NPRQVFDL---TKKGPAVAL--------------VIFRDVPDFNRVLVCGGDGTV 62
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 488235898    86 HQVLDTFYQMEV---EFPVAYIPAGSGNDFARGADLPKNPKK 124
Cdd:smart00046  63 GWVLNALDKRELplpEPPVAVLPLGTGNDLARSLGWGGGYDG 104
PRK11914 PRK11914
diacylglycerol kinase; Reviewed
7-252 3.51e-13

diacylglycerol kinase; Reviewed


Pssm-ID: 237021 [Multi-domain]  Cd Length: 306  Bit Score: 69.04  E-value: 3.51e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488235898   7 ILINPSAGSGNGYKVAERILPVLKNKHIDYTlhysEYKGHDAEIAETLAKETLipwieeeQKTIDTfplLIIVGGDGTLH 86
Cdd:PRK11914  13 VLTNPLSGHGAAPHAAERAIARLHHRGVDVV----EIVGTDAHDARHLVAAAL-------AKGTDA---LVVVGGDGVIS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488235898  87 QVLDTFYQMEVefPVAYIPAGSGNDFARGADLP-KNPKKGLQLILAAQSpEKVHImayeEKISEKKGiAVNNFGI----G 161
Cdd:PRK11914  79 NALQVLAGTDI--PLGIIPAGTGNDHAREFGIPtGDPEAAADVIVDGWT-ETVDL----GRIQDDDG-IVKWFGTvaatG 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488235898 162 LDAAIVHATNHSSTKKRLNKYNLGSFSYLfSILRALftqkGFPILVDaGGKQLSfSNAFLCTATKHPFFGGGIAIVPTAD 241
Cdd:PRK11914 151 FDSLVTDRANRMRWPHGRMRYNLAMLAEL-SKLRPL----PFRLVLD-GTEEIV-TDLTLAAFGNTRSYGGGMLICPNAD 223
                        250
                 ....*....|.
gi 488235898 242 ASKPVIDFVVV 252
Cdd:PRK11914 224 HTDGLLDITMV 234
PRK00861 PRK00861
putative lipid kinase; Reviewed
6-311 4.17e-10

putative lipid kinase; Reviewed


Pssm-ID: 234850 [Multi-domain]  Cd Length: 300  Bit Score: 59.64  E-value: 4.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488235898   6 HILINPSAGSGNGYKVAERILPVLKNK---HIDYTlhySEYKGHDAeiaetLAKETlipwIEEEQKTIdtfpllIIVGGD 82
Cdd:PRK00861   6 CLIFNPVAGQGNPEVDLALIRAILEPEmdlDIYLT---TPEIGADQ-----LAQEA----IERGAELI------IASGGD 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488235898  83 GTLHQVLDTFyqMEVEFPVAYIPAGSGNDFARGADLPKNPKKGLQLILAAQsPEKVHImAYeekisekkgiaVNNF---- 158
Cdd:PRK00861  68 GTLSAVAGAL--IGTDIPLGIIPRGTANAFAAALGIPDTIEEACRTILQGK-TRRVDV-AY-----------CNGQpmil 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488235898 159 --GIGLDAAIVHATNhsstkkRLNKYNLGSFSYLFSILRALFTQKGFPILVDAGGKQLSFSNAFLCTATKHP---FFGGG 233
Cdd:PRK00861 133 laGIGFEAETVEEAD------REAKNRFGILAYILSGLQQLRELESFEVEIETEDQIITTNAVAVTVANAAPptsVLAQG 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488235898 234 IAIVPTADAskpVIDFVVVERINFFKILWLILLLIQKKQLKSKYFH----HYTTNRLRIVSTTPQHGQEDGEEMEKRPFD 309
Cdd:PRK00861 207 PGAVIPDDG---LLDVTIVAPKNLAEAVAASYHLLQTALQGNPAERddigYLRAKQVKITTDPPQKVVIDGEVVGTTPIE 283

