NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1046885425|ref|XP_017448335|]
View 

acylglycerol kinase, mitochondrial isoform X3 [Rattus norvegicus]

Protein Classification

acylglycerol kinase family protein( domain architecture ID 18164179)

acylglycerol kinase family protein similar to mitochondrial acylglycerol kinase, which is a lipid kinase that can phosphorylate both monoacylglycerol and diacylglycerol to form lysophosphatidic acid (LPA) and phosphatidic acid (PA), respectively

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
AGK_C pfam19712
Acylglycerol kinase C-terminal; This domain corresponds to the C-terminal of mitochondrial ...
 170-384 9.19e-155

Acylglycerol kinase C-terminal; This domain corresponds to the C-terminal of mitochondrial Acylglycerol kinase (AGK, also known as MuLK). AGK is a metazoan-specific protein integrated into the mitochondrial inner membrane through a short N-terminal transmembrane domain. This large C-terminal domain is adjacent the kinase domain and it is oriented to the intermembrane space. AGK is a subunit of the human TIM22 complex which stabilizes the complex and regulates the import and assembly of mitochondrial carrier proteins, a function independent of its kinase activity. Disturbances in both functions of AGK (phospholipid metabolism and mitochondrial protein biogenesis) contribute to the pathogenesis of Sengers syndrome.


:

Pssm-ID: 466156  Cd Length: 215  Bit Score: 434.50  E-value: 9.19e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046885425 170 MTGLRWGSFRDAGVKVSKYWYLGPLKTKAAHFFSTLQEWPQTHQASISYTGPTERPPIGPEDAAPRPSLYRRILRRLASF 249
Cdd:pfam19712   1 LTGLRWGSYRDAGAKVSKYWYLGPLKTKAAHLFSTLKEWPQVHQASLSYLGPTERPPEEPEEKPPRPPLYRRIYRRLKSY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046885425 250 WAQPQDAFSPEVSPEVWKDVQLSTIELSITTRNTQLDLTSKEDFMNICIEPDTVSKGDFIIIGSKKVRDPGLRAAGTECL 329
Cdd:pfam19712  81 WAPPQEEPPQEVEPEPWEEMQLSTIELSITTQNRQLDLTRTEDFMNICIEPDTVSKGDFITVGSQKMKDPTLCPEGSQCL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1046885425 330 HASRCTLSLPEGTEGSFSIDSEEYEAMPVEVKLLPRKLQFFCDPRKREQMLQSTS 384
Cdd:pfam19712 161 QASRCILQLPEGTGGFFSIDSEEYEAMPVEVRLLPRKLRFFCDPERREQLLSQTQ 215
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 26-159 1.94e-28

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: 107.67  E-value: 1.94e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046885425  26 KATVFLNPAACKGKARTLFEKnAAPILHLSGMDVTVVKTDYEGQAKKLLELM--ETTDVIIVAGGDGTLQEVVTGVLRRt 103
Cdd:pfam00781   1 KLLVIVNPKSGGGKGKKLLRK-VRPLLNKAGVEVELVLTEGPGDALELAREAaeDGYDRIVVAGGDGTVNEVLNGLAGL- 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1046885425 104 deatFSKIPIGFIPLGQTSSLSHTLfaesGNKVQHVTdAALAIVKGETVPLDVLQI 159
Cdd:pfam00781  79 ----ATRPPLGIIPLGTGNDFARAL----GIPGDPEE-ALEAILKGQTRPVDVGKV 125
 
Name Accession Description Interval E-value
AGK_C pfam19712
Acylglycerol kinase C-terminal; This domain corresponds to the C-terminal of mitochondrial ...
 170-384 9.19e-155

Acylglycerol kinase C-terminal; This domain corresponds to the C-terminal of mitochondrial Acylglycerol kinase (AGK, also known as MuLK). AGK is a metazoan-specific protein integrated into the mitochondrial inner membrane through a short N-terminal transmembrane domain. This large C-terminal domain is adjacent the kinase domain and it is oriented to the intermembrane space. AGK is a subunit of the human TIM22 complex which stabilizes the complex and regulates the import and assembly of mitochondrial carrier proteins, a function independent of its kinase activity. Disturbances in both functions of AGK (phospholipid metabolism and mitochondrial protein biogenesis) contribute to the pathogenesis of Sengers syndrome.


