NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|15241456|ref|NP_196409|]
View 

diacylglycerol kinase1 [Arabidopsis thaliana]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 507-664 3.36e-78

Diacylglycerol kinase accessory 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 might either be an accessory domain or else contribute to the catalytic domain. Bacterial homologues are known.


:

Pssm-ID: 214486  Cd Length: 160  Bit Score: 247.63  E-value: 3.36e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241456    507 YMNNYIGVGCDAKVALEIHNLREENPERFYSQFMNKVLYAREGARSIMDRTFEDFPWQVRVEVDGVDIEVPEDAEGILVA 586
Cdd:smart00045   1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLPNSLEGIAVL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241456    587 NIGSYMGGVDLWQNEDETYENFDPQSMHDKIVEVVSISGTWHLGKLQVGLSRARRLAQGSAVKIQL--CAPLPVQIDGEP 664
Cdd:smart00045  81 NIPSYGGGTNLWGTTDKEDLNFSKQSHDDGLLEVVGLTGAMHMAQIRQVGLAGRRIAQCSEVRITIktSKTIPMQVDGEP 160
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 363-489 1.07e-40

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: 145.13  E-value: 1.07e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241456    363 LVFINKKSGAQRGDSLRQRLHLHLNPVQVFELSsVQGPEVGLFLFRKVPHF-RVLVCGGDGTAGWVLDAIEKQNFISP-P 440
Cdd:smart00046   1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLT-KKGPAVALVIFRDVPDFnRVLVCGGDGTVGWVLNALDKRELPLPeP 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 15241456    441 AVAILPAGTGNDLSRVLNWGGGLGSverQGGLSTVLQNIEhAAVTVLDR 489
Cdd:smart00046  80 PVAVLPLGTGNDLARSLGWGGGYDG---EKLLKTLRDALE-SDTVKLDR 124
C1_DGK_rpt2 cd20805
second protein kinase C conserved region 1 (C1 domain) found in the diacylglycerol kinase ...
 150-215 4.17e-16

second protein kinase C conserved region 1 (C1 domain) found in the diacylglycerol kinase family; The diacylglycerol kinase (DGK, EC 2.7.1.107) family of enzymes plays critical roles in lipid signaling pathways by converting diacylglycerol to phosphatidic acid, thereby downregulating signaling by the former and upregulating signaling by the latter second messenger. Ten DGK family isozymes have been identified to date, which possess different interaction motifs imparting distinct temporal and spatial control of DGK activity to each isozyme. They have been classified into five types (I-V), according to domain architecture and some common features. All DGK isozymes, except for DGKtheta, contain two copies of the C1 domain. This model corresponds to the second one. DGKtheta harbors three C1 domains. Its third C1 domain is included here. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


:

Pssm-ID: 410355  Cd Length: 55  Bit Score: 72.86  E-value: 4.17e-16
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15241456 150 HQWAVRWTegadqtDDSSFCSYCDESCSSSFlgGSPIWCCLWCQRLVHVDCHSNMSNETgdiCDLG 215
Cdd:cd20805   1 HHWVEGNL------PSGAKCSVCGKKCGSSF--GLAGYRCSWCKRTVHSECIDKLGPEE---CDLG 55
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
 80-137 2.19e-06

Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.


:

Pssm-ID: 197519  Cd Length: 50  Bit Score: 45.15  E-value: 2.19e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 15241456     80 HSWELDPiaRAKNLNCCVCLKSMSPSQaivaseSFFHRCTICGAAAHFNCSSSAPKDC 137
Cdd:smart00109   1 HKHVFRT--FTKPTFCCVCRKSIWGSF------KQGLRCSECKVKCHKKCADKVPKAC 50
 
Name Accession Description Interval E-value
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 507-664 3.36e-78

Diacylglycerol kinase accessory 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 might either be an accessory domain or else contribute to the catalytic domain. Bacterial homologues are known.


Pssm-ID: 214486  Cd Length: 160  Bit Score: 247.63  E-value: 3.36e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241456    507 YMNNYIGVGCDAKVALEIHNLREENPERFYSQFMNKVLYAREGARSIMDRTFEDFPWQVRVEVDGVDIEVPEDAEGILVA 586
Cdd:smart00045   1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLPNSLEGIAVL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241456    587 NIGSYMGGVDLWQNEDETYENFDPQSMHDKIVEVVSISGTWHLGKLQVGLSRARRLAQGSAVKIQL--CAPLPVQIDGEP 664
Cdd:smart00045  81 NIPSYGGGTNLWGTTDKEDLNFSKQSHDDGLLEVVGLTGAMHMAQIRQVGLAGRRIAQCSEVRITIktSKTIPMQVDGEP 160
DAGK_acc pfam00609
Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts ...
 508-664 1.32e-75

Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. This domain is assumed to be an accessory domain: its function is unknown.


Pssm-ID: 459866  Cd Length: 158  Bit Score: 240.58  E-value: 1.32e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241456   508 MNNYIGVGCDAKVALEIHNLREENPERFYSQFMNKVLYAREGARSIMDRTFEDFPWQVRVEVDGVDIEVPEDAEGILVAN 587
Cdd:pfam00609   2 MNNYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDMFQRSCKNLIEKVELEVDGKDLPLPKSLEGIVVLN 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15241456   588 IGSYMGGVDLWQNEDETYENFDPQSMHDKIVEVVSISGTWHLGKLQVGLSRARRLAQGSAVKIQLCAPLPVQIDGEP 664
Cdd:pfam00609  82 IPSYAGGTDLWGNSKEDGLGFAPQSVDDGLLEVVGLTGALHLGQVQVGLGSAKRIAQGGPIRITTKKKIPMQVDGEP 158
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 363-489 1.07e-40

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: 145.13  E-value: 1.07e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241456    363 LVFINKKSGAQRGDSLRQRLHLHLNPVQVFELSsVQGPEVGLFLFRKVPHF-RVLVCGGDGTAGWVLDAIEKQNFISP-P 440
Cdd:smart00046   1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLT-KKGPAVALVIFRDVPDFnRVLVCGGDGTVGWVLNALDKRELPLPeP 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 15241456    441 AVAILPAGTGNDLSRVLNWGGGLGSverQGGLSTVLQNIEhAAVTVLDR 489
Cdd:smart00046  80 PVAVLPLGTGNDLARSLGWGGGYDG---EKLLKTLRDALE-SDTVKLDR 124
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 361-461 8.40e-30

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: 114.22  E-value: 8.40e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241456   361 PLLVFINKKSGAQRGDSLRQRLHLHLNPVQV-FELSSVQGPEVGLFLFRKVP---HFRVLVCGGDGTAGWVLDAIEKqnF 436
Cdd:pfam00781   1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVeVELVLTEGPGDALELAREAAedgYDRIVVAGGDGTVNEVLNGLAG--L 78

                          90       100
                  ....*....|....*....|....*
gi 15241456   437 ISPPAVAILPAGTGNDLSRVLNWGG 461
Cdd:pfam00781  79 ATRPPLGIIPLGTGNDFARALGIPG 103
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 358-674 3.90e-21

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


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 94.53  E-value: 3.90e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241456 358 DARPLLVFINKKSGAQRGDSLRQRLHLHLN----PVQVFELSSvQGPEVGL---FLFRKVPhfRVLVCGGDGTAGWVLDA 430
Cdd:COG1597   1 AMMRALLIVNPASGRGRAARLLERLVAALRaaglEVEVLETES-PGDATELareAAAEGAD--LVVAAGGDGTVNEVANG 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241456 431 IEKqnfiSPPAVAILPAGTGNDLSRVLnwggglgsverqgGLStvlQNIEHAAVTVLDRWKVSI----LNQqgkqlqppK 506
Cdd:COG1597  78 LAG----TGPPLGILPLGTGNDFARAL-------------GIP---LDPEAALEALLTGRTRRIdlgrVNG--------R 129

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241456 507 YMNNYIGVGCDAKVAleihnlreENPERFYSQFMNKVLYAREGARSImdRTFEdfPWQVRVEVDGVDIEVpeDAEGILVA 586
Cdd:COG1597 130 YFLNVAGIGFDAEVV--------ERANRALKRRLGKLAYVLAALRAL--LRYR--PFRLRIELDGEEIEG--EALLVAVG 195

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241456 587 NIGSYMGGVdlwqnedetyeNFDPQ-SMHDKIVEVVSI--SGTWHLGKLQVGLSRAR-------RLAQGSAVKIQLCAPL 656
Cdd:COG1597 196 NGPYYGGGL-----------RLAPDaSLDDGLLDVVVVrpLSRLRLLRLLPRLLRGRhlrhpgvRYFRAREVEIESDRPL 264

                       330
                ....*....|....*....
gi 15241456 657 PVQIDGEP-WNQQPCTLTI 674
Cdd:COG1597 265 PVQLDGEPlGLATPLEFEV 283
C1_DGK_rpt2 cd20805
second protein kinase C conserved region 1 (C1 domain) found in the diacylglycerol kinase ...
 150-215 4.17e-16

second protein kinase C conserved region 1 (C1 domain) found in the diacylglycerol kinase family; The diacylglycerol kinase (DGK, EC 2.7.1.107) family of enzymes plays critical roles in lipid signaling pathways by converting diacylglycerol to phosphatidic acid, thereby downregulating signaling by the former and upregulating signaling by the latter second messenger. Ten DGK family isozymes have been identified to date, which possess different interaction motifs imparting distinct temporal and spatial control of DGK activity to each isozyme. They have been classified into five types (I-V), according to domain architecture and some common features. All DGK isozymes, except for DGKtheta, contain two copies of the C1 domain. This model corresponds to the second one. DGKtheta harbors three C1 domains. Its third C1 domain is included here. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410355  Cd Length: 55  Bit Score: 72.86  E-value: 4.17e-16
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15241456 150 HQWAVRWTegadqtDDSSFCSYCDESCSSSFlgGSPIWCCLWCQRLVHVDCHSNMSNETgdiCDLG 215
Cdd:cd20805   1 HHWVEGNL------PSGAKCSVCGKKCGSSF--GLAGYRCSWCKRTVHSECIDKLGPEE---CDLG 55
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
 150-210 1.55e-10

Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the Protein kinase C conserved region 1 (C1) domain.


Pssm-ID: 395079  Cd Length: 53  Bit Score: 57.07  E-value: 1.55e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15241456   150 HQWAVRWTegadqtDDSSFCSYCDESCsssFLGGSPIWCCLWCQRLVHVDCHSNMSNETGD 210
Cdd:pfam00130   1 HHFVHRNF------KQPTFCDHCGEFL---WGLGKQGLKCSWCKLNVHKRCHEKVPPECGC 52
TIGR00147 TIGR00147
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ...
 414-675 4.78e-09

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: 58.28  E-value: 4.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241456   414 RVLVCGGDGTAGWVLDAIEKQNFIspPAVAILPAGTGNDLSRVLNwggglgsverqgglstVLQNIEHAAVTVLDRWKVS 493
Cdd:TIGR00147  60 TVIAGGGDGTINEVVNALIQLDDI--PALGILPLGTANDFARSLG----------------IPEDLDKAAKLVIAGDARA 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241456   494 I-LNQQGKQLQppkYMnNYIGVGCDAKVALEIhnlreenPERFYSQfMNKVLYAREGARsiMDRTFEDFPWQVRVEvdgv 572
Cdd:TIGR00147 122 IdMGQVNKQYC---FI-NMAGGGFGTEITTET-------PEKLKAA-LGSLSYILSGLM--RMDTLQPFRCEIRGE---- 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241456   573 DIEVPEDAEGILVANIGSYMGGVDLWQNedetyenfdpQSMHDKIVEVVSISGTWHLGKLQVGLSRARR---------LA 643
Cdd:TIGR00147 184 GEHWQGEAVVFLVGNGRQAGGGQKLAPD----------ASINDGLLDLRIFTNDNLLPALVLTLMSDEGkhtdnpniiYG 253

                         250       260       270
                  ....*....|....*....|....*....|..
gi 15241456   644 QGSAVKIQLCAPLPVQIDGEPWNQQPCTLTIS 675
Cdd:TIGR00147 254 KASRIDIQTPHKITFNLDGEPLGGTPFHIEIL 285
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
 150-206 7.01e-07

Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.


Pssm-ID: 197519  Cd Length: 50  Bit Score: 46.31  E-value: 7.01e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 15241456    150 HQWAVRWTegadqtDDSSFCSYCDESCSSSFLggsPIWCCLWCQRLVHVDCHSNMSN 206
Cdd:smart00109   1 HKHVFRTF------TKPTFCCVCRKSIWGSFK---QGLRCSECKVKCHKKCADKVPK 48
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
 80-137 2.19e-06

Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.


Pssm-ID: 197519  Cd Length: 50  Bit Score: 45.15  E-value: 2.19e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 15241456     80 HSWELDPiaRAKNLNCCVCLKSMSPSQaivaseSFFHRCTICGAAAHFNCSSSAPKDC 137
Cdd:smart00109   1 HKHVFRT--FTKPTFCCVCRKSIWGSF------KQGLRCSECKVKCHKKCADKVPKAC 50
C1 cd00029
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ...
 80-137 2.10e-05

protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains. It contains the motif HX12CX2CXnCX2CX4HX2CX7C, where C and H are cysteine and histidine, respectively; X represents other residues; and n is either 13 or 14. C1 has a globular fold with two separate Zn(2+)-binding sites. It was originally discovered as lipid-binding modules in protein kinase C (PKC) isoforms. C1 domains that bind and respond to phorbol esters (PE) and diacylglycerol (DAG) are referred to as typical, and those that do not respond to PE and DAG are deemed atypical. A C1 domain may also be referred to as PKC or non-PKC C1, based on the parent protein's activity. Most C1 domain-containing non-PKC proteins act as lipid kinases and scaffolds, except PKD which acts as a protein kinase. PKC C1 domains play roles in membrane translocation and activation of the enzyme.


Pssm-ID: 410341  Cd Length: 50  Bit Score: 42.50  E-value: 2.10e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15241456  80 HSWEldPIARAKNLNCCVCLKSmspsqaIVASESFFHRCTICGAAAHFNCSSSAPKDC 137
Cdd:cd00029   1 HRFV--PTTFSSPTFCDVCGKL------IWGLFKQGLKCSDCGLVCHKKCLDKAPSPC 50
PRK13059 PRK13059
putative lipid kinase; Reviewed
 415-458 2.95e-04

putative lipid kinase; Reviewed


Pssm-ID: 183858  Cd Length: 295  Bit Score: 43.49  E-value: 2.95e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 15241456  415 VLVCGGDGTAGWVLDAIEKQNfISPPaVAILPAGTGNDLSRVLN 458
Cdd:PRK13059  60 ILIAGGDGTVDNVVNAMKKLN-IDLP-IGILPVGTANDFAKFLG 101
 
Name Accession Description Interval E-value
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 507-664 3.36e-78

Diacylglycerol kinase accessory 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 might either be an accessory domain or else contribute to the catalytic domain. Bacterial homologues are known.


Pssm-ID: 214486  Cd Length: 160  Bit Score: 247.63  E-value: 3.36e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241456    507 YMNNYIGVGCDAKVALEIHNLREENPERFYSQFMNKVLYAREGARSIMDRTFEDFPWQVRVEVDGVDIEVPEDAEGILVA 586
Cdd:smart00045   1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLPNSLEGIAVL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241456    587 NIGSYMGGVDLWQNEDETYENFDPQSMHDKIVEVVSISGTWHLGKLQVGLSRARRLAQGSAVKIQL--CAPLPVQIDGEP 664
Cdd:smart00045  81 NIPSYGGGTNLWGTTDKEDLNFSKQSHDDGLLEVVGLTGAMHMAQIRQVGLAGRRIAQCSEVRITIktSKTIPMQVDGEP 160
DAGK_acc pfam00609
Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts ...
 508-664 1.32e-75

Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. This domain is assumed to be an accessory domain: its function is unknown.


Pssm-ID: 459866  Cd Length: 158  Bit Score: 240.58  E-value: 1.32e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241456   508 MNNYIGVGCDAKVALEIHNLREENPERFYSQFMNKVLYAREGARSIMDRTFEDFPWQVRVEVDGVDIEVPEDAEGILVAN 587
Cdd:pfam00609   2 MNNYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDMFQRSCKNLIEKVELEVDGKDLPLPKSLEGIVVLN 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15241456   588 IGSYMGGVDLWQNEDETYENFDPQSMHDKIVEVVSISGTWHLGKLQVGLSRARRLAQGSAVKIQLCAPLPVQIDGEP 664
Cdd:pfam00609  82 IPSYAGGTDLWGNSKEDGLGFAPQSVDDGLLEVVGLTGALHLGQVQVGLGSAKRIAQGGPIRITTKKKIPMQVDGEP 158
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 363-489 1.07e-40

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: 145.13  E-value: 1.07e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241456    363 LVFINKKSGAQRGDSLRQRLHLHLNPVQVFELSsVQGPEVGLFLFRKVPHF-RVLVCGGDGTAGWVLDAIEKQNFISP-P 440
Cdd:smart00046   1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLT-KKGPAVALVIFRDVPDFnRVLVCGGDGTVGWVLNALDKRELPLPeP 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 15241456    441 AVAILPAGTGNDLSRVLNWGGGLGSverQGGLSTVLQNIEhAAVTVLDR 489
Cdd:smart00046  80 PVAVLPLGTGNDLARSLGWGGGYDG---EKLLKTLRDALE-SDTVKLDR 124
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 361-461 8.40e-30

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: 114.22  E-value: 8.40e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241456   361 PLLVFINKKSGAQRGDSLRQRLHLHLNPVQV-FELSSVQGPEVGLFLFRKVP---HFRVLVCGGDGTAGWVLDAIEKqnF 436
Cdd:pfam00781   1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVeVELVLTEGPGDALELAREAAedgYDRIVVAGGDGTVNEVLNGLAG--L 78

                          90       100
                  ....*....|....*....|....*
gi 15241456   437 ISPPAVAILPAGTGNDLSRVLNWGG 461
Cdd:pfam00781  79 ATRPPLGIIPLGTGNDFARALGIPG 103
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 358-674 3.90e-21

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


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 94.53  E-value: 3.90e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241456 358 DARPLLVFINKKSGAQRGDSLRQRLHLHLN----PVQVFELSSvQGPEVGL---FLFRKVPhfRVLVCGGDGTAGWVLDA 430
Cdd:COG1597   1 AMMRALLIVNPASGRGRAARLLERLVAALRaaglEVEVLETES-PGDATELareAAAEGAD--LVVAAGGDGTVNEVANG 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241456 431 IEKqnfiSPPAVAILPAGTGNDLSRVLnwggglgsverqgGLStvlQNIEHAAVTVLDRWKVSI----LNQqgkqlqppK 506
Cdd:COG1597  78 LAG----TGPPLGILPLGTGNDFARAL-------------GIP---LDPEAALEALLTGRTRRIdlgrVNG--------R 129

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241456 507 YMNNYIGVGCDAKVAleihnlreENPERFYSQFMNKVLYAREGARSImdRTFEdfPWQVRVEVDGVDIEVpeDAEGILVA 586
Cdd:COG1597 130 YFLNVAGIGFDAEVV--------ERANRALKRRLGKLAYVLAALRAL--LRYR--PFRLRIELDGEEIEG--EALLVAVG 195

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241456 587 NIGSYMGGVdlwqnedetyeNFDPQ-SMHDKIVEVVSI--SGTWHLGKLQVGLSRAR-------RLAQGSAVKIQLCAPL 656
Cdd:COG1597 196 NGPYYGGGL-----------RLAPDaSLDDGLLDVVVVrpLSRLRLLRLLPRLLRGRhlrhpgvRYFRAREVEIESDRPL 264

                       330
                ....*....|....*....
gi 15241456 657 PVQIDGEP-WNQQPCTLTI 674
Cdd:COG1597 265 PVQLDGEPlGLATPLEFEV 283
C1_DGK_rpt2 cd20805
second protein kinase C conserved region 1 (C1 domain) found in the diacylglycerol kinase ...
 150-215 4.17e-16

second protein kinase C conserved region 1 (C1 domain) found in the diacylglycerol kinase family; The diacylglycerol kinase (DGK, EC 2.7.1.107) family of enzymes plays critical roles in lipid signaling pathways by converting diacylglycerol to phosphatidic acid, thereby downregulating signaling by the former and upregulating signaling by the latter second messenger. Ten DGK family isozymes have been identified to date, which possess different interaction motifs imparting distinct temporal and spatial control of DGK activity to each isozyme. They have been classified into five types (I-V), according to domain architecture and some common features. All DGK isozymes, except for DGKtheta, contain two copies of the C1 domain. This model corresponds to the second one. DGKtheta harbors three C1 domains. Its third C1 domain is included here. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410355  Cd Length: 55  Bit Score: 72.86  E-value: 4.17e-16
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15241456 150 HQWAVRWTegadqtDDSSFCSYCDESCSSSFlgGSPIWCCLWCQRLVHVDCHSNMSNETgdiCDLG 215
Cdd:cd20805   1 HHWVEGNL------PSGAKCSVCGKKCGSSF--GLAGYRCSWCKRTVHSECIDKLGPEE---CDLG 55
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
 150-210 1.55e-10

Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the Protein kinase C conserved region 1 (C1) domain.


Pssm-ID: 395079  Cd Length: 53  Bit Score: 57.07  E-value: 1.55e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15241456   150 HQWAVRWTegadqtDDSSFCSYCDESCsssFLGGSPIWCCLWCQRLVHVDCHSNMSNETGD 210
Cdd:pfam00130   1 HHFVHRNF------KQPTFCDHCGEFL---WGLGKQGLKCSWCKLNVHKRCHEKVPPECGC 52
C1_DGKepsilon_typeIII_rpt2 cd20853
second protein kinase C conserved region 1 (C1 domain) found in type III diacylglycerol kinase, ...
 167-224 1.77e-10

second protein kinase C conserved region 1 (C1 domain) found in type III diacylglycerol kinase, DAG kinase epsilon, and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase epsilon, also called diglyceride kinase epsilon (DGK-epsilon), is the only isoform classified as type III; it possesses a hydrophobic domain in addition to C1 and catalytic domains that are present in all DGKs, and shows selectivity for acyl chains. It is highly selective for arachidonate-containing species of DAG. It may terminate signals transmitted through arachidonoyl-DAG or may contribute to the synthesis of phospholipids with defined fatty acid composition. DAG kinase epsilon contains two copies of the C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410403  Cd Length: 63  Bit Score: 56.90  E-value: 1.77e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15241456 167 SFCSYCDESCsssflGGSPIWC---CLWCQRLVHVDCHSNMSNEtgdiCDLGPLRRLILCP 224
Cdd:cd20853  12 SVCCVCNEQC-----GNQPGLCdyrCCWCQRTVHDDCLAKLPKE----CDLGAFRNFIVPP 63
TIGR00147 TIGR00147
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ...
 414-675 4.78e-09

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: 58.28  E-value: 4.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241456   414 RVLVCGGDGTAGWVLDAIEKQNFIspPAVAILPAGTGNDLSRVLNwggglgsverqgglstVLQNIEHAAVTVLDRWKVS 493
Cdd:TIGR00147  60 TVIAGGGDGTINEVVNALIQLDDI--PALGILPLGTANDFARSLG----------------IPEDLDKAAKLVIAGDARA 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241456   494 I-LNQQGKQLQppkYMnNYIGVGCDAKVALEIhnlreenPERFYSQfMNKVLYAREGARsiMDRTFEDFPWQVRVEvdgv 572
Cdd:TIGR00147 122 IdMGQVNKQYC---FI-NMAGGGFGTEITTET-------PEKLKAA-LGSLSYILSGLM--RMDTLQPFRCEIRGE---- 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241456   573 DIEVPEDAEGILVANIGSYMGGVDLWQNedetyenfdpQSMHDKIVEVVSISGTWHLGKLQVGLSRARR---------LA 643
Cdd:TIGR00147 184 GEHWQGEAVVFLVGNGRQAGGGQKLAPD----------ASINDGLLDLRIFTNDNLLPALVLTLMSDEGkhtdnpniiYG 253

                         250       260       270
                  ....*....|....*....|....*....|..
gi 15241456   644 QGSAVKIQLCAPLPVQIDGEPWNQQPCTLTIS 675
Cdd:TIGR00147 254 KASRIDIQTPHKITFNLDGEPLGGTPFHIEIL 285
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
 150-206 7.01e-07

Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.


Pssm-ID: 197519  Cd Length: 50  Bit Score: 46.31  E-value: 7.01e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 15241456    150 HQWAVRWTegadqtDDSSFCSYCDESCSSSFLggsPIWCCLWCQRLVHVDCHSNMSN 206
Cdd:smart00109   1 HKHVFRTF------TKPTFCCVCRKSIWGSFK---QGLRCSECKVKCHKKCADKVPK 48
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
 80-137 2.19e-06

Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.


Pssm-ID: 197519  Cd Length: 50  Bit Score: 45.15  E-value: 2.19e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 15241456     80 HSWELDPiaRAKNLNCCVCLKSMSPSQaivaseSFFHRCTICGAAAHFNCSSSAPKDC 137
Cdd:smart00109   1 HKHVFRT--FTKPTFCCVCRKSIWGSF------KQGLRCSECKVKCHKKCADKVPKAC 50
C1_DGKtheta_typeV_rpt3 cd20854
third protein kinase C conserved region 1 (C1 domain) found in type V diacylglycerol kinase, ...
 166-224 9.70e-06

third protein kinase C conserved region 1 (C1 domain) found in type V diacylglycerol kinase, DAG kinase theta, and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase theta, also called diglyceride kinase theta (DGK-theta), is the only isoform classified as type V; it contains a pleckstrin homology (PH)-like domain and an additional C1 domain, compared to other DGKs. It may regulate the activity of protein kinase C by controlling the balance between the two signaling lipids, diacylglycerol and phosphatidic acid. DAG kinase theta contains three copies of the C1 domain. This model corresponds to the third one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410404  Cd Length: 63  Bit Score: 43.79  E-value: 9.70e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241456 166 SSFCSYCDESCSSS-FLGGspiWCCLWCQRLVHVDCHSNMSNEtgdiCDLGPLRRLILCP 224
Cdd:cd20854  11 NSKCEVCKKSCGSSeCLAG---MRCEWCGITAHASCYKSLPKE----CNFGRLRNIILPP 63
C1 cd00029
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ...
 80-137 2.10e-05

protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains. It contains the motif HX12CX2CXnCX2CX4HX2CX7C, where C and H are cysteine and histidine, respectively; X represents other residues; and n is either 13 or 14. C1 has a globular fold with two separate Zn(2+)-binding sites. It was originally discovered as lipid-binding modules in protein kinase C (PKC) isoforms. C1 domains that bind and respond to phorbol esters (PE) and diacylglycerol (DAG) are referred to as typical, and those that do not respond to PE and DAG are deemed atypical. A C1 domain may also be referred to as PKC or non-PKC C1, based on the parent protein's activity. Most C1 domain-containing non-PKC proteins act as lipid kinases and scaffolds, except PKD which acts as a protein kinase. PKC C1 domains play roles in membrane translocation and activation of the enzyme.


Pssm-ID: 410341  Cd Length: 50  Bit Score: 42.50  E-value: 2.10e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15241456  80 HSWEldPIARAKNLNCCVCLKSmspsqaIVASESFFHRCTICGAAAHFNCSSSAPKDC 137
Cdd:cd00029   1 HRFV--PTTFSSPTFCDVCGKL------IWGLFKQGLKCSDCGLVCHKKCLDKAPSPC 50
PRK13059 PRK13059
putative lipid kinase; Reviewed
 415-458 2.95e-04

putative lipid kinase; Reviewed


Pssm-ID: 183858  Cd Length: 295  Bit Score: 43.49  E-value: 2.95e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 15241456  415 VLVCGGDGTAGWVLDAIEKQNfISPPaVAILPAGTGNDLSRVLN 458
Cdd:PRK13059  60 ILIAGGDGTVDNVVNAMKKLN-IDLP-IGILPVGTANDFAKFLG 101
C1_DGK_typeII_rpt2 cd20852
second protein kinase C conserved region 1 (C1 domain) found in type II diacylglycerol kinases; ...
 166-215 4.39e-04

second protein kinase C conserved region 1 (C1 domain) found in type II diacylglycerol kinases; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. Type II DAG kinases (DGKs) contain pleckstrin homology (PH) and sterile alpha motifs (SAM) domains, in addition to C1 and catalytic domains that are present in all DGKs. The SAM domain mediates oligomerization of type II DGKs. Three DGK isozymes (delta, eta and kappa) are classified as type II. DAG kinase delta, also called 130 kDa DAG kinase, or diglyceride kinase delta (DGK-delta), is a residential lipid kinase in the endoplasmic reticulum. It promotes lipogenesis and is involved in triglyceride biosynthesis. DAG kinase eta, also called diglyceride kinase eta (DGK-eta), plays a key role in promoting cell growth. The DAG kinase eta gene, DGKH, is a replicated risk gene of bipolar disorder (BPD). DAG kinase kappa is also called diglyceride kinase kappa (DGK-kappa) or 142 kDa DAG kinase. Members of this family contain two copies of the C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410402  Cd Length: 54  Bit Score: 38.84  E-value: 4.39e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 15241456 166 SSFCSYCDESCSSSFLggSPIWCCLWCQRLVHVDCHSNMSNEtgdiCDLG 215
Cdd:cd20852  11 SSKCAVCDKTCGSVLR--LQDWRCLWCGATVHTACKDSLPTK----CSLG 54
C1_DGKalpha_rpt2 cd20890
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase alpha ...
 188-224 5.04e-04

second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase alpha (DAG kinase alpha) and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase alpha, also called 80 kDa diacylglycerol kinase, or diglyceride kinase alpha (DGK-alpha), converts the second messenger diacylglycerol into phosphatidate upon cell stimulation, initiating the resynthesis of phosphatidylinositols and attenuating protein kinase C activity. It is classified as a type I DAG kinase (DGK), containing EF-hand structures that bind Ca(2+) and a recoverin homology domain, in addition to C1 and catalytic domains that are present in all DGKs. As a type I DGK, it is regulated by calcium binding. DAG kinase alpha contains two copies of the C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410440  Cd Length: 62  Bit Score: 38.67  E-value: 5.04e-04
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 15241456 188 CCLWCQRLVHVDCHSNMSNEtgdiCDLGPLRRLILCP 224
Cdd:cd20890  30 HCVWCHLKRHDECLSSVPST----CDCGPLRDHILPP 62
PRK13054 PRK13054
lipid kinase; Reviewed
 414-455 1.45e-03

lipid kinase; Reviewed


Pssm-ID: 237281 [Multi-domain]  Cd Length: 300  Bit Score: 41.40  E-value: 1.45e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 15241456  414 RVLVCGGDGTAGWVLDAIEKQNFISPPAVAILPAGTGNDLSR 455
Cdd:PRK13054  59 TVIAGGGDGTINEVATALAQLEGDARPALGILPLGTANDFAT 100
C1_DGKdelta_rpt2 cd20893
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase delta ...
 155-200 1.52e-03

second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase delta (DAG kinase delta) and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase delta, also called 130 kDa diacylglycerol kinase, or diglyceride kinase delta (DGK-delta), is a residential lipid kinase in the endoplasmic reticulum. It promotes lipogenesis and is involved in triglyceride biosynthesis. It is classified as a type II DAG kinase (DGK), containing pleckstrin homology (PH) and sterile alpha motifs (SAM) domains, in addition to C1 and catalytic domains that are present in all DGKs. The SAM domain mediates oligomerization of type II DGKs. DAG kinase delta contains two copies of the C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410443  Cd Length: 61  Bit Score: 37.35  E-value: 1.52e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 15241456 155 RWTEGadQTDDSSFCSYCDESCSSSFLGGSpiWCCLWCQRLVHVDC 200
Cdd:cd20893   7 QWLEG--NLPVSAKCTVCDKTCGSVLRLQD--WRCLWCKAMVHTSC 48
C1_DGKeta_rpt2 cd20894
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase eta (DAG ...
 155-218 2.12e-03

second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase eta (DAG kinase eta) and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase eta, also called diglyceride kinase eta (DGK-eta), plays a key role in promoting cell growth. It is classified as a type II DAG kinase (DGK), containing pleckstrin homology (PH) and sterile alpha motifs (SAM) domains, in addition to C1 and catalytic domains that are present in all DGKs. The SAM domain mediates oligomerization of type II DGKs. The diacylglycerol kinase eta gene, DGKH, is a replicated risk gene of bipolar disorder (BPD). DAG kinase eta contains two copies of the C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410444  Cd Length: 62  Bit Score: 37.19  E-value: 2.12e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15241456 155 RWTEGadQTDDSSFCSYCDESCSSSFLGGSpiWCCLWCQRLVHVDCHSNMSNetgdICDLGPLR 218
Cdd:cd20894   7 QWLEG--NLPVSAKCSVCDKTCGSVLRLQD--WRCLWCKAMVHTACKDQYPR----KCPLGQCR 62
C1_DGKtheta_typeV_rpt2 cd20804
second protein kinase C conserved region 1 (C1 domain) found in type V diacylglycerol kinase, ...
 74-138 2.27e-03

second protein kinase C conserved region 1 (C1 domain) found in type V diacylglycerol kinase, DAG kinase theta, and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase theta, also called diglyceride kinase theta (DGK-theta), is the only isoform classified as type V; it contains a pleckstrin homology (PH)-like domain and an additional C1 domain, compared to other DGKs. It may regulate the activity of protein kinase C by controlling the balance between the two signaling lipids, diacylglycerol and phosphatidic acid. DAG kinase theta contains three copies of the C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410354  Cd Length: 57  Bit Score: 36.90  E-value: 2.27e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15241456  74 KVPVaPHSWEldPIARAKNLNCCVCLKSMSPSQAIvasesffhRCTICGAAAHFNCSSSAPKDCK 138
Cdd:cd20804   1 KNPV-AHCWS--EPGHSKRKFCNVCRKRLEDSPAF--------RCEVCEYYVHSDCQDFAVSDCR 54
C1_DGKgamma_rpt2 cd20892
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase gamma ...
 156-224 3.58e-03

second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase gamma (DAG kinase gamma) and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase gamma, also called diglyceride kinase gamma (DGK-gamma), reverses the normal flow of glycerolipid biosynthesis by phosphorylating diacylglycerol back to phosphatidic acid. It is classified as a type I DAG kinase (DGK), containing EF-hand structures that bind Ca(2+) and a recoverin homology domain, in addition to C1 and catalytic domains that are present in all DGKs. As a type I DGK, it is regulated by calcium binding. DGK-gamma contains two copies of the C1 domain. This model corresponds to the second one. DGK-gamma contains typical C1 domains that bind DAG and phorbol esters. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410442  Cd Length: 61  Bit Score: 36.33  E-value: 3.58e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15241456 156 WTEGADQTDdssfCSYCDESCSSsFLGGSPIWCcLWCQRLVHVDCHSNMSNEtgdiCDLGPLRRLILCP 224
Cdd:cd20892   3 WVEGNSPVK----CDRCHKSIKC-YQGLTGLHC-VWCQITLHNKCASHVSPE----CDGGQLKDHILLP 61
C1_DGK_typeI_like_rpt2 cd20851
second protein kinase C conserved region 1 (C1 domain) found in type I diacylglycerol kinases; ...
 156-215 4.36e-03

second protein kinase C conserved region 1 (C1 domain) found in type I diacylglycerol kinases; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. Type I DAG kinases (DGKs) contain EF-hand structures that bind Ca(2+) and recoverin homology domains, in addition to C1 and catalytic domains that are present in all DGKs. Type I DGKs, regulated by calcium binding, include three DGK isozymes (alpha, beta and gamma). DAG kinase alpha, also called 80 kDa DAG kinase, or diglyceride kinase alpha (DGK-alpha), is active upon cell stimulation, initiating the resynthesis of phosphatidylinositols and attenuating protein kinase C activity. DAG kinase beta, also called 90 kDa DAG kinase, or diglyceride kinase beta (DGK-beta), exhibits high phosphorylation activity for long-chain diacylglycerols. DAG kinase gamma, also called diglyceride kinase gamma (DGK-gamma), reverses the normal flow of glycerolipid biosynthesis by phosphorylating diacylglycerol back to phosphatidic acid. Members of this family contain two copies of the C1 domain. This model corresponds to the second one. DGK-alpha contains atypical C1 domains, while DGK-beta and DGK-gamma contain typical C1 domains that bind DAG and phorbol esters. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410401  Cd Length: 52  Bit Score: 35.79  E-value: 4.36e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15241456 156 WTEGadqtDDSSFCSYCDES--CSSSFLGgspiWCCLWCQRLVHVDCHSNMSNEtgdiCDLG 215
Cdd:cd20851   3 WVEG----NCPGKCDKCHKSikSYQGLTG----LHCVWCHITLHNKCASHVKPE----CDLG 52
PRK13055 PRK13055
putative lipid kinase; Reviewed
 415-458 6.43e-03

putative lipid kinase; Reviewed


Pssm-ID: 237282 [Multi-domain]  Cd Length: 334  Bit Score: 39.59  E-value: 6.43e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 15241456  415 VLVCGGDGTAGWVLDAI---EKqnfisPPAVAILPAGTGNDLSRVLN 458
Cdd:PRK13055  63 IIAAGGDGTINEVVNGIaplEK-----RPKMAIIPAGTTNDYARALK 104
PRK13057 PRK13057
lipid kinase;
363-458 7.33e-03

lipid kinase;


Pssm-ID: 183857 [Multi-domain]  Cd Length: 287  Bit Score: 39.13  E-value: 7.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241456  363 LVFINKKS--GAQRGDSLRQRLH-LHLNPVQVFELSSVQGPEVGLFLFRKVPhfRVLVCGGDGTAGWVLDAIEKQNFisp 439
Cdd:PRK13057   1 LLLVNRHArsGRAALAAARAALEaAGLELVEPPAEDPDDLSEVIEAYADGVD--LVIVGGGDGTLNAAAPALVETGL--- 75

                         90
                 ....*....|....*....
gi 15241456  440 pAVAILPAGTGNDLSRVLN 458
Cdd:PRK13057  76 -PLGILPLGTANDLARTLG 93
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH