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Conserved domains on  [gi|1002302025|ref|XP_015614395|]
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sphingoid long-chain bases kinase 1 [Oryza sativa Japonica Group]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
234-365 1.78e-38

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: 138.87  E-value: 1.78e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302025 234 KILVILNPRSGHGRSSKVFHgKVEPIFKLAGFKMEVVKTTHAGHAKSLVSTIDFSTcPDGIVCVGGDGIVNEVLNGLLCR 313
Cdd:pfam00781   1 KLLVIVNPKSGGGKGKKLLR-KVRPLLNKAGVEVELVLTEGPGDALELAREAAEDG-YDRIVVAGGDGTVNEVLNGLAGL 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1002302025 314 DDQnvavsVPIGIIPAGSDNSLVWTVLGVKDPISAAMSIVRGGFTPIDVFAV 365
Cdd:pfam00781  79 ATR-----PPLGIIPLGTGNDFARALGIPGDPEEALEAILKGQTRPVDVGKV 125
YegS_C super family cl29908
YegS C-terminal NAD kinase beta sandwich-like domain; This entry represents the C-terminal ...
661-749 1.49e-04

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.


The actual alignment was detected with superfamily member pfam19279:

Pssm-ID: 453080  Cd Length: 158  Bit Score: 42.95  E-value: 1.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302025 661 IAPKAEYDDNCLDLLLVGGSGRLRLLKFLVLLQFGKHISLPNVEYLKVKSVRLKA-GPNTHDGcgiDGELLHVkGQVRCS 739
Cdd:pfam19279  73 IAPDARVDDGLLDVVVIEAASRRTLLRLLPKVYDGRHVRLPQVEVLRGREVRIEAdRPLPAGA---DGEVLGP-LPVRVE 148
                          90
                  ....*....|
gi 1002302025 740 LLPQQCRLIG 749
Cdd:pfam19279 149 VLPGALRVLA 158
 
Name Accession Description Interval E-value
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
234-365 1.78e-38

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: 138.87  E-value: 1.78e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302025 234 KILVILNPRSGHGRSSKVFHgKVEPIFKLAGFKMEVVKTTHAGHAKSLVSTIDFSTcPDGIVCVGGDGIVNEVLNGLLCR 313
Cdd:pfam00781   1 KLLVIVNPKSGGGKGKKLLR-KVRPLLNKAGVEVELVLTEGPGDALELAREAAEDG-YDRIVVAGGDGTVNEVLNGLAGL 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1002302025 314 DDQnvavsVPIGIIPAGSDNSLVWTVLGVKDPISAAMSIVRGGFTPIDVFAV 365
Cdd:pfam00781  79 ATR-----PPLGIIPLGTGNDFARALGIPGDPEEALEAILKGQTRPVDVGKV 125
PLN02958 PLN02958
diacylglycerol kinase/D-erythro-sphingosine kinase
232-426 7.23e-33

diacylglycerol kinase/D-erythro-sphingosine kinase


Pssm-ID: 215517 [Multi-domain]  Cd Length: 481  Bit Score: 133.06  E-value: 7.23e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302025 232 PPKILVILNPRSGHGRSSKVFHGKVEPIFKLAGFKMEVVKTTHAGHAKSLVSTIDFSTCpDGIVCVGGDGIVNEVLNGLL 311
Cdd:PLN02958  111 PKRLLVFVNPFGGKKSASKIFFDVVKPLLEDADIQLTIQETKYQLHAKEVVRTMDLSKY-DGIVCVSGDGILVEVVNGLL 189
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302025 312 CRDDQNVAVSVPIGIIPAGSDNSLVWTVL-GVKDPISAA---MSIVRGGFTPIDVFAVewIQSGTIHFGTTVSYFGFVSD 387
Cdd:PLN02958  190 EREDWKTAIKLPIGMVPAGTGNGMAKSLLdSVGEPCSATnavLAIIRGHKCSLDVATI--LQGETKFFSVLMLAWGLVAD 267
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1002302025 388 VLELSERYqKRFGPLRYFVAGFLKFLCLPKYNFELEYLP 426
Cdd:PLN02958  268 IDIESEKY-RWMGSARLDFYGLQRILCLRQYNGRISFVP 305
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
231-438 3.04e-31

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


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 124.19  E-value: 3.04e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302025 231 SPPKILVILNPRSGHGRSSKVFhGKVEPIFKLAGFKMEVVKTTHAGHAKSLVSTIDFSTcPDGIVCVGGDGIVNEVLNGL 310
Cdd:COG1597     1 AMMRALLIVNPASGRGRAARLL-ERLVAALRAAGLEVEVLETESPGDATELAREAAAEG-ADLVVAAGGDGTVNEVANGL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302025 311 LCRDdqnvavsVPIGIIPAGSDNSLVWTvLGV-KDPISAAMSIVRGGFTPIDVFAVewiqsGTIHFGTTVSyFGFVSDVL 389
Cdd:COG1597    79 AGTG-------PPLGILPLGTGNDFARA-LGIpLDPEAALEALLTGRTRRIDLGRV-----NGRYFLNVAG-IGFDAEVV 144
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1002302025 390 ELSERYQK-RFGPLRYFVAGFLKFLCLPKYNFELEYlpisDGGGGEHKIV 438
Cdd:COG1597   145 ERANRALKrRLGKLAYVLAALRALLRYRPFRLRIEL----DGEEIEGEAL 190
TIGR00147 TIGR00147
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ...
234-424 2.17e-14

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: 74.46  E-value: 2.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302025 234 KILVILNPRSGHGRSSKVFhGKVEPIFKLAGFKMEVVKTTHAGHAKSLVSTI-DFSTcpDGIVCVGGDGIVNEVLNGLLC 312
Cdd:TIGR00147   3 EAPAILNPTAGKSNDNKPL-REVIMLLREEGMEIHVRVTWEKGDAARYVEEArKFGV--DTVIAGGGDGTINEVVNALIQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302025 313 RDDQNVavsvpIGIIPAGSDNSLVwTVLGVK-DPISAAMSIVRGGFTPIDVFAV----EWIQSGTIHFGTTVSYfgfvsd 387
Cdd:TIGR00147  80 LDDIPA-----LGILPLGTANDFA-RSLGIPeDLDKAAKLVIAGDARAIDMGQVnkqyCFINMAGGGFGTEITT------ 147
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1002302025 388 vlELSERYQKRFGPLRYFVAGFLKFLCLPKYNFELEY 424
Cdd:TIGR00147 148 --ETPEKLKAALGSLSYILSGLMRMDTLQPFRCEIRG 182
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
236-355 2.72e-12

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: 64.24  E-value: 2.72e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302025  236 LVILNPRSGHGRsskvfHGKVEPIFKLAGFKMEVVKTTHAGHAKSLVSTIDFStCPDGIVCVGGDGIVNEVLNGLLCRDD 315
Cdd:smart00046   1 LVFVNPKSGGGK-----GEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVP-DFNRVLVCGGDGTVGWVLNALDKREL 74
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1002302025  316 QnvAVSVPIGIIPAGSDN----SLVW-TVLGVKDPISAAMSIVRG 355
Cdd:smart00046  75 P--LPEPPVAVLPLGTGNdlarSLGWgGGYDGEKLLKTLRDALES 117
YegS_C pfam19279
YegS C-terminal NAD kinase beta sandwich-like domain; This entry represents the C-terminal ...
661-749 1.49e-04

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: 42.95  E-value: 1.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302025 661 IAPKAEYDDNCLDLLLVGGSGRLRLLKFLVLLQFGKHISLPNVEYLKVKSVRLKA-GPNTHDGcgiDGELLHVkGQVRCS 739
Cdd:pfam19279  73 IAPDARVDDGLLDVVVIEAASRRTLLRLLPKVYDGRHVRLPQVEVLRGREVRIEAdRPLPAGA---DGEVLGP-LPVRVE 148
                          90
                  ....*....|
gi 1002302025 740 LLPQQCRLIG 749
Cdd:pfam19279 149 VLPGALRVLA 158
 
Name Accession Description Interval E-value
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
234-365 1.78e-38

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: 138.87  E-value: 1.78e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302025 234 KILVILNPRSGHGRSSKVFHgKVEPIFKLAGFKMEVVKTTHAGHAKSLVSTIDFSTcPDGIVCVGGDGIVNEVLNGLLCR 313
Cdd:pfam00781   1 KLLVIVNPKSGGGKGKKLLR-KVRPLLNKAGVEVELVLTEGPGDALELAREAAEDG-YDRIVVAGGDGTVNEVLNGLAGL 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1002302025 314 DDQnvavsVPIGIIPAGSDNSLVWTVLGVKDPISAAMSIVRGGFTPIDVFAV 365
Cdd:pfam00781  79 ATR-----PPLGIIPLGTGNDFARALGIPGDPEEALEAILKGQTRPVDVGKV 125
PLN02958 PLN02958
diacylglycerol kinase/D-erythro-sphingosine kinase
232-426 7.23e-33

diacylglycerol kinase/D-erythro-sphingosine kinase


Pssm-ID: 215517 [Multi-domain]  Cd Length: 481  Bit Score: 133.06  E-value: 7.23e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302025 232 PPKILVILNPRSGHGRSSKVFHGKVEPIFKLAGFKMEVVKTTHAGHAKSLVSTIDFSTCpDGIVCVGGDGIVNEVLNGLL 311
Cdd:PLN02958  111 PKRLLVFVNPFGGKKSASKIFFDVVKPLLEDADIQLTIQETKYQLHAKEVVRTMDLSKY-DGIVCVSGDGILVEVVNGLL 189
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302025 312 CRDDQNVAVSVPIGIIPAGSDNSLVWTVL-GVKDPISAA---MSIVRGGFTPIDVFAVewIQSGTIHFGTTVSYFGFVSD 387
Cdd:PLN02958  190 EREDWKTAIKLPIGMVPAGTGNGMAKSLLdSVGEPCSATnavLAIIRGHKCSLDVATI--LQGETKFFSVLMLAWGLVAD 267
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1002302025 388 VLELSERYqKRFGPLRYFVAGFLKFLCLPKYNFELEYLP 426
Cdd:PLN02958  268 IDIESEKY-RWMGSARLDFYGLQRILCLRQYNGRISFVP 305
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
231-438 3.04e-31

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


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 124.19  E-value: 3.04e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302025 231 SPPKILVILNPRSGHGRSSKVFhGKVEPIFKLAGFKMEVVKTTHAGHAKSLVSTIDFSTcPDGIVCVGGDGIVNEVLNGL 310
Cdd:COG1597     1 AMMRALLIVNPASGRGRAARLL-ERLVAALRAAGLEVEVLETESPGDATELAREAAAEG-ADLVVAAGGDGTVNEVANGL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302025 311 LCRDdqnvavsVPIGIIPAGSDNSLVWTvLGV-KDPISAAMSIVRGGFTPIDVFAVewiqsGTIHFGTTVSyFGFVSDVL 389
Cdd:COG1597    79 AGTG-------PPLGILPLGTGNDFARA-LGIpLDPEAALEALLTGRTRRIDLGRV-----NGRYFLNVAG-IGFDAEVV 144
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1002302025 390 ELSERYQK-RFGPLRYFVAGFLKFLCLPKYNFELEYlpisDGGGGEHKIV 438
Cdd:COG1597   145 ERANRALKrRLGKLAYVLAALRALLRYRPFRLRIEL----DGEEIEGEAL 190
PLN02204 PLN02204
diacylglycerol kinase
232-425 4.63e-22

diacylglycerol kinase


Pssm-ID: 215126 [Multi-domain]  Cd Length: 601  Bit Score: 101.12  E-value: 4.63e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302025 232 PPKILVILNPRSGHGRSSKVFHgKVEPIFKLAGFKMEVVKTTHAGHAKSLVSTIDFSTCP--DGIVCVGGDGIVNEVLNG 309
Cdd:PLN02204  159 PKNLLVFVHPLSGKGSGSRTWE-TVSPIFIRAKVKTKVIVTERAGHAFDVMASISNKELKsyDGVIAVGGDGFFNEILNG 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302025 310 LL--------------------------------------------------------------CRDDQNVAVSVP---- 323
Cdd:PLN02204  238 YLlsrlkvpyppspsdsvhsvqsrgsssvhepnetvhecdnedhspllsdsvqevmnfrtengsCEGDQDSDFPFPnerf 317
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302025 324 -IGIIPAGSDNSLVWTVLGVKDPISAAMSIVRGGFTPIDVF-AVEWIQSGTIHFGTTVSY------FGFVSDVLELSERY 395
Cdd:PLN02204  318 rFGIIPAGSTDAIVMCTTGERDPVTSALHIILGRRVCLDIAqVVRWKTTSTSEIEPYVRYaasfagYGFYGDVISESEKY 397
                         250       260       270
                  ....*....|....*....|....*....|
gi 1002302025 396 qKRFGPLRYFVAGFLKFLCLPKYNFELEYL 425
Cdd:PLN02204  398 -RWMGPKRYDYAGTKVFLKHRSYEAEVAYL 426
TIGR00147 TIGR00147
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ...
234-424 2.17e-14

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: 74.46  E-value: 2.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302025 234 KILVILNPRSGHGRSSKVFhGKVEPIFKLAGFKMEVVKTTHAGHAKSLVSTI-DFSTcpDGIVCVGGDGIVNEVLNGLLC 312
Cdd:TIGR00147   3 EAPAILNPTAGKSNDNKPL-REVIMLLREEGMEIHVRVTWEKGDAARYVEEArKFGV--DTVIAGGGDGTINEVVNALIQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302025 313 RDDQNVavsvpIGIIPAGSDNSLVwTVLGVK-DPISAAMSIVRGGFTPIDVFAV----EWIQSGTIHFGTTVSYfgfvsd 387
Cdd:TIGR00147  80 LDDIPA-----LGILPLGTANDFA-RSLGIPeDLDKAAKLVIAGDARAIDMGQVnkqyCFINMAGGGFGTEITT------ 147
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1002302025 388 vlELSERYQKRFGPLRYFVAGFLKFLCLPKYNFELEY 424
Cdd:TIGR00147 148 --ETPEKLKAALGSLSYILSGLMRMDTLQPFRCEIRG 182
PRK11914 PRK11914
diacylglycerol kinase; Reviewed
230-407 6.58e-14

diacylglycerol kinase; Reviewed


Pssm-ID: 237021 [Multi-domain]  Cd Length: 306  Bit Score: 73.28  E-value: 6.58e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302025 230 RSPPKILVILNPRSGHGRSSKVFHGKVEPiFKLAGFKMEVVKTTHAGHAKSLV-STIDFSTcpDGIVCVGGDGIVNEVLN 308
Cdd:PRK11914    6 HEIGKVTVLTNPLSGHGAAPHAAERAIAR-LHHRGVDVVEIVGTDAHDARHLVaAALAKGT--DALVVVGGDGVISNALQ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302025 309 GLLCRDdqnvavsVPIGIIPAGSDNSLVWTV-LGVKDPISAAMSIVRGGFTPIDVFAVEWIQSGTIHFGTTVSYfGFVSD 387
Cdd:PRK11914   83 VLAGTD-------IPLGIIPAGTGNDHAREFgIPTGDPEAAADVIVDGWTETVDLGRIQDDDGIVKWFGTVAAT-GFDSL 154
                         170       180
                  ....*....|....*....|
gi 1002302025 388 VLELSERYQKRFGPLRYFVA 407
Cdd:PRK11914  155 VTDRANRMRWPHGRMRYNLA 174
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
236-355 2.72e-12

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: 64.24  E-value: 2.72e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302025  236 LVILNPRSGHGRsskvfHGKVEPIFKLAGFKMEVVKTTHAGHAKSLVSTIDFStCPDGIVCVGGDGIVNEVLNGLLCRDD 315
Cdd:smart00046   1 LVFVNPKSGGGK-----GEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVP-DFNRVLVCGGDGTVGWVLNALDKREL 74
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1002302025  316 QnvAVSVPIGIIPAGSDN----SLVW-TVLGVKDPISAAMSIVRG 355
Cdd:smart00046  75 P--LPEPPVAVLPLGTGNdlarSLGWgGGYDGEKLLKTLRDALES 117
PRK13337 PRK13337
putative lipid kinase; Reviewed
237-424 3.28e-08

putative lipid kinase; Reviewed


Pssm-ID: 183982 [Multi-domain]  Cd Length: 304  Bit Score: 55.82  E-value: 3.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302025 237 VILNPRSGHGRSSKVFhGKVEPIFKLAGFKMEVVKTTHAG---HAKSLVSTIDFstcpDGIVCVGGDGIVNEVLNGLLCR 313
Cdd:PRK13337    6 IIYNPTSGRELFKKNL-PDVLQKLEQAGYETSAHATTGPGdatLAAERAVERKF----DLVIAAGGDGTLNEVVNGIAEK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302025 314 DDQnvavsvP-IGIIPAGSDNSLVwTVLGV-KDPISAAMSIVRGGFTPIDVFAVE---WIQ---SGTIhfgTTVSYfgfv 385
Cdd:PRK13337   81 ENR------PkLGIIPVGTTNDFA-RALHVpRDIEKAADVIIEGHTVPVDIGKANnryFINiagGGRL---TELTY---- 146
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1002302025 386 sdvlELSERYQKRFGPLRYFVAGFLKFLCLPKYNFELEY 424
Cdd:PRK13337  147 ----EVPSKLKTMLGQLAYYLKGIEMLPSLKATDVRIEY 181
PRK13057 PRK13057
lipid kinase;
236-409 1.55e-06

lipid kinase;


Pssm-ID: 183857 [Multi-domain]  Cd Length: 287  Bit Score: 50.69  E-value: 1.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302025 236 LVILNPRSGHGRSSKvfhGKVEPIFKLAGFKMEVVKTTHAGHAKSLVSTIDFSTcpDGIVCVGGDGIVNEVLNGLLCRDd 315
Cdd:PRK13057    1 LLLVNRHARSGRAAL---AAARAALEAAGLELVEPPAEDPDDLSEVIEAYADGV--DLVIVGGGDGTLNAAAPALVETG- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302025 316 qnvavsVPIGIIPAGSDNSLVWTvLGV-KDPISAAMSIVRGGFTPIDVFAVewiqSGTIHFgtTVSYFGFVSDVL-ELSE 393
Cdd:PRK13057   75 ------LPLGILPLGTANDLART-LGIpLDLEAAARVIATGQVRRIDLGWV----NGHYFF--NVASLGLSAELArRLTK 141
                         170
                  ....*....|....*.
gi 1002302025 394 RYQKRFGPLRYFVAGF 409
Cdd:PRK13057  142 ELKRRWGTLGYAIAAL 157
PRK13054 PRK13054
lipid kinase; Reviewed
232-423 6.51e-05

lipid kinase; Reviewed


Pssm-ID: 237281 [Multi-domain]  Cd Length: 300  Bit Score: 45.63  E-value: 6.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302025 232 PPKILVILNprsghGRSSkvfhGKVE---PIFKL--AGFKMEVVKTTHAGHAKSLVS---TIDFSTcpdgIVCVGGDGIV 303
Cdd:PRK13054    3 FPKSLLILN-----GKSA----GNEElreAVGLLreEGHTLHVRVTWEKGDAARYVEealALGVAT----VIAGGGDGTI 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302025 304 NEVLNGLLCRDDQNVAVsvpIGIIPAGSDNSLVwTVLGVKDPISAAMS-IVRGGFTPIDVFAVE----WIQSGTIHFGTT 378
Cdd:PRK13054   70 NEVATALAQLEGDARPA---LGILPLGTANDFA-TAAGIPLEPDKALKlAIEGRAQPIDLARVNdrtyFINMATGGFGTR 145
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1002302025 379 VSyfgfvsdvLELSERYQKRFGPLRYFVAGFLKFLCLPKYNFELE 423
Cdd:PRK13054  146 VT--------TETPEKLKAALGGVAYLIHGLMRMDTLKPDRCEIR 182
YegS_C pfam19279
YegS C-terminal NAD kinase beta sandwich-like domain; This entry represents the C-terminal ...
661-749 1.49e-04

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: 42.95  E-value: 1.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302025 661 IAPKAEYDDNCLDLLLVGGSGRLRLLKFLVLLQFGKHISLPNVEYLKVKSVRLKA-GPNTHDGcgiDGELLHVkGQVRCS 739
Cdd:pfam19279  73 IAPDARVDDGLLDVVVIEAASRRTLLRLLPKVYDGRHVRLPQVEVLRGREVRIEAdRPLPAGA---DGEVLGP-LPVRVE 148
                          90
                  ....*....|
gi 1002302025 740 LLPQQCRLIG 749
Cdd:pfam19279 149 VLPGALRVLA 158
PRK13055 PRK13055
putative lipid kinase; Reviewed
237-333 7.30e-04

putative lipid kinase; Reviewed


Pssm-ID: 237282 [Multi-domain]  Cd Length: 334  Bit Score: 42.28  E-value: 7.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302025 237 VILNPRSGHGRSSKVFhGKVEPIFKLAGFKMEVVKTTHAGHAKSLVSTIDFSTCPDGIVCVGGDGIVNEVLNGLLcrddq 316
Cdd:PRK13055    7 LIYNPTSGQEIMKKNV-ADILDILEQAGYETSAFQTTPEPNSAKNEAKRAAEAGFDLIIAAGGDGTINEVVNGIA----- 80
                          90
                  ....*....|....*..
gi 1002302025 317 NVAVSVPIGIIPAGSDN 333
Cdd:PRK13055   81 PLEKRPKMAIIPAGTTN 97
PRK13059 PRK13059
putative lipid kinase; Reviewed
234-408 7.71e-04

putative lipid kinase; Reviewed


Pssm-ID: 183858  Cd Length: 295  Bit Score: 42.33  E-value: 7.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302025 234 KILVILNPRSG-HGRSSKVfhGKVEPIFKLAGFKMEVVKTTHAGHAKSLVSTIDFSTcpDGIVCVGGDGIVNEVLNGLLC 312
Cdd:PRK13059    3 KVKFIYNPYSGeNAIISEL--DKVIRIHQEKGYLVVPYRISLEYDLKNAFKDIDESY--KYILIAGGDGTVDNVVNAMKK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302025 313 RDdqnvaVSVPIGIIPAGSDNSLVwTVLGVKDPISAAMS-IVRGGFTPIDVFAVE---WIQSGTIHFGTTVSyfgFVSDV 388
Cdd:PRK13059   79 LN-----IDLPIGILPVGTANDFA-KFLGMPTDIGEACEqILKSKPKKVDLGKINdkyFINVASTGLFTDVS---QKTDV 149
                         170       180
                  ....*....|....*....|
gi 1002302025 389 lELseryQKRFGPLRYFVAG 408
Cdd:PRK13059  150 -NL----KNTIGKLAYYLKG 164
 
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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