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Conserved domains on  [gi|1370510573|ref|XP_024302603|]
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acylglycerol kinase, mitochondrial isoform X1 [Homo sapiens]

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 ...
206-421 1.93e-159

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: 447.99  E-value: 1.93e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510573 206 MTGLRWGSFRDAGVKVSKYWYLGPLKIKAAHFFSTLKEWPQTHQASISYTGPTERPPNEPEETPvQRPSLYRRILRRLAS 285
Cdd:pfam19712   1 LTGLRWGSYRDAGAKVSKYWYLGPLKTKAAHLFSTLKEWPQVHQASLSYLGPTERPPEEPEEKP-PRPPLYRRIYRRLKS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510573 286 YWAQPQDALSQEVSPEVWKDVQLSTIELSITTRNNQLDPTSKEDFLNICIEPDTISKGDFITIGSRKVRNPKLHVEGTEC 365
Cdd:pfam19712  80 YWAPPQEEPPQEVEPEPWEEMQLSTIELSITTQNRQLDLTRTEDFMNICIEPDTVSKGDFITVGSQKMKDPTLCPEGSQC 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370510573 366 LQASQCTLLIPEGAGGSFSIDSEEYEAMPVEVKLLPRKLQFFCDPRKREQMLTSPT 421
Cdd:pfam19712 160 LQASRCILQLPEGTGGFFSIDSEEYEAMPVEVRLLPRKLRFFCDPERREQLLSQTQ 215
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
62-195 4.83e-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: 107.29  E-value: 4.83e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510573  62 KATVFLNPAACKGKARTLFEKnAAPILHLSGMDVTIVKTDYEGQAKKLLELMEN--TDVIIVAGGDGTLQEVVTGVLRRt 139
Cdd:pfam00781   1 KLLVIVNPKSGGGKGKKLLRK-VRPLLNKAGVEVELVLTEGPGDALELAREAAEdgYDRIVVAGGDGTVNEVLNGLAGL- 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370510573 140 deatFSKIPIGFIPLGETSSLSHTLfaesGNKvQHITDATLAIVKGETVPLDVLQI 195
Cdd:pfam00781  79 ----ATRPPLGIIPLGTGNDFARAL----GIP-GDPEEALEAILKGQTRPVDVGKV 125
 
Name Accession Description Interval E-value
AGK_C pfam19712
Acylglycerol kinase C-terminal; This domain corresponds to the C-terminal of mitochondrial ...
206-421 1.93e-159

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: 447.99  E-value: 1.93e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510573 206 MTGLRWGSFRDAGVKVSKYWYLGPLKIKAAHFFSTLKEWPQTHQASISYTGPTERPPNEPEETPvQRPSLYRRILRRLAS 285
Cdd:pfam19712   1 LTGLRWGSYRDAGAKVSKYWYLGPLKTKAAHLFSTLKEWPQVHQASLSYLGPTERPPEEPEEKP-PRPPLYRRIYRRLKS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510573 286 YWAQPQDALSQEVSPEVWKDVQLSTIELSITTRNNQLDPTSKEDFLNICIEPDTISKGDFITIGSRKVRNPKLHVEGTEC 365
Cdd:pfam19712  80 YWAPPQEEPPQEVEPEPWEEMQLSTIELSITTQNRQLDLTRTEDFMNICIEPDTVSKGDFITVGSQKMKDPTLCPEGSQC 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370510573 366 LQASQCTLLIPEGAGGSFSIDSEEYEAMPVEVKLLPRKLQFFCDPRKREQMLTSPT 421
Cdd:pfam19712 160 LQASRCILQLPEGTGGFFSIDSEEYEAMPVEVRLLPRKLRFFCDPERREQLLSQTQ 215
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
62-195 4.83e-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: 107.29  E-value: 4.83e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510573  62 KATVFLNPAACKGKARTLFEKnAAPILHLSGMDVTIVKTDYEGQAKKLLELMEN--TDVIIVAGGDGTLQEVVTGVLRRt 139
Cdd:pfam00781   1 KLLVIVNPKSGGGKGKKLLRK-VRPLLNKAGVEVELVLTEGPGDALELAREAAEdgYDRIVVAGGDGTVNEVLNGLAGL- 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370510573 140 deatFSKIPIGFIPLGETSSLSHTLfaesGNKvQHITDATLAIVKGETVPLDVLQI 195
Cdd:pfam00781  79 ----ATRPPLGIIPLGTGNDFARAL----GIP-GDPEEALEAILKGQTRPVDVGKV 125
PLN02958 PLN02958
diacylglycerol kinase/D-erythro-sphingosine kinase
39-232 1.04e-20

diacylglycerol kinase/D-erythro-sphingosine kinase


Pssm-ID: 215517 [Multi-domain]  Cd Length: 481  Bit Score: 93.77  E-value: 1.04e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510573  39 RRAACQEAQVFGNQLIPPnaqvKKATVFLNPAACKGKARTLFEKNAAPILHLSGMDVTIVKTDYEGQAKKLLELMENT-- 116
Cdd:PLN02958   94 RRLWCQKLRDYLDSLGRP----KRLLVFVNPFGGKKSASKIFFDVVKPLLEDADIQLTIQETKYQLHAKEVVRTMDLSky 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510573 117 DVIIVAGGDGTLQEVVTGVLRRTDEATFSKIPIGFIPLGETSSLSHTLFAESGNKVQhITDATLAIVKGETVPLDVLQIK 196
Cdd:PLN02958  170 DGIVCVSGDGILVEVVNGLLEREDWKTAIKLPIGMVPAGTGNGMAKSLLDSVGEPCS-ATNAVLAIIRGHKCSLDVATIL 248
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1370510573 197 gEKEQPVFAMTGLRWGSFRDAGVKVSKYWYLGPLKI 232
Cdd:PLN02958  249 -QGETKFFSVLMLAWGLVADIDIESEKYRWMGSARL 283
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
61-198 1.36e-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: 1.36e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510573  61 KKATVFLNPAACKGKARTLFEKnAAPILHLSGMDVTIVKTDYEGQAKKLLE--LMENTDVIIVAGGDGTLQEVVTGVLRr 138
Cdd:COG1597     3 MRALLIVNPASGRGRAARLLER-LVAALRAAGLEVEVLETESPGDATELAReaAAEGADLVVAAGGDGTVNEVANGLAG- 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510573 139 tdeatfSKIPIGFIPLGETSSLSHTLFAEsgnkvQHITDATLAIVKGETVPLDVLQIKGE 198
Cdd:COG1597    81 ------TGPPLGILPLGTGNDFARALGIP-----LDPEAALEALLTGRTRRIDLGRVNGR 129
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
65-155 9.28e-07

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: 47.68  E-value: 9.28e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510573   65 VFLNPAACKGKARTLFEKnaAPILHLSGMDVTIVKTDYEGQAKKLLELmENTDVIIVAGGDGTLQEVVTGVLRRTDeaTF 144
Cdd:smart00046   2 VFVNPKSGGGKGEKLLRK--FRLLLNPRQVFDLTKKGPAVALVIFRDV-PDFNRVLVCGGDGTVGWVLNALDKREL--PL 76
                           90
                   ....*....|.
gi 1370510573  145 SKIPIGFIPLG 155
Cdd:smart00046  77 PEPPVAVLPLG 87
TIGR00147 TIGR00147
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ...
61-197 4.46e-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: 48.27  E-value: 4.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510573  61 KKATVFLNPAAckgkARTLFEK---NAAPILHLSGMDVTIVKTDYEGQAKKLLE--LMENTDVIIVAGGDGTLQEVVTGV 135
Cdd:TIGR00147   2 AEAPAILNPTA----GKSNDNKplrEVIMLLREEGMEIHVRVTWEKGDAARYVEeaRKFGVDTVIAGGGDGTINEVVNAL 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370510573 136 lrrtdeATFSKIP-IGFIPLGETSSlshtlFAESGNKVQHITDATLAIVKGETVPLDVLQIKG 197
Cdd:TIGR00147  78 ------IQLDDIPaLGILPLGTAND-----FARSLGIPEDLDKAAKLVIAGDARAIDMGQVNK 129
 
Name Accession Description Interval E-value
AGK_C pfam19712
Acylglycerol kinase C-terminal; This domain corresponds to the C-terminal of mitochondrial ...
206-421 1.93e-159

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: 447.99  E-value: 1.93e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510573 206 MTGLRWGSFRDAGVKVSKYWYLGPLKIKAAHFFSTLKEWPQTHQASISYTGPTERPPNEPEETPvQRPSLYRRILRRLAS 285
Cdd:pfam19712   1 LTGLRWGSYRDAGAKVSKYWYLGPLKTKAAHLFSTLKEWPQVHQASLSYLGPTERPPEEPEEKP-PRPPLYRRIYRRLKS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510573 286 YWAQPQDALSQEVSPEVWKDVQLSTIELSITTRNNQLDPTSKEDFLNICIEPDTISKGDFITIGSRKVRNPKLHVEGTEC 365
Cdd:pfam19712  80 YWAPPQEEPPQEVEPEPWEEMQLSTIELSITTQNRQLDLTRTEDFMNICIEPDTVSKGDFITVGSQKMKDPTLCPEGSQC 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370510573 366 LQASQCTLLIPEGAGGSFSIDSEEYEAMPVEVKLLPRKLQFFCDPRKREQMLTSPT 421
Cdd:pfam19712 160 LQASRCILQLPEGTGGFFSIDSEEYEAMPVEVRLLPRKLRFFCDPERREQLLSQTQ 215
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
62-195 4.83e-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: 107.29  E-value: 4.83e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510573  62 KATVFLNPAACKGKARTLFEKnAAPILHLSGMDVTIVKTDYEGQAKKLLELMEN--TDVIIVAGGDGTLQEVVTGVLRRt 139
Cdd:pfam00781   1 KLLVIVNPKSGGGKGKKLLRK-VRPLLNKAGVEVELVLTEGPGDALELAREAAEdgYDRIVVAGGDGTVNEVLNGLAGL- 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370510573 140 deatFSKIPIGFIPLGETSSLSHTLfaesGNKvQHITDATLAIVKGETVPLDVLQI 195
Cdd:pfam00781  79 ----ATRPPLGIIPLGTGNDFARAL----GIP-GDPEEALEAILKGQTRPVDVGKV 125
PLN02958 PLN02958
diacylglycerol kinase/D-erythro-sphingosine kinase
39-232 1.04e-20

diacylglycerol kinase/D-erythro-sphingosine kinase


Pssm-ID: 215517 [Multi-domain]  Cd Length: 481  Bit Score: 93.77  E-value: 1.04e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510573  39 RRAACQEAQVFGNQLIPPnaqvKKATVFLNPAACKGKARTLFEKNAAPILHLSGMDVTIVKTDYEGQAKKLLELMENT-- 116
Cdd:PLN02958   94 RRLWCQKLRDYLDSLGRP----KRLLVFVNPFGGKKSASKIFFDVVKPLLEDADIQLTIQETKYQLHAKEVVRTMDLSky 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510573 117 DVIIVAGGDGTLQEVVTGVLRRTDEATFSKIPIGFIPLGETSSLSHTLFAESGNKVQhITDATLAIVKGETVPLDVLQIK 196
Cdd:PLN02958  170 DGIVCVSGDGILVEVVNGLLEREDWKTAIKLPIGMVPAGTGNGMAKSLLDSVGEPCS-ATNAVLAIIRGHKCSLDVATIL 248
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1370510573 197 gEKEQPVFAMTGLRWGSFRDAGVKVSKYWYLGPLKI 232
Cdd:PLN02958  249 -QGETKFFSVLMLAWGLVADIDIESEKYRWMGSARL 283
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
61-198 1.36e-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: 1.36e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510573  61 KKATVFLNPAACKGKARTLFEKnAAPILHLSGMDVTIVKTDYEGQAKKLLE--LMENTDVIIVAGGDGTLQEVVTGVLRr 138
Cdd:COG1597     3 MRALLIVNPASGRGRAARLLER-LVAALRAAGLEVEVLETESPGDATELAReaAAEGADLVVAAGGDGTVNEVANGLAG- 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510573 139 tdeatfSKIPIGFIPLGETSSLSHTLFAEsgnkvQHITDATLAIVKGETVPLDVLQIKGE 198
Cdd:COG1597    81 ------TGPPLGILPLGTGNDFARALGIP-----LDPEAALEALLTGRTRRIDLGRVNGR 129
PRK12361 PRK12361
hypothetical protein; Provisional
61-191 1.39e-12

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 69.26  E-value: 1.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510573  61 KKATVFLNPAACKGKartlFEKNAAPIL-HLSG-MDVTIVKTDYEGQAKKLLE--LMENTDVIIVAGGDGTLQEVVTgVL 136
Cdd:PRK12361  243 KRAWLIANPVSGGGK----WQEYGEQIQrELKAyFDLTVKLTTPEISAEALAKqaRKAGADIVIACGGDGTVTEVAS-EL 317
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1370510573 137 RRTDeatfskIPIGFIPLGETSSLSHTLFAeSGNKVQHITDATLAIVKGETVPLD 191
Cdd:PRK12361  318 VNTD------ITLGIIPLGTANALSHALFG-LGSKLIPVEQACDNIIQGHTQRID 365
PRK13337 PRK13337
putative lipid kinase; Reviewed
61-192 4.80e-11

putative lipid kinase; Reviewed


Pssm-ID: 183982 [Multi-domain]  Cd Length: 304  Bit Score: 63.53  E-value: 4.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510573  61 KKATVFLNPAAckgkARTLFEKNAAPIL---HLSGMDVTIVKTDYEGQAKKLLE--LMENTDVIIVAGGDGTLQEVVTGV 135
Cdd:PRK13337    2 KRARIIYNPTS----GRELFKKNLPDVLqklEQAGYETSAHATTGPGDATLAAEraVERKFDLVIAAGGDGTLNEVVNGI 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370510573 136 lrrtdeATFSKIP-IGFIPLGETSSlshtlFAESGNKVQHITDATLAIVKGETVPLDV 192
Cdd:PRK13337   78 ------AEKENRPkLGIIPVGTTND-----FARALHVPRDIEKAADVIIEGHTVPVDI 124
PRK13055 PRK13055
putative lipid kinase; Reviewed
61-199 6.12e-09

putative lipid kinase; Reviewed


Pssm-ID: 237282 [Multi-domain]  Cd Length: 334  Bit Score: 57.31  E-value: 6.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510573  61 KKATVFLNPAAckgkARTLFEKNAAPILHL---SGMDVTIVKTDYE-----GQAKKLLElmENTDVIIVAGGDGTLQEVV 132
Cdd:PRK13055    3 KRARLIYNPTS----GQEIMKKNVADILDIleqAGYETSAFQTTPEpnsakNEAKRAAE--AGFDLIIAAGGDGTINEVV 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370510573 133 TGVlrrtdeATFSKIP-IGFIPLGETSSLSHTLFAESGNKVqhitDATLAIVKGETVPLDVLQIKGEK 199
Cdd:PRK13055   77 NGI------APLEKRPkMAIIPAGTTNDYARALKIPRDNPV----EAAKVILKNQTIKMDIGRANEDK 134
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
65-155 9.28e-07

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: 47.68  E-value: 9.28e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510573   65 VFLNPAACKGKARTLFEKnaAPILHLSGMDVTIVKTDYEGQAKKLLELmENTDVIIVAGGDGTLQEVVTGVLRRTDeaTF 144
Cdd:smart00046   2 VFVNPKSGGGKGEKLLRK--FRLLLNPRQVFDLTKKGPAVALVIFRDV-PDFNRVLVCGGDGTVGWVLNALDKREL--PL 76
                           90
                   ....*....|.
gi 1370510573  145 SKIPIGFIPLG 155
Cdd:smart00046  77 PEPPVAVLPLG 87
PRK00861 PRK00861
putative lipid kinase; Reviewed
61-192 1.89e-06

putative lipid kinase; Reviewed


Pssm-ID: 234850 [Multi-domain]  Cd Length: 300  Bit Score: 49.23  E-value: 1.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510573  61 KKATVFLNPAACKGKARTlfEKNAAPILHLSGMDVTIVKTDYEGQAKKLLE--LMENTDVIIVAGGDGTLQeVVTGVLRR 138
Cdd:PRK00861    3 RSACLIFNPVAGQGNPEV--DLALIRAILEPEMDLDIYLTTPEIGADQLAQeaIERGAELIIASGGDGTLS-AVAGALIG 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370510573 139 TDeatfskIPIGFIPLGETSSLSHTLfaesgNKVQHITDATLAIVKGETVPLDV 192
Cdd:PRK00861   80 TD------IPLGIIPRGTANAFAAAL-----GIPDTIEEACRTILQGKTRRVDV 122
TIGR00147 TIGR00147
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ...
61-197 4.46e-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: 48.27  E-value: 4.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510573  61 KKATVFLNPAAckgkARTLFEK---NAAPILHLSGMDVTIVKTDYEGQAKKLLE--LMENTDVIIVAGGDGTLQEVVTGV 135
Cdd:TIGR00147   2 AEAPAILNPTA----GKSNDNKplrEVIMLLREEGMEIHVRVTWEKGDAARYVEeaRKFGVDTVIAGGGDGTINEVVNAL 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370510573 136 lrrtdeATFSKIP-IGFIPLGETSSlshtlFAESGNKVQHITDATLAIVKGETVPLDVLQIKG 197
Cdd:TIGR00147  78 ------IQLDDIPaLGILPLGTAND-----FARSLGIPEDLDKAAKLVIAGDARAIDMGQVNK 129
PRK13054 PRK13054
lipid kinase; Reviewed
103-198 3.19e-05

lipid kinase; Reviewed


Pssm-ID: 237281 [Multi-domain]  Cd Length: 300  Bit Score: 45.63  E-value: 3.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510573 103 EGQAKKLLE--LMENTDVIIVAGGDGTLQEVVTGVLRRTDEATFSkipIGFIPLGETSSlshtlFAESGNKVQHITDA-T 179
Cdd:PRK13054   42 KGDAARYVEeaLALGVATVIAGGGDGTINEVATALAQLEGDARPA---LGILPLGTAND-----FATAAGIPLEPDKAlK 113
                          90
                  ....*....|....*....
gi 1370510573 180 LAIvKGETVPLDVLQIKGE 198
Cdd:PRK13054  114 LAI-EGRAQPIDLARVNDR 131
PRK13059 PRK13059
putative lipid kinase; Reviewed
107-192 5.18e-05

putative lipid kinase; Reviewed


Pssm-ID: 183858  Cd Length: 295  Bit Score: 44.64  E-value: 5.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510573 107 KKLLELMENT-DVIIVAGGDGTLQEVVTGVLRRTdeatfSKIPIGFIPLGETSSlshtlFAESGNKVQHITDATLAIVKG 185
Cdd:PRK13059   47 KNAFKDIDESyKYILIAGGDGTVDNVVNAMKKLN-----IDLPIGILPVGTAND-----FAKFLGMPTDIGEACEQILKS 116

                  ....*..
gi 1370510573 186 ETVPLDV 192
Cdd:PRK13059  117 KPKKVDL 123
 
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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