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Conserved domains on  [gi|672049278|ref|XP_008761043|]
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acylglycerol kinase, mitochondrial isoform X1 [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

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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 ...
 206-420 5.95e-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: 436.43  E-value: 5.95e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672049278  206 MTGLRWGSFRDAGVKVSKYWYLGPLKTKAAHFFSTLQEWPQTHQASISYTGPTERPPIGPEDAAPRPSLYRRILRRLASF 285
Cdd:pfam19712   1 LTGLRWGSYRDAGAKVSKYWYLGPLKTKAAHLFSTLKEWPQVHQASLSYLGPTERPPEEPEEKPPRPPLYRRIYRRLKSY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672049278  286 WAQPQDAFSPEVSPEVWKDVQLSTIELSITTRNTQLDLTSKEDFMNICIEPDTVSKGDFIIIGSKKVRDPGLRAAGTECL 365
Cdd:pfam19712  81 WAPPQEEPPQEVEPEPWEEMQLSTIELSITTQNRQLDLTRTEDFMNICIEPDTVSKGDFITVGSQKMKDPTLCPEGSQCL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 672049278  366 HASRCTLSLPEGTEGSFSIDSEEYEAMPVEVKLLPRKLQFFCDPRKREQMLQSTS 420
Cdd:pfam19712 161 QASRCILQLPEGTGGFFSIDSEEYEAMPVEVRLLPRKLRFFCDPERREQLLSQTQ 215
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 62-195 3.20e-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: 3.20e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672049278   62 KATVFLNPAACKGKARTLFEKnAAPILHLSGMDVTVVKTDYEGQAKKLLELM--ETTDVIIVAGGDGTLQEVVTGVLRRt 139
Cdd:pfam00781   1 KLLVIVNPKSGGGKGKKLLRK-VRPLLNKAGVEVELVLTEGPGDALELAREAaeDGYDRIVVAGGDGTVNEVLNGLAGL- 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 672049278  140 deatFSKIPIGFIPLGQTSSLSHTLfaesGNKVQHVTdAALAIVKGETVPLDVLQI 195
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 ...
 206-420 5.95e-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: 436.43  E-value: 5.95e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672049278  206 MTGLRWGSFRDAGVKVSKYWYLGPLKTKAAHFFSTLQEWPQTHQASISYTGPTERPPIGPEDAAPRPSLYRRILRRLASF 285
Cdd:pfam19712   1 LTGLRWGSYRDAGAKVSKYWYLGPLKTKAAHLFSTLKEWPQVHQASLSYLGPTERPPEEPEEKPPRPPLYRRIYRRLKSY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672049278  286 WAQPQDAFSPEVSPEVWKDVQLSTIELSITTRNTQLDLTSKEDFMNICIEPDTVSKGDFIIIGSKKVRDPGLRAAGTECL 365
Cdd:pfam19712  81 WAPPQEEPPQEVEPEPWEEMQLSTIELSITTQNRQLDLTRTEDFMNICIEPDTVSKGDFITVGSQKMKDPTLCPEGSQCL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 672049278  366 HASRCTLSLPEGTEGSFSIDSEEYEAMPVEVKLLPRKLQFFCDPRKREQMLQSTS 420
Cdd:pfam19712 161 QASRCILQLPEGTGGFFSIDSEEYEAMPVEVRLLPRKLRFFCDPERREQLLSQTQ 215
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 62-195 3.20e-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: 3.20e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672049278   62 KATVFLNPAACKGKARTLFEKnAAPILHLSGMDVTVVKTDYEGQAKKLLELM--ETTDVIIVAGGDGTLQEVVTGVLRRt 139
Cdd:pfam00781   1 KLLVIVNPKSGGGKGKKLLRK-VRPLLNKAGVEVELVLTEGPGDALELAREAaeDGYDRIVVAGGDGTVNEVLNGLAGL- 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 672049278  140 deatFSKIPIGFIPLGQTSSLSHTLfaesGNKVQHVTdAALAIVKGETVPLDVLQI 195
Cdd:pfam00781  79 ----ATRPPLGIIPLGTGNDFARAL----GIPGDPEE-ALEAILKGQTRPVDVGKV 125
PLN02958 PLN02958
diacylglycerol kinase/D-erythro-sphingosine kinase
 39-228 6.75e-20

