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Conserved domains on  [gi|1032283489|gb|OAO97816|]
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DGK7 [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 1032283489 287 VFYNYFSIGMDAQVAYGFHHLRNEKPYLAQGPVTNKIIYSSYSCTQGwFCTPCVNNPALRGLrnimkihikkaNCsEWEE 366
Cdd:pfam00609   1 VMNNYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDM-FQRSCKNLIEKVEL-----------EV-DGKD 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283489 367 IHVPKSVRSIVVLNLYNYGSGRHPWGNLRPKYLekrGFVEAHCDDGLIEIFGLKQGWHASFVMAEIISAKHIAQAAAIRF 446
Cdd:pfam00609  68 LPLPKSLEGIVVLNIPSYAGGTDLWGNSKEDGL---GFAPQSVDDGLLEVVGLTGALHLGQVQVGLGSAKRIAQGGPIRI 144

                         170
                  ....*....|....*...
gi 1032283489 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 1032283489  94 PMVVFINPKSGGRHGPVLKERLQQLMTEEQV-FDLTEVKPhefvryglgcldtlAAKGDECARECREKI--RIMVAGGDG 170
Cdd:pfam00781   1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVeVELVLTEG--------------PGDALELAREAAEDGydRIVVAGGDG 66

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1032283489 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 1032283489 287 VFYNYFSIGMDAQVAYGFHHLRNEKPYLAQGPVTNKIIYSSYSCTQGwFCTPCVNNPALRGLrnimkihikkaNCsEWEE 366
Cdd:pfam00609   1 VMNNYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDM-FQRSCKNLIEKVEL-----------EV-DGKD 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283489 367 IHVPKSVRSIVVLNLYNYGSGRHPWGNLRPKYLekrGFVEAHCDDGLIEIFGLKQGWHASFVMAEIISAKHIAQAAAIRF 446
Cdd:pfam00609  68 LPLPKSLEGIVVLNIPSYAGGTDLWGNSKEDGL---GFAPQSVDDGLLEVVGLTGALHLGQVQVGLGSAKRIAQGGPIRI 144

                         170
                  ....*....|....*...
gi 1032283489 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 1032283489  94 PMVVFINPKSGGRHGPVLKERLQQLMTEEQV-FDLTEVKPhefvryglgcldtlAAKGDECARECREKI--RIMVAGGDG 170
Cdd:pfam00781   1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVeVELVLTEG--------------PGDALELAREAAEDGydRIVVAGGDG 66

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1032283489 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 1032283489   96 VVFINPKSGGRHGPVLKERLQQLMTEEQVFDLTEVKPhefvryglgcldtlaAKGDECARECREKIRIMVAGGDGTVGWV 175
Cdd:smart00046   1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGP---------------AVALVIFRDVPDFNRVLVCGGDGTVGWV 65

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1032283489  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 1032283489  287 VFYNYFSIGMDAQVAYGFHHLRNEKPYLAQGPVTNKIIYSSYsctqgwfctpcvnnpalrGLRNIMKIHIKkaNCSEW-- 364
Cdd:smart00045   1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFEL------------------GTKDLFFRTCK--DLHERie 60

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283489  365 -----EEIHVPKSVRSIVVLNLYNYGSGRHPWGNLRPKYLEkrgFVEAHCDDGLIEIFGLKQGWHASFVMAEIISAKHIA 439
Cdd:smart00045  61 lecdgVDVDLPNSLEGIAVLNIPSYGGGTNLWGTTDKEDLN---FSKQSHDDGLLEVVGLTGAMHMAQIRQVGLAGRRIA 137

                          170       180
                   ....*....|....*....|....*.
gi 1032283489  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 1032283489  96 VVFINPKSGGRHGPVLKERLQQLMtEEQVFDLTEVKPHEfvryglgcldtlAAKGDECARE-CREKI-RIMVAGGDGTVG 173
Cdd:COG1597     6 LLIVNPASGRGRAARLLERLVAAL-RAAGLEVEVLETES------------PGDATELAREaAAEGAdLVVAAGGDGTVN 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283489 174 WVLGCLgeLHKDgkshiPPVGVIPLGTGNDLSRSFswggSFPFAWRSAMKRTLHratlGSIARLDswkivvsmpSGEVvd 253
Cdd:COG1597    73 EVANGL--AGTG-----PPLGILPLGTGNDFARAL----GIPLDPEAALEALLT----GRTRRID---------LGRV-- 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283489 254 ppyslkptieetaldqaldaDGDvppkaksyegVFYNYFSIGMDAQVAYGFHHLRNEKPylaqGPVtnkiiysSYsctqg 333
Cdd:COG1597   127 --------------------NGR----------YFLNVAGIGFDAEVVERANRALKRRL----GKL-------AY----- 160

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283489 334 wfctpcvnnpALRGLRNIMKIHIKKANCsEWEEIHVPKSVRSIVVLNLYNYGSGRHPwgnlrpkylekrgFVEAHCDDGL 413
Cdd:COG1597   161 ----------VLAALRALLRYRPFRLRI-ELDGEEIEGEALLVAVGNGPYYGGGLRL-------------APDASLDDGL 216

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283489 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 1032283489  92 HAPMVvfINPKSGGRHGPVLKERLQQLMTEEQVFDLTEVKPHEFVryglgcldtlAAKGDECAREcREKIRIMVAGGDGT 171
Cdd:TIGR00147   3 EAPAI--LNPTAGKSNDNKPLREVIMLLREEGMEIHVRVTWEKGD----------AARYVEEARK-FGVDTVIAGGGDGT 69

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1032283489 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 1032283489  89 MAPHAPMVVFINPKSGGRHGPVLKERLQQLMTEEqvFDLTEVKPHEFVRyglgcLDTLAAKgdecARECREKIrIMVAGG 168
Cdd:PRK12361  239 LNIHKRAWLIANPVSGGGKWQEYGEQIQRELKAY--FDLTVKLTTPEIS-----AEALAKQ----ARKAGADI-VIACGG 306

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1032283489 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 1032283489 287 VFYNYFSIGMDAQVAYGFHHLRNEKPYLAQGPVTNKIIYSSYSCTQGwFCTPCVNNPALRGLrnimkihikkaNCsEWEE 366
Cdd:pfam00609   1 VMNNYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDM-FQRSCKNLIEKVEL-----------EV-DGKD 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283489 367 IHVPKSVRSIVVLNLYNYGSGRHPWGNLRPKYLekrGFVEAHCDDGLIEIFGLKQGWHASFVMAEIISAKHIAQAAAIRF 446
Cdd:pfam00609  68 LPLPKSLEGIVVLNIPSYAGGTDLWGNSKEDGL---GFAPQSVDDGLLEVVGLTGALHLGQVQVGLGSAKRIAQGGPIRI 144

                         170
                  ....*....|....*...
gi 1032283489 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 1032283489  94 PMVVFINPKSGGRHGPVLKERLQQLMTEEQV-FDLTEVKPhefvryglgcldtlAAKGDECARECREKI--RIMVAGGDG 170
Cdd:pfam00781   1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVeVELVLTEG--------------PGDALELAREAAEDGydRIVVAGGDG 66

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1032283489 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 1032283489   96 VVFINPKSGGRHGPVLKERLQQLMTEEQVFDLTEVKPhefvryglgcldtlaAKGDECARECREKIRIMVAGGDGTVGWV 175
Cdd:smart00046   1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGP---------------AVALVIFRDVPDFNRVLVCGGDGTVGWV 65

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1032283489  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 1032283489  287 VFYNYFSIGMDAQVAYGFHHLRNEKPYLAQGPVTNKIIYSSYsctqgwfctpcvnnpalrGLRNIMKIHIKkaNCSEW-- 364
Cdd:smart00045   1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFEL------------------GTKDLFFRTCK--DLHERie 60

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283489  365 -----EEIHVPKSVRSIVVLNLYNYGSGRHPWGNLRPKYLEkrgFVEAHCDDGLIEIFGLKQGWHASFVMAEIISAKHIA 439
Cdd:smart00045  61 lecdgVDVDLPNSLEGIAVLNIPSYGGGTNLWGTTDKEDLN---FSKQSHDDGLLEVVGLTGAMHMAQIRQVGLAGRRIA 137

                          170       180
                   ....*....|....*....|....*.
gi 1032283489  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 1032283489  96 VVFINPKSGGRHGPVLKERLQQLMtEEQVFDLTEVKPHEfvryglgcldtlAAKGDECARE-CREKI-RIMVAGGDGTVG 173
Cdd:COG1597     6 LLIVNPASGRGRAARLLERLVAAL-RAAGLEVEVLETES------------PGDATELAREaAAEGAdLVVAAGGDGTVN 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283489 174 WVLGCLgeLHKDgkshiPPVGVIPLGTGNDLSRSFswggSFPFAWRSAMKRTLHratlGSIARLDswkivvsmpSGEVvd 253
Cdd:COG1597    73 EVANGL--AGTG-----PPLGILPLGTGNDFARAL----GIPLDPEAALEALLT----GRTRRID---------LGRV-- 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283489 254 ppyslkptieetaldqaldaDGDvppkaksyegVFYNYFSIGMDAQVAYGFHHLRNEKPylaqGPVtnkiiysSYsctqg 333
Cdd:COG1597   127 --------------------NGR----------YFLNVAGIGFDAEVVERANRALKRRL----GKL-------AY----- 160

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283489 334 wfctpcvnnpALRGLRNIMKIHIKKANCsEWEEIHVPKSVRSIVVLNLYNYGSGRHPwgnlrpkylekrgFVEAHCDDGL 413
Cdd:COG1597   161 ----------VLAALRALLRYRPFRLRI-ELDGEEIEGEALLVAVGNGPYYGGGLRL-------------APDASLDDGL 216

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283489 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 1032283489  92 HAPMVvfINPKSGGRHGPVLKERLQQLMTEEQVFDLTEVKPHEFVryglgcldtlAAKGDECAREcREKIRIMVAGGDGT 171
Cdd:TIGR00147   3 EAPAI--LNPTAGKSNDNKPLREVIMLLREEGMEIHVRVTWEKGD----------AARYVEEARK-FGVDTVIAGGGDGT 69

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1032283489 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 1032283489  89 MAPHAPMVVFINPKSGGRHGPVLKERLQQLMTEEqvFDLTEVKPHEFVRyglgcLDTLAAKgdecARECREKIrIMVAGG 168
Cdd:PRK12361  239 LNIHKRAWLIANPVSGGGKWQEYGEQIQRELKAY--FDLTVKLTTPEIS-----AEALAKQ----ARKAGADI-VIACGG 306

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1032283489 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 1032283489  97 VFINPKSggRHGpvlKERLQQLMTEEQVFDLTEVKPHEfvryglgcldtlaakgdECARECREKIR--------IMVAGG 168
Cdd:PRK13057    2 LLVNRHA--RSG---RAALAAARAALEAAGLELVEPPA-----------------EDPDDLSEVIEayadgvdlVIVGGG 59

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1032283489 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 1032283489 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 1032283489 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 1032283489 100 NPKSG----GRHGPVLKERLQQLMTEEQVFDLTEVkphefvryglGCLdTLAAkgdECARECREKIrIMVAGGDGTVGWV 175
Cdd:PRK13337    9 NPTSGrelfKKNLPDVLQKLEQAGYETSAHATTGP----------GDA-TLAA---ERAVERKFDL-VIAAGGDGTLNEV 73

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1032283489 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 1032283489 100 NPKSGGRHGPVLKERLQQLMTEEqvFDLtEVkphefvryglgCLDTLAAKGDECARECREK--IRIMVAGGDGTVGWVLG 177
Cdd:PRK00861   10 NPVAGQGNPEVDLALIRAILEPE--MDL-DI-----------YLTTPEIGADQLAQEAIERgaELIIASGGDGTLSAVAG 75

                          90       100
                  ....*....|....*....|....*
gi 1032283489 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 1032283489  97 VFINPKSGGRHGPVLKERLQQLMTEEQVfDLTEVkphefvryglgcLDTLAAKGDECARECREK--IRIMVAGGDGTVGW 174
Cdd:PRK11914   13 VLTNPLSGHGAAPHAAERAIARLHHRGV-DVVEI------------VGTDAHDARHLVAAALAKgtDALVVVGGDGVISN 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1032283489 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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