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Conserved domains on  [gi|1572047467|ref|NP_001355400|]
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Diacylglycerol kinase [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 621-774 5.33e-76

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: 246.09  E-value: 5.33e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047467  621 VMTNYFSIGADAHVALQFHHSRSANPQMLNSRLKNRIAYGGLGTIDLFKRSWKDLCEYITLECDGVDVTPRIkelKLHCI 700
Cdd:smart00045   1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLPN---SLEGI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047467  701 LFHNITYYAGGTIPWGESSD-----NKPSCCDGKVEVLGFTTATLAA--LQMGGKGERIAQCSRVRV--ITNKAIPMQVD 771
Cdd:smart00045  78 AVLNIPSYGGGTNLWGTTDKedlnfSKQSHDDGLLEVVGLTGAMHMAqiRQVGLAGRRIAQCSEVRItiKTSKTIPMQVD 157


                   ...
gi 1572047467  772 GEP 774
Cdd:smart00045 158 GEP 160
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 469-593 7.78e-49

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: 169.01  E-value: 7.78e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047467  469 LVFVNPKSGGNKGSKALHTLCWLLNPRQVFDITSlKGPKFGLEMFRKVVTQLRILVCGGDGTVGWVLSTLDNLNWPA-YP 547
Cdd:smart00046   1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTK-KGPAVALVIFRDVPDFNRVLVCGGDGTVGWVLNALDKRELPLpEP 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1572047467  548 PMAIMPLGTGNDLARCMGWGGVFSDEPISQLMQAILhETIVTHLDR 593
Cdd:smart00046  80 PVAVLPLGTGNDLARSLGWGGGYDGEKLLKTLRDAL-ESDTVKLDR 124
C1_DGK_typeIV_rpt2 cd20855
second protein kinase C conserved region 1 (C1 domain) found in type IV diacylglycerol kinases; ...
 351-414 2.56e-30

second protein kinase C conserved region 1 (C1 domain) found in type IV diacylglycerol kinases; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. Type IV DAG kinases (DGKs) contain myristoylated alanine-rich protein kinase C substrate (MARCKS), PDZ-binding, and ankyrin domains, in addition to C1 and catalytic domains that are present in all DGKs. The MARCKS domain regulates the nuclear localizations of type IV DGKs while the PDZ-binding and ankyrin domains regulate interactions with several proteins. Two DGK isozymes (zeta and iota) are classified as type IV. DAG kinase zeta, also called diglyceride kinase zeta (DGK-zeta), displays a strong preference for 1,2-diacylglycerols over 1,3-diacylglycerols, but lacks substrate specificity among molecular species of long chain diacylglycerols. DAG kinase iota, also called diglyceride kinase iota (DGK-iota), or DGKI, is a homolog of Drosophila DGK2, RdgA. It may have important cellular functions in the retina and brain. Members of this family contain two copies of the C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


:

Pssm-ID: 410405  Cd Length: 62  Bit Score: 113.98  E-value: 2.56e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1572047467 351 HHWVHKWRHEGRCNTCAKSFQQKMFFQGkekKETIAVTCSWCKESYHLK-NCFARDKLEERCNRG 414
Cdd:cd20855     1 HHWVHRRKQEGKCKQCGKSFQQKLSFSS---KEIVAISCSWCKEAYHNKdSCFNMKKIEEPCNLG 62
C1_DGK_typeIV_rpt1 cd20802
first protein kinase C conserved region 1 (C1 domain) found in type IV diacylglycerol kinases; ...
 267-333 1.66e-27

first protein kinase C conserved region 1 (C1 domain) found in type IV diacylglycerol kinases; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. Type IV DAG kinases (DGKs) contain myristoylated alanine-rich protein kinase C substrate (MARCKS), PDZ-binding, and ankyrin domains, in addition to C1 and catalytic domains that are present in all DGKs. The MARCKS domain regulates the nuclear localizations of type IV DGKs while the PDZ-binding and ankyrin domains regulate interactions with several proteins. Two DGK isozymes (zeta and iota) are classified as type IV. DAG kinase zeta, also called diglyceride kinase zeta (DGK-zeta), displays a strong preference for 1,2-diacylglycerols over 1,3-diacylglycerols, but lacks substrate specificity among molecular species of long chain diacylglycerols. DAG kinase iota, also called diglyceride kinase iota (DGK-iota), or DGKI, is a homolog of Drosophila DGK2, RdgA. It may have important cellular functions in the retina and brain. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


:

Pssm-ID: 410352  Cd Length: 62  Bit Score: 105.84  E-value: 1.66e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1572047467 267 ILPSEHVWLPSStgssASADsECYVGEKDCRRSGEKRRCAACHIVAHTNCFSLLAKLNLNCKTTFRD 333
Cdd:cd20802     1 AVNGEHLWTDTS----ASGD-LCYVGEQDCLKSGSRKKCSACKIVVHTGCIPQLEKINFKCKPTFRE 62
 
Name Accession Description Interval E-value
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 621-774 5.33e-76

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: 246.09  E-value: 5.33e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047467  621 VMTNYFSIGADAHVALQFHHSRSANPQMLNSRLKNRIAYGGLGTIDLFKRSWKDLCEYITLECDGVDVTPRIkelKLHCI 700
Cdd:smart00045   1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLPN---SLEGI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047467  701 LFHNITYYAGGTIPWGESSD-----NKPSCCDGKVEVLGFTTATLAA--LQMGGKGERIAQCSRVRV--ITNKAIPMQVD 771
Cdd:smart00045  78 AVLNIPSYGGGTNLWGTTDKedlnfSKQSHDDGLLEVVGLTGAMHMAqiRQVGLAGRRIAQCSEVRItiKTSKTIPMQVD 157


                   ...
gi 1572047467  772 GEP 774
Cdd:smart00045 158 GEP 160
DAGK_acc pfam00609
Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts ...
 621-774 1.34e-67

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: 222.86  E-value: 1.34e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047467 621 VMTNYFSIGADAHVALQFHHSRSANPQMLNSRLKNRIAYGGLGTIDLFKRSWKDLCEYITLECDGVDVTPRikeLKLHCI 700
Cdd:pfam00609   1 VMNNYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDMFQRSCKNLIEKVELEVDGKDLPLP---KSLEGI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047467 701 LFHNITYYAGGTIPWGESSDN-----KPSCCDGKVEVLGFT-TATLAALQMG-GKGERIAQCSRVRVITNKAIPMQVDGE 773
Cdd:pfam00609  78 VVLNIPSYAGGTDLWGNSKEDglgfaPQSVDDGLLEVVGLTgALHLGQVQVGlGSAKRIAQGGPIRITTKKKIPMQVDGE 157


                  .
gi 1572047467 774 P 774
Cdd:pfam00609 158 P 158
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 469-593 7.78e-49

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: 169.01  E-value: 7.78e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047467  469 LVFVNPKSGGNKGSKALHTLCWLLNPRQVFDITSlKGPKFGLEMFRKVVTQLRILVCGGDGTVGWVLSTLDNLNWPA-YP 547
Cdd:smart00046   1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTK-KGPAVALVIFRDVPDFNRVLVCGGDGTVGWVLNALDKRELPLpEP 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1572047467  548 PMAIMPLGTGNDLARCMGWGGVFSDEPISQLMQAILhETIVTHLDR 593
Cdd:smart00046  80 PVAVLPLGTGNDLARSLGWGGGYDGEKLLKTLRDAL-ESDTVKLDR 124
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 467-598 2.89e-36

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: 133.09  E-value: 2.89e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047467 467 PLLVFVNPKSGGNKGSKALHTLCWLLNPRQV-FDITSLKGPKFGLEMFRKVVTQ--LRILVCGGDGTVGWVLSTLDNLnw 543
Cdd:pfam00781   1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVeVELVLTEGPGDALELAREAAEDgyDRIVVAGGDGTVNEVLNGLAGL-- 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1572047467 544 PAYPPMAIMPLGTGNDLARCMGWGGvfsdEPISQLMQAILHETIvthldrwRIDV 598
Cdd:pfam00781  79 ATRPPLGIIPLGTGNDFARALGIPG----DPEEALEAILKGQTR-------PVDV 122
C1_DGK_typeIV_rpt2 cd20855
second protein kinase C conserved region 1 (C1 domain) found in type IV diacylglycerol kinases; ...
 351-414 2.56e-30

second protein kinase C conserved region 1 (C1 domain) found in type IV diacylglycerol kinases; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. Type IV DAG kinases (DGKs) contain myristoylated alanine-rich protein kinase C substrate (MARCKS), PDZ-binding, and ankyrin domains, in addition to C1 and catalytic domains that are present in all DGKs. The MARCKS domain regulates the nuclear localizations of type IV DGKs while the PDZ-binding and ankyrin domains regulate interactions with several proteins. Two DGK isozymes (zeta and iota) are classified as type IV. DAG kinase zeta, also called diglyceride kinase zeta (DGK-zeta), displays a strong preference for 1,2-diacylglycerols over 1,3-diacylglycerols, but lacks substrate specificity among molecular species of long chain diacylglycerols. DAG kinase iota, also called diglyceride kinase iota (DGK-iota), or DGKI, is a homolog of Drosophila DGK2, RdgA. It may have important cellular functions in the retina and brain. Members of this family contain two copies of the C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410405  Cd Length: 62  Bit Score: 113.98  E-value: 2.56e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1572047467 351 HHWVHKWRHEGRCNTCAKSFQQKMFFQGkekKETIAVTCSWCKESYHLK-NCFARDKLEERCNRG 414
Cdd:cd20855     1 HHWVHRRKQEGKCKQCGKSFQQKLSFSS---KEIVAISCSWCKEAYHNKdSCFNMKKIEEPCNLG 62
C1_DGK_typeIV_rpt1 cd20802
first protein kinase C conserved region 1 (C1 domain) found in type IV diacylglycerol kinases; ...
 267-333 1.66e-27

first protein kinase C conserved region 1 (C1 domain) found in type IV diacylglycerol kinases; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. Type IV DAG kinases (DGKs) contain myristoylated alanine-rich protein kinase C substrate (MARCKS), PDZ-binding, and ankyrin domains, in addition to C1 and catalytic domains that are present in all DGKs. The MARCKS domain regulates the nuclear localizations of type IV DGKs while the PDZ-binding and ankyrin domains regulate interactions with several proteins. Two DGK isozymes (zeta and iota) are classified as type IV. DAG kinase zeta, also called diglyceride kinase zeta (DGK-zeta), displays a strong preference for 1,2-diacylglycerols over 1,3-diacylglycerols, but lacks substrate specificity among molecular species of long chain diacylglycerols. DAG kinase iota, also called diglyceride kinase iota (DGK-iota), or DGKI, is a homolog of Drosophila DGK2, RdgA. It may have important cellular functions in the retina and brain. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410352  Cd Length: 62  Bit Score: 105.84  E-value: 1.66e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1572047467 267 ILPSEHVWLPSStgssASADsECYVGEKDCRRSGEKRRCAACHIVAHTNCFSLLAKLNLNCKTTFRD 333
Cdd:cd20802     1 AVNGEHLWTDTS----ASGD-LCYVGEQDCLKSGSRKKCSACKIVVHTGCIPQLEKINFKCKPTFRE 62
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 464-781 6.80e-23

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


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 99.93  E-value: 6.80e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047467 464 PSQPLLVFVNPKSGGNKGSKALHTLCWLLNPRQV-FDITSLKGPKFGLEMFRKVVTQL--RILVCGGDGTVGWVLSTLDN 540
Cdd:COG1597     1 AMMRALLIVNPASGRGRAARLLERLVAALRAAGLeVEVLETESPGDATELAREAAAEGadLVVAAGGDGTVNEVANGLAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047467 541 LNwpayPPMAIMPLGTGNDLARCMGWggvfsDEPISQLMQAILHETIVthldrwRIDV-EPNTscnleeeddgmqsalpl 619
Cdd:COG1597    81 TG----PPLGILPLGTGNDFARALGI-----PLDPEAALEALLTGRTR------RIDLgRVNG----------------- 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047467 620 TVMTNYFSIGADAHVALQFhhsrsanpqmlNSRLKNRI---AY--GGLGTIDLFKRswkdlcEYITLECDGVDVtprikE 694
Cdd:COG1597   129 RYFLNVAGIGFDAEVVERA-----------NRALKRRLgklAYvlAALRALLRYRP------FRLRIELDGEEI-----E 186

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047467 695 LKLHCILFHNITYYAGG-TIPWGESSDnkpsccDGKVEVLGFTT-------ATLAALQMGGKGE----RIAQCSRVRVIT 762
Cdd:COG1597   187 GEALLVAVGNGPYYGGGlRLAPDASLD------DGLLDVVVVRPlsrlrllRLLPRLLRGRHLRhpgvRYFRAREVEIES 260

                         330
                  ....*....|....*....
gi 1572047467 763 NKAIPMQVDGEPCLLAPSI 781
Cdd:COG1597   261 DRPLPVQLDGEPLGLATPL 279
PRK12361 PRK12361
hypothetical protein; Provisional
 466-583 4.21e-07

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 53.86  E-value: 4.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047467 466 QPLLVFVNPKSGGNKGSKALHTLCWLLNPRqvFDIT-SLKGPKFGLEMFRKvvtQLR------ILVCGGDGTVGWVLSTL 538
Cdd:PRK12361  243 KRAWLIANPVSGGGKWQEYGEQIQRELKAY--FDLTvKLTTPEISAEALAK---QARkagadiVIACGGDGTVTEVASEL 317

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1572047467 539 DNLNwpayPPMAIMPLGTGNDLARC-MGWGGVFSdePISQLMQAIL 583
Cdd:PRK12361  318 VNTD----ITLGIIPLGTANALSHAlFGLGSKLI--PVEQACDNII 357
TIGR00147 TIGR00147
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ...
 521-782 1.68e-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: 50.97  E-value: 1.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047467 521 RILVCGGDGTVGWV---LSTLDNLnwpayPPMAIMPLGTGNDLARCMGwggvfsdepISQ-LMQAIlhETIVTHLDRwRI 596
Cdd:TIGR00147  60 TVIAGGGDGTINEVvnaLIQLDDI-----PALGILPLGTANDFARSLG---------IPEdLDKAA--KLVIAGDAR-AI 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047467 597 DVepntsCNLEEEDDGMqsalpltvmtNYFSIGADAHVALQFhhsrsanPQMLNSRLKnRIAY--GGLGTIDLFKRSwkd 674
Cdd:TIGR00147 123 DM-----GQVNKQYCFI----------NMAGGGFGTEITTET-------PEKLKAALG-SLSYilSGLMRMDTLQPF--- 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047467 675 lceyiTLECDGVDvtpriKELKLHCILF--HNITYYAGGTIPWGESSDNkpsccDGKVEVLGFTTATLAA----LQMGGK 748
Cdd:TIGR00147 177 -----RCEIRGEG-----EHWQGEAVVFlvGNGRQAGGGQKLAPDASIN-----DGLLDLRIFTNDNLLPalvlTLMSDE 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1572047467 749 GERI-------AQCSRVRVITNKAIPMQVDGEPCLLAPSII 782
Cdd:TIGR00147 242 GKHTdnpniiyGKASRIDIQTPHKITFNLDGEPLGGTPFHI 282
 
Name Accession Description Interval E-value
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 621-774 5.33e-76

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: 246.09  E-value: 5.33e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047467  621 VMTNYFSIGADAHVALQFHHSRSANPQMLNSRLKNRIAYGGLGTIDLFKRSWKDLCEYITLECDGVDVTPRIkelKLHCI 700
Cdd:smart00045   1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLPN---SLEGI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047467  701 LFHNITYYAGGTIPWGESSD-----NKPSCCDGKVEVLGFTTATLAA--LQMGGKGERIAQCSRVRV--ITNKAIPMQVD 771
Cdd:smart00045  78 AVLNIPSYGGGTNLWGTTDKedlnfSKQSHDDGLLEVVGLTGAMHMAqiRQVGLAGRRIAQCSEVRItiKTSKTIPMQVD 157


                   ...
gi 1572047467  772 GEP 774
Cdd:smart00045 158 GEP 160
DAGK_acc pfam00609
Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts ...
 621-774 1.34e-67

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: 222.86  E-value: 1.34e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047467 621 VMTNYFSIGADAHVALQFHHSRSANPQMLNSRLKNRIAYGGLGTIDLFKRSWKDLCEYITLECDGVDVTPRikeLKLHCI 700
Cdd:pfam00609   1 VMNNYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDMFQRSCKNLIEKVELEVDGKDLPLP---KSLEGI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047467 701 LFHNITYYAGGTIPWGESSDN-----KPSCCDGKVEVLGFT-TATLAALQMG-GKGERIAQCSRVRVITNKAIPMQVDGE 773
Cdd:pfam00609  78 VVLNIPSYAGGTDLWGNSKEDglgfaPQSVDDGLLEVVGLTgALHLGQVQVGlGSAKRIAQGGPIRITTKKKIPMQVDGE 157


                  .
gi 1572047467 774 P 774
Cdd:pfam00609 158 P 158
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 469-593 7.78e-49

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: 169.01  E-value: 7.78e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047467  469 LVFVNPKSGGNKGSKALHTLCWLLNPRQVFDITSlKGPKFGLEMFRKVVTQLRILVCGGDGTVGWVLSTLDNLNWPA-YP 547
Cdd:smart00046   1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTK-KGPAVALVIFRDVPDFNRVLVCGGDGTVGWVLNALDKRELPLpEP 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1572047467  548 PMAIMPLGTGNDLARCMGWGGVFSDEPISQLMQAILhETIVTHLDR 593
Cdd:smart00046  80 PVAVLPLGTGNDLARSLGWGGGYDGEKLLKTLRDAL-ESDTVKLDR 124
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 467-598 2.89e-36

