NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|661903014|ref|NP_001284358|]
View 

diacylglycerol kinase eta isoform 5 [Homo sapiens]

Protein Classification

diacylglycerol kinase( domain architecture ID 10207246)

diacylglycerol kinase catalyzes the conversion of diacylglycerol (DAG) to phosphatidic acid (PA), utilizing ATP as a source of the phosphate

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 ...
 525-682 9.56e-82

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: 260.73  E-value: 9.56e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903014   525 VMNNYFGIGLDAKISLEFNNKREEHPEKCRSRTKNLMWYGVLGTRELLQRSYKNLEQRVQLECDGQYIPLP-SLQGIAVL 603
Cdd:smart00045   1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLPnSLEGIAVL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903014   604 NIPSYAGGTNFWGGT-KEDDIFAAPSFDDKILEVVAIFDSMQMAVSRVIKLQHHRIAQCRTVKITIFGDEGVPVQVDGEA 682
Cdd:smart00045  81 NIPSYGGGTNLWGTTdKEDLNFSKQSHDDGLLEVVGLTGAMHMAQIRQVGLAGRRIAQCSEVRITIKTSKTIPMQVDGEP 160
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 89-211 6.15e-48

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: 166.32  E-value: 6.15e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903014    89 LVFVNSKSGDNQGVKFLRRFKQLLNPAQVFDLMNGGPHLGLRLFQKFDNF-RILVCGGDGSVGWVLSEIDKLNLNKQC-Q 166
Cdd:smart00046   1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVPDFnRVLVCGGDGTVGWVLNALDKRELPLPEpP 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 661903014   167 LGVLPLGTGNDLARVLGWGGSYDDDTQLPqILEKLERASTKMLDR 211
Cdd:smart00046  81 VAVLPLGTGNDLARSLGWGGGYDGEKLLK-TLRDALESDTVKLDR 124
C1 super family cl00040
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ...
 37-59 1.19e-06

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.


The actual alignment was detected with superfamily member cd20894:

Pssm-ID: 412127  Cd Length: 62  Bit Score: 46.43  E-value: 1.19e-06
                         10        20
                 ....*....|....*....|...
gi 661903014  37 CPAKVHTACKDLYHPICPLGQCK 59
Cdd:cd20894   40 CKAMVHTACKDQYPRKCPLGQCR 62
 
Name Accession Description Interval E-value
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 525-682 9.56e-82

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: 260.73  E-value: 9.56e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903014   525 VMNNYFGIGLDAKISLEFNNKREEHPEKCRSRTKNLMWYGVLGTRELLQRSYKNLEQRVQLECDGQYIPLP-SLQGIAVL 603
Cdd:smart00045   1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLPnSLEGIAVL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903014   604 NIPSYAGGTNFWGGT-KEDDIFAAPSFDDKILEVVAIFDSMQMAVSRVIKLQHHRIAQCRTVKITIFGDEGVPVQVDGEA 682
Cdd:smart00045  81 NIPSYGGGTNLWGTTdKEDLNFSKQSHDDGLLEVVGLTGAMHMAQIRQVGLAGRRIAQCSEVRITIKTSKTIPMQVDGEP 160
DAGK_acc pfam00609
Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts ...
 525-682 8.82e-72

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: 233.65  E-value: 8.82e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903014  525 VMNNYFGIGLDAKISLEFNNKREEHPEKCRSRTKNLMWYGVLGTRELLQRSYKNLEQRVQLECDGQYIPLP-SLQGIAVL 603
Cdd:pfam00609   1 VMNNYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDMFQRSCKNLIEKVELEVDGKDLPLPkSLEGIVVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903014  604 NIPSYAGGTNFWGGTKEDDI-FAAPSFDDKILEVVAIFDSMQMAVSRVIKLQHHRIAQCRTVKITIfgDEGVPVQVDGEA 682
Cdd:pfam00609  81 NIPSYAGGTDLWGNSKEDGLgFAPQSVDDGLLEVVGLTGALHLGQVQVGLGSAKRIAQGGPIRITT--KKKIPMQVDGEP 158
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 89-211 6.15e-48

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: 166.32  E-value: 6.15e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903014    89 LVFVNSKSGDNQGVKFLRRFKQLLNPAQVFDLMNGGPHLGLRLFQKFDNF-RILVCGGDGSVGWVLSEIDKLNLNKQC-Q 166
Cdd:smart00046   1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVPDFnRVLVCGGDGTVGWVLNALDKRELPLPEpP 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 661903014   167 LGVLPLGTGNDLARVLGWGGSYDDDTQLPqILEKLERASTKMLDR 211
Cdd:smart00046  81 VAVLPLGTGNDLARSLGWGGGYDGEKLLK-TLRDALESDTVKLDR 124
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 87-204 4.20e-32

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: 121.15  E-value: 4.20e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903014   87 PLLVFVNSKSGDNQGVKFLRRFKQLLNPAQV-FDLMN-GGPHLGLRLFQKFDN---FRILVCGGDGSVGWVLSEIDKLNl 161
Cdd:pfam00781   1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVeVELVLtEGPGDALELAREAAEdgyDRIVVAGGDGTVNEVLNGLAGLA- 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 661903014  162 nKQCQLGVLPLGTGNDLARVLGWGGsyDDDTQLPQILEKLERA 204
Cdd:pfam00781  80 -TRPPLGIIPLGTGNDFARALGIPG--DPEEALEAILKGQTRP 119
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 88-210 1.56e-11

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


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 66.03  E-value: 1.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903014  88 LLVFVNSKSGDNQGVKFLRRFKQLLN----PAQVFDLMNGGPhlGLRLFQK-----FDnfRILVCGGDGSVGWVLSEIdk 158
Cdd:COG1597    5 ALLIVNPASGRGRAARLLERLVAALRaaglEVEVLETESPGD--ATELAREaaaegAD--LVVAAGGDGTVNEVANGL-- 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 661903014 159 lnLNKQCQLGVLPLGTGNDLARVLGWggsyddDTQLPQILEKLERASTKMLD 210
Cdd:COG1597   79 --AGTGPPLGILPLGTGNDFARALGI------PLDPEAALEALLTGRTRRID 122
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 528-681 1.09e-08

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


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 57.55  E-value: 1.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903014 528 NYFGIGLDAKISLEFNNKReehpekcRSRTKNLMwYGVLGTRELlqRSYKNLeqRVQLECDGQYIPLPSLQgIAVLNIPS 607
Cdd:COG1597  133 NVAGIGFDAEVVERANRAL-------KRRLGKLA-YVLAALRAL--LRYRPF--RLRIELDGEEIEGEALL-VAVGNGPY 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903014 608 YAGGTNfwggtkeddIFAAPSFDDKILEVVAI-----FDSMQMAVS----RVIKLQHHRIAQCRTVKITifGDEGVPVQV 678
Cdd:COG1597  200 YGGGLR---------LAPDASLDDGLLDVVVVrplsrLRLLRLLPRllrgRHLRHPGVRYFRAREVEIE--SDRPLPVQL 268


                 ...
gi 661903014 679 DGE 681
Cdd:COG1597  269 DGE 271
PRK12361 PRK12361
hypothetical protein; Provisional
 140-210 2.70e-07

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 54.24  E-value: 2.70e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 661903014 140 ILVCGGDGSVGWVLSEIdklnLNKQCQLGVLPLGTGNDLARVL-GWGGSYDDdtqLPQILEKLERASTKMLD 210
Cdd:PRK12361 301 VIACGGDGTVTEVASEL----VNTDITLGIIPLGTANALSHALfGLGSKLIP---VEQACDNIIQGHTQRID 365
C1_DGKeta_rpt2 cd20894
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase eta (DAG ...
 37-59 1.19e-06

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: 46.43  E-value: 1.19e-06
                         10        20
                 ....*....|....*....|...
gi 661903014  37 CPAKVHTACKDLYHPICPLGQCK 59
Cdd:cd20894   40 CKAMVHTACKDQYPRKCPLGQCR 62
TIGR00147 TIGR00147
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ...
 133-183 1.27e-03

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: 41.72  E-value: 1.27e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 661903014  133 QKFDNFRILVCGGDGSVGWVLSEIdkLNLNKQCQLGVLPLGTGNDLARVLG 183
Cdd:TIGR00147  54 RKFGVDTVIAGGGDGTINEVVNAL--IQLDDIPALGILPLGTANDFARSLG 102
 
Name Accession Description Interval E-value
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 525-682 9.56e-82

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: 260.73  E-value: 9.56e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903014   525 VMNNYFGIGLDAKISLEFNNKREEHPEKCRSRTKNLMWYGVLGTRELLQRSYKNLEQRVQLECDGQYIPLP-SLQGIAVL 603
Cdd:smart00045   1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLPnSLEGIAVL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903014   604 NIPSYAGGTNFWGGT-KEDDIFAAPSFDDKILEVVAIFDSMQMAVSRVIKLQHHRIAQCRTVKITIFGDEGVPVQVDGEA 682
Cdd:smart00045  81 NIPSYGGGTNLWGTTdKEDLNFSKQSHDDGLLEVVGLTGAMHMAQIRQVGLAGRRIAQCSEVRITIKTSKTIPMQVDGEP 160
DAGK_acc pfam00609
Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts ...
 525-682 8.82e-72

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: 233.65  E-value: 8.82e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903014  525 VMNNYFGIGLDAKISLEFNNKREEHPEKCRSRTKNLMWYGVLGTRELLQRSYKNLEQRVQLECDGQYIPLP-SLQGIAVL 603
Cdd:pfam00609   1 VMNNYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDMFQRSCKNLIEKVELEVDGKDLPLPkSLEGIVVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903014  604 NIPSYAGGTNFWGGTKEDDI-FAAPSFDDKILEVVAIFDSMQMAVSRVIKLQHHRIAQCRTVKITIfgDEGVPVQVDGEA 682
Cdd:pfam00609  81 NIPSYAGGTDLWGNSKEDGLgFAPQSVDDGLLEVVGLTGALHLGQVQVGLGSAKRIAQGGPIRITT--KKKIPMQVDGEP 158
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 89-211 6.15e-48

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: 166.32  E-value: 6.15e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903014    89 LVFVNSKSGDNQGVKFLRRFKQLLNPAQVFDLMNGGPHLGLRLFQKFDNF-RILVCGGDGSVGWVLSEIDKLNLNKQC-Q 166
Cdd:smart00046   1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVPDFnRVLVCGGDGTVGWVLNALDKRELPLPEpP 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 661903014   167 LGVLPLGTGNDLARVLGWGGSYDDDTQLPqILEKLERASTKMLDR 211
Cdd:smart00046  81 VAVLPLGTGNDLARSLGWGGGYDGEKLLK-TLRDALESDTVKLDR 124
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 87-204 4.20e-32

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: 121.15  E-value: 4.20e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903014   87 PLLVFVNSKSGDNQGVKFLRRFKQLLNPAQV-FDLMN-GGPHLGLRLFQKFDN---FRILVCGGDGSVGWVLSEIDKLNl 161
Cdd:pfam00781   1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVeVELVLtEGPGDALELAREAAEdgyDRIVVAGGDGTVNEVLNGLAGLA- 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 661903014  162 nKQCQLGVLPLGTGNDLARVLGWGGsyDDDTQLPQILEKLERA 204
Cdd:pfam00781  80 -TRPPLGIIPLGTGNDFARALGIPG--DPEEALEAILKGQTRP 119
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 88-210 1.56e-11

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


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 66.03  E-value: 1.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903014  88 LLVFVNSKSGDNQGVKFLRRFKQLLN----PAQVFDLMNGGPhlGLRLFQK-----FDnfRILVCGGDGSVGWVLSEIdk 158
Cdd:COG1597    5 ALLIVNPASGRGRAARLLERLVAALRaaglEVEVLETESPGD--ATELAREaaaegAD--LVVAAGGDGTVNEVANGL-- 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 661903014 159 lnLNKQCQLGVLPLGTGNDLARVLGWggsyddDTQLPQILEKLERASTKMLD 210
Cdd:COG1597   79 --AGTGPPLGILPLGTGNDFARALGI------PLDPEAALEALLTGRTRRID 122
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 528-681 1.09e-08

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


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 57.55  E-value: 1.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903014 528 NYFGIGLDAKISLEFNNKReehpekcRSRTKNLMwYGVLGTRELlqRSYKNLeqRVQLECDGQYIPLPSLQgIAVLNIPS 607
Cdd:COG1597  133 NVAGIGFDAEVVERANRAL-------KRRLGKLA-YVLAALRAL--LRYRPF--RLRIELDGEEIEGEALL-VAVGNGPY 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903014 608 YAGGTNfwggtkeddIFAAPSFDDKILEVVAI-----FDSMQMAVS----RVIKLQHHRIAQCRTVKITifGDEGVPVQV 678
Cdd:COG1597  200 YGGGLR---------LAPDASLDDGLLDVVVVrplsrLRLLRLLPRllrgRHLRHPGVRYFRAREVEIE--SDRPLPVQL 268


                 ...
gi 661903014 679 DGE 681
Cdd:COG1597  269 DGE 271
PRK12361 PRK12361
hypothetical protein; Provisional
 140-210 2.70e-07

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 54.24  E-value: 2.70e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 661903014 140 ILVCGGDGSVGWVLSEIdklnLNKQCQLGVLPLGTGNDLARVL-GWGGSYDDdtqLPQILEKLERASTKMLD 210
Cdd:PRK12361 301 VIACGGDGTVTEVASEL----VNTDITLGIIPLGTANALSHALfGLGSKLIP---VEQACDNIIQGHTQRID 365
C1_DGKeta_rpt2 cd20894
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase eta (DAG ...
 37-59 1.19e-06

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: 46.43  E-value: 1.19e-06
                         10        20
                 ....*....|....*....|...
gi 661903014  37 CPAKVHTACKDLYHPICPLGQCK 59
Cdd:cd20894   40 CKAMVHTACKDQYPRKCPLGQCR 62
PRK13057 PRK13057
lipid kinase;
139-183 4.06e-05

lipid kinase;


Pssm-ID: 183857 [Multi-domain]  Cd Length: 287  Bit Score: 46.45  E-value: 4.06e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 661903014 139 RILVCGGDGSVGWVLSEIDKLNLnkqcQLGVLPLGTGNDLARVLG 183
Cdd:PRK13057  53 LVIVGGGDGTLNAAAPALVETGL----PLGILPLGTANDLARTLG 93
PRK13054 PRK13054
lipid kinase; Reviewed
 139-183 5.11e-05

lipid kinase; Reviewed


Pssm-ID: 237281 [Multi-domain]  Cd Length: 300  Bit Score: 46.40  E-value: 5.11e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 661903014 139 RILVCGGDGSVGWVLSEIDKLNLNKQCQLGVLPLGTGNDLARVLG 183
Cdd:PRK13054  59 TVIAGGGDGTINEVATALAQLEGDARPALGILPLGTANDFATAAG 103
PRK13059 PRK13059
putative lipid kinase; Reviewed
 140-183 2.01e-04

putative lipid kinase; Reviewed


Pssm-ID: 183858  Cd Length: 295  Bit Score: 44.26  E-value: 2.01e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 661903014 140 ILVCGGDGSVGWVLSEIDKLNLNkqCQLGVLPLGTGNDLARVLG 183
Cdd:PRK13059  60 ILIAGGDGTVDNVVNAMKKLNID--LPIGILPVGTANDFAKFLG 101
TIGR00147 TIGR00147
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ...
 133-183 1.27e-03

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: 41.72  E-value: 1.27e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 661903014  133 QKFDNFRILVCGGDGSVGWVLSEIdkLNLNKQCQLGVLPLGTGNDLARVLG 183
Cdd:TIGR00147  54 RKFGVDTVIAGGGDGTINEVVNAL--IQLDDIPALGILPLGTANDFARSLG 102
C1_DGKdelta_rpt2 cd20893
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase delta ...
 37-58 3.32e-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: 36.96  E-value: 3.32e-03
                         10        20
                 ....*....|....*....|..
gi 661903014  37 CPAKVHTACKDLYHPICPLGQC 58
Cdd:cd20893   40 CKAMVHTSCKELLLTKCPLGQC 61
 
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