diacylglycerol kinase/D-erythro-sphingosine kinase


Pssm-ID: 215517 [Multi-domain]  Cd Length: 481  Bit Score: 91.46  E-value: 6.75e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672049278  39 RRAACQEAQVFGNQLIPPnaqvKKATVFLNPAACKGKARTLFEKNAAPILHLSGMDVTVVKTDYEGQAKKLLELMETT-- 116
Cdd:PLN02958  94 RRLWCQKLRDYLDSLGRP----KRLLVFVNPFGGKKSASKIFFDVVKPLLEDADIQLTIQETKYQLHAKEVVRTMDLSky 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672049278 117 DVIIVAGGDGTLQEVVTGVLRRTDEATFSKIPIGFIPLGQTSSLSHTLFAESGNKVQhVTDAALAIVKGETVPLDVLQIK 196
Cdd:PLN02958 170 DGIVCVSGDGILVEVVNGLLEREDWKTAIKLPIGMVPAGTGNGMAKSLLDSVGEPCS-ATNAVLAIIRGHKCSLDVATIL 248

                        170       180       190
                 ....*....|....*....|....*....|..
gi 672049278 197 gEKEQPVYAMTGLRWGSFRDAGVKVSKYWYLG 228
Cdd:PLN02958 249 -QGETKFFSVLMLAWGLVADIDIESEKYRWMG 279
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 61-198 1.34e-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: 1.34e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672049278  61 KKATVFLNPAACKGKARTLFEKnAAPILHLSGMDVTVVKTDYEGQAKKLLE--LMETTDVIIVAGGDGTLQEVVTGVLRr 138
Cdd:COG1597    3 MRALLIVNPASGRGRAARLLER-LVAALRAAGLEVEVLETESPGDATELAReaAAEGADLVVAAGGDGTVNEVANGLAG- 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 672049278 139 tdeatfSKIPIGFIPLGQTSSLSHTLFAEsgnkvQHVTDAALAIVKGETVPLDVLQIKGE 198
Cdd:COG1597   81 ------TGPPLGILPLGTGNDFARALGIP-----LDPEAALEALLTGRTRRIDLGRVNGR 129
TIGR00147 TIGR00147
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ...
 61-197 2.45e-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: 2.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672049278   61 KKATVFLNPAAckgkARTLFEK---NAAPILHLSGMDVTVVKTDYEGQAKKLLE--LMETTDVIIVAGGDGTLQEVVTGV 135
Cdd:TIGR00147   2 AEAPAILNPTA----GKSNDNKplrEVIMLLREEGMEIHVRVTWEKGDAARYVEeaRKFGVDTVIAGGGDGTINEVVNAL 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 672049278  136 lrrtdeATFSKIP-IGFIPLGQTSSlshtlFAESGNKVQHVTDAALAIVKGETVPLDVLQIKG 197
Cdd:TIGR00147  78 ------IQLDDIPaLGILPLGTAND-----FARSLGIPEDLDKAAKLVIAGDARAIDMGQVNK 129
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 65-164 2.95e-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: 46.14  E-value: 2.95e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672049278    65 VFLNPAACKGKARTLFEKnaAPILHLSGMDVTVVKTDYEGQAKKLLELmETTDVIIVAGGDGTLQEVVTGVLRRTDeaTF 144
Cdd:smart00046   2 VFVNPKSGGGKGEKLLRK--FRLLLNPRQVFDLTKKGPAVALVIFRDV-PDFNRVLVCGGDGTVGWVLNALDKREL--PL 76

                           90       100
                   ....*....|....*....|
gi 672049278   145 SKIPIGFIPLGQTSSLSHTL 164
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 ...
 206-420 5.95e-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: 436.43  E-value: 5.95e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672049278  206 MTGLRWGSFRDAGVKVSKYWYLGPLKTKAAHFFSTLQEWPQTHQASISYTGPTERPPIGPEDAAPRPSLYRRILRRLASF 285
Cdd:pfam19712   1 LTGLRWGSYRDAGAKVSKYWYLGPLKTKAAHLFSTLKEWPQVHQASLSYLGPTERPPEEPEEKPPRPPLYRRIYRRLKSY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672049278  286 WAQPQDAFSPEVSPEVWKDVQLSTIELSITTRNTQLDLTSKEDFMNICIEPDTVSKGDFIIIGSKKVRDPGLRAAGTECL 365
Cdd:pfam19712  81 WAPPQEEPPQEVEPEPWEEMQLSTIELSITTQNRQLDLTRTEDFMNICIEPDTVSKGDFITVGSQKMKDPTLCPEGSQCL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 672049278  366 HASRCTLSLPEGTEGSFSIDSEEYEAMPVEVKLLPRKLQFFCDPRKREQMLQSTS 420
Cdd:pfam19712 161 QASRCILQLPEGTGGFFSIDSEEYEAMPVEVRLLPRKLRFFCDPERREQLLSQTQ 215
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 62-195 3.20e-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: 3.20e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672049278   62 KATVFLNPAACKGKARTLFEKnAAPILHLSGMDVTVVKTDYEGQAKKLLELM--ETTDVIIVAGGDGTLQEVVTGVLRRt 139
Cdd:pfam00781   1 KLLVIVNPKSGGGKGKKLLRK-VRPLLNKAGVEVELVLTEGPGDALELAREAaeDGYDRIVVAGGDGTVNEVLNGLAGL- 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 672049278  140 deatFSKIPIGFIPLGQTSSLSHTLfaesGNKVQHVTdAALAIVKGETVPLDVLQI 195
Cdd:pfam00781  79 ----ATRPPLGIIPLGTGNDFARAL----GIPGDPEE-ALEAILKGQTRPVDVGKV 125
PLN02958 PLN02958
diacylglycerol kinase/D-erythro-sphingosine kinase
 39-228 6.75e-20

diacylglycerol kinase/D-erythro-sphingosine kinase


Pssm-ID: 215517 [Multi-domain]  Cd Length: 481  Bit Score: 91.46  E-value: 6.75e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672049278  39 RRAACQEAQVFGNQLIPPnaqvKKATVFLNPAACKGKARTLFEKNAAPILHLSGMDVTVVKTDYEGQAKKLLELMETT-- 116
Cdd:PLN02958  94 RRLWCQKLRDYLDSLGRP----KRLLVFVNPFGGKKSASKIFFDVVKPLLEDADIQLTIQETKYQLHAKEVVRTMDLSky 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672049278 117 DVIIVAGGDGTLQEVVTGVLRRTDEATFSKIPIGFIPLGQTSSLSHTLFAESGNKVQhVTDAALAIVKGETVPLDVLQIK 196
Cdd:PLN02958 170 DGIVCVSGDGILVEVVNGLLEREDWKTAIKLPIGMVPAGTGNGMAKSLLDSVGEPCS-ATNAVLAIIRGHKCSLDVATIL 248

                        170       180       190
                 ....*....|....*....|....*....|..
gi 672049278 197 gEKEQPVYAMTGLRWGSFRDAGVKVSKYWYLG 228
Cdd:PLN02958 249 -QGETKFFSVLMLAWGLVADIDIESEKYRWMG 279
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 61-198 1.34e-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: 1.34e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672049278  61 KKATVFLNPAACKGKARTLFEKnAAPILHLSGMDVTVVKTDYEGQAKKLLE--LMETTDVIIVAGGDGTLQEVVTGVLRr 138
Cdd:COG1597    3 MRALLIVNPASGRGRAARLLER-LVAALRAAGLEVEVLETESPGDATELAReaAAEGADLVVAAGGDGTVNEVANGLAG- 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 672049278 139 tdeatfSKIPIGFIPLGQTSSLSHTLFAEsgnkvQHVTDAALAIVKGETVPLDVLQIKGE 198
Cdd:COG1597   81 ------TGPPLGILPLGTGNDFARALGIP-----LDPEAALEALLTGRTRRIDLGRVNGR 129
PRK12361 PRK12361
hypothetical protein; Provisional
 61-191 1.11e-12

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 69.65  E-value: 1.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672049278  61 KKATVFLNPAACKGKartlFEKNAAPIL-HLSG-MDVTVVKTDYEGQAKKLLE--LMETTDVIIVAGGDGTLQEVVTgVL 136
Cdd:PRK12361 243 KRAWLIANPVSGGGK----WQEYGEQIQrELKAyFDLTVKLTTPEISAEALAKqaRKAGADIVIACGGDGTVTEVAS-EL 317

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 672049278 137 RRTDeatfskIPIGFIPLGQTSSLSHTLFAeSGNKVQHVTDAALAIVKGETVPLD 191
Cdd:PRK12361 318 VNTD------ITLGIIPLGTANALSHALFG-LGSKLIPVEQACDNIIQGHTQRID 365
PRK13337 PRK13337
putative lipid kinase; Reviewed
 61-192 4.06e-10

putative lipid kinase; Reviewed


Pssm-ID: 183982 [Multi-domain]  Cd Length: 304  Bit Score: 60.45  E-value: 4.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672049278  61 KKATVFLNPAAckgkARTLFEKNAAPIL---HLSGMDVTVVKTDYEGQAKKLLE--LMETTDVIIVAGGDGTLQEVVTGV 135
Cdd:PRK13337   2 KRARIIYNPTS----GRELFKKNLPDVLqklEQAGYETSAHATTGPGDATLAAEraVERKFDLVIAAGGDGTLNEVVNGI 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 672049278 136 lrrtdeATFSKIP-IGFIPLGQTSSlshtlFAESGNKVQHVTDAALAIVKGETVPLDV 192
Cdd:PRK13337  78 ------AEKENRPkLGIIPVGTTND-----FARALHVPRDIEKAADVIIEGHTVPVDI 124
PRK13055 PRK13055
putative lipid kinase; Reviewed
 61-199 8.84e-10

putative lipid kinase; Reviewed


Pssm-ID: 237282 [Multi-domain]  Cd Length: 334  Bit Score: 59.62  E-value: 8.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672049278  61 KKATVFLNPAAckgkARTLFEKNAAPILHL---SGMDVTVVKTdyegQAKKLLELMETT-------DVIIVAGGDGTLQE 130
Cdd:PRK13055   3 KRARLIYNPTS----GQEIMKKNVADILDIleqAGYETSAFQT----TPEPNSAKNEAKraaeagfDLIIAAGGDGTINE 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672049278 131 VVTGVlrrtdeATFSKIP-IGFIPLGQTSSLSHTLFAESGNKVqhvtDAALAIVKGETVPLDVLQIKGEK 199
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 ...
 61-197 2.45e-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: 2.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672049278   61 KKATVFLNPAAckgkARTLFEK---NAAPILHLSGMDVTVVKTDYEGQAKKLLE--LMETTDVIIVAGGDGTLQEVVTGV 135
Cdd:TIGR00147   2 AEAPAILNPTA----GKSNDNKplrEVIMLLREEGMEIHVRVTWEKGDAARYVEeaRKFGVDTVIAGGGDGTINEVVNAL 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 672049278  136 lrrtdeATFSKIP-IGFIPLGQTSSlshtlFAESGNKVQHVTDAALAIVKGETVPLDVLQIKG 197
Cdd:TIGR00147  78 ------IQLDDIPaLGILPLGTAND-----FARSLGIPEDLDKAAKLVIAGDARAIDMGQVNK 129
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 65-164 2.95e-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: 46.14  E-value: 2.95e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672049278    65 VFLNPAACKGKARTLFEKnaAPILHLSGMDVTVVKTDYEGQAKKLLELmETTDVIIVAGGDGTLQEVVTGVLRRTDeaTF 144
Cdd:smart00046   2 VFVNPKSGGGKGEKLLRK--FRLLLNPRQVFDLTKKGPAVALVIFRDV-PDFNRVLVCGGDGTVGWVLNALDKREL--PL 76

                           90       100
                   ....*....|....*....|
gi 672049278   145 SKIPIGFIPLGQTSSLSHTL 164
Cdd:smart00046  77 PEPPVAVLPLGTGNDLARSL 96
PRK00861 PRK00861
putative lipid kinase; Reviewed
 61-192 1.04e-05

putative lipid kinase; Reviewed


Pssm-ID: 234850 [Multi-domain]  Cd Length: 300  Bit Score: 46.92  E-value: 1.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672049278  61 KKATVFLNPAACKGKARTlfEKNAAPILHLSGMDVTVVKTDYEGQAKKLLE--LMETTDVIIVAGGDGTLQeVVTGVLRR 138
Cdd:PRK00861   3 RSACLIFNPVAGQGNPEV--DLALIRAILEPEMDLDIYLTTPEIGADQLAQeaIERGAELIIASGGDGTLS-AVAGALIG 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 672049278 139 TDeatfskIPIGFIPLGQTSSLSHTLfaesgNKVQHVTDAALAIVKGETVPLDV 192
Cdd:PRK00861  80 TD------IPLGIIPRGTANAFAAAL-----GIPDTIEEACRTILQGKTRRVDV 122
PRK13059 PRK13059
putative lipid kinase; Reviewed
 114-192 2.91e-05

putative lipid kinase; Reviewed


Pssm-ID: 183858  Cd Length: 295  Bit Score: 45.41  E-value: 2.91e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 672049278 114 ETTDVIIVAGGDGTLQEVVTGVLRRTdeatfSKIPIGFIPLGQTSSlshtlFAESGNKVQHVTDAALAIVKGETVPLDV 192
Cdd:PRK13059  55 ESYKYILIAGGDGTVDNVVNAMKKLN-----IDLPIGILPVGTAND-----FAKFLGMPTDIGEACEQILKSKPKKVDL 123
PRK13054 PRK13054
lipid kinase; Reviewed
 91-198 7.31e-05

lipid kinase; Reviewed


Pssm-ID: 237281 [Multi-domain]  Cd Length: 300  Bit Score: 44.48  E-value: 7.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672049278  91 SGMDVTVVKTDYEGQAKKLLE--LMETTDVIIVAGGDGTLQEVVTGVLRRTDEATFSkipIGFIPLGQTSSlshtlFAES 168
Cdd:PRK13054  30 EGHTLHVRVTWEKGDAARYVEeaLALGVATVIAGGGDGTINEVATALAQLEGDARPA---LGILPLGTAND-----FATA 101

                         90       100       110
                 ....*....|....*....|....*....|.
gi 672049278 169 GNkVQHVTDAALA-IVKGETVPLDVLQIKGE 198
Cdd:PRK13054 102 AG-IPLEPDKALKlAIEGRAQPIDLARVNDR 131
PLN02204 PLN02204
diacylglycerol kinase
 61-172 5.71e-03

diacylglycerol kinase


Pssm-ID: 215126 [Multi-domain]  Cd Length: 601  Bit Score: 39.10  E-value: 5.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672049278  61 KKATVFLNPAACKGKARTLFEkNAAPILHLSGMDVTVVKTDYEGQAKKLL-----ELMETTDVIIVAGGDGTLQEVVTGV 135
Cdd:PLN02204 160 KNLLVFVHPLSGKGSGSRTWE-TVSPIFIRAKVKTKVIVTERAGHAFDVMasisnKELKSYDGVIAVGGDGFFNEILNGY 238

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 672049278 136 LRRTDEATFSKIPIGFIplGQTSSLSHTLFAESGNKV 172
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.
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