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Conserved domains on  [gi|585133314|gb|AHJ21784|]
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putative secreted protein with presumed diacylglycerol kinase catalytic domain [Bifidobacterium breve NCFB 2258]

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 \tphospholipid 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, ...
51-362 4.09e-70

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


:

Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 222.42  E-value: 4.09e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585133314  51 YAFVVNPSKPQATARRL--HIQEFCKAKGLnRVRFYDTQLDKDGRDCALEALEDGADVVIAVGGDGTVRTVASAVSGTGH 128
Cdd:COG1597    5 ALLIVNPASGRGRAARLleRLVAALRAAGL-EVEVLETESPGDATELAREAAAEGADLVVAAGGDGTVNEVANGLAGTGP 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585133314 129 ALGIVPIGTGNLFARNMGIPVdDIDAALTVATSHGSRMVDMGRLTlldhpeddhGHAFLIIAGIGFDAAMIDDTDPDLKA 208
Cdd:COG1597   84 PLGILPLGTGNDFARALGIPL-DPEAALEALLTGRTRRIDLGRVN---------GRYFLNVAGIGFDAEVVERANRALKR 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585133314 209 NISWLAYFVGGVKNLFapKFRGNLTVISADGSTHTTNnlaFRTVMAGNCGQIP-VFSLMPAASYDDGILDFEIIdTTGGI 287
Cdd:COG1597  154 RLGKLAYVLAALRALL--RYRPFRLRIELDGEEIEGE---ALLVAVGNGPYYGgGLRLAPDASLDDGLLDVVVV-RPLSR 227
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 585133314 288 LGWANLFGDVVHQTIIGKPEqnplstnstIEQVQGLSAEIVLEKPAKAQVDGDMLPETKHIRFSVDHRALIVRVP 362
Cdd:COG1597  228 LRLLRLLPRLLRGRHLRHPG---------VRYFRAREVEIESDRPLPVQLDGEPLGLATPLEFEVLPGALRVLVP 293
 
Name Accession Description Interval E-value
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
51-362 4.09e-70

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


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 222.42  E-value: 4.09e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585133314  51 YAFVVNPSKPQATARRL--HIQEFCKAKGLnRVRFYDTQLDKDGRDCALEALEDGADVVIAVGGDGTVRTVASAVSGTGH 128
Cdd:COG1597    5 ALLIVNPASGRGRAARLleRLVAALRAAGL-EVEVLETESPGDATELAREAAAEGADLVVAAGGDGTVNEVANGLAGTGP 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585133314 129 ALGIVPIGTGNLFARNMGIPVdDIDAALTVATSHGSRMVDMGRLTlldhpeddhGHAFLIIAGIGFDAAMIDDTDPDLKA 208
Cdd:COG1597   84 PLGILPLGTGNDFARALGIPL-DPEAALEALLTGRTRRIDLGRVN---------GRYFLNVAGIGFDAEVVERANRALKR 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585133314 209 NISWLAYFVGGVKNLFapKFRGNLTVISADGSTHTTNnlaFRTVMAGNCGQIP-VFSLMPAASYDDGILDFEIIdTTGGI 287
Cdd:COG1597  154 RLGKLAYVLAALRALL--RYRPFRLRIELDGEEIEGE---ALLVAVGNGPYYGgGLRLAPDASLDDGLLDVVVV-RPLSR 227
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 585133314 288 LGWANLFGDVVHQTIIGKPEqnplstnstIEQVQGLSAEIVLEKPAKAQVDGDMLPETKHIRFSVDHRALIVRVP 362
Cdd:COG1597  228 LRLLRLLPRLLRGRHLRHPG---------VRYFRAREVEIESDRPLPVQLDGEPLGLATPLEFEVLPGALRVLVP 293
PRK00861 PRK00861
putative lipid kinase; Reviewed
84-362 2.99e-33

putative lipid kinase; Reviewed


Pssm-ID: 234850 [Multi-domain]  Cd Length: 300  Bit Score: 125.89  E-value: 2.99e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585133314  84 YDTQLDKDGRDCALEALEDGADVVIAVGGDGTVRTVASAVSGTGHALGIVPIGTGNLFARNMGIPvDDIDAALTVATSHG 163
Cdd:PRK00861  38 YLTTPEIGADQLAQEAIERGAELIIASGGDGTLSAVAGALIGTDIPLGIIPRGTANAFAAALGIP-DTIEEACRTILQGK 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585133314 164 SRMVDMGRLtlldhpeddHGHAFLIIAGIGFDAAMIDDTDPDLKANISWLAYFVGGVKNLFA-PKFRGNL----TVISAD 238
Cdd:PRK00861 117 TRRVDVAYC---------NGQPMILLAGIGFEAETVEEADREAKNRFGILAYILSGLQQLRElESFEVEIetedQIITTN 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585133314 239 GSTHTTNNLA-FRTVMAGNCGqipvfslmpAASYDDGILDFEIIDTTggilgwaNLFGDV---VH--QT-IIGKPEQNPL 311
Cdd:PRK00861 188 AVAVTVANAApPTSVLAQGPG---------AVIPDDGLLDVTIVAPK-------NLAEAVaasYHllQTaLQGNPAERDD 251
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 585133314 312 STNSTIEQVQglsaeIVLEKPAKAQVDGDMLPETKhIRFSVDHRALIVRVP 362
Cdd:PRK00861 252 IGYLRAKQVK-----ITTDPPQKVVIDGEVVGTTP-IEIECLPRSLKVFAP 296
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
53-172 7.73e-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: 106.13  E-value: 7.73e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585133314   53 FVVNPSKPQATARRL--HIQEFCKAKGLnRVRFYDTQLDKDGRDCALEALEDGADVVIAVGGDGTVRTVASAVSGTGH-- 128
Cdd:pfam00781   4 VIVNPKSGGGKGKKLlrKVRPLLNKAGV-EVELVLTEGPGDALELAREAAEDGYDRIVVAGGDGTVNEVLNGLAGLATrp 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 585133314  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 1.76e-18

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: 84.86  E-value: 1.76e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585133314   98 EALEDGADVVIAVGGDGTVRTVASAVSGTGH--ALGIVPIGTGNLFARNMGIPvDDIDAALTVATSHGSRMVDMGRLTLL 175
Cdd:TIGR00147  52 EARKFGVDTVIAGGGDGTINEVVNALIQLDDipALGILPLGTANDFARSLGIP-EDLDKAAKLVIAGDARAIDMGQVNKQ 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585133314  176 dhpeddhgHAFLIIAGIGFDAAMIDDTDPDLKANISWLAYFVGGVKNLfaPKFRGNLTVISADGSTHTTNNLAFrTVMAG 255
Cdd:TIGR00147 131 --------YCFINMAGGGFGTEITTETPEKLKAALGSLSYILSGLMRM--DTLQPFRCEIRGEGEHWQGEAVVF-LVGNG 199
                         170       180       190
                  ....*....|....*....|....*....|..
gi 585133314  256 N---CGQIPvfslMPAASYDDGILDFEIIDTT 284
Cdd:TIGR00147 200 RqagGGQKL----APDASINDGLLDLRIFTND 227
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
69-148 1.05e-07

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: 1.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585133314    69 IQEFCKAkgLNRVRFYDTqlDKDGRDCALEALEDGAD--VVIAVGGDGTVRTVASAVS-----GTGHALGIVPIGTGNLF 141
Cdd:smart00046  17 LRKFRLL--LNPRQVFDL--TKKGPAVALVIFRDVPDfnRVLVCGGDGTVGWVLNALDkrelpLPEPPVAVLPLGTGNDL 92

                   ....*..
gi 585133314   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 4.09e-70

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


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 222.42  E-value: 4.09e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585133314  51 YAFVVNPSKPQATARRL--HIQEFCKAKGLnRVRFYDTQLDKDGRDCALEALEDGADVVIAVGGDGTVRTVASAVSGTGH 128
Cdd:COG1597    5 ALLIVNPASGRGRAARLleRLVAALRAAGL-EVEVLETESPGDATELAREAAAEGADLVVAAGGDGTVNEVANGLAGTGP 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585133314 129 ALGIVPIGTGNLFARNMGIPVdDIDAALTVATSHGSRMVDMGRLTlldhpeddhGHAFLIIAGIGFDAAMIDDTDPDLKA 208
Cdd:COG1597   84 PLGILPLGTGNDFARALGIPL-DPEAALEALLTGRTRRIDLGRVN---------GRYFLNVAGIGFDAEVVERANRALKR 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585133314 209 NISWLAYFVGGVKNLFapKFRGNLTVISADGSTHTTNnlaFRTVMAGNCGQIP-VFSLMPAASYDDGILDFEIIdTTGGI 287
Cdd:COG1597  154 RLGKLAYVLAALRALL--RYRPFRLRIELDGEEIEGE---ALLVAVGNGPYYGgGLRLAPDASLDDGLLDVVVV-RPLSR 227
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 585133314 288 LGWANLFGDVVHQTIIGKPEqnplstnstIEQVQGLSAEIVLEKPAKAQVDGDMLPETKHIRFSVDHRALIVRVP 362
Cdd:COG1597  228 LRLLRLLPRLLRGRHLRHPG---------VRYFRAREVEIESDRPLPVQLDGEPLGLATPLEFEVLPGALRVLVP 293
PRK00861 PRK00861
putative lipid kinase; Reviewed
84-362 2.99e-33

putative lipid kinase; Reviewed


Pssm-ID: 234850 [Multi-domain]  Cd Length: 300  Bit Score: 125.89  E-value: 2.99e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585133314  84 YDTQLDKDGRDCALEALEDGADVVIAVGGDGTVRTVASAVSGTGHALGIVPIGTGNLFARNMGIPvDDIDAALTVATSHG 163
Cdd:PRK00861  38 YLTTPEIGADQLAQEAIERGAELIIASGGDGTLSAVAGALIGTDIPLGIIPRGTANAFAAALGIP-DTIEEACRTILQGK 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585133314 164 SRMVDMGRLtlldhpeddHGHAFLIIAGIGFDAAMIDDTDPDLKANISWLAYFVGGVKNLFA-PKFRGNL----TVISAD 238
Cdd:PRK00861 117 TRRVDVAYC---------NGQPMILLAGIGFEAETVEEADREAKNRFGILAYILSGLQQLRElESFEVEIetedQIITTN 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585133314 239 GSTHTTNNLA-FRTVMAGNCGqipvfslmpAASYDDGILDFEIIDTTggilgwaNLFGDV---VH--QT-IIGKPEQNPL 311
Cdd:PRK00861 188 AVAVTVANAApPTSVLAQGPG---------AVIPDDGLLDVTIVAPK-------NLAEAVaasYHllQTaLQGNPAERDD 251
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 585133314 312 STNSTIEQVQglsaeIVLEKPAKAQVDGDMLPETKhIRFSVDHRALIVRVP 362
Cdd:PRK00861 252 IGYLRAKQVK-----ITTDPPQKVVIDGEVVGTTP-IEIECLPRSLKVFAP 296
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
53-172 7.73e-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: 106.13  E-value: 7.73e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585133314   53 FVVNPSKPQATARRL--HIQEFCKAKGLnRVRFYDTQLDKDGRDCALEALEDGADVVIAVGGDGTVRTVASAVSGTGH-- 128
Cdd:pfam00781   4 VIVNPKSGGGKGKKLlrKVRPLLNKAGV-EVELVLTEGPGDALELAREAAEDGYDRIVVAGGDGTVNEVLNGLAGLATrp 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 585133314  129 ALGIVPIGTGNLFARNMGIPVdDIDAALTVATSHGSRMVDMGRL 172
Cdd:pfam00781  83 PLGIIPLGTGNDFARALGIPG-DPEEALEAILKGQTRPVDVGKV 125
PRK13054 PRK13054
lipid kinase; Reviewed
98-367 8.07e-22

lipid kinase; Reviewed


Pssm-ID: 237281 [Multi-domain]  Cd Length: 300  Bit Score: 94.55  E-value: 8.07e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585133314  98 EALEDGADVVIAVGGDGTVRTVASAVSGTGH----ALGIVPIGTGNLFARNMGIPvDDIDAALTVATSHGSRMVDMGRLt 173
Cdd:PRK13054  51 EALALGVATVIAGGGDGTINEVATALAQLEGdarpALGILPLGTANDFATAAGIP-LEPDKALKLAIEGRAQPIDLARV- 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585133314 174 lldhpeDDHgHAFLIIAGIGFDAAMIDDTDPDLKANISWLAYFVGGVKNLfapkfrgnLTVISADGSTHT---TNNLAFR 250
Cdd:PRK13054 129 ------NDR-TYFINMATGGFGTRVTTETPEKLKAALGGVAYLIHGLMRM--------DTLKPDRCEIRGpdfHWQGDAL 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585133314 251 TVMAGNC-----GQIpvfsLMPAASYDDGILDFEIIDTTGGILGwanlfgdVVHQTIIGKPEQNPLSTNSTIEQVqglsa 325
Cdd:PRK13054 194 VIGIGNGrqaggGQQ----LCPEALINDGLLDLRILPAPQELLP-------TLLSTLTGGSEDNPNIIRARLPWL----- 257
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 585133314 326 EIVLEKPAKAQVDGDMLpETKHIRFSVDHRALIVRVPDTSAL 367
Cdd:PRK13054 258 EIQAPHELTFNLDGEPL-SGRHFRIEVLPAALRCRLPPDCPL 298
PRK13057 PRK13057
lipid kinase;
91-278 6.14e-21

lipid kinase;


Pssm-ID: 183857 [Multi-domain]  Cd Length: 287  Bit Score: 91.90  E-value: 6.14e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585133314  91 DGRDCA--LEALEDGADVVIAVGGDGTVRTVASAVSGTGHALGIVPIGTGNLFARNMGIPVDDIDAALTVATSHgSRMVD 168
Cdd:PRK13057  36 DPDDLSevIEAYADGVDLVIVGGGDGTLNAAAPALVETGLPLGILPLGTANDLARTLGIPLDLEAAARVIATGQ-VRRID 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585133314 169 MGRLtlldhpeddHGHAFLIIAGIGFDAAMIDDTDPDLKANISWLAYFVGGVKNLF-APKFRgnlTVISADGSThttnnL 247
Cdd:PRK13057 115 LGWV---------NGHYFFNVASLGLSAELARRLTKELKRRWGTLGYAIAALRVLRrSRPFT---AEIEHDGRT-----E 177
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 585133314 248 AFRTVMA--GN----CGQIPVFslmPAASYDDGILDF 278
Cdd:PRK13057 178 RVKTLQVavGNgryyGGGMTVA---HDATIDDGRLDL 211
TIGR00147 TIGR00147
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ...
98-284 1.76e-18

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: 84.86  E-value: 1.76e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585133314   98 EALEDGADVVIAVGGDGTVRTVASAVSGTGH--ALGIVPIGTGNLFARNMGIPvDDIDAALTVATSHGSRMVDMGRLTLL 175
Cdd:TIGR00147  52 EARKFGVDTVIAGGGDGTINEVVNALIQLDDipALGILPLGTANDFARSLGIP-EDLDKAAKLVIAGDARAIDMGQVNKQ 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585133314  176 dhpeddhgHAFLIIAGIGFDAAMIDDTDPDLKANISWLAYFVGGVKNLfaPKFRGNLTVISADGSTHTTNNLAFrTVMAG 255
Cdd:TIGR00147 131 --------YCFINMAGGGFGTEITTETPEKLKAALGSLSYILSGLMRM--DTLQPFRCEIRGEGEHWQGEAVVF-LVGNG 199
                         170       180       190
                  ....*....|....*....|....*....|..
gi 585133314  256 N---CGQIPvfslMPAASYDDGILDFEIIDTT 284
Cdd:TIGR00147 200 RqagGGQKL----APDASINDGLLDLRIFTND 227
PRK12361 PRK12361
hypothetical protein; Provisional
86-365 1.87e-18

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 86.98  E-value: 1.87e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585133314  86 TQLDKDGRDCALEALEDGADVVIAVGGDGTVRTVASAVSGTGHALGIVPIGTGN-----LF-ARNMGIPVDdiDAALTVA 159
Cdd:PRK12361 280 TTPEISAEALAKQARKAGADIVIACGGDGTVTEVASELVNTDITLGIIPLGTANalshaLFgLGSKLIPVE--QACDNII 357
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585133314 160 TSHgSRMVDMGRLtlldhpeddHGHAFLIIAGIGFDAAMIDDTDPDLKANISWLAYFVG---GVKNLFAPKFRgnLTVIS 236
Cdd:PRK12361 358 QGH-TQRIDTARC---------NDRLMLLLVGIGFEQKMIESADRERKNALGQLAYLDGlwrAVNENETLTLT--VTLDD 425
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585133314 237 ADGSTHTTNNLA------FRTVMAGNCGQiPVfslmpaasYDDGILDFEIIDTTGGILGWANLFGDVVHQTIIGKPEqnp 310
Cdd:PRK12361 426 AEPQTISTHSLVvanaapFTSLLAQGGGE-PN--------MTDGLLDITWLDSGGEPGEQLLSLAELALSGLGKEPE--- 493
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 585133314 311 lstNSTIEQVQGLSAEIVLEKPAKAQVDGDmLPETKHIRFSVDHRALIVRVPDTS 365
Cdd:PRK12361 494 ---ANKVHHAHAKKVTISSQKPIKYVIDGE-LFEDEDLTIEVQPASLKVFVPYQE 544
PRK13337 PRK13337
putative lipid kinase; Reviewed
84-284 6.57e-18

putative lipid kinase; Reviewed


Pssm-ID: 183982 [Multi-domain]  Cd Length: 304  Bit Score: 83.56  E-value: 6.57e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585133314  84 YDTQLDKDGRDCALEALEDGADVVIAVGGDGTVRTVASAVSGTGH--ALGIVPIGTGNLFARNMGIPVDDIDAALTVATS 161
Cdd:PRK13337  38 HATTGPGDATLAAERAVERKFDLVIAAGGDGTLNEVVNGIAEKENrpKLGIIPVGTTNDFARALHVPRDIEKAADVIIEG 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585133314 162 HgSRMVDMGRLTlldhpeddhGHAFLIIAGIGFDAAMIDDTDPDLKANISWLAYFVGGVKNLfaPKFRGNLTVISADGST 241
Cdd:PRK13337 118 H-TVPVDIGKAN---------NRYFINIAGGGRLTELTYEVPSKLKTMLGQLAYYLKGIEML--PSLKATDVRIEYDGKL 185
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 585133314 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 585133314  91 DGRDCALEALEDGADVVIAVGGDGTVRTVASAVSGTGHALGIVPIGTGNLFARNMGIPVDDIDAALTVATSHGSRMVDMG 170
Cdd:PRK11914  52 DARHLVAAALAKGTDALVVVGGDGVISNALQVLAGTDIPLGIIPAGTGNDHAREFGIPTGDPEAAADVIVDGWTETVDLG 131
                         90       100       110
                 ....*....|....*....|....*....|....
gi 585133314 171 RLTLldhpeDDHGHA-FLIIAGIGFDAAMIDDTD 203
Cdd:PRK11914 132 RIQD-----DDGIVKwFGTVAATGFDSLVTDRAN 160
PRK13059 PRK13059
putative lipid kinase; Reviewed
89-281 9.18e-14

putative lipid kinase; Reviewed


Pssm-ID: 183858  Cd Length: 295  Bit Score: 71.22  E-value: 9.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585133314  89 DKDGRDCALEALEDGADVVIAVGGDGTVRTVASAVSGTGHAL--GIVPIGTGNLFARNMGIPvDDIDAALTVATSHGSRM 166
Cdd:PRK13059  42 LEYDLKNAFKDIDESYKYILIAGGDGTVDNVVNAMKKLNIDLpiGILPVGTANDFAKFLGMP-TDIGEACEQILKSKPKK 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585133314 167 VDMGRLtlldhpeDDhgHAFLIIAGIGFDAAMIDDTDPDLKANISWLAYFVGGVKNLfaPKFRGNLTVISADGSTHTTNN 246
Cdd:PRK13059 121 VDLGKI-------ND--KYFINVASTGLFTDVSQKTDVNLKNTIGKLAYYLKGLEEL--PNFRKLKVKVTSEEVNFDGDM 189
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 585133314 247 ---LAFRTVMAGNcgqipvFSLMPAASYDDGILDFEII 281
Cdd:PRK13059 190 ylmLVFNGQTAGN------FNLAYKAEVDDGLLDVIII 221
PRK13055 PRK13055
putative lipid kinase; Reviewed
93-294 1.66e-12

putative lipid kinase; Reviewed


Pssm-ID: 237282 [Multi-domain]  Cd Length: 334  Bit Score: 67.71  E-value: 1.66e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585133314  93 RDCALEALEDGADVVIAVGGDGTVRTVASAVSGTGH--ALGIVPIGTGNLFARNMGIPVDDIDAALTVATSHGSRMVDMG 170
Cdd:PRK13055  49 KNEAKRAAEAGFDLIIAAGGDGTINEVVNGIAPLEKrpKMAIIPAGTTNDYARALKIPRDNPVEAAKVILKNQTIKMDIG 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585133314 171 RLtlldhpedDHGHAFLIIAGIGFDAAMIDDTDPDLKANISWLAYFVGGVKNLfaPKFRGNLTVISADGSTHTTNNLAFR 250
Cdd:PRK13055 129 RA--------NEDKYFINIAAGGSLTELTYSVPSQLKSMFGYLAYLAKGAELL--PRVSPVPVRITYDEGVFEGKISMFF 198
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 585133314 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 1.05e-07

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: 1.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585133314    69 IQEFCKAkgLNRVRFYDTqlDKDGRDCALEALEDGAD--VVIAVGGDGTVRTVASAVS-----GTGHALGIVPIGTGNLF 141
Cdd:smart00046  17 LRKFRLL--LNPRQVFDL--TKKGPAVALVIFRDVPDfnRVLVCGGDGTVGWVLNALDkrelpLPEPPVAVLPLGTGNDL 92

                   ....*..
gi 585133314   142 ARNMGIP 148
Cdd:smart00046  93 ARSLGWG 99
NadK COG0061
NAD kinase [Coenzyme transport and metabolism];
52-156 1.03e-06

NAD kinase [Coenzyme transport and metabolism];


Pssm-ID: 439831 [Multi-domain]  Cd Length: 279  Bit Score: 49.75  E-value: 1.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585133314  52 AFVVNPSKPQATARRLHIQEFCKAKGLNRVRFYDTQLDKdgrdCALEALEDGADVVIAVGGDGTVRTVASAVSGTGhaLG 131
Cdd:COG0061    5 AIVAKPGKPEALEAAEELAELLEERGIEVVLDEDTAVPG----VPLEELGEEADLVIVLGGDGTLLRAARLLAPLG--IP 78
                         90       100
                 ....*....|....*....|....*....
gi 585133314 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 1.33e-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: 1.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585133314   33 RRRKLAETLEKRRddevqyAFVVNPSKPQATARRLHIQEFCKAKGLNRVRFYDTQLDkdgrdcALEALEDGADVVIAVGG 112
Cdd:pfam01513  15 RAREVARWLLDRL------GITVTVEEKMGESLAFAAGDRPEVIGCLKKVVDDTRRA------TRAFADAGVDLIIVLGG 82
                          90       100
                  ....*....|....*....|....*...
gi 585133314  113 DGTVRTVASAVsgTGHALGIVPIGTGNL 140
Cdd:pfam01513  83 DGTALRAARLL--QKAVIPILGVNTGVL 108
COG3199 COG3199
NAD kinase [Nucleotide transport and metabolism];
91-137 8.00e-04

NAD kinase [Nucleotide transport and metabolism];


Pssm-ID: 442432 [Multi-domain]  Cd Length: 367  Bit Score: 41.02  E-value: 8.00e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 585133314  91 DGRDCALEALEDGADVVIAVGGDGTVRTVASAVSGTGHALGIvPIGT 137
Cdd:COG3199   93 DTRRAARAMLEAGVDLIVFLGGDGTARDVAKAVGDSVPVLGI-PAGV 138
 
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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