                 ..
gi 488235898 310 IT 311
Cdd:PRK00861 284 IE 285
PRK13057 PRK13057
lipid kinase;
45-301 5.64e-10

lipid kinase;


Pssm-ID: 183857 [Multi-domain]  Cd Length: 287  Bit Score: 59.16  E-value: 5.64e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488235898  45 GHDAEIAETLAKETLIPWIEEEQKTIDtfpLLIIVGGDGTLHQVLDTFyqMEVEFPVAYIPAGSGNDFARGADLPKNPKK 124
Cdd:PRK13057  26 GLELVEPPAEDPDDLSEVIEAYADGVD---LVIVGGGDGTLNAAAPAL--VETGLPLGILPLGTANDLARTLGIPLDLEA 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488235898 125 GLQLILAAQspekVHIMayeeKISEKKGIAVNNFG-IGLDAAIVHATnHSSTKKRlnkynLGSFSYLFSILRALFTQKGF 203
Cdd:PRK13057 101 AARVIATGQ----VRRI----DLGWVNGHYFFNVAsLGLSAELARRL-TKELKRR-----WGTLGYAIAALRVLRRSRPF 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488235898 204 PILVDAGGK-------QLSFSNAflctatkhPFFGGGIAIVPTADASKPVIDFVVVERINFFKILWLILLLIQKKQLKSK 276
Cdd:PRK13057 167 TAEIEHDGRtervktlQVAVGNG--------RYYGGGMTVAHDATIDDGRLDLYSLEVAHWWRLLALLPALRRGRHGEWP 238
                        250       260
                 ....*....|....*....|....*
gi 488235898 277 YFHHYTTNRLRIVSTTPQHGQEDGE 301
Cdd:PRK13057 239 DVRAFRTTELELRTRKPRPINTDGE 263
PRK13055 PRK13055
putative lipid kinase; Reviewed
64-146 5.92e-08

putative lipid kinase; Reviewed


Pssm-ID: 237282 [Multi-domain]  Cd Length: 334  Bit Score: 53.46  E-value: 5.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488235898  64 EEEQKTIDTFPLLIIVGGDGTLHQVLDTFYQMEVEFPVAYIPAGSGNDFARGADLPK-NPKKGLQLILAAQSpEKVHI-M 141
Cdd:PRK13055  51 EAKRAAEAGFDLIIAAGGDGTINEVVNGIAPLEKRPKMAIIPAGTTNDYARALKIPRdNPVEAAKVILKNQT-IKMDIgR 129

                 ....*
gi 488235898 142 AYEEK 146
Cdd:PRK13055 130 ANEDK 134
YegS_C pfam19279
YegS C-terminal NAD kinase beta sandwich-like domain; This entry represents the C-terminal ...
161-253 1.60e-07

YegS C-terminal NAD kinase beta sandwich-like domain; This entry represents the C-terminal domain found in the YegS protein. It is related to the beta sandwich domain of NAD kinases. The structure of YegS reveals a two-domain protein with the active site crevice found between the two domains. The C-terminal domain contains 13 beta-strands and two alpha-helices. The likely substrate for YegS is phosphatidylglycerol.


Pssm-ID: 437111  Cd Length: 158  Bit Score: 50.27  E-value: 1.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488235898  161 GLDAAIVHATNHSstkkrlnKYNLGSFSYLFSILRAL--FTQKGFPILVDAGGKQLSfsnAFLCTATKHPFFGGGIAIVP 238
Cdd:pfam19279   6 GVDARVNRRANRS-------RLLPGALSYPAAALRALatFRPLRYRVTVDGEVREFS---AALVAVANSGYYGGGMRIAP 75
                          90
                  ....*....|....*
gi 488235898  239 TADASKPVIDFVVVE 253
Cdd:pfam19279  76 DARVDDGLLDVVVIE 90
PRK13054 PRK13054
lipid kinase; Reviewed
76-134 3.90e-07

lipid kinase; Reviewed


Pssm-ID: 237281 [Multi-domain]  Cd Length: 300  Bit Score: 50.64  E-value: 3.90e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488235898  76 LIIVGGDGTLHQVLDTFYQMEVE-FPV-AYIPAGSGNDFARGADLPKNPKKGLQLILAAQS 134
Cdd:PRK13054  60 VIAGGGDGTINEVATALAQLEGDaRPAlGILPLGTANDFATAAGIPLEPDKALKLAIEGRA 120
PRK13059 PRK13059
putative lipid kinase; Reviewed
71-209 2.45e-06

putative lipid kinase; Reviewed


Pssm-ID: 183858  Cd Length: 295  Bit Score: 48.11  E-value: 2.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488235898  71 DTFPLLIIVGGDGTLHQVLDTFYQMEVEFPVAYIPAGSGNDFARGADLPKNPKKGLQLILAAqSPEKVHImayeEKISEK 150
Cdd:PRK13059  55 ESYKYILIAGGDGTVDNVVNAMKKLNIDLPIGILPVGTANDFAKFLGMPTDIGEACEQILKS-KPKKVDL----GKINDK 129
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488235898 151 KGIAVNNFGIGLDAaivhatnhsSTKKRLN-KYNLGSFSYLFSILRALFTQKGFPILVDA 209
Cdd:PRK13059 130 YFINVASTGLFTDV---------SQKTDVNlKNTIGKLAYYLKGLEELPNFRKLKVKVTS 180
PRK13337 PRK13337
putative lipid kinase; Reviewed
63-134 8.30e-06

putative lipid kinase; Reviewed


Pssm-ID: 183982 [Multi-domain]  Cd Length: 304  Bit Score: 46.58  E-value: 8.30e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488235898  63 IEEEQKTIDTFPLLIIVGGDGTLHQVLDTFYQMEVEFPVAYIPAGSGNDFARGADLPKNPKKGLQLILAAQS 134
Cdd:PRK13337  48 LAAERAVERKFDLVIAAGGDGTLNEVVNGIAEKENRPKLGIIPVGTTNDFARALHVPRDIEKAADVIIEGHT 119
PLN02958 PLN02958
diacylglycerol kinase/D-erythro-sphingosine kinase
7-114 1.02e-04

diacylglycerol kinase/D-erythro-sphingosine kinase


Pssm-ID: 215517 [Multi-domain]  Cd Length: 481  Bit Score: 43.70  E-value: 1.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488235898   7 ILINPSAGSGNGYKV-AERILPVLKNKHIDYTLHYSEYKGHDAEIAETLaketlipwieeeqkTIDTFPLLIIVGGDGTL 85
Cdd:PLN02958 116 VFVNPFGGKKSASKIfFDVVKPLLEDADIQLTIQETKYQLHAKEVVRTM--------------DLSKYDGIVCVSGDGIL 181
                         90       100       110
                 ....*....|....*....|....*....|....
gi 488235898  86 HQVLDTFYQME-----VEFPVAYIPAGSGNDFAR 114
Cdd:PLN02958 182 VEVVNGLLEREdwktaIKLPIGMVPAGTGNGMAK 215
PRK12361 PRK12361
hypothetical protein; Provisional
7-110 4.71e-03

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 38.45  E-value: 4.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488235898   7 ILINPSAGSGNGYKVAERILPVLKnKHIDYTLHYSeykghDAEI-AETLAKETLipwieeeQKTIDtfpLLIIVGGDGTL 85
Cdd:PRK12361 247 LIANPVSGGGKWQEYGEQIQRELK-AYFDLTVKLT-----TPEIsAEALAKQAR-------KAGAD---IVIACGGDGTV 310
                         90       100
                 ....*....|....*....|....*
gi 488235898  86 HQVLDTFYQMEVEFPVayIPAGSGN 110
Cdd:PRK12361 311 TEVASELVNTDITLGI--IPLGTAN 333
 
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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