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: 133.09  E-value: 2.89e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047467 467 PLLVFVNPKSGGNKGSKALHTLCWLLNPRQV-FDITSLKGPKFGLEMFRKVVTQ--LRILVCGGDGTVGWVLSTLDNLnw 543
Cdd:pfam00781   1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVeVELVLTEGPGDALELAREAAEDgyDRIVVAGGDGTVNEVLNGLAGL-- 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1572047467 544 PAYPPMAIMPLGTGNDLARCMGWGGvfsdEPISQLMQAILHETIvthldrwRIDV 598
Cdd:pfam00781  79 ATRPPLGIIPLGTGNDFARALGIPG----DPEEALEAILKGQTR-------PVDV 122
C1_DGK_typeIV_rpt2 cd20855
second protein kinase C conserved region 1 (C1 domain) found in type IV diacylglycerol kinases; ...
 351-414 2.56e-30

second protein kinase C conserved region 1 (C1 domain) found in type IV diacylglycerol kinases; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. Type IV DAG kinases (DGKs) contain myristoylated alanine-rich protein kinase C substrate (MARCKS), PDZ-binding, and ankyrin domains, in addition to C1 and catalytic domains that are present in all DGKs. The MARCKS domain regulates the nuclear localizations of type IV DGKs while the PDZ-binding and ankyrin domains regulate interactions with several proteins. Two DGK isozymes (zeta and iota) are classified as type IV. DAG kinase zeta, also called diglyceride kinase zeta (DGK-zeta), displays a strong preference for 1,2-diacylglycerols over 1,3-diacylglycerols, but lacks substrate specificity among molecular species of long chain diacylglycerols. DAG kinase iota, also called diglyceride kinase iota (DGK-iota), or DGKI, is a homolog of Drosophila DGK2, RdgA. It may have important cellular functions in the retina and brain. Members of this family contain two copies of the C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410405  Cd Length: 62  Bit Score: 113.98  E-value: 2.56e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1572047467 351 HHWVHKWRHEGRCNTCAKSFQQKMFFQGkekKETIAVTCSWCKESYHLK-NCFARDKLEERCNRG 414
Cdd:cd20855     1 HHWVHRRKQEGKCKQCGKSFQQKLSFSS---KEIVAISCSWCKEAYHNKdSCFNMKKIEEPCNLG 62
C1_DGK_typeIV_rpt1 cd20802
first protein kinase C conserved region 1 (C1 domain) found in type IV diacylglycerol kinases; ...
 267-333 1.66e-27

first protein kinase C conserved region 1 (C1 domain) found in type IV diacylglycerol kinases; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. Type IV DAG kinases (DGKs) contain myristoylated alanine-rich protein kinase C substrate (MARCKS), PDZ-binding, and ankyrin domains, in addition to C1 and catalytic domains that are present in all DGKs. The MARCKS domain regulates the nuclear localizations of type IV DGKs while the PDZ-binding and ankyrin domains regulate interactions with several proteins. Two DGK isozymes (zeta and iota) are classified as type IV. DAG kinase zeta, also called diglyceride kinase zeta (DGK-zeta), displays a strong preference for 1,2-diacylglycerols over 1,3-diacylglycerols, but lacks substrate specificity among molecular species of long chain diacylglycerols. DAG kinase iota, also called diglyceride kinase iota (DGK-iota), or DGKI, is a homolog of Drosophila DGK2, RdgA. It may have important cellular functions in the retina and brain. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410352  Cd Length: 62  Bit Score: 105.84  E-value: 1.66e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1572047467 267 ILPSEHVWLPSStgssASADsECYVGEKDCRRSGEKRRCAACHIVAHTNCFSLLAKLNLNCKTTFRD 333
Cdd:cd20802     1 AVNGEHLWTDTS----ASGD-LCYVGEQDCLKSGSRKKCSACKIVVHTGCIPQLEKINFKCKPTFRE 62
C1_DGKzeta_rpt2 cd20895
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta ...
 351-425 2.81e-23

second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta (DAG kinase zeta) and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase zeta, also called diglyceride kinase zeta (DGK-zeta), displays a strong preference for 1,2-diacylglycerols over 1,3-diacylglycerols, but lacks substrate specificity among molecular species of long chain diacylglycerols. It is classified as a type IV DAG kinase (DGK), containing myristoylated alanine-rich protein kinase C substrate (MARCKS), PDZ-binding, and ankyrin domains, in addition to C1 and catalytic domains that are present in all DGKs. The MARCKS domain regulates the nuclear localizations of type IV DGKs while the PDZ-binding and ankyrin domains regulate interactions with several proteins. DAG kinase zeta contains two copies of the C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410445  Cd Length: 75  Bit Score: 94.38  E-value: 2.81e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1572047467 351 HHWVHKWRHEGRCNTCAKSFQQKMFFQgkeKKETIAVTCSWCKESYHLK-NCFARDKLEERCNRGALKEMIVPPTW 425
Cdd:cd20895     3 HHWVHRRRQEGKCRQCGKGFQQKFAFH---SKEIVAISCSWCKQAYHSKvSCFMLQQIEEPCSLGAHAAVIVPPTW 75
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 464-781 6.80e-23

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


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 99.93  E-value: 6.80e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047467 464 PSQPLLVFVNPKSGGNKGSKALHTLCWLLNPRQV-FDITSLKGPKFGLEMFRKVVTQL--RILVCGGDGTVGWVLSTLDN 540
Cdd:COG1597     1 AMMRALLIVNPASGRGRAARLLERLVAALRAAGLeVEVLETESPGDATELAREAAAEGadLVVAAGGDGTVNEVANGLAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047467 541 LNwpayPPMAIMPLGTGNDLARCMGWggvfsDEPISQLMQAILHETIVthldrwRIDV-EPNTscnleeeddgmqsalpl 619
Cdd:COG1597    81 TG----PPLGILPLGTGNDFARALGI-----PLDPEAALEALLTGRTR------RIDLgRVNG----------------- 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047467 620 TVMTNYFSIGADAHVALQFhhsrsanpqmlNSRLKNRI---AY--GGLGTIDLFKRswkdlcEYITLECDGVDVtprikE 694
Cdd:COG1597   129 RYFLNVAGIGFDAEVVERA-----------NRALKRRLgklAYvlAALRALLRYRP------FRLRIELDGEEI-----E 186

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047467 695 LKLHCILFHNITYYAGG-TIPWGESSDnkpsccDGKVEVLGFTT-------ATLAALQMGGKGE----RIAQCSRVRVIT 762
Cdd:COG1597   187 GEALLVAVGNGPYYGGGlRLAPDASLD------DGLLDVVVVRPlsrlrllRLLPRLLRGRHLRhpgvRYFRAREVEIES 260

                         330
                  ....*....|....*....
gi 1572047467 763 NKAIPMQVDGEPCLLAPSI 781
Cdd:COG1597   261 DRPLPVQLDGEPLGLATPL 279
C1_DGKiota_rpt2 cd20896
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase iota ...
 351-425 2.42e-22

second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase iota (DAG kinase iota) and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase iota, also called diglyceride kinase iota (DGK-iota), or DGKI, is a homolog of Drosophila DGK2, RdgA. It may have important cellular functions in the retina and brain. It is classified as a type IV DAG kinase (DGK), containing myristoylated alanine-rich protein kinase C substrate (MARCKS), PDZ-binding, and ankyrin domains, in addition to C1 and catalytic domains that are present in all DGKs. The MARCKS domain regulates the nuclear localizations of type IV DGKs while the PDZ-binding and ankyrin domains regulate interactions with several proteins. DAG kinase iota contains two copies of the C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410446  Cd Length: 75  Bit Score: 91.69  E-value: 2.42e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1572047467 351 HHWVHKWRHEGRCNTCAKSFQQKMFFQgkeKKETIAVTCSWCKESYHLK-NCFARDKLEERCNRGALKEMIVPPTW 425
Cdd:cd20896     3 HHWVHRRRQEGKCKQCGKGFQQKFSFH---SKEIVAISCSWCKQAFHNKvTCFMLHHIEEPCSLGAHAAVIVPPTW 75
C1_DGKiota_rpt1 cd20850
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase iota (DAG ...
 271-333 2.62e-13

first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase iota (DAG kinase iota) and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase iota, also called diglyceride kinase iota (DGK-iota), or DGKI, is a homolog of Drosophila DGK2, RdgA. It may have important cellular functions in the retina and brain. It is classified as a type IV DAG kinase (DGK), containing myristoylated alanine-rich protein kinase C substrate (MARCKS), PDZ-binding, and ankyrin domains, in addition to C1 and catalytic domains that are present in all DGKs. The MARCKS domain regulates the nuclear localizations of type IV DGKs while the PDZ-binding and ankyrin domains regulate interactions with several proteins. DAG kinase iota contains two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410400  Cd Length: 73  Bit Score: 65.82  E-value: 2.62e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1572047467 271 EHVWLPSStgssASADSeCYVGEKDCR----RSGEKRRCAACHIVAHTNCFSLLAKLNLNCKTTFRD 333
Cdd:cd20850    10 EHLWLETN----VSGDL-CYLGEENCQvkfaKSALRRKCAACKIVVHTACIEQLEKINFRCKPTFRE 71
C1_DGKzeta_rpt1 cd20849
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta (DAG ...
 271-333 3.63e-11

first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta (DAG kinase zeta) and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase zeta, also called diglyceride kinase zeta (DGK-zeta), displays a strong preference for 1,2-diacylglycerols over 1,3-diacylglycerols, but lacks substrate specificity among molecular species of long chain diacylglycerols. It is classified as a type IV DAG kinase (DGK), containing myristoylated alanine-rich protein kinase C substrate (MARCKS), PDZ-binding, and ankyrin domains, in addition to C1 and catalytic domains that are present in all DGKs. The MARCKS domain regulates the nuclear localizations of type IV DGKs while the PDZ-binding and ankyrin domains regulate interactions with several proteins. DAG kinase zeta contains two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410399  Cd Length: 74  Bit Score: 59.95  E-value: 3.63e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1572047467 271 EHVWLPSSTgssaSADSeCYVGEKDC-----RRSGEKRRCAACHIVAHTNCFSLLAKLNLNCKTTFRD 333
Cdd:cd20849    10 EHIWFETNV----SGDF-CYVGEQNCvakqlQKSVSRKKCAACKIVVHTPCIEQLEKINFRCKPSFRE 72
PRK12361 PRK12361
hypothetical protein; Provisional
 466-583 4.21e-07

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 53.86  E-value: 4.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047467 466 QPLLVFVNPKSGGNKGSKALHTLCWLLNPRqvFDIT-SLKGPKFGLEMFRKvvtQLR------ILVCGGDGTVGWVLSTL 538
Cdd:PRK12361  243 KRAWLIANPVSGGGKWQEYGEQIQRELKAY--FDLTvKLTTPEISAEALAK---QARkagadiVIACGGDGTVTEVASEL 317

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1572047467 539 DNLNwpayPPMAIMPLGTGNDLARC-MGWGGVFSdePISQLMQAIL 583
Cdd:PRK12361  318 VNTD----ITLGIIPLGTANALSHAlFGLGSKLI--PVEQACDNII 357
TIGR00147 TIGR00147
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ...
 521-782 1.68e-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: 50.97  E-value: 1.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047467 521 RILVCGGDGTVGWV---LSTLDNLnwpayPPMAIMPLGTGNDLARCMGwggvfsdepISQ-LMQAIlhETIVTHLDRwRI 596
Cdd:TIGR00147  60 TVIAGGGDGTINEVvnaLIQLDDI-----PALGILPLGTANDFARSLG---------IPEdLDKAA--KLVIAGDAR-AI 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047467 597 DVepntsCNLEEEDDGMqsalpltvmtNYFSIGADAHVALQFhhsrsanPQMLNSRLKnRIAY--GGLGTIDLFKRSwkd 674
Cdd:TIGR00147 123 DM-----GQVNKQYCFI----------NMAGGGFGTEITTET-------PEKLKAALG-SLSYilSGLMRMDTLQPF--- 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047467 675 lceyiTLECDGVDvtpriKELKLHCILF--HNITYYAGGTIPWGESSDNkpsccDGKVEVLGFTTATLAA----LQMGGK 748
Cdd:TIGR00147 177 -----RCEIRGEG-----EHWQGEAVVFlvGNGRQAGGGQKLAPDASIN-----DGLLDLRIFTNDNLLPalvlTLMSDE 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1572047467 749 GERI-------AQCSRVRVITNKAIPMQVDGEPCLLAPSII 782
Cdd:TIGR00147 242 GKHTdnpniiyGKASRIDIQTPHKITFNLDGEPLGGTPFHI 282
PRK13054 PRK13054
lipid kinase; Reviewed
 521-565 4.36e-06

lipid kinase; Reviewed


Pssm-ID: 237281 [Multi-domain]  Cd Length: 300  Bit Score: 49.87  E-value: 4.36e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1572047467 521 RILVCGGDGTVGWVLSTLDNLNWPAYPPMAIMPLGTGNDLARCMG 565
Cdd:PRK13054   59 TVIAGGGDGTINEVATALAQLEGDARPALGILPLGTANDFATAAG 103
PRK13059 PRK13059
putative lipid kinase; Reviewed
 522-565 1.77e-05

putative lipid kinase; Reviewed


Pssm-ID: 183858  Cd Length: 295  Bit Score: 47.72  E-value: 1.77e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1572047467 522 ILVCGGDGTVGWVLSTLDNLNWPAypPMAIMPLGTGNDLARCMG 565
Cdd:PRK13059   60 ILIAGGDGTVDNVVNAMKKLNIDL--PIGILPVGTANDFAKFLG 101
C1_DGKepsilon_typeIII_rpt2 cd20853
second protein kinase C conserved region 1 (C1 domain) found in type III diacylglycerol kinase, ...
 389-423 2.05e-04

second protein kinase C conserved region 1 (C1 domain) found in type III diacylglycerol kinase, DAG kinase epsilon, and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase epsilon, also called diglyceride kinase epsilon (DGK-epsilon), is the only isoform classified as type III; it possesses a hydrophobic domain in addition to C1 and catalytic domains that are present in all DGKs, and shows selectivity for acyl chains. It is highly selective for arachidonate-containing species of DAG. It may terminate signals transmitted through arachidonoyl-DAG or may contribute to the synthesis of phospholipids with defined fatty acid composition. DAG kinase epsilon contains two copies of the C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410403  Cd Length: 63  Bit Score: 40.34  E-value: 2.05e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1572047467 389 CSWCKESYHLKnCFArdKLEERCNRGALKEMIVPP 423
Cdd:cd20853    32 CCWCQRTVHDD-CLA--KLPKECDLGAFRNFIVPP 63
C1_DGK_rpt2 cd20805
second protein kinase C conserved region 1 (C1 domain) found in the diacylglycerol kinase ...
 351-414 4.65e-04

second protein kinase C conserved region 1 (C1 domain) found in the diacylglycerol kinase family; The diacylglycerol kinase (DGK, EC 2.7.1.107) family of enzymes plays critical roles in lipid signaling pathways by converting diacylglycerol to phosphatidic acid, thereby downregulating signaling by the former and upregulating signaling by the latter second messenger. Ten DGK family isozymes have been identified to date, which possess different interaction motifs imparting distinct temporal and spatial control of DGK activity to each isozyme. They have been classified into five types (I-V), according to domain architecture and some common features. All DGK isozymes, except for DGKtheta, contain two copies of the C1 domain. This model corresponds to the second one. DGKtheta harbors three C1 domains. Its third C1 domain is included here. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410355  Cd Length: 55  Bit Score: 38.97  E-value: 4.65e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1572047467 351 HHWVHKWRH-EGRCNTCAKSFQQKMFFQGKekketiavTCSWCKESYHLKnCFARDKLEErCNRG 414
Cdd:cd20805     1 HHWVEGNLPsGAKCSVCGKKCGSSFGLAGY--------RCSWCKRTVHSE-CIDKLGPEE-CDLG 55
PRK13057 PRK13057
lipid kinase;
469-565 1.02e-03

lipid kinase;


Pssm-ID: 183857 [Multi-domain]  Cd Length: 287  Bit Score: 42.21  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047467 469 LVFVNPKSggNKGSKALHTLCWLLnprQVFDITSLKGPKFGLEMFRKVVTQL-----RILVCGGDGTVGWVLSTL--DNL 541
Cdd:PRK13057    1 LLLVNRHA--RSGRAALAAARAAL---EAAGLELVEPPAEDPDDLSEVIEAYadgvdLVIVGGGDGTLNAAAPALveTGL 75

                          90       100
                  ....*....|....*....|....
gi 1572047467 542 nwpaypPMAIMPLGTGNDLARCMG 565
Cdd:PRK13057   76 ------PLGILPLGTANDLARTLG 93
PRK13055 PRK13055
putative lipid kinase; Reviewed
 522-562 1.49e-03

putative lipid kinase; Reviewed


Pssm-ID: 237282 [Multi-domain]  Cd Length: 334  Bit Score: 41.90  E-value: 1.49e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1572047467 522 ILVCGGDGTVGWVLSTLDNLNWPayPPMAIMPLGTGNDLAR 562
Cdd:PRK13055   63 IIAAGGDGTINEVVNGIAPLEKR--PKMAIIPAGTTNDYAR 101
 
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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