Pssm-ID: 466156  Cd Length: 215  Bit Score: 434.50  E-value: 9.19e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046885425 170 MTGLRWGSFRDAGVKVSKYWYLGPLKTKAAHFFSTLQEWPQTHQASISYTGPTERPPIGPEDAAPRPSLYRRILRRLASF 249
Cdd:pfam19712   1 LTGLRWGSYRDAGAKVSKYWYLGPLKTKAAHLFSTLKEWPQVHQASLSYLGPTERPPEEPEEKPPRPPLYRRIYRRLKSY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046885425 250 WAQPQDAFSPEVSPEVWKDVQLSTIELSITTRNTQLDLTSKEDFMNICIEPDTVSKGDFIIIGSKKVRDPGLRAAGTECL 329
Cdd:pfam19712  81 WAPPQEEPPQEVEPEPWEEMQLSTIELSITTQNRQLDLTRTEDFMNICIEPDTVSKGDFITVGSQKMKDPTLCPEGSQCL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1046885425 330 HASRCTLSLPEGTEGSFSIDSEEYEAMPVEVKLLPRKLQFFCDPRKREQMLQSTS 384
Cdd:pfam19712 161 QASRCILQLPEGTGGFFSIDSEEYEAMPVEVRLLPRKLRFFCDPERREQLLSQTQ 215
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 26-159 1.94e-28

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: 107.67  E-value: 1.94e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046885425  26 KATVFLNPAACKGKARTLFEKnAAPILHLSGMDVTVVKTDYEGQAKKLLELM--ETTDVIIVAGGDGTLQEVVTGVLRRt 103
Cdd:pfam00781   1 KLLVIVNPKSGGGKGKKLLRK-VRPLLNKAGVEVELVLTEGPGDALELAREAaeDGYDRIVVAGGDGTVNEVLNGLAGL- 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1046885425 104 deatFSKIPIGFIPLGQTSSLSHTLfaesGNKVQHVTdAALAIVKGETVPLDVLQI 159
Cdd:pfam00781  79 ----ATRPPLGIIPLGTGNDFARAL----GIPGDPEE-ALEAILKGQTRPVDVGKV 125
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 25-162 1.05e-19

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


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 88.37  E-value: 1.05e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046885425  25 KKATVFLNPAACKGKARTLFEKnAAPILHLSGMDVTVVKTDYEGQAKKLLE--LMETTDVIIVAGGDGTLQEVVTGVLRr 102
Cdd:COG1597     3 MRALLIVNPASGRGRAARLLER-LVAALRAAGLEVEVLETESPGDATELAReaAAEGADLVVAAGGDGTVNEVANGLAG- 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046885425 103 tdeatfSKIPIGFIPLGQTSSLSHTLFAEsgnkvQHVTDAALAIVKGETVPLDVLQIKGE 162
Cdd:COG1597    81 ------TGPPLGILPLGTGNDFARALGIP-----LDPEAALEALLTGRTRRIDLGRVNGR 129
PLN02958 PLN02958
diacylglycerol kinase/D-erythro-sphingosine kinase
 25-192 1.80e-19

