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Conserved domains on  [gi|1811472993|ref|XP_032364597|]
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LOW QUALITY PROTEIN: diacylglycerol kinase zeta-like, partial [Etheostoma spectabile]

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 ...
 412-569 3.69e-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: 240.31  E-value: 3.69e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811472993  412 VFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGTAFSDFLMGSSKDLSKHIKVVCDGTDLTSKvqdLKLQCL 491
Cdd:smart00045   1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLP---NSLEGI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811472993  492 VFLNIPRYCAGTTPWGNPGEH-HDFEPQRHDDGYIEVIGFTMTSLA--TLQVGGHGERLNQCREV--TLTTTKPLPVQVD 566
Cdd:smart00045  78 AVLNIPSYGGGTNLWGTTDKEdLNFSKQSHDDGLLEVVGLTGAMHMaqIRQVGLAGRRIAQCSEVriTIKTSKTIPMQVD 157


                   ...
gi 1811472993  567 GEP 569
Cdd:smart00045 158 GEP 160
C1_DGKzeta_rpt2 cd20895
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta ...
 136-210 1.46e-49

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: 166.80  E-value: 1.46e-49
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1811472993 136 VRHHWVHRRRQEGKCKQCGKGFQQKFAFHSKEIVAISCSWCKQAYHNKVSCFMLQQIEEACPIGAHAALIVPPTW 210
Cdd:cd20895     1 VRHHWVHRRRQEGKCRQCGKGFQQKFAFHSKEIVAISCSWCKQAYHSKVSCFMLQQIEEPCSLGAHAAVIVPPTW 75
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 264-385 8.04e-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: 166.32  E-value: 8.04e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811472993  264 LVFVNPKSGGNQGNKILQSFMWYLNPRQVFDLSQGGPHEGLELYRKVHNLS-ILACGGDGTVGWILSCLDELALNPQ-PP 341
Cdd:smart00046   1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVPDFNrVLVCGGDGTVGWVLNALDKRELPLPePP 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1811472993  342 VAVLPLGTGNDLARTLNWGGGFTDEPLSKILSHVEDGTVVQLDR 385
Cdd:smart00046  81 VAVLPLGTGNDLARSLGWGGGYDGEKLLKTLRDALESDTVKLDR 124
C1 super family cl00040
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ...
 32-126 4.40e-39

protein kinase C conserved region 1 (C1 domain) superfamily; 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 the motif HX12CX2CXnCX2CX4HX2CX7C, where C and H are cysteine and histidine, respectively; X represents other residues; and n is either 13 or 14. C1 has a globular fold with two separate Zn(2+)-binding sites. It was originally discovered as lipid-binding modules in protein kinase C (PKC) isoforms. C1 domains that bind and respond to phorbol esters (PE) and diacylglycerol (DAG) are referred to as typical, and those that do not respond to PE and DAG are deemed atypical. A C1 domain may also be referred to as PKC or non-PKC C1, based on the parent protein's activity. Most C1 domain-containing non-PKC proteins act as lipid kinases and scaffolds, except PKD which acts as a protein kinase. PKC C1 domains play roles in membrane translocation and activation of the enzyme.


The actual alignment was detected with superfamily member cd20849:

Pssm-ID: 412127  Cd Length: 74  Bit Score: 138.15  E-value: 4.40e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811472993  32 DWTDSAVYGDHIWFETNVSGDYCYVGETTLYCQALQKSVSRRKCAACKIVAHTICIEQLEKfpssrailldatlplndpn 111
Cdd:cd20849     1 DWSESAVYGEHIWFETNVSGDFCYVGEQNCVAKQLQKSVSRKKCAACKIVVHTPCIEQLEK------------------- 61

                          90
                  ....*....|....*
gi 1811472993 112 frINFRCKPSFRESG 126
Cdd:cd20849    62 --INFRCKPSFRESG 74
 
Name Accession Description Interval E-value
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 412-569 3.69e-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: 240.31  E-value: 3.69e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811472993  412 VFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGTAFSDFLMGSSKDLSKHIKVVCDGTDLTSKvqdLKLQCL 491
Cdd:smart00045   1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLP---NSLEGI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811472993  492 VFLNIPRYCAGTTPWGNPGEH-HDFEPQRHDDGYIEVIGFTMTSLA--TLQVGGHGERLNQCREV--TLTTTKPLPVQVD 566
Cdd:smart00045  78 AVLNIPSYGGGTNLWGTTDKEdLNFSKQSHDDGLLEVVGLTGAMHMaqIRQVGLAGRRIAQCSEVriTIKTSKTIPMQVD 157


                   ...
gi 1811472993  567 GEP 569
Cdd:smart00045 158 GEP 160
DAGK_acc pfam00609
Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts ...
 412-569 8.02e-69

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: 220.94  E-value: 8.02e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811472993 412 VFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGTAFSDFLMGSSKDLSKHIKVVCDGTDLTSKvqdLKLQCL 491
Cdd:pfam00609   1 VMNNYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDMFQRSCKNLIEKVELEVDGKDLPLP---KSLEGI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811472993 492 VFLNIPRYCAGTTPWGNPGEHHD-FEPQRHDDGYIEVIGFT-MTSLATLQVGGHGE-RLNQCREVTLTTTKPLPVQVDGE 568
Cdd:pfam00609  78 VVLNIPSYAGGTDLWGNSKEDGLgFAPQSVDDGLLEVVGLTgALHLGQVQVGLGSAkRIAQGGPIRITTKKKIPMQVDGE 157


                  .
gi 1811472993 569 P 569
Cdd:pfam00609 158 P 158
C1_DGKzeta_rpt2 cd20895
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta ...
 136-210 1.46e-49

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: 166.80  E-value: 1.46e-49
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1811472993 136 VRHHWVHRRRQEGKCKQCGKGFQQKFAFHSKEIVAISCSWCKQAYHNKVSCFMLQQIEEACPIGAHAALIVPPTW 210
Cdd:cd20895     1 VRHHWVHRRRQEGKCRQCGKGFQQKFAFHSKEIVAISCSWCKQAYHSKVSCFMLQQIEEPCSLGAHAAVIVPPTW 75
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 264-385 8.04e-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: 166.32  E-value: 8.04e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811472993  264 LVFVNPKSGGNQGNKILQSFMWYLNPRQVFDLSQGGPHEGLELYRKVHNLS-ILACGGDGTVGWILSCLDELALNPQ-PP 341
Cdd:smart00046   1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVPDFNrVLVCGGDGTVGWVLNALDKRELPLPePP 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1811472993  342 VAVLPLGTGNDLARTLNWGGGFTDEPLSKILSHVEDGTVVQLDR 385
Cdd:smart00046  81 VAVLPLGTGNDLARSLGWGGGYDGEKLLKTLRDALESDTVKLDR 124
C1_DGKzeta_rpt1 cd20849
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta (DAG ...
 32-126 4.40e-39

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: 138.15  E-value: 4.40e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811472993  32 DWTDSAVYGDHIWFETNVSGDYCYVGETTLYCQALQKSVSRRKCAACKIVAHTICIEQLEKfpssrailldatlplndpn 111
Cdd:cd20849     1 DWSESAVYGEHIWFETNVSGDFCYVGEQNCVAKQLQKSVSRKKCAACKIVVHTPCIEQLEK------------------- 61

                          90
                  ....*....|....*
gi 1811472993 112 frINFRCKPSFRESG 126
Cdd:cd20849    62 --INFRCKPSFRESG 74
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 262-374 2.63e-35

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: 129.24  E-value: 2.63e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811472993 262 PLLVFVNPKSGGNQGNKILQSFMWYLNPRQV-FDLSQ-GGPHEGLELYRKVHNLS---ILACGGDGTVGWILSCLDELAl 336
Cdd:pfam00781   1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVeVELVLtEGPGDALELAREAAEDGydrIVVAGGDGTVNEVLNGLAGLA- 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1811472993 337 nPQPPVAVLPLGTGNDLARTLNWGGGFtDