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Conserved domains on  [gi|386767330|ref|NP_995775|]
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diacyl glycerol kinase, isoform I [Drosophila melanogaster]

Protein Classification

diacylglycerol kinase( domain architecture ID 10637089)

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

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 ...
 520-711 8.50e-80

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: 252.26  E-value: 8.50e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767330   520 IINNYFSVGVDAAICVKFHLEREKNPHKFNSRMKNKLWYFEYATSETFAASCKNLHESIEIVCDGVALDLANgpHLQGVA 599
Cdd:smart00045   1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLPN--SLEGIA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767330   600 LLNIPYTHGGSNLWGEhlsqkrirksagpfgkskklragdkefsatsFNSVDLSVAIQDFGDRLIEVIGLENCLHMGQVR 679
Cdd:smart00045  79 VLNIPSYGGGTNLWGT-------------------------------TDKEDLNFSKQSHDDGLLEVVGLTGAMHMAQIR 127

                          170       180       190
                   ....*....|....*....|....*....|....
gi 386767330   680 tGLRASGRRLAQCSEV--IIKTKKTFPMQIDGEP 711
Cdd:smart00045 128 -QVGLAGRRIAQCSEVriTIKTSKTIPMQVDGEP 160
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 90-211 1.87e-55

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: 185.96  E-value: 1.87e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767330    90 LVFVNPKSGGRQGDRILRKFQYMLNPRQVYDLSKGGPKEGLTLFKDLPRF-RVICCGGDGTVGWVLEAMDSIELASQ-PA 167
Cdd:smart00046   1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVPDFnRVLVCGGDGTVGWVLNALDKRELPLPePP 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 386767330   168 IGVIPLGTGNDLARCLRWGGGYEGENIPKLMDKFRRASTVMLDR 211
Cdd:smart00046  81 VAVLPLGTGNDLARSLGWGGGYDGEKLLKTLRDALESDTVKLDR 124
 
Name Accession Description Interval E-value
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 520-711 8.50e-80

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: 252.26  E-value: 8.50e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767330   520 IINNYFSVGVDAAICVKFHLEREKNPHKFNSRMKNKLWYFEYATSETFAASCKNLHESIEIVCDGVALDLANgpHLQGVA 599
Cdd:smart00045   1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLPN--SLEGIA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767330   600 LLNIPYTHGGSNLWGEhlsqkrirksagpfgkskklragdkefsatsFNSVDLSVAIQDFGDRLIEVIGLENCLHMGQVR 679
Cdd:smart00045  79 VLNIPSYGGGTNLWGT-------------------------------TDKEDLNFSKQSHDDGLLEVVGLTGAMHMAQIR 127

                          170       180       190
                   ....*....|....*....|....*....|....
gi 386767330   680 tGLRASGRRLAQCSEV--IIKTKKTFPMQIDGEP 711
Cdd:smart00045 128 -QVGLAGRRIAQCSEVriTIKTSKTIPMQVDGEP 160
DAGK_acc pfam00609
Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts ...
 520-711 6.03e-63

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: 207.45  E-value: 6.03e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767330  520 IINNYFSVGVDAAICVKFHLEREKNPHKFNSRMKNKLWYFEYATSETFAASCKNLHESIEIVCDGVALDLanGPHLQGVA 599
Cdd:pfam00609   1 VMNNYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDMFQRSCKNLIEKVELEVDGKDLPL--PKSLEGIV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767330  600 LLNIPYTHGGSNLWGEhlsqkrirksagpfgkSKKlragdkefsatsfnsVDLSVAIQDFGDRLIEVIGLENCLHMGQVR 679
Cdd:pfam00609  79 VLNIPSYAGGTDLWGN----------------SKE---------------DGLGFAPQSVDDGLLEVVGLTGALHLGQVQ 127

                         170       180       190
                  ....*....|....*....|....*....|..
gi 386767330  680 TGLRaSGRRLAQCSEVIIKTKKTFPMQIDGEP 711
Cdd:pfam00609 128 VGLG-SAKRIAQGGPIRITTKKKIPMQVDGEP 158
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 90-211 1.87e-55

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: 185.96  E-value: 1.87e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767330    90 LVFVNPKSGGRQGDRILRKFQYMLNPRQVYDLSKGGPKEGLTLFKDLPRF-RVICCGGDGTVGWVLEAMDSIELASQ-PA 167
Cdd:smart00046   1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVPDFnRVLVCGGDGTVGWVLNALDKRELPLPePP 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 386767330   168 IGVIPLGTGNDLARCLRWGGGYEGENIPKLMDKFRRASTVMLDR 211
Cdd:smart00046  81 VAVLPLGTGNDLARSLGWGGGYDGEKLLKTLRDALESDTVKLDR 124
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 88-210 8.38e-38

Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. The catalytic domain is assumed from the finding of bacterial homologs. YegS is the Escherichia coli protein in this family whose crystal structure reveals an active site in the inter-domain cleft formed by four conserved sequence motifs, revealing a novel metal-binding site. The residues of this site are conserved across the family.


Pssm-ID: 425868 [Multi-domain]  Cd Length: 125  Bit Score: 136.95  E-value: 8.38e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767330   88 PLLVFVNPKSGGRQGDRILRKFQYMLNPRQV-YDLSK-GGPKEGLTLFKDLPR---FRVICCGGDGTVGWVLEAMDsiEL 162
Cdd:pfam00781   1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVeVELVLtEGPGDALELAREAAEdgyDRIVVAGGDGTVNEVLNGLA--GL 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 386767330  163 ASQPAIGVIPLGTGNDLARCLRWGGgyegeNIPKLMDKFRRASTVMLD 210
Cdd:pfam00781  79 ATRPPLGIIPLGTGNDFARALGIPG-----DPEEALEAILKGQTRPVD 121
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 89-183 1.20e-13

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


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 72.19  E-value: 1.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767330  89 LLVFVNPKSGGRQGDRILRKFQYMLNPR----QVYDLSKGGPKEGLT--LFKDLPRfRVICCGGDGTVGWVLEAMdsieL 162
Cdd:COG1597    5 ALLIVNPASGRGRAARLLERLVAALRAAglevEVLETESPGDATELAreAAAEGAD-LVVAAGGDGTVNEVANGL----A 79

                         90       100
                 ....*....|....*....|.
gi 386767330 163 ASQPAIGVIPLGTGNDLARCL 183
Cdd:COG1597   80 GTGPPLGILPLGTGNDFARAL 100
PRK13054 PRK13054
lipid kinase; Reviewed
 140-181 1.83e-08

lipid kinase; Reviewed


Pssm-ID: 237281 [Multi-domain]  Cd Length: 300  Bit Score: 56.42  E-value: 1.83e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 386767330 140 RVICCGGDGTVGWVLEAMDSIELASQPAIGVIPLGTGNDLAR 181
Cdd:PRK13054  59 TVIAGGGDGTINEVATALAQLEGDARPALGILPLGTANDFAT 100
TIGR00147 TIGR00147
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ...
 90-183 3.40e-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: 49.42  E-value: 3.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767330   90 LVFVNPKSGGRQGDRILRKFQYMLNPRQVYDLSKGGPKEGltlfkDLPRF----------RVICCGGDGTVGWVLEAMds 159
Cdd:TIGR00147   5 PAILNPTAGKSNDNKPLREVIMLLREEGMEIHVRVTWEKG-----DAARYveearkfgvdTVIAGGGDGTINEVVNAL-- 77

                          90       100
                  ....*....|....*....|....
gi 386767330  160 IELASQPAIGVIPLGTGNDLARCL 183
Cdd:TIGR00147  78 IQLDDIPALGILPLGTANDFARSL 101
 
Name Accession Description Interval E-value
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 520-711 8.50e-80

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: 252.26  E-value: 8.50e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767330   520 IINNYFSVGVDAAICVKFHLEREKNPHKFNSRMKNKLWYFEYATSETFAASCKNLHESIEIVCDGVALDLANgpHLQGVA 599
Cdd:smart00045   1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLPN--SLEGIA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767330   600 LLNIPYTHGGSNLWGEhlsqkrirksagpfgkskklragdkefsatsFNSVDLSVAIQDFGDRLIEVIGLENCLHMGQVR 679
Cdd:smart00045  79 VLNIPSYGGGTNLWGT-------------------------------TDKEDLNFSKQSHDDGLLEVVGLTGAMHMAQIR 127

                          170       180       190
                   ....*....|....*....|....*....|....
gi 386767330   680 tGLRASGRRLAQCSEV--IIKTKKTFPMQIDGEP 711
Cdd:smart00045 128 -QVGLAGRRIAQCSEVriTIKTSKTIPMQVDGEP 160
DAGK_acc pfam00609
Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts ...
 520-711 6.03e-63

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: 207.45  E-value: 6.03e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767330  520 IINNYFSVGVDAAICVKFHLEREKNPHKFNSRMKNKLWYFEYATSETFAASCKNLHESIEIVCDGVALDLanGPHLQGVA 599
Cdd:pfam00609   1 VMNNYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDMFQRSCKNLIEKVELEVDGKDLPL--PKSLEGIV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767330  600 LLNIPYTHGGSNLWGEhlsqkrirksagpfgkSKKlragdkefsatsfnsVDLSVAIQDFGDRLIEVIGLENCLHMGQVR 679
Cdd:pfam00609  79 VLNIPSYAGGTDLWGN----------------SKE---------------DGLGFAPQSVDDGLLEVVGLTGALHLGQVQ 127

                         170       180       190
                  ....*....|....*....|....*....|..
gi 386767330  680 TGLRaSGRRLAQCSEVIIKTKKTFPMQIDGEP 711
Cdd:pfam00609 128 VGLG-SAKRIAQGGPIRITTKKKIPMQVDGEP 158
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 90-211 1.87e-55

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: 185.96  E-value: 1.87e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767330    90 LVFVNPKSGGRQGDRILRKFQYMLNPRQVYDLSKGGPKEGLTLFKDLPRF-RVICCGGDGTVGWVLEAMDSIELASQ-PA 167
Cdd:smart00046   1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVPDFnRVLVCGGDGTVGWVLNALDKRELPLPePP 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 386767330   168 IGVIPLGTGNDLARCLRWGGGYEGENIPKLMDKFRRASTVMLDR 211
Cdd:smart00046  81 VAVLPLGTGNDLARSLGWGGGYDGEKLLKTLRDALESDTVKLDR 124
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 88-210 8.38e-38

Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. The catalytic domain is assumed from the finding of bacterial homologs. YegS is the Escherichia coli protein in this family whose crystal structure reveals an active site in the inter-domain cleft formed by four conserved sequence motifs, revealing a novel metal-binding site. The residues of this site are conserved across the family.


Pssm-ID: 425868 [Multi-domain]  Cd Length: 125  Bit Score: 136.95  E-value: 8.38e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767330   88 PLLVFVNPKSGGRQGDRILRKFQYMLNPRQV-YDLSK-GGPKEGLTLFKDLPR---FRVICCGGDGTVGWVLEAMDsiEL 162
Cdd:pfam00781   1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVeVELVLtEGPGDALELAREAAEdgyDRIVVAGGDGTVNEVLNGLA--GL 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 386767330  163 ASQPAIGVIPLGTGNDLARCLRWGGgyegeNIPKLMDKFRRASTVMLD 210
Cdd:pfam00781  79 ATRPPLGIIPLGTGNDFARALGIPG-----DPEEALEAILKGQTRPVD 121
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 89-183 1.20e-13

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


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 72.19  E-value: 1.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767330  89 LLVFVNPKSGGRQGDRILRKFQYMLNPR----QVYDLSKGGPKEGLT--LFKDLPRfRVICCGGDGTVGWVLEAMdsieL 162
Cdd:COG1597    5 ALLIVNPASGRGRAARLLERLVAALRAAglevEVLETESPGDATELAreAAAEGAD-LVVAAGGDGTVNEVANGL----A 79

                         90       100
                 ....*....|....*....|.
gi 386767330 163 ASQPAIGVIPLGTGNDLARCL 183
Cdd:COG1597   80 GTGPPLGILPLGTGNDFARAL 100
PRK13054 PRK13054
lipid kinase; Reviewed
 140-181 1.83e-08

lipid kinase; Reviewed


Pssm-ID: 237281 [Multi-domain]  Cd Length: 300  Bit Score: 56.42  E-value: 1.83e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 386767330 140 RVICCGGDGTVGWVLEAMDSIELASQPAIGVIPLGTGNDLAR 181
Cdd:PRK13054  59 TVIAGGGDGTINEVATALAQLEGDARPALGILPLGTANDFAT 100
PRK13059 PRK13059
putative lipid kinase; Reviewed
 94-183 1.26e-06

putative lipid kinase; Reviewed


Pssm-ID: 183858  Cd Length: 295  Bit Score: 50.81  E-value: 1.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767330  94 NPKSGGR----QGDRILRKFQ---YMLNPrqvYDLSKGGP-KEGLTLFKDLPRFrVICCGGDGTVGWVLEAMDSIELaSQ 165
Cdd:PRK13059   9 NPYSGENaiisELDKVIRIHQekgYLVVP---YRISLEYDlKNAFKDIDESYKY-ILIAGGDGTVDNVVNAMKKLNI-DL 83

                         90
                 ....*....|....*...
gi 386767330 166 PaIGVIPLGTGNDLARCL 183
Cdd:PRK13059  84 P-IGILPVGTANDFAKFL 100
TIGR00147 TIGR00147
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ...
 90-183 3.40e-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: 49.42  E-value: 3.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767330   90 LVFVNPKSGGRQGDRILRKFQYMLNPRQVYDLSKGGPKEGltlfkDLPRF----------RVICCGGDGTVGWVLEAMds 159
Cdd:TIGR00147   5 PAILNPTAGKSNDNKPLREVIMLLREEGMEIHVRVTWEKG-----DAARYveearkfgvdTVIAGGGDGTINEVVNAL-- 77

                          90       100
                  ....*....|....*....|....
gi 386767330  160 IELASQPAIGVIPLGTGNDLARCL 183
Cdd:TIGR00147  78 IQLDDIPALGILPLGTANDFARSL 101
PRK12361 PRK12361
hypothetical protein; Provisional
 91-183 4.44e-06

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 50.00  E-value: 4.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767330  91 VFVNPKSGGRQGDR----ILRKFQ--YMLNPRQV------YDLSKGGPKEGLTLfkdlprfrVICCGGDGTVGwvleamd 158
Cdd:PRK12361 247 LIANPVSGGGKWQEygeqIQRELKayFDLTVKLTtpeisaEALAKQARKAGADI--------VIACGGDGTVT------- 311

                         90       100       110
                 ....*....|....*....|....*....|
gi 386767330 159 siELASQPA-----IGVIPLGTGNDLARCL 183
Cdd:PRK12361 312 --EVASELVntditLGIIPLGTANALSHAL 339
PRK13057 PRK13057
lipid kinase;
140-184 3.94e-05

lipid kinase;


Pssm-ID: 183857 [Multi-domain]  Cd Length: 287  Bit Score: 46.06  E-value: 3.94e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 386767330 140 RVICCGGDGTVGWVLEAMdsieLASQPAIGVIPLGTGNDLARCLR 184
Cdd:PRK13057  53 LVIVGGGDGTLNAAAPAL----VETGLPLGILPLGTANDLARTLG 93
PRK13055 PRK13055
putative lipid kinase; Reviewed
 141-184 1.24e-03

putative lipid kinase; Reviewed


Pssm-ID: 237282 [Multi-domain]  Cd Length: 334  Bit Score: 41.90  E-value: 1.24e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 386767330 141 VICCGGDGTVGWVLEAMdsIELASQPAIGVIPLGTGNDLARCLR 184
Cdd:PRK13055  63 IIAAGGDGTINEVVNGI--APLEKRPKMAIIPAGTTNDYARALK 104
PRK00861 PRK00861
putative lipid kinase; Reviewed
 90-183 5.94e-03

putative lipid kinase; Reviewed


Pssm-ID: 234850 [Multi-domain]  Cd Length: 300  Bit Score: 39.60  E-value: 5.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767330  90 LVFvNPKSGGRQGDRILRKFQYMLNPRQVYDLSKGGPKEGLTLFKDLPRFR----VICCGGDGTVGWVLEAMdsieLASQ 165
Cdd:PRK00861   7 LIF-NPVAGQGNPEVDLALIRAILEPEMDLDIYLTTPEIGADQLAQEAIERgaelIIASGGDGTLSAVAGAL----IGTD 81

                         90
                 ....*....|....*...
gi 386767330 166 PAIGVIPLGTGNDLARCL 183
Cdd:PRK00861  82 IPLGIIPRGTANAFAAAL 99
 
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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