diacylglycerol kinase/D-erythro-sphingosine kinase


Pssm-ID: 215517 [Multi-domain]  Cd Length: 481  Bit Score: 89.53  E-value: 1.80e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046885425  25 KKATVFLNPAACKGKARTLFEKNAAPILHLSGMDVTVVKTDYEGQAKKLLELMETT--DVIIVAGGDGTLQEVVTGVLRR 102
Cdd:PLN02958  112 KRLLVFVNPFGGKKSASKIFFDVVKPLLEDADIQLTIQETKYQLHAKEVVRTMDLSkyDGIVCVSGDGILVEVVNGLLER 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046885425 103 TDEATFSKIPIGFIPLGQTSSLSHTLFAESGNKVQhVTDAALAIVKGETVPLDVLQIKgEKEQPVYAMTGLRWGSFRDAG 182
Cdd:PLN02958  192 EDWKTAIKLPIGMVPAGTGNGMAKSLLDSVGEPCS-ATNAVLAIIRGHKCSLDVATIL-QGETKFFSVLMLAWGLVADID 269

                         170
                  ....*....|
gi 1046885425 183 VKVSKYWYLG 192
Cdd:PLN02958  270 IESEKYRWMG 279
TIGR00147 TIGR00147
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ...
 25-161 2.12e-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: 49.04  E-value: 2.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046885425  25 KKATVFLNPAAckgkARTLFEK---NAAPILHLSGMDVTVVKTDYEGQAKKLLE--LMETTDVIIVAGGDGTLQEVVTGV 99
Cdd:TIGR00147   2 AEAPAILNPTA----GKSNDNKplrEVIMLLREEGMEIHVRVTWEKGDAARYVEeaRKFGVDTVIAGGGDGTINEVVNAL 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046885425 100 lrrtdeATFSKIP-IGFIPLGQTSSlshtlFAESGNKVQHVTDAALAIVKGETVPLDVLQIKG 161
Cdd:TIGR00147  78 ------IQLDDIPaLGILPLGTAND-----FARSLGIPEDLDKAAKLVIAGDARAIDMGQVNK 129
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 29-128 3.22e-06

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: 45.75  E-value: 3.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046885425   29 VFLNPAACKGKARTLFEKnaAPILHLSGMDVTVVKTDYEGQAKKLLELmETTDVIIVAGGDGTLQEVVTGVLRRTDeaTF 108
Cdd:smart00046   2 VFVNPKSGGGKGEKLLRK--FRLLLNPRQVFDLTKKGPAVALVIFRDV-PDFNRVLVCGGDGTVGWVLNALDKREL--PL 76

                           90       100
                   ....*....|....*....|
gi 1046885425  109 SKIPIGFIPLGQTSSLSHTL 128
Cdd:smart00046  77 PEPPVAVLPLGTGNDLARSL 96
 
Name Accession Description Interval E-value
AGK_C pfam19712
Acylglycerol kinase C-terminal; This domain corresponds to the C-terminal of mitochondrial ...
 170-384 9.19e-155

Acylglycerol kinase C-terminal; This domain corresponds to the C-terminal of mitochondrial Acylglycerol kinase (AGK, also known as MuLK). AGK is a metazoan-specific protein integrated into the mitochondrial inner membrane through a short N-terminal transmembrane domain. This large C-terminal domain is adjacent the kinase domain and it is oriented to the intermembrane space. AGK is a subunit of the human TIM22 complex which stabilizes the complex and regulates the import and assembly of mitochondrial carrier proteins, a function independent of its kinase activity. Disturbances in both functions of AGK (phospholipid metabolism and mitochondrial protein biogenesis) contribute to the pathogenesis of Sengers syndrome.


Pssm-ID: 466156  Cd Length: 215  Bit Score: 434.50  E-value: 9.19e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046885425 170 MTGLRWGSFRDAGVKVSKYWYLGPLKTKAAHFFSTLQEWPQTHQASISYTGPTERPPIGPEDAAPRPSLYRRILRRLASF 249
Cdd:pfam19712   1 LTGLRWGSYRDAGAKVSKYWYLGPLKTKAAHLFSTLKEWPQVHQASLSYLGPTERPPEEPEEKPPRPPLYRRIYRRLKSY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046885425 250 WAQPQDAFSPEVSPEVWKDVQLSTIELSITTRNTQLDLTSKEDFMNICIEPDTVSKGDFIIIGSKKVRDPGLRAAGTECL 329
Cdd:pfam19712  81 WAPPQEEPPQEVEPEPWEEMQLSTIELSITTQNRQLDLTRTEDFMNICIEPDTVSKGDFITVGSQKMKDPTLCPEGSQCL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1046885425 330 HASRCTLSLPEGTEGSFSIDSEEYEAMPVEVKLLPRKLQFFCDPRKREQMLQSTS 384
Cdd:pfam19712 161 QASRCILQLPEGTGGFFSIDSEEYEAMPVEVRLLPRKLRFFCDPERREQLLSQTQ 215
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 26-159 1.94e-28

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: 107.67  E-value: 1.94e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046885425  26 KATVFLNPAACKGKARTLFEKnAAPILHLSGMDVTVVKTDYEGQAKKLLELM--ETTDVIIVAGGDGTLQEVVTGVLRRt 103
Cdd:pfam00781   1 KLLVIVNPKSGGGKGKKLLRK-VRPLLNKAGVEVELVLTEGPGDALELAREAaeDGYDRIVVAGGDGTVNEVLNGLAGL- 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1046885425 104 deatFSKIPIGFIPLGQTSSLSHTLfaesGNKVQHVTdAALAIVKGETVPLDVLQI 159
Cdd:pfam00781  79 ----ATRPPLGIIPLGTGNDFARAL----GIPGDPEE-ALEAILKGQTRPVDVGKV 125
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 25-162 1.05e-19

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


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 88.37  E-value: 1.05e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046885425  25 KKATVFLNPAACKGKARTLFEKnAAPILHLSGMDVTVVKTDYEGQAKKLLE--LMETTDVIIVAGGDGTLQEVVTGVLRr 102
Cdd:COG1597     3 MRALLIVNPASGRGRAARLLER-LVAALRAAGLEVEVLETESPGDATELAReaAAEGADLVVAAGGDGTVNEVANGLAG- 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046885425 103 tdeatfSKIPIGFIPLGQTSSLSHTLFAEsgnkvQHVTDAALAIVKGETVPLDVLQIKGE 162
Cdd:COG1597    81 ------TGPPLGILPLGTGNDFARALGIP-----LDPEAALEALLTGRTRRIDLGRVNGR 129
PLN02958 PLN02958
diacylglycerol kinase/D-erythro-sphingosine kinase
 25-192 1.80e-19

diacylglycerol kinase/D-erythro-sphingosine kinase


Pssm-ID: 215517 [Multi-domain]  Cd Length: 481  Bit Score: 89.53  E-value: 1.80e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046885425  25 KKATVFLNPAACKGKARTLFEKNAAPILHLSGMDVTVVKTDYEGQAKKLLELMETT--DVIIVAGGDGTLQEVVTGVLRR 102
Cdd:PLN02958  112 KRLLVFVNPFGGKKSASKIFFDVVKPLLEDADIQLTIQETKYQLHAKEVVRTMDLSkyDGIVCVSGDGILVEVVNGLLER 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046885425 103 TDEATFSKIPIGFIPLGQTSSLSHTLFAESGNKVQhVTDAALAIVKGETVPLDVLQIKgEKEQPVYAMTGLRWGSFRDAG 182
Cdd:PLN02958  192 EDWKTAIKLPIGMVPAGTGNGMAKSLLDSVGEPCS-ATNAVLAIIRGHKCSLDVATIL-QGETKFFSVLMLAWGLVADID 269

                         170
                  ....*....|
gi 1046885425 183 VKVSKYWYLG 192
Cdd:PLN02958  270 IESEKYRWMG 279
PRK12361 PRK12361
hypothetical protein; Provisional
 25-155 8.55e-13

