|
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
|
|
|