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Conserved domains on  [gi|1907082537|ref|XP_036012756|]
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diacylglycerol kinase epsilon isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 326-481 3.72e-79

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: 244.94  E-value: 3.72e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082537  326 TMNNYFSVGPDALMALNFHAHREKAPSLFSSRILNKAVYLFYGTKDCLVQECKDLNKKIELELDGERVELPN-LEGIIVL 404
Cdd:smart00045   1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLPNsLEGIAVL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082537  405 NIGYWGGGCRLW--EGMGDETYPLARHDDGLLEIVGVYGSFHCAQIQVKLANPFRIGQAHTVRLTLKCS-MMPMQVDGEP 481
Cdd:smart00045  81 NIPSYGGGTNLWgtTDKEDLNFSKQSHDDGLLEVVGLTGAMHMAQIRQVGLAGRRIAQCSEVRITIKTSkTIPMQVDGEP 160
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 206-306 7.96e-35

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: 127.03  E-value: 7.96e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082537  206 VFDVTKTPPIKALQLCTLLPYYsVRVLVCGGDGTVGWVLDAIDEMKIKGQEkyiPEVAVLPLGTGNDLSNTLGWGTGYAG 285
Cdd:smart00046  29 VFDLTKKGPAVALVIFRDVPDF-NRVLVCGGDGTVGWVLNALDKRELPLPE---PPVAVLPLGTGNDLARSLGWGGGYDG 104

                           90       100
                   ....*....|....*....|.
gi 1907082537  286 EIPVAqVLRNVMEADGIKLDR 306
Cdd:smart00046 105 EKLLK-TLRDALESDTVKLDR 124
C1_DGKepsilon_typeIII_rpt2 cd20853
second protein kinase C conserved region 1 (C1 domain) found in type III diacylglycerol kinase, ...
 122-186 6.63e-33

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: 119.69  E-value: 6.63e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907082537 122 HHWIRGNVPLCSYCVFCRQQCGSQPKLCDYRCIWCQKTVHDECMRGSlrSEKCDFGEFRNLIIPP 186
Cdd:cd20853     1 HHWVRGNLPLCSVCCVCNEQCGNQPGLCDYRCCWCQRTVHDDCLAKL--PKECDLGAFRNFIVPP 63
C1_DGKepsilon_typeIII_rpt1 cd20801
first protein kinase C conserved region 1 (C1 domain) found in type III diacylglycerol kinase, ...
 55-108 4.10e-25

first 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 first 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: 410351  Cd Length: 54  Bit Score: 97.77  E-value: 4.10e-25
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907082537  55 KSKHCWRDTDLFSHPTYCCVCAQHILQGAFCDCCGLRVDEGCLKKVDKRFPCKE 108
Cdd:cd20801     1 SKGHHWVSTDLFSKPTYCSVCETLILSGAFCDCCGLCVDEGCLRKADKRFPCKA 54
 
Name Accession Description Interval E-value
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 326-481 3.72e-79

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: 244.94  E-value: 3.72e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082537  326 TMNNYFSVGPDALMALNFHAHREKAPSLFSSRILNKAVYLFYGTKDCLVQECKDLNKKIELELDGERVELPN-LEGIIVL 404
Cdd:smart00045   1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLPNsLEGIAVL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082537  405 NIGYWGGGCRLW--EGMGDETYPLARHDDGLLEIVGVYGSFHCAQIQVKLANPFRIGQAHTVRLTLKCS-MMPMQVDGEP 481
Cdd:smart00045  81 NIPSYGGGTNLWgtTDKEDLNFSKQSHDDGLLEVVGLTGAMHMAQIRQVGLAGRRIAQCSEVRITIKTSkTIPMQVDGEP 160
DAGK_acc pfam00609
Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts ...
 326-481 3.96e-73

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: 229.02  E-value: 3.96e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082537 326 TMNNYFSVGPDALMALNFHAHREKAPSLFSSRILNKAVYLFYGTKDCLVQECKDLNKKIELELDGERVELP-NLEGIIVL 404
Cdd:pfam00609   1 VMNNYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDMFQRSCKNLIEKVELEVDGKDLPLPkSLEGIVVL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082537 405 NIGYWGGGCRLWEGMGD--ETYPLARHDDGLLEIVGVYGSFHCAQIQVKLANPFRIGQAHTVRLTLKCsMMPMQVDGEP 481
Cdd:pfam00609  81 NIPSYAGGTDLWGNSKEdgLGFAPQSVDDGLLEVVGLTGALHLGQVQVGLGSAKRIAQGGPIRITTKK-KIPMQVDGEP 158
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 206-306 7.96e-35

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: 127.03  E-value: 7.96e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082537  206 VFDVTKTPPIKALQLCTLLPYYsVRVLVCGGDGTVGWVLDAIDEMKIKGQEkyiPEVAVLPLGTGNDLSNTLGWGTGYAG 285
Cdd:smart00046  29 VFDLTKKGPAVALVIFRDVPDF-NRVLVCGGDGTVGWVLNALDKRELPLPE---PPVAVLPLGTGNDLARSLGWGGGYDG 104

                           90       100
                   ....*....|....*....|.
gi 1907082537  286 EIPVAqVLRNVMEADGIKLDR 306
Cdd:smart00046 105 EKLLK-TLRDALESDTVKLDR 124
C1_DGKepsilon_typeIII_rpt2 cd20853
second protein kinase C conserved region 1 (C1 domain) found in type III diacylglycerol kinase, ...
 122-186 6.63e-33

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: 119.69  E-value: 6.63e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907082537 122 HHWIRGNVPLCSYCVFCRQQCGSQPKLCDYRCIWCQKTVHDECMRGSlrSEKCDFGEFRNLIIPP 186
Cdd:cd20853     1 HHWVRGNLPLCSVCCVCNEQCGNQPGLCDYRCCWCQRTVHDDCLAKL--PKECDLGAFRNFIVPP 63
C1_DGKepsilon_typeIII_rpt1 cd20801
first protein kinase C conserved region 1 (C1 domain) found in type III diacylglycerol kinase, ...
 55-108 4.10e-25

first 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 first 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: 410351  Cd Length: 54  Bit Score: 97.77  E-value: 4.10e-25
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907082537  55 KSKHCWRDTDLFSHPTYCCVCAQHILQGAFCDCCGLRVDEGCLKKVDKRFPCKE 108
Cdd:cd20801     1 SKGHHWVSTDLFSKPTYCSVCETLILSGAFCDCCGLCVDEGCLRKADKRFPCKA 54
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 207-281 1.81e-18

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: 81.48  E-value: 1.81e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082537 207 FDVTKT-PPIKALQLCTLLPYYSV-RVLVCGGDGTVGWVLDAIDEmkikgqEKYIPEVAVLPLGTGNDLSNTLGWGT 281
Cdd:pfam00781  33 VELVLTeGPGDALELAREAAEDGYdRIVVAGGDGTVNEVLNGLAG------LATRPPLGIIPLGTGNDFARALGIPG 103
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 230-494 4.19e-17

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


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 81.82  E-value: 4.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082537 230 RVLVCGGDGTVGWVLDAIDEMKikgqekyiPEVAVLPLGTGNDLSNTLGwgtgyageIP--VAQVLRNVMEADGIKLDRW 307
Cdd:COG1597    61 LVVAAGGDGTVNEVANGLAGTG--------PPLGILPLGTGNDFARALG--------IPldPEAALEALLTGRTRRIDLG 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082537 308 KVQvtnkGYYnlrkpkeFTMNnyFSVGPDALMALNFHAHRekapslfsSRILNKAVYLFYGTKdcLVQECKDLnkKIELE 387
Cdd:COG1597   125 RVN----GRY-------FLNV--AGIGFDAEVVERANRAL--------KRRLGKLAYVLAALR--ALLRYRPF--RLRIE 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082537 388 LDGERVELPNLeGIIVLNIGYWGGGCRLWegmgdetyPLARHDDGLLEIVgVYGSFHCAQIqVKLA----------NP-F 456
Cdd:COG1597   180 LDGEEIEGEAL-LVAVGNGPYYGGGLRLA--------PDASLDDGLLDVV-VVRPLSRLRL-LRLLprllrgrhlrHPgV 248

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1907082537 457 RIGQAHTVRLTLKcSMMPMQVDGEP-WAQGPCTVTITHK 494
Cdd:COG1597   249 RYFRAREVEIESD-RPLPVQLDGEPlGLATPLEFEVLPG 286
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
 58-107 3.86e-08

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: 49.75  E-value: 3.86e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907082537  58 HCWRDTDlFSHPTYCCVCAQHI----LQGAFCDCCGLRVDEGCLKKVDKRFPCK 107
Cdd:pfam00130   1 HHFVHRN-FKQPTFCDHCGEFLwglgKQGLKCSWCKLNVHKRCHEKVPPECGCD 53
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
 122-166 7.22e-08

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: 49.00  E-value: 7.22e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1907082537  122 HHWIRGNVPLCSYCVFCRQQCGSQPKlCDYRCIWCQKTVHDECMR 166
Cdd:smart00109   1 HKHVFRTFTKPTFCCVCRKSIWGSFK-QGLRCSECKVKCHKKCAD 44
TIGR00147 TIGR00147
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ...
 203-486 1.46e-06

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: 50.20  E-value: 1.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082537 203 YEGVFDVTKTPPIKALQLCTLLPYYSVRVLVCGGDGTVGWVLDAIDEMKikgqekYIPEVAVLPLGTGNDLSNTLGwgtg 282
Cdd:TIGR00147  33 MEIHVRVTWEKGDAARYVEEARKFGVDTVIAGGGDGTINEVVNALIQLD------DIPALGILPLGTANDFARSLG---- 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082537 283 yageIP--VAQVLRNVMEADGIKLDRWKVqvtNKGYYNLrkpkeftmnNYFSVGPDALMALNFHAhREKApslfssrILN 360
Cdd:TIGR00147 103 ----IPedLDKAAKLVIAGDARAIDMGQV---NKQYCFI---------NMAGGGFGTEITTETPE-KLKA-------ALG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082537 361 KAVYLFYG--TKDCLVQEckdlnkKIELELDGERVELPNLEgIIVLNIGYWGGGCRLwegmgdetYPLARHDDGLLEIVG 438
Cdd:TIGR00147 159 SLSYILSGlmRMDTLQPF------RCEIRGEGEHWQGEAVV-FLVGNGRQAGGGQKL--------APDASINDGLLDLRI 223

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082537 439 VYGSFHCAQIQVKLANPFRI---------GQAHTVRLTLKcSMMPMQVDGEPWAQGP 486
Cdd:TIGR00147 224 FTNDNLLPALVLTLMSDEGKhtdnpniiyGKASRIDIQTP-HKITFNLDGEPLGGTP 279
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
 66-102 2.10e-05

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: 42.07  E-value: 2.10e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1907082537   66 FSHPTYCCVCAQHI----LQGAFCDCCGLRVDEGCLKKVDK 102
Cdd:smart00109   8 FTKPTFCCVCRKSIwgsfKQGLRCSECKVKCHKKCADKVPK 48
PRK12361 PRK12361
hypothetical protein; Provisional
 231-298 2.82e-05

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 46.54  E-value: 2.82e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082537 231 VLVCGGDGTVGWVLDAIDEMKIKgqekyipeVAVLPLGTGNDLSNTL-GWGTGYageIPVAQVLRNVME 298
Cdd:PRK12361  301 VIACGGDGTVTEVASELVNTDIT--------LGIIPLGTANALSHALfGLGSKL---IPVEQACDNIIQ 358
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
 122-166 3.27e-04

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: 38.58  E-value: 3.27e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1907082537 122 HHWIRGNVPLCSYCVFCRQQCGSQPKLCdYRCIWCQKTVHDECMR 166
Cdd:pfam00130   1 HHFVHRNFKQPTFCDHCGEFLWGLGKQG-LKCSWCKLNVHKRCHE 44
 
Name Accession Description Interval E-value
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 326-481 3.72e-79

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: 244.94  E-value: 3.72e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082537  326 TMNNYFSVGPDALMALNFHAHREKAPSLFSSRILNKAVYLFYGTKDCLVQECKDLNKKIELELDGERVELPN-LEGIIVL 404
Cdd:smart00045   1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLPNsLEGIAVL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082537  405 NIGYWGGGCRLW--EGMGDETYPLARHDDGLLEIVGVYGSFHCAQIQVKLANPFRIGQAHTVRLTLKCS-MMPMQVDGEP 481
Cdd:smart00045  81 NIPSYGGGTNLWgtTDKEDLNFSKQSHDDGLLEVVGLTGAMHMAQIRQVGLAGRRIAQCSEVRITIKTSkTIPMQVDGEP 160
DAGK_acc pfam00609
Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts ...
 326-481 3.96e-73

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: 229.02  E-value: 3.96e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082537 326 TMNNYFSVGPDALMALNFHAHREKAPSLFSSRILNKAVYLFYGTKDCLVQECKDLNKKIELELDGERVELP-NLEGIIVL 404
Cdd:pfam00609   1 VMNNYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDMFQRSCKNLIEKVELEVDGKDLPLPkSLEGIVVL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082537 405 NIGYWGGGCRLWEGMGD--ETYPLARHDDGLLEIVGVYGSFHCAQIQVKLANPFRIGQAHTVRLTLKCsMMPMQVDGEP 481
Cdd:pfam00609  81 NIPSYAGGTDLWGNSKEdgLGFAPQSVDDGLLEVVGLTGALHLGQVQVGLGSAKRIAQGGPIRITTKK-KIPMQVDGEP 158
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 206-306 7.96e-35

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: 127.03  E-value: 7.96e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082537  206 VFDVTKTPPIKALQLCTLLPYYsVRVLVCGGDGTVGWVLDAIDEMKIKGQEkyiPEVAVLPLGTGNDLSNTLGWGTGYAG 285
Cdd:smart00046  29 VFDLTKKGPAVALVIFRDVPDF-NRVLVCGGDGTVGWVLNALDKRELPLPE---PPVAVLPLGTGNDLARSLGWGGGYDG 104

                           90       100
                   ....*....|....*....|.
gi 1907082537  286 EIPVAqVLRNVMEADGIKLDR 306
Cdd:smart00046 105 EKLLK-TLRDALESDTVKLDR 124
C1_DGKepsilon_typeIII_rpt2 cd20853
second protein kinase C conserved region 1 (C1 domain) found in type III diacylglycerol kinase, ...
 122-186 6.63e-33

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: 119.69  E-value: 6.63e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907082537 122 HHWIRGNVPLCSYCVFCRQQCGSQPKLCDYRCIWCQKTVHDECMRGSlrSEKCDFGEFRNLIIPP 186
Cdd:cd20853     1 HHWVRGNLPLCSVCCVCNEQCGNQPGLCDYRCCWCQRTVHDDCLAKL--PKECDLGAFRNFIVPP 63
C1_DGKepsilon_typeIII_rpt1 cd20801
first protein kinase C conserved region 1 (C1 domain) found in type III diacylglycerol kinase, ...
 55-108 4.10e-25

first 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 first 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: 410351  Cd Length: 54  Bit Score: 97.77  E-value: 4.10e-25
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907082537  55 KSKHCWRDTDLFSHPTYCCVCAQHILQGAFCDCCGLRVDEGCLKKVDKRFPCKE 108
Cdd:cd20801     1 SKGHHWVSTDLFSKPTYCSVCETLILSGAFCDCCGLCVDEGCLRKADKRFPCKA 54
C1_DGK_rpt2 cd20805
second protein kinase C conserved region 1 (C1 domain) found in the diacylglycerol kinase ...
 122-177 1.08e-18

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: 79.80  E-value: 1.08e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082537 122 HHWIRGNVPLCSYCVFCRQQCGSQPKLCDYRCIWCQKTVHDECMRgSLRSEKCDFG 177
Cdd:cd20805     1 HHWVEGNLPSGAKCSVCGKKCGSSFGLAGYRCSWCKRTVHSECID-KLGPEECDLG 55
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 207-281 1.81e-18

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: 81.48  E-value: 1.81e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082537 207 FDVTKT-PPIKALQLCTLLPYYSV-RVLVCGGDGTVGWVLDAIDEmkikgqEKYIPEVAVLPLGTGNDLSNTLGWGT 281
Cdd:pfam00781  33 VELVLTeGPGDALELAREAAEDGYdRIVVAGGDGTVNEVLNGLAG------LATRPPLGIIPLGTGNDFARALGIPG 103
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 230-494 4.19e-17

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


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 81.82  E-value: 4.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082537 230 RVLVCGGDGTVGWVLDAIDEMKikgqekyiPEVAVLPLGTGNDLSNTLGwgtgyageIP--VAQVLRNVMEADGIKLDRW 307
Cdd:COG1597    61 LVVAAGGDGTVNEVANGLAGTG--------PPLGILPLGTGNDFARALG--------IPldPEAALEALLTGRTRRIDLG 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082537 308 KVQvtnkGYYnlrkpkeFTMNnyFSVGPDALMALNFHAHRekapslfsSRILNKAVYLFYGTKdcLVQECKDLnkKIELE 387
Cdd:COG1597   125 RVN----GRY-------FLNV--AGIGFDAEVVERANRAL--------KRRLGKLAYVLAALR--ALLRYRPF--RLRIE 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082537 388 LDGERVELPNLeGIIVLNIGYWGGGCRLWegmgdetyPLARHDDGLLEIVgVYGSFHCAQIqVKLA----------NP-F 456
Cdd:COG1597   180 LDGEEIEGEAL-LVAVGNGPYYGGGLRLA--------PDASLDDGLLDVV-VVRPLSRLRL-LRLLprllrgrhlrHPgV 248

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1907082537 457 RIGQAHTVRLTLKcSMMPMQVDGEP-WAQGPCTVTITHK 494
Cdd:COG1597   249 RYFRAREVEIESD-RPLPVQLDGEPlGLATPLEFEVLPG 286
C1_DGKtheta_typeV_rpt3 cd20854
third protein kinase C conserved region 1 (C1 domain) found in type V diacylglycerol kinase, ...
 122-186 1.06e-14

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: 68.44  E-value: 1.06e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907082537 122 HHWIRGNVPLCSYCVFCRQQCGSQPKLCDYRCIWCQKTVHDECMRgSLRSEkCDFGEFRNLIIPP 186
Cdd:cd20854     1 HHWREGNLPSNSKCEVCKKSCGSSECLAGMRCEWCGITAHASCYK-SLPKE-CNFGRLRNIILPP 63
C1_DGK_typeII_rpt2 cd20852
second protein kinase C conserved region 1 (C1 domain) found in type II diacylglycerol kinases; ...
 122-177 1.09e-14

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: 68.12  E-value: 1.09e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082537 122 HHWIRGNVPLCSYCVFCRQQCGSQPKLCDYRCIWCQKTVHDECMRGSLRseKCDFG 177
Cdd:cd20852     1 HQWLEGNLPVSSKCAVCDKTCGSVLRLQDWRCLWCGATVHTACKDSLPT--KCSLG 54
C1_DGKdelta_rpt2 cd20893
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase delta ...
 119-178 3.35e-13

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: 64.31  E-value: 3.35e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082537 119 AMPHHWIRGNVPLCSYCVFCRQQCGSQPKLCDYRCIWCQKTVHDECMRGSLRseKCDFGE 178
Cdd:cd20893     3 SMPHQWLEGNLPVSAKCTVCDKTCGSVLRLQDWRCLWCKAMVHTSCKELLLT--KCPLGQ 60
C1_DGKeta_rpt2 cd20894
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase eta (DAG ...
 119-180 2.30e-12

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: 61.84  E-value: 2.30e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907082537 119 AMPHHWIRGNVPLCSYCVFCRQQCGSQPKLCDYRCIWCQKTVHDECMrgSLRSEKCDFGEFR 180
Cdd:cd20894     3 AMPHQWLEGNLPVSAKCSVCDKTCGSVLRLQDWRCLWCKAMVHTACK--DQYPRKCPLGQCR 62
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
 58-107 3.86e-08

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: 49.75  E-value: 3.86e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907082537  58 HCWRDTDlFSHPTYCCVCAQHI----LQGAFCDCCGLRVDEGCLKKVDKRFPCK 107
Cdd:pfam00130   1 HHFVHRN-FKQPTFCDHCGEFLwglgKQGLKCSWCKLNVHKRCHEKVPPECGCD 53
C1_DGKalpha_rpt2 cd20890
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase alpha ...
 122-186 5.34e-08

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: 49.46  E-value: 5.34e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907082537 122 HHWIRGNVPlCSYCVFCRQQCGSQPKLCDYRCIWCQKTVHDECMrgSLRSEKCDFGEFRNLIIPP 186
Cdd:cd20890     1 HVWVSGGCE-SSKCDKCQKKIKSFQSLTGLHCVWCHLKRHDECL--SSVPSTCDCGPLRDHILPP 62
C1_DGK_typeI_like_rpt2 cd20851
second protein kinase C conserved region 1 (C1 domain) found in type I diacylglycerol kinases; ...
 122-177 6.19e-08

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: 49.27  E-value: 6.19e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082537 122 HHWIRGNVPlcSYCVFCRQQCGSQPKLCDYRCIWCQKTVHDECMrgSLRSEKCDFG 177
Cdd:cd20851     1 HHWVEGNCP--GKCDKCHKSIKSYQGLTGLHCVWCHITLHNKCA--SHVKPECDLG 52
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
 122-166 7.22e-08

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: 49.00  E-value: 7.22e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1907082537  122 HHWIRGNVPLCSYCVFCRQQCGSQPKlCDYRCIWCQKTVHDECMR 166
Cdd:smart00109   1 HKHVFRTFTKPTFCCVCRKSIWGSFK-QGLRCSECKVKCHKKCAD 44
TIGR00147 TIGR00147
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ...
 203-486 1.46e-06

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: 50.20  E-value: 1.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082537 203 YEGVFDVTKTPPIKALQLCTLLPYYSVRVLVCGGDGTVGWVLDAIDEMKikgqekYIPEVAVLPLGTGNDLSNTLGwgtg 282
Cdd:TIGR00147  33 MEIHVRVTWEKGDAARYVEEARKFGVDTVIAGGGDGTINEVVNALIQLD------DIPALGILPLGTANDFARSLG---- 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082537 283 yageIP--VAQVLRNVMEADGIKLDRWKVqvtNKGYYNLrkpkeftmnNYFSVGPDALMALNFHAhREKApslfssrILN 360
Cdd:TIGR00147 103 ----IPedLDKAAKLVIAGDARAIDMGQV---NKQYCFI---------NMAGGGFGTEITTETPE-KLKA-------ALG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082537 361 KAVYLFYG--TKDCLVQEckdlnkKIELELDGERVELPNLEgIIVLNIGYWGGGCRLwegmgdetYPLARHDDGLLEIVG 438
Cdd:TIGR00147 159 SLSYILSGlmRMDTLQPF------RCEIRGEGEHWQGEAVV-FLVGNGRQAGGGQKL--------APDASINDGLLDLRI 223

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082537 439 VYGSFHCAQIQVKLANPFRI---------GQAHTVRLTLKcSMMPMQVDGEPWAQGP 486
Cdd:TIGR00147 224 FTNDNLLPALVLTLMSDEGKhtdnpniiyGKASRIDIQTP-HKITFNLDGEPLGGTP 279
YegS_C pfam19279
YegS C-terminal NAD kinase beta sandwich-like domain; This entry represents the C-terminal ...
 386-491 2.80e-06

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: 47.19  E-value: 2.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082537 386 LELDGERVELPNLEgIIVLNIGYWGGGCRLwegmgdetYPLARHDDGLLEIVG---------------VYGSFHCAQIQV 450
Cdd:pfam19279  45 VTVDGEVREFSAAL-VAVANSGYYGGGMRI--------APDARVDDGLLDVVVieaasrrtllrllpkVYDGRHVRLPQV 115

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1907082537 451 klanpfRIGQAHTVRLTlKCSMMPMQVDGEPWAQGPCTVTI 491
Cdd:pfam19279 116 ------EVLRGREVRIE-ADRPLPAGADGEVLGPLPVRVEV 149
C1 cd00029
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ...
 58-106 1.54e-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: 42.12  E-value: 1.54e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907082537  58 HCWRDTDlFSHPTYCCVCAQHIL----QGAFCDCCGLRVDEGCLKKVDKrfPC 106
Cdd:cd00029     1 HRFVPTT-FSSPTFCDVCGKLIWglfkQGLKCSDCGLVCHKKCLDKAPS--PC 50
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
 66-102 2.10e-05

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: 42.07  E-value: 2.10e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1907082537   66 FSHPTYCCVCAQHI----LQGAFCDCCGLRVDEGCLKKVDK 102
Cdd:smart00109   8 FTKPTFCCVCRKSIwgsfKQGLRCSECKVKCHKKCADKVPK 48
PRK12361 PRK12361
hypothetical protein; Provisional
 231-298 2.82e-05

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 46.54  E-value: 2.82e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082537 231 VLVCGGDGTVGWVLDAIDEMKIKgqekyipeVAVLPLGTGNDLSNTL-GWGTGYageIPVAQVLRNVME 298
Cdd:PRK12361  301 VIACGGDGTVTEVASELVNTDIT--------LGIIPLGTANALSHALfGLGSKL---IPVEQACDNIIQ 358
C1_DGKbeta_rpt2 cd20891
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase beta ...
 120-181 6.99e-05

second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase beta (DAG kinase beta) and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase beta, also called 90 kDa diacylglycerol kinase, or diglyceride kinase beta (DGK-beta), exhibits high phosphorylation activity for long-chain diacylglycerols. 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 beta contains two copies of the C1 domain. This model corresponds to the second one. DGK-beta 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: 410441  Cd Length: 59  Bit Score: 40.74  E-value: 6.99e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907082537 120 MPHHWIRGNVPlcSYCVFCRQQCGSQPKLCDYRCIWCQKTVHDECmrGSLRSEKCDFGEFRN 181
Cdd:cd20891     1 MHHFWVEGNCP--TKCDKCHKTIKCYQGLTGLHCVWCQITLHNKC--ASHVKPECDCGPLKD 58
C1_DGKgamma_rpt2 cd20892
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase gamma ...
 122-186 1.18e-04

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: 40.18  E-value: 1.18e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907082537 122 HHWIRGNVPLcsYCVFCRQQCGSQPKLCDYRCIWCQKTVHDECmrGSLRSEKCDFGEFRNLIIPP 186
Cdd:cd20892     1 HVWVEGNSPV--KCDRCHKSIKCYQGLTGLHCVWCQITLHNKC--ASHVSPECDGGQLKDHILLP 61
PRK13054 PRK13054
lipid kinase; Reviewed
 230-272 1.28e-04

lipid kinase; Reviewed


Pssm-ID: 237281 [Multi-domain]  Cd Length: 300  Bit Score: 44.09  E-value: 1.28e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1907082537 230 RVLVCGGDGTVGWVLDAIdemkIKGQEKYIPEVAVLPLGTGND 272
Cdd:PRK13054   59 TVIAGGGDGTINEVATAL----AQLEGDARPALGILPLGTAND 97
PRK13059 PRK13059
putative lipid kinase; Reviewed
 231-278 2.98e-04

putative lipid kinase; Reviewed


Pssm-ID: 183858  Cd Length: 295  Bit Score: 42.72  E-value: 2.98e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1907082537 231 VLVCGGDGTVGWVLDAIDEMKIKgqekyIPeVAVLPLGTGNDLSNTLG 278
Cdd:PRK13059   60 ILIAGGDGTVDNVVNAMKKLNID-----LP-IGILPVGTANDFAKFLG 101
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
 122-166 3.27e-04

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: 38.58  E-value: 3.27e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1907082537 122 HHWIRGNVPLCSYCVFCRQQCGSQPKLCdYRCIWCQKTVHDECMR 166
Cdd:pfam00130   1 HHFVHRNFKQPTFCDHCGEFLWGLGKQG-LKCSWCKLNVHKRCHE 44
PRK13057 PRK13057
lipid kinase;
230-278 2.34e-03

lipid kinase;


Pssm-ID: 183857 [Multi-domain]  Cd Length: 287  Bit Score: 39.90  E-value: 2.34e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1907082537 230 RVLVCGGDGTVGWVLDAIDEMKIKgqekyipeVAVLPLGTGNDLSNTLG 278
Cdd:PRK13057   53 LVIVGGGDGTLNAAAPALVETGLP--------LGILPLGTANDLARTLG 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.
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