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 69.65  E-value: 8.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046885425  25 KKATVFLNPAACKGKartlFEKNAAPIL-HLSG-MDVTVVKTDYEGQAKKLLE--LMETTDVIIVAGGDGTLQEVVTgVL 100
Cdd:PRK12361  243 KRAWLIANPVSGGGK----WQEYGEQIQrELKAyFDLTVKLTTPEISAEALAKqaRKAGADIVIACGGDGTVTEVAS-EL 317

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1046885425 101 RRTDeatfskIPIGFIPLGQTSSLSHTLFAeSGNKVQHVTDAALAIVKGETVPLD 155
Cdd:PRK12361  318 VNTD------ITLGIIPLGTANALSHALFG-LGSKLIPVEQACDNIIQGHTQRID 365
PRK13337 PRK13337
putative lipid kinase; Reviewed
 25-156 3.42e-10

putative lipid kinase; Reviewed


Pssm-ID: 183982 [Multi-domain]  Cd Length: 304  Bit Score: 60.45  E-value: 3.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046885425  25 KKATVFLNPAAckgkARTLFEKNAAPIL---HLSGMDVTVVKTDYEGQAKKLLE--LMETTDVIIVAGGDGTLQEVVTGV 99
Cdd:PRK13337    2 KRARIIYNPTS----GRELFKKNLPDVLqklEQAGYETSAHATTGPGDATLAAEraVERKFDLVIAAGGDGTLNEVVNGI 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1046885425 100 lrrtdeATFSKIP-IGFIPLGQTSSlshtlFAESGNKVQHVTDAALAIVKGETVPLDV 156
Cdd:PRK13337   78 ------AEKENRPkLGIIPVGTTND-----FARALHVPRDIEKAADVIIEGHTVPVDI 124
PRK13055 PRK13055
putative lipid kinase; Reviewed
 25-163 7.41e-10

putative lipid kinase; Reviewed


Pssm-ID: 237282 [Multi-domain]  Cd Length: 334  Bit Score: 59.62  E-value: 7.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046885425  25 KKATVFLNPAAckgkARTLFEKNAAPILHL---SGMDVTVVKTdyegQAKKLLELMETT-------DVIIVAGGDGTLQE 94
Cdd:PRK13055    3 KRARLIYNPTS----GQEIMKKNVADILDIleqAGYETSAFQT----TPEPNSAKNEAKraaeagfDLIIAAGGDGTINE 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046885425  95 VVTGVlrrtdeATFSKIP-IGFIPLGQTSSLSHTLFAESGNKVqhvtDAALAIVKGETVPLDVLQIKGEK 163
Cdd:PRK13055   75 VVNGI------APLEKRPkMAIIPAGTTNDYARALKIPRDNPV----EAAKVILKNQTIKMDIGRANEDK 134
TIGR00147 TIGR00147
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ...
 25-161 2.12e-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: 49.04  E-value: 2.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046885425  25 KKATVFLNPAAckgkARTLFEK---NAAPILHLSGMDVTVVKTDYEGQAKKLLE--LMETTDVIIVAGGDGTLQEVVTGV 99
Cdd:TIGR00147   2 AEAPAILNPTA----GKSNDNKplrEVIMLLREEGMEIHVRVTWEKGDAARYVEeaRKFGVDTVIAGGGDGTINEVVNAL 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046885425 100 lrrtdeATFSKIP-IGFIPLGQTSSlshtlFAESGNKVQHVTDAALAIVKGETVPLDVLQIKG 161
Cdd:TIGR00147  78 ------IQLDDIPaLGILPLGTAND-----FARSLGIPEDLDKAAKLVIAGDARAIDMGQVNK 129
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 29-128 3.22e-06

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: 45.75  E-value: 3.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046885425   29 VFLNPAACKGKARTLFEKnaAPILHLSGMDVTVVKTDYEGQAKKLLELmETTDVIIVAGGDGTLQEVVTGVLRRTDeaTF 108
Cdd:smart00046   2 VFVNPKSGGGKGEKLLRK--FRLLLNPRQVFDLTKKGPAVALVIFRDV-PDFNRVLVCGGDGTVGWVLNALDKREL--PL 76

                           90       100
                   ....*....|....*....|
gi 1046885425  109 SKIPIGFIPLGQTSSLSHTL 128
Cdd:smart00046  77 PEPPVAVLPLGTGNDLARSL 96
PRK00861 PRK00861
putative lipid kinase; Reviewed
 25-156 1.44e-05

putative lipid kinase; Reviewed


Pssm-ID: 234850 [Multi-domain]  Cd Length: 300  Bit Score: 46.54  E-value: 1.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046885425  25 KKATVFLNPAACKGKARTlfEKNAAPILHLSGMDVTVVKTDYEGQAKKLLE--LMETTDVIIVAGGDGTLQeVVTGVLRR 102
Cdd:PRK00861    3 RSACLIFNPVAGQGNPEV--DLALIRAILEPEMDLDIYLTTPEIGADQLAQeaIERGAELIIASGGDGTLS-AVAGALIG 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1046885425 103 TDeatfskIPIGFIPLGQTSSLSHTLfaesgNKVQHVTDAALAIVKGETVPLDV 156
Cdd:PRK00861   80 TD------IPLGIIPRGTANAFAAAL-----GIPDTIEEACRTILQGKTRRVDV 122
PRK13059 PRK13059
putative lipid kinase; Reviewed
 78-156 2.53e-05

putative lipid kinase; Reviewed


Pssm-ID: 183858  Cd Length: 295  Bit Score: 45.41  E-value: 2.53e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1046885425  78 ETTDVIIVAGGDGTLQEVVTGVLRRTdeatfSKIPIGFIPLGQTSSlshtlFAESGNKVQHVTDAALAIVKGETVPLDV 156
Cdd:PRK13059   55 ESYKYILIAGGDGTVDNVVNAMKKLN-----IDLPIGILPVGTAND-----FAKFLGMPTDIGEACEQILKSKPKKVDL 123
PRK13054 PRK13054
lipid kinase; Reviewed
 55-162 7.27e-05

lipid kinase; Reviewed


Pssm-ID: 237281 [Multi-domain]  Cd Length: 300  Bit Score: 44.09  E-value: 7.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046885425  55 SGMDVTVVKTDYEGQAKKLLE--LMETTDVIIVAGGDGTLQEVVTGVLRRTDEATFSkipIGFIPLGQTSSlshtlFAES 132
Cdd:PRK13054   30 EGHTLHVRVTWEKGDAARYVEeaLALGVATVIAGGGDGTINEVATALAQLEGDARPA---LGILPLGTAND-----FATA 101

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1046885425 133 GNkVQHVTDAALA-IVKGETVPLDVLQIKGE 162
Cdd:PRK13054  102 AG-IPLEPDKALKlAIEGRAQPIDLARVNDR 131
PLN02204 PLN02204
diacylglycerol kinase
 25-136 4.98e-03

diacylglycerol kinase


Pssm-ID: 215126 [Multi-domain]  Cd Length: 601  Bit Score: 39.10  E-value: 4.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046885425  25 KKATVFLNPAACKGKARTLFEkNAAPILHLSGMDVTVVKTDYEGQAKKLL-----ELMETTDVIIVAGGDGTLQEVVTGV 99
Cdd:PLN02204  160 KNLLVFVHPLSGKGSGSRTWE-TVSPIFIRAKVKTKVIVTERAGHAFDVMasisnKELKSYDGVIAVGGDGFFNEILNGY 238

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1046885425 100 LRRTDEATFSKIPIGFIplGQTSSLSHTLFAESGNKV 136
Cdd:PLN02204  239 LLSRLKVPYPPSPSDSV--HSVQSRGSSSVHEPNETV 273
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH