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Conserved domains on  [gi|240256105|ref|NP_567845|]
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diacylglycerol kinase 7 [Arabidopsis thaliana]

Protein Classification

diacylglycerol kinase( domain architecture ID 10466505)

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
DAGK_acc pfam00609
Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts ...
287-464 4.39e-62

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: 199.75  E-value: 4.39e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256105  287 VFYNYFSIGMDAQVAYGFHHLRNEKPYLAQGPVTNKIIYSSYSCTQGwFCTPCVNNPALRGLrnimkihikkaNCsEWEE 366
Cdd:pfam00609   1 VMNNYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDM-FQRSCKNLIEKVEL-----------EV-DGKD 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256105  367 IHVPKSVRSIVVLNLYNYGSGRHPWGNLRPKYLekrGFVEAHCDDGLIEIFGLKQGWHASFVMAEIISAKHIAQAAAIRF 446
Cdd:pfam00609  68 LPLPKSLEGIVVLNIPSYAGGTDLWGNSKEDGL---GFAPQSVDDGLLEVVGLTGALHLGQVQVGLGSAKRIAQGGPIRI 144
                         170
                  ....*....|....*...
gi 240256105  447 ELRggdwKNAFLQMDGEP 464
Cdd:pfam00609 145 TTK----KKIPMQVDGEP 158
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
94-234 3.67e-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: 119.23  E-value: 3.67e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256105   94 PMVVFINPKSGGRHGPVLKERLQQLMTEEQV-FDLTEVKPhefvryglgcldtlAAKGDECARECREKI--RIMVAGGDG 170
Cdd:pfam00781   1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVeVELVLTEG--------------PGDALELAREAAEDGydRIVVAGGDG 66
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 240256105  171 TVGWVLGCLGELHkdgksHIPPVGVIPLGTGNDLSRSFSWGGSFPFAWRSAMKRTLHRATLGSI 234
Cdd:pfam00781  67 TVNEVLNGLAGLA-----TRPPLGIIPLGTGNDFARALGIPGDPEEALEAILKGQTRPVDVGKV 125
 
Name Accession Description Interval E-value
DAGK_acc pfam00609
Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts ...
287-464 4.39e-62

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: 199.75  E-value: 4.39e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256105  287 VFYNYFSIGMDAQVAYGFHHLRNEKPYLAQGPVTNKIIYSSYSCTQGwFCTPCVNNPALRGLrnimkihikkaNCsEWEE 366
Cdd:pfam00609   1 VMNNYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDM-FQRSCKNLIEKVEL-----------EV-DGKD 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256105  367 IHVPKSVRSIVVLNLYNYGSGRHPWGNLRPKYLekrGFVEAHCDDGLIEIFGLKQGWHASFVMAEIISAKHIAQAAAIRF 446
Cdd:pfam00609  68 LPLPKSLEGIVVLNIPSYAGGTDLWGNSKEDGL---GFAPQSVDDGLLEVVGLTGALHLGQVQVGLGSAKRIAQGGPIRI 144
                         170
                  ....*....|....*...
gi 240256105  447 ELRggdwKNAFLQMDGEP 464
Cdd:pfam00609 145 TTK----KKIPMQVDGEP 158
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
94-234 3.67e-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: 119.23  E-value: 3.67e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256105   94 PMVVFINPKSGGRHGPVLKERLQQLMTEEQV-FDLTEVKPhefvryglgcldtlAAKGDECARECREKI--RIMVAGGDG 170
Cdd:pfam00781   1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVeVELVLTEG--------------PGDALELAREAAEDGydRIVVAGGDG 66
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 240256105  171 TVGWVLGCLGELHkdgksHIPPVGVIPLGTGNDLSRSFSWGGSFPFAWRSAMKRTLHRATLGSI 234
Cdd:pfam00781  67 TVNEVLNGLAGLA-----TRPPLGIIPLGTGNDFARALGIPGDPEEALEAILKGQTRPVDVGKV 125
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
96-212 2.56e-25

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: 100.45  E-value: 2.56e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256105    96 VVFINPKSGGRHGPVLKERLQQLMTEEQVFDLTEVKPhefvryglgcldtlaAKGDECARECREKIRIMVAGGDGTVGWV 175
Cdd:smart00046   1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGP---------------AVALVIFRDVPDFNRVLVCGGDGTVGWV 65
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 240256105   176 LGCLgeLHKDGKSHIPPVGVIPLGTGNDLSRSFSWGG 212
Cdd:smart00046  66 LNAL--DKRELPLPEPPVAVLPLGTGNDLARSLGWGG 100
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
287-464 1.21e-24

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: 99.72  E-value: 1.21e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256105   287 VFYNYFSIGMDAQVAYGFHHLRNEKPYLAQGPVTNKIIYSSYsctqgwfctpcvnnpalrGLRNIMKIHIKkaNCSEW-- 364
Cdd:smart00045   1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFEL------------------GTKDLFFRTCK--DLHERie 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256105   365 -----EEIHVPKSVRSIVVLNLYNYGSGRHPWGNLRPKYLEkrgFVEAHCDDGLIEIFGLKQGWHASFVMAEIISAKHIA 439
Cdd:smart00045  61 lecdgVDVDLPNSLEGIAVLNIPSYGGGTNLWGTTDKEDLN---FSKQSHDDGLLEVVGLTGAMHMAQIRQVGLAGRRIA 137
                          170       180
                   ....*....|....*....|....*.
gi 240256105   440 QAAAIRFELRGgdwKNAF-LQMDGEP 464
Cdd:smart00045 138 QCSEVRITIKT---SKTIpMQVDGEP 160
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
96-464 6.94e-13

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


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 69.11  E-value: 6.94e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256105  96 VVFINPKSGGRHGPVLKERLQQLMtEEQVFDLTEVKPHEfvryglgcldtlAAKGDECARE-CREKI-RIMVAGGDGTVG 173
Cdd:COG1597    6 LLIVNPASGRGRAARLLERLVAAL-RAAGLEVEVLETES------------PGDATELAREaAAEGAdLVVAAGGDGTVN 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256105 174 WVLGCLgeLHKDgkshiPPVGVIPLGTGNDLSRSFswggSFPFAWRSAMKRTLHratlGSIARLDswkivvsmpSGEVvd 253
Cdd:COG1597   73 EVANGL--AGTG-----PPLGILPLGTGNDFARAL----GIPLDPEAALEALLT----GRTRRID---------LGRV-- 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256105 254 ppyslkptieetaldqaldaDGDvppkaksyegVFYNYFSIGMDAQVAYGFHHLRNEKPylaqGPVtnkiiysSYsctqg 333
Cdd:COG1597  127 --------------------NGR----------YFLNVAGIGFDAEVVERANRALKRRL----GKL-------AY----- 160
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256105 334 wfctpcvnnpALRGLRNIMKIHIKKANCsEWEEIHVPKSVRSIVVLNLYNYGSGRHPwgnlrpkylekrgFVEAHCDDGL 413
Cdd:COG1597  161 ----------VLAALRALLRYRPFRLRI-ELDGEEIEGEALLVAVGNGPYYGGGLRL-------------APDASLDDGL 216
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256105 414 IEIFGLKQG--WHASFVMAEIISAKHIA-------QAAAIRFELRggdwKNAFLQMDGEP 464
Cdd:COG1597  217 LDVVVVRPLsrLRLLRLLPRLLRGRHLRhpgvryfRAREVEIESD----RPLPVQLDGEP 272
TIGR00147 TIGR00147
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ...
92-209 3.72e-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: 48.65  E-value: 3.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256105   92 HAPMVvfINPKSGGRHGPVLKERLQQLMTEEQVFDLTEVKPHEFVryglgcldtlAAKGDECAREcREKIRIMVAGGDGT 171
Cdd:TIGR00147   3 EAPAI--LNPTAGKSNDNKPLREVIMLLREEGMEIHVRVTWEKGD----------AARYVEEARK-FGVDTVIAGGGDGT 69
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 240256105  172 VGWVLGCLGELHKdgkshIPPVGVIPLGTGNDLSRSFS 209
Cdd:TIGR00147  70 INEVVNALIQLDD-----IPALGILPLGTANDFARSLG 102
PRK12361 PRK12361
hypothetical protein; Provisional
89-205 8.12e-05

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 45.00  E-value: 8.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256105  89 MAPHAPMVVFINPKSGGRHGPVLKERLQQLMTEEqvFDLTEVKPHEFVRyglgcLDTLAAKgdecARECREKIrIMVAGG 168
Cdd:PRK12361 239 LNIHKRAWLIANPVSGGGKWQEYGEQIQRELKAY--FDLTVKLTTPEIS-----AEALAKQ----ARKAGADI-VIACGG 306
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 240256105 169 DGTVGWVLGCLgeLHKDGKshippVGVIPLGTGNDLS 205
Cdd:PRK12361 307 DGTVTEVASEL--VNTDIT-----LGIIPLGTANALS 336
 
Name Accession Description Interval E-value
DAGK_acc pfam00609
Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts ...
287-464 4.39e-62

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: 199.75  E-value: 4.39e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256105  287 VFYNYFSIGMDAQVAYGFHHLRNEKPYLAQGPVTNKIIYSSYSCTQGwFCTPCVNNPALRGLrnimkihikkaNCsEWEE 366
Cdd:pfam00609   1 VMNNYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDM-FQRSCKNLIEKVEL-----------EV-DGKD 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256105  367 IHVPKSVRSIVVLNLYNYGSGRHPWGNLRPKYLekrGFVEAHCDDGLIEIFGLKQGWHASFVMAEIISAKHIAQAAAIRF 446
Cdd:pfam00609  68 LPLPKSLEGIVVLNIPSYAGGTDLWGNSKEDGL---GFAPQSVDDGLLEVVGLTGALHLGQVQVGLGSAKRIAQGGPIRI 144
                         170
                  ....*....|....*...
gi 240256105  447 ELRggdwKNAFLQMDGEP 464
Cdd:pfam00609 145 TTK----KKIPMQVDGEP 158
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
94-234 3.67e-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: 119.23  E-value: 3.67e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256105   94 PMVVFINPKSGGRHGPVLKERLQQLMTEEQV-FDLTEVKPhefvryglgcldtlAAKGDECARECREKI--RIMVAGGDG 170
Cdd:pfam00781   1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVeVELVLTEG--------------PGDALELAREAAEDGydRIVVAGGDG 66
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 240256105  171 TVGWVLGCLGELHkdgksHIPPVGVIPLGTGNDLSRSFSWGGSFPFAWRSAMKRTLHRATLGSI 234
Cdd:pfam00781  67 TVNEVLNGLAGLA-----TRPPLGIIPLGTGNDFARALGIPGDPEEALEAILKGQTRPVDVGKV 125
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
96-212 2.56e-25

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: 100.45  E-value: 2.56e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256105    96 VVFINPKSGGRHGPVLKERLQQLMTEEQVFDLTEVKPhefvryglgcldtlaAKGDECARECREKIRIMVAGGDGTVGWV 175
Cdd:smart00046   1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGP---------------AVALVIFRDVPDFNRVLVCGGDGTVGWV 65
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 240256105   176 LGCLgeLHKDGKSHIPPVGVIPLGTGNDLSRSFSWGG 212
Cdd:smart00046  66 LNAL--DKRELPLPEPPVAVLPLGTGNDLARSLGWGG 100
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
287-464 1.21e-24

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: 99.72  E-value: 1.21e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256105   287 VFYNYFSIGMDAQVAYGFHHLRNEKPYLAQGPVTNKIIYSSYsctqgwfctpcvnnpalrGLRNIMKIHIKkaNCSEW-- 364
Cdd:smart00045   1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFEL------------------GTKDLFFRTCK--DLHERie 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256105   365 -----EEIHVPKSVRSIVVLNLYNYGSGRHPWGNLRPKYLEkrgFVEAHCDDGLIEIFGLKQGWHASFVMAEIISAKHIA 439
Cdd:smart00045  61 lecdgVDVDLPNSLEGIAVLNIPSYGGGTNLWGTTDKEDLN---FSKQSHDDGLLEVVGLTGAMHMAQIRQVGLAGRRIA 137
                          170       180
                   ....*....|....*....|....*.
gi 240256105   440 QAAAIRFELRGgdwKNAF-LQMDGEP 464
Cdd:smart00045 138 QCSEVRITIKT---SKTIpMQVDGEP 160
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
96-464 6.94e-13

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


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 69.11  E-value: 6.94e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256105  96 VVFINPKSGGRHGPVLKERLQQLMtEEQVFDLTEVKPHEfvryglgcldtlAAKGDECARE-CREKI-RIMVAGGDGTVG 173
Cdd:COG1597    6 LLIVNPASGRGRAARLLERLVAAL-RAAGLEVEVLETES------------PGDATELAREaAAEGAdLVVAAGGDGTVN 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256105 174 WVLGCLgeLHKDgkshiPPVGVIPLGTGNDLSRSFswggSFPFAWRSAMKRTLHratlGSIARLDswkivvsmpSGEVvd 253
Cdd:COG1597   73 EVANGL--AGTG-----PPLGILPLGTGNDFARAL----GIPLDPEAALEALLT----GRTRRID---------LGRV-- 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256105 254 ppyslkptieetaldqaldaDGDvppkaksyegVFYNYFSIGMDAQVAYGFHHLRNEKPylaqGPVtnkiiysSYsctqg 333
Cdd:COG1597  127 --------------------NGR----------YFLNVAGIGFDAEVVERANRALKRRL----GKL-------AY----- 160
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256105 334 wfctpcvnnpALRGLRNIMKIHIKKANCsEWEEIHVPKSVRSIVVLNLYNYGSGRHPwgnlrpkylekrgFVEAHCDDGL 413
Cdd:COG1597  161 ----------VLAALRALLRYRPFRLRI-ELDGEEIEGEALLVAVGNGPYYGGGLRL-------------APDASLDDGL 216
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256105 414 IEIFGLKQG--WHASFVMAEIISAKHIA-------QAAAIRFELRggdwKNAFLQMDGEP 464
Cdd:COG1597  217 LDVVVVRPLsrLRLLRLLPRLLRGRHLRhpgvryfRAREVEIESD----RPLPVQLDGEP 272
TIGR00147 TIGR00147
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ...
92-209 3.72e-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: 48.65  E-value: 3.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256105   92 HAPMVvfINPKSGGRHGPVLKERLQQLMTEEQVFDLTEVKPHEFVryglgcldtlAAKGDECAREcREKIRIMVAGGDGT 171
Cdd:TIGR00147   3 EAPAI--LNPTAGKSNDNKPLREVIMLLREEGMEIHVRVTWEKGD----------AARYVEEARK-FGVDTVIAGGGDGT 69
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 240256105  172 VGWVLGCLGELHKdgkshIPPVGVIPLGTGNDLSRSFS 209
Cdd:TIGR00147  70 INEVVNALIQLDD-----IPALGILPLGTANDFARSLG 102
PRK12361 PRK12361
hypothetical protein; Provisional
89-205 8.12e-05

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 45.00  E-value: 8.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256105  89 MAPHAPMVVFINPKSGGRHGPVLKERLQQLMTEEqvFDLTEVKPHEFVRyglgcLDTLAAKgdecARECREKIrIMVAGG 168
Cdd:PRK12361 239 LNIHKRAWLIANPVSGGGKWQEYGEQIQRELKAY--FDLTVKLTTPEIS-----AEALAKQ----ARKAGADI-VIACGG 306
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 240256105 169 DGTVGWVLGCLgeLHKDGKshippVGVIPLGTGNDLS 205
Cdd:PRK12361 307 DGTVTEVASEL--VNTDIT-----LGIIPLGTANALS 336
PRK13057 PRK13057
lipid kinase;
97-207 1.30e-04

lipid kinase;


Pssm-ID: 183857 [Multi-domain]  Cd Length: 287  Bit Score: 43.75  E-value: 1.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256105  97 VFINPKSggRHGpvlKERLQQLMTEEQVFDLTEVKPHEfvryglgcldtlaakgdECARECREKIR--------IMVAGG 168
Cdd:PRK13057   2 LLVNRHA--RSG---RAALAAARAALEAAGLELVEPPA-----------------EDPDDLSEVIEayadgvdlVIVGGG 59
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 240256105 169 DGTVGWVLGCLGE--LhkdgkshipPVGVIPLGTGNDLSRS 207
Cdd:PRK13057  60 DGTLNAAAPALVEtgL---------PLGILPLGTANDLART 91
PRK13054 PRK13054
lipid kinase; Reviewed
149-207 2.47e-04

lipid kinase; Reviewed


Pssm-ID: 237281 [Multi-domain]  Cd Length: 300  Bit Score: 42.94  E-value: 2.47e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 240256105 149 KGDeCARECREKI-----RIMVAGGDGTVGWVLGCLGELHKDgksHIPPVGVIPLGTGNDLSRS 207
Cdd:PRK13054  42 KGD-AARYVEEALalgvaTVIAGGGDGTINEVATALAQLEGD---ARPALGILPLGTANDFATA 101
PRK13059 PRK13059
putative lipid kinase; Reviewed
163-206 2.80e-04

putative lipid kinase; Reviewed


Pssm-ID: 183858  Cd Length: 295  Bit Score: 42.72  E-value: 2.80e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 240256105 163 IMVAGGDGTVGWVLGCLGELHKDgkshiPPVGVIPLGTGNDLSR 206
Cdd:PRK13059  60 ILIAGGDGTVDNVVNAMKKLNID-----LPIGILPVGTANDFAK 98
PRK13337 PRK13337
putative lipid kinase; Reviewed
100-207 2.95e-04

putative lipid kinase; Reviewed


Pssm-ID: 183982 [Multi-domain]  Cd Length: 304  Bit Score: 42.73  E-value: 2.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256105 100 NPKSG----GRHGPVLKERLQQLMTEEQVFDLTEVkphefvryglGCLdTLAAkgdECARECREKIrIMVAGGDGTVGWV 175
Cdd:PRK13337   9 NPTSGrelfKKNLPDVLQKLEQAGYETSAHATTGP----------GDA-TLAA---ERAVERKFDL-VIAAGGDGTLNEV 73
                         90       100       110
                 ....*....|....*....|....*....|..
gi 240256105 176 LGCLGElhkdgKSHIPPVGVIPLGTGNDLSRS 207
Cdd:PRK13337  74 VNGIAE-----KENRPKLGIIPVGTTNDFARA 100
PRK00861 PRK00861
putative lipid kinase; Reviewed
100-202 3.70e-04

putative lipid kinase; Reviewed


Pssm-ID: 234850 [Multi-domain]  Cd Length: 300  Bit Score: 42.30  E-value: 3.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256105 100 NPKSGGRHGPVLKERLQQLMTEEqvFDLtEVkphefvryglgCLDTLAAKGDECARECREK--IRIMVAGGDGTVGWVLG 177
Cdd:PRK00861  10 NPVAGQGNPEVDLALIRAILEPE--MDL-DI-----------YLTTPEIGADQLAQEAIERgaELIIASGGDGTLSAVAG 75
                         90       100
                 ....*....|....*....|....*
gi 240256105 178 CLGElhkdgkSHIPpVGVIPLGTGN 202
Cdd:PRK00861  76 ALIG------TDIP-LGIIPRGTAN 93
PRK11914 PRK11914
diacylglycerol kinase; Reviewed
97-208 1.14e-03

diacylglycerol kinase; Reviewed


Pssm-ID: 237021 [Multi-domain]  Cd Length: 306  Bit Score: 40.92  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256105  97 VFINPKSGGRHGPVLKERLQQLMTEEQVfDLTEVkphefvryglgcLDTLAAKGDECARECREK--IRIMVAGGDGTVGW 174
Cdd:PRK11914  13 VLTNPLSGHGAAPHAAERAIARLHHRGV-DVVEI------------VGTDAHDARHLVAAALAKgtDALVVVGGDGVISN 79
                         90       100       110
                 ....*....|....*....|....*....|....
gi 240256105 175 VLGCLGElhkdgkSHIPpVGVIPLGTGNDLSRSF 208
Cdd:PRK11914  80 ALQVLAG------TDIP-LGIIPAGTGNDHAREF 106
 
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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