|
Name |
Accession |
Description |
Interval |
E-value |
| LCB5 |
COG1597 |
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ... |
51-362 |
2.52e-70 |
|
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, General function prediction only];
Pssm-ID: 441205 [Multi-domain] Cd Length: 295 Bit Score: 222.81 E-value: 2.52e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307891685 51 YAFVVNPSKPQATARRL--HIQEFCKAKGLnRVRFYDTQLDKDGRDCALEALEDGADVVIAVGGDGTVRTVASAVSGTGH 128
Cdd:COG1597 5 ALLIVNPASGRGRAARLleRLVAALRAAGL-EVEVLETESPGDATELAREAAAEGADLVVAAGGDGTVNEVANGLAGTGP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307891685 129 ALGIVPIGTGNLFARNMGIPVdDIDAALTVATSHGSRMVDMGRLTlldhpeddhGHAFLIIAGIGFDAAMIDDTDPDLKA 208
Cdd:COG1597 84 PLGILPLGTGNDFARALGIPL-DPEAALEALLTGRTRRIDLGRVN---------GRYFLNVAGIGFDAEVVERANRALKR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307891685 209 NISWLAYFVGGVKNLFAPKFRgNLTVTsADGSTHTTNnlaFRTVMAGNCGQIP-VFSLMPAASYDDGILDFEIIdTTGGI 287
Cdd:COG1597 154 RLGKLAYVLAALRALLRYRPF-RLRIE-LDGEEIEGE---ALLVAVGNGPYYGgGLRLAPDASLDDGLLDVVVV-RPLSR 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1307891685 288 LGWANLFGDVVHQTIIGKPEqnplstnstIEQVQGLSAEIVLEKPAKAQVDGDMLPETKHIRFSVDHRALIVRVP 362
Cdd:COG1597 228 LRLLRLLPRLLRGRHLRHPG---------VRYFRAREVEIESDRPLPVQLDGEPLGLATPLEFEVLPGALRVLVP 293
|
|
| PRK00861 |
PRK00861 |
putative lipid kinase; Reviewed |
84-362 |
1.45e-32 |
|
putative lipid kinase; Reviewed
Pssm-ID: 234850 [Multi-domain] Cd Length: 300 Bit Score: 123.96 E-value: 1.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307891685 84 YDTQLDKDGRDCALEALEDGADVVIAVGGDGTVRTVASAVSGTGHALGIVPIGTGNLFARNMGIPvDDIDAALTVATSHG 163
Cdd:PRK00861 38 YLTTPEIGADQLAQEAIERGAELIIASGGDGTLSAVAGALIGTDIPLGIIPRGTANAFAAALGIP-DTIEEACRTILQGK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307891685 164 SRMVDMGRLtlldhpeddHGHAFLIIAGIGFDAAMIDDTDPDLKANISWLAYFVGGVKNLFAPKfrgNLTVT-SADGSTH 242
Cdd:PRK00861 117 TRRVDVAYC---------NGQPMILLAGIGFEAETVEEADREAKNRFGILAYILSGLQQLRELE---SFEVEiETEDQII 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307891685 243 TTNNLAF--------RTVMAGNCGqipvfslmpAASYDDGILDFEIIDTTggilgwaNLFGDV---VH--QT-IIGKPEQ 308
Cdd:PRK00861 185 TTNAVAVtvanaappTSVLAQGPG---------AVIPDDGLLDVTIVAPK-------NLAEAVaasYHllQTaLQGNPAE 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1307891685 309 NPLSTNSTIEQVQglsaeIVLEKPAKAQVDGDMLPETKhIRFSVDHRALIVRVP 362
Cdd:PRK00861 249 RDDIGYLRAKQVK-----ITTDPPQKVVIDGEVVGTTP-IEIECLPRSLKVFAP 296
|
|
| DAGK_cat |
pfam00781 |
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ... |
53-172 |
6.69e-28 |
|
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: 106.52 E-value: 6.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307891685 53 FVVNPSKPQATARRL--HIQEFCKAKGLnRVRFYDTQLDKDGRDCALEALEDGADVVIAVGGDGTVRTVASAVSGTGH-- 128
Cdd:pfam00781 4 VIVNPKSGGGKGKKLlrKVRPLLNKAGV-EVELVLTEGPGDALELAREAAEDGYDRIVVAGGDGTVNEVLNGLAGLATrp 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1307891685 129 ALGIVPIGTGNLFARNMGIPVdDIDAALTVATSHGSRMVDMGRL 172
Cdd:pfam00781 83 PLGIIPLGTGNDFARALGIPG-DPEEALEAILKGQTRPVDVGKV 125
|
|
| TIGR00147 |
TIGR00147 |
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ... |
98-284 |
1.11e-17 |
|
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: 82.55 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307891685 98 EALEDGADVVIAVGGDGTVRTVASAVSGTGH--ALGIVPIGTGNLFARNMGIPvDDIDAALTVATSHGSRMVDMGRLTLL 175
Cdd:TIGR00147 52 EARKFGVDTVIAGGGDGTINEVVNALIQLDDipALGILPLGTANDFARSLGIP-EDLDKAAKLVIAGDARAIDMGQVNKQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307891685 176 dhpeddhgHAFLIIAGIGFDAAMIDDTDPDLKANISWLAYFVGGVKNL--FAPkFRGNLTVtsaDGSTHTTNNLAFrTVM 253
Cdd:TIGR00147 131 --------YCFINMAGGGFGTEITTETPEKLKAALGSLSYILSGLMRMdtLQP-FRCEIRG---EGEHWQGEAVVF-LVG 197
|
170 180 190
....*....|....*....|....*....|....
gi 1307891685 254 AGN---CGQIPvfslMPAASYDDGILDFEIIDTT 284
Cdd:TIGR00147 198 NGRqagGGQKL----APDASINDGLLDLRIFTND 227
|
|
| DAGKc |
smart00046 |
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ... |
69-148 |
9.76e-08 |
|
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: 50.37 E-value: 9.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307891685 69 IQEFCKAkgLNRVRFYDTqlDKDGRDCALEALEDGAD--VVIAVGGDGTVRTVASAVS-----GTGHALGIVPIGTGNLF 141
Cdd:smart00046 17 LRKFRLL--LNPRQVFDL--TKKGPAVALVIFRDVPDfnRVLVCGGDGTVGWVLNALDkrelpLPEPPVAVLPLGTGNDL 92
|
....*..
gi 1307891685 142 ARNMGIP 148
Cdd:smart00046 93 ARSLGWG 99
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| LCB5 |
COG1597 |
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ... |
51-362 |
2.52e-70 |
|
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, General function prediction only];
Pssm-ID: 441205 [Multi-domain] Cd Length: 295 Bit Score: 222.81 E-value: 2.52e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307891685 51 YAFVVNPSKPQATARRL--HIQEFCKAKGLnRVRFYDTQLDKDGRDCALEALEDGADVVIAVGGDGTVRTVASAVSGTGH 128
Cdd:COG1597 5 ALLIVNPASGRGRAARLleRLVAALRAAGL-EVEVLETESPGDATELAREAAAEGADLVVAAGGDGTVNEVANGLAGTGP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307891685 129 ALGIVPIGTGNLFARNMGIPVdDIDAALTVATSHGSRMVDMGRLTlldhpeddhGHAFLIIAGIGFDAAMIDDTDPDLKA 208
Cdd:COG1597 84 PLGILPLGTGNDFARALGIPL-DPEAALEALLTGRTRRIDLGRVN---------GRYFLNVAGIGFDAEVVERANRALKR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307891685 209 NISWLAYFVGGVKNLFAPKFRgNLTVTsADGSTHTTNnlaFRTVMAGNCGQIP-VFSLMPAASYDDGILDFEIIdTTGGI 287
Cdd:COG1597 154 RLGKLAYVLAALRALLRYRPF-RLRIE-LDGEEIEGE---ALLVAVGNGPYYGgGLRLAPDASLDDGLLDVVVV-RPLSR 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1307891685 288 LGWANLFGDVVHQTIIGKPEqnplstnstIEQVQGLSAEIVLEKPAKAQVDGDMLPETKHIRFSVDHRALIVRVP 362
Cdd:COG1597 228 LRLLRLLPRLLRGRHLRHPG---------VRYFRAREVEIESDRPLPVQLDGEPLGLATPLEFEVLPGALRVLVP 293
|
|
| PRK00861 |
PRK00861 |
putative lipid kinase; Reviewed |
84-362 |
1.45e-32 |
|
putative lipid kinase; Reviewed
Pssm-ID: 234850 [Multi-domain] Cd Length: 300 Bit Score: 123.96 E-value: 1.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307891685 84 YDTQLDKDGRDCALEALEDGADVVIAVGGDGTVRTVASAVSGTGHALGIVPIGTGNLFARNMGIPvDDIDAALTVATSHG 163
Cdd:PRK00861 38 YLTTPEIGADQLAQEAIERGAELIIASGGDGTLSAVAGALIGTDIPLGIIPRGTANAFAAALGIP-DTIEEACRTILQGK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307891685 164 SRMVDMGRLtlldhpeddHGHAFLIIAGIGFDAAMIDDTDPDLKANISWLAYFVGGVKNLFAPKfrgNLTVT-SADGSTH 242
Cdd:PRK00861 117 TRRVDVAYC---------NGQPMILLAGIGFEAETVEEADREAKNRFGILAYILSGLQQLRELE---SFEVEiETEDQII 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307891685 243 TTNNLAF--------RTVMAGNCGqipvfslmpAASYDDGILDFEIIDTTggilgwaNLFGDV---VH--QT-IIGKPEQ 308
Cdd:PRK00861 185 TTNAVAVtvanaappTSVLAQGPG---------AVIPDDGLLDVTIVAPK-------NLAEAVaasYHllQTaLQGNPAE 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1307891685 309 NPLSTNSTIEQVQglsaeIVLEKPAKAQVDGDMLPETKhIRFSVDHRALIVRVP 362
Cdd:PRK00861 249 RDDIGYLRAKQVK-----ITTDPPQKVVIDGEVVGTTP-IEIECLPRSLKVFAP 296
|
|
| DAGK_cat |
pfam00781 |
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ... |
53-172 |
6.69e-28 |
|
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: 106.52 E-value: 6.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307891685 53 FVVNPSKPQATARRL--HIQEFCKAKGLnRVRFYDTQLDKDGRDCALEALEDGADVVIAVGGDGTVRTVASAVSGTGH-- 128
Cdd:pfam00781 4 VIVNPKSGGGKGKKLlrKVRPLLNKAGV-EVELVLTEGPGDALELAREAAEDGYDRIVVAGGDGTVNEVLNGLAGLATrp 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1307891685 129 ALGIVPIGTGNLFARNMGIPVdDIDAALTVATSHGSRMVDMGRL 172
Cdd:pfam00781 83 PLGIIPLGTGNDFARALGIPG-DPEEALEAILKGQTRPVDVGKV 125
|
|
| PRK13054 |
PRK13054 |
lipid kinase; Reviewed |
98-367 |
2.55e-22 |
|
lipid kinase; Reviewed
Pssm-ID: 237281 [Multi-domain] Cd Length: 300 Bit Score: 96.10 E-value: 2.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307891685 98 EALEDGADVVIAVGGDGTVRTVASAVSGTGH----ALGIVPIGTGNLFARNMGIPvDDIDAALTVATSHGSRMVDMGRLt 173
Cdd:PRK13054 51 EALALGVATVIAGGGDGTINEVATALAQLEGdarpALGILPLGTANDFATAAGIP-LEPDKALKLAIEGRAQPIDLARV- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307891685 174 lldhpeDDHgHAFLIIAGIGFDAAMIDDTDPDLKANISWLAYFVGGVKNLfapkfrgnLTVTSADGSTHT---TNNLAFR 250
Cdd:PRK13054 129 ------NDR-TYFINMATGGFGTRVTTETPEKLKAALGGVAYLIHGLMRM--------DTLKPDRCEIRGpdfHWQGDAL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307891685 251 TVMAGNC-----GQIpvfsLMPAASYDDGILDFEIIDTTGGILGwanlfgdVVHQTIIGKPEQNPLSTNSTIEQVqglsa 325
Cdd:PRK13054 194 VIGIGNGrqaggGQQ----LCPEALINDGLLDLRILPAPQELLP-------TLLSTLTGGSEDNPNIIRARLPWL----- 257
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1307891685 326 EIVLEKPAKAQVDGDMLpETKHIRFSVDHRALIVRVPDTSAL 367
Cdd:PRK13054 258 EIQAPHELTFNLDGEPL-SGRHFRIEVLPAALRCRLPPDCPL 298
|
|
| PRK13057 |
PRK13057 |
lipid kinase; |
91-278 |
2.94e-20 |
|
lipid kinase;
Pssm-ID: 183857 [Multi-domain] Cd Length: 287 Bit Score: 89.98 E-value: 2.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307891685 91 DGRDCA--LEALEDGADVVIAVGGDGTVRTVASAVSGTGHALGIVPIGTGNLFARNMGIPVDDIDAALTVATSHgSRMVD 168
Cdd:PRK13057 36 DPDDLSevIEAYADGVDLVIVGGGDGTLNAAAPALVETGLPLGILPLGTANDLARTLGIPLDLEAAARVIATGQ-VRRID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307891685 169 MGRLtlldhpeddHGHAFLIIAGIGFDAAMIDDTDPDLKANISWLAYFVGGVKNLF-APKFRGNLtvtSADGSThttnnL 247
Cdd:PRK13057 115 LGWV---------NGHYFFNVASLGLSAELARRLTKELKRRWGTLGYAIAALRVLRrSRPFTAEI---EHDGRT-----E 177
|
170 180 190
....*....|....*....|....*....|....*..
gi 1307891685 248 AFRTVMA--GN----CGQIPVFslmPAASYDDGILDF 278
Cdd:PRK13057 178 RVKTLQVavGNgryyGGGMTVA---HDATIDDGRLDL 211
|
|
| PRK12361 |
PRK12361 |
hypothetical protein; Provisional |
86-365 |
3.38e-19 |
|
hypothetical protein; Provisional
Pssm-ID: 183473 [Multi-domain] Cd Length: 547 Bit Score: 89.29 E-value: 3.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307891685 86 TQLDKDGRDCALEALEDGADVVIAVGGDGTVRTVASAVSGTGHALGIVPIGTGN-----LF-ARNMGIPVDdiDAALTVA 159
Cdd:PRK12361 280 TTPEISAEALAKQARKAGADIVIACGGDGTVTEVASELVNTDITLGIIPLGTANalshaLFgLGSKLIPVE--QACDNII 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307891685 160 TSHgSRMVDMGRLtlldhpeddHGHAFLIIAGIGFDAAMIDDTDPDLKANISWLAYfVGGVKNLFAPKFRGNLTVTSADG 239
Cdd:PRK12361 358 QGH-TQRIDTARC---------NDRLMLLLVGIGFEQKMIESADRERKNALGQLAY-LDGLWRAVNENETLTLTVTLDDA 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307891685 240 -----STHT---TNNLAFRTVMAGNCGQiPVfslmpaasYDDGILDFEIIDTTGGILGWANLFGDVVHQTIIGKPEqnpl 311
Cdd:PRK12361 427 epqtiSTHSlvvANAAPFTSLLAQGGGE-PN--------MTDGLLDITWLDSGGEPGEQLLSLAELALSGLGKEPE---- 493
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1307891685 312 stNSTIEQVQGLSAEIVLEKPAKAQVDGDmLPETKHIRFSVDHRALIVRVPDTS 365
Cdd:PRK12361 494 --ANKVHHAHAKKVTISSQKPIKYVIDGE-LFEDEDLTIEVQPASLKVFVPYQE 544
|
|
| TIGR00147 |
TIGR00147 |
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ... |
98-284 |
1.11e-17 |
|
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: 82.55 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307891685 98 EALEDGADVVIAVGGDGTVRTVASAVSGTGH--ALGIVPIGTGNLFARNMGIPvDDIDAALTVATSHGSRMVDMGRLTLL 175
Cdd:TIGR00147 52 EARKFGVDTVIAGGGDGTINEVVNALIQLDDipALGILPLGTANDFARSLGIP-EDLDKAAKLVIAGDARAIDMGQVNKQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307891685 176 dhpeddhgHAFLIIAGIGFDAAMIDDTDPDLKANISWLAYFVGGVKNL--FAPkFRGNLTVtsaDGSTHTTNNLAFrTVM 253
Cdd:TIGR00147 131 --------YCFINMAGGGFGTEITTETPEKLKAALGSLSYILSGLMRMdtLQP-FRCEIRG---EGEHWQGEAVVF-LVG 197
|
170 180 190
....*....|....*....|....*....|....
gi 1307891685 254 AGN---CGQIPvfslMPAASYDDGILDFEIIDTT 284
Cdd:TIGR00147 198 NGRqagGGQKL----APDASINDGLLDLRIFTND 227
|
|
| PRK13337 |
PRK13337 |
putative lipid kinase; Reviewed |
84-284 |
7.80e-17 |
|
putative lipid kinase; Reviewed
Pssm-ID: 183982 [Multi-domain] Cd Length: 304 Bit Score: 80.48 E-value: 7.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307891685 84 YDTQLDKDGRDCALEALEDGADVVIAVGGDGTVRTVASAVSGTGH--ALGIVPIGTGNLFARNMGIPVDDIDAALTVATS 161
Cdd:PRK13337 38 HATTGPGDATLAAERAVERKFDLVIAAGGDGTLNEVVNGIAEKENrpKLGIIPVGTTNDFARALHVPRDIEKAADVIIEG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307891685 162 HgSRMVDMGRLTlldhpeddhGHAFLIIAGIGFDAAMIDDTDPDLKANISWLAYFVGGVKNLfaPKFRGNLTVTSADGST 241
Cdd:PRK13337 118 H-TVPVDIGKAN---------NRYFINIAGGGRLTELTYEVPSKLKTMLGQLAYYLKGIEML--PSLKATDVRIEYDGKL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1307891685 242 HTTNNLAFrtvMAGNCGQIPVFS-LMPAASYDDGILDFEIIDTT 284
Cdd:PRK13337 186 FQGEIMLF---LLGLTNSVGGFEkLAPDASLDDGYFDLIIVKKA 226
|
|
| PRK11914 |
PRK11914 |
diacylglycerol kinase; Reviewed |
91-203 |
8.67e-15 |
|
diacylglycerol kinase; Reviewed
Pssm-ID: 237021 [Multi-domain] Cd Length: 306 Bit Score: 74.44 E-value: 8.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307891685 91 DGRDCALEALEDGADVVIAVGGDGTVRTVASAVSGTGHALGIVPIGTGNLFARNMGIPVDDIDAALTVATSHGSRMVDMG 170
Cdd:PRK11914 52 DARHLVAAALAKGTDALVVVGGDGVISNALQVLAGTDIPLGIIPAGTGNDHAREFGIPTGDPEAAADVIVDGWTETVDLG 131
|
90 100 110
....*....|....*....|....*....|....
gi 1307891685 171 RLTLldhpeDDHGHA-FLIIAGIGFDAAMIDDTD 203
Cdd:PRK11914 132 RIQD-----DDGIVKwFGTVAATGFDSLVTDRAN 160
|
|
| PRK13059 |
PRK13059 |
putative lipid kinase; Reviewed |
89-281 |
2.19e-14 |
|
putative lipid kinase; Reviewed
Pssm-ID: 183858 Cd Length: 295 Bit Score: 73.15 E-value: 2.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307891685 89 DKDGRDCALEALEDGADVVIAVGGDGTVRTVASAVSGTGHAL--GIVPIGTGNLFARNMGIPvDDIDAALTVATSHGSRM 166
Cdd:PRK13059 42 LEYDLKNAFKDIDESYKYILIAGGDGTVDNVVNAMKKLNIDLpiGILPVGTANDFAKFLGMP-TDIGEACEQILKSKPKK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307891685 167 VDMGRLtlldhpeDDhgHAFLIIAGIGFDAAMIDDTDPDLKANISWLAYFVGGVKNLfaPKFRG-NLTVTSA----DGST 241
Cdd:PRK13059 121 VDLGKI-------ND--KYFINVASTGLFTDVSQKTDVNLKNTIGKLAYYLKGLEEL--PNFRKlKVKVTSEevnfDGDM 189
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1307891685 242 HTTnnLAFRTVMAGNcgqipvFSLMPAASYDDGILDFEII 281
Cdd:PRK13059 190 YLM--LVFNGQTAGN------FNLAYKAEVDDGLLDVIII 221
|
|
| PRK13055 |
PRK13055 |
putative lipid kinase; Reviewed |
93-294 |
1.48e-11 |
|
putative lipid kinase; Reviewed
Pssm-ID: 237282 [Multi-domain] Cd Length: 334 Bit Score: 65.01 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307891685 93 RDCALEALEDGADVVIAVGGDGTVRTVASAVSGTGH--ALGIVPIGTGNLFARNMGIPVDDIDAALTVATSHGSRMVDMG 170
Cdd:PRK13055 49 KNEAKRAAEAGFDLIIAAGGDGTINEVVNGIAPLEKrpKMAIIPAGTTNDYARALKIPRDNPVEAAKVILKNQTIKMDIG 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307891685 171 RLtlldhpedDHGHAFLIIAGIGFDAAMIDDTDPDLKANISWLAYFVGGVKNLfaPKFRGNLTVTSADGSTHTTNNLAFR 250
Cdd:PRK13055 129 RA--------NEDKYFINIAAGGSLTELTYSVPSQLKSMFGYLAYLAKGAELL--PRVSPVPVRITYDEGVFEGKISMFF 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1307891685 251 TVMAGNCGQIPvfSLMPAASYDDGIldFEIIdttggILGWANLF 294
Cdd:PRK13055 199 LALTNSVGGFE--QIVPDAKLDDGK--FTLI-----IVKTANLF 233
|
|
| DAGKc |
smart00046 |
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ... |
69-148 |
9.76e-08 |
|
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: 50.37 E-value: 9.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307891685 69 IQEFCKAkgLNRVRFYDTqlDKDGRDCALEALEDGAD--VVIAVGGDGTVRTVASAVS-----GTGHALGIVPIGTGNLF 141
Cdd:smart00046 17 LRKFRLL--LNPRQVFDL--TKKGPAVALVIFRDVPDfnRVLVCGGDGTVGWVLNALDkrelpLPEPPVAVLPLGTGNDL 92
|
....*..
gi 1307891685 142 ARNMGIP 148
Cdd:smart00046 93 ARSLGWG 99
|
|
| NadK |
COG0061 |
NAD kinase [Coenzyme transport and metabolism]; |
52-156 |
9.36e-07 |
|
NAD kinase [Coenzyme transport and metabolism];
Pssm-ID: 439831 [Multi-domain] Cd Length: 279 Bit Score: 49.75 E-value: 9.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307891685 52 AFVVNPSKPQATARRLHIQEFCKAKGLNRVRFYDTQLDKdgrdCALEALEDGADVVIAVGGDGTVRTVASAVSGTGhaLG 131
Cdd:COG0061 5 AIVAKPGKPEALEAAEELAELLEERGIEVVLDEDTAVPG----VPLEELGEEADLVIVLGGDGTLLRAARLLAPLG--IP 78
|
90 100
....*....|....*....|....*....
gi 1307891685 132 IVPIGTGNLfarnmG----IPVDDIDAAL 156
Cdd:COG0061 79 ILGINLGRL-----GflteIEPEELEEAL 102
|
|
| NAD_kinase |
pfam01513 |
ATP-NAD kinase N-terminal domain; Members of this family include ATP-NAD kinases EC:2.7.1.23, ... |
33-140 |
1.27e-04 |
|
ATP-NAD kinase N-terminal domain; Members of this family include ATP-NAD kinases EC:2.7.1.23, which catalyzes the phosphorylation of NAD to NADP utilizing ATP and other nucleoside triphosphates as well as inorganic polyphosphate as a source of phosphorus. Also includes NADH kinases EC:2.7.1.86.
Pssm-ID: 426300 [Multi-domain] Cd Length: 128 Bit Score: 41.58 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307891685 33 RRRKLAETLEKRRddevqyAFVVNPSKPQATARRLHIQEFCKAKGLNRVRFYDTQLDkdgrdcALEALEDGADVVIAVGG 112
Cdd:pfam01513 15 RAREVARWLLDRL------GITVTVEEKMGESLAFAAGDRPEVIGCLKKVVDDTRRA------TRAFADAGVDLIIVLGG 82
|
90 100
....*....|....*....|....*...
gi 1307891685 113 DGTVRTVASAVsgTGHALGIVPIGTGNL 140
Cdd:pfam01513 83 DGTALRAARLL--QKAVIPILGVNTGVL 108
|
|
| COG3199 |
COG3199 |
NAD kinase [Nucleotide transport and metabolism]; |
91-137 |
7.80e-04 |
|
NAD kinase [Nucleotide transport and metabolism];
Pssm-ID: 442432 [Multi-domain] Cd Length: 367 Bit Score: 41.41 E-value: 7.80e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1307891685 91 DGRDCALEALEDGADVVIAVGGDGTVRTVASAVSGTGHALGIvPIGT 137
Cdd:COG3199 93 DTRRAARAMLEAGVDLIVFLGGDGTARDVAKAVGDSVPVLGI-PAGV 138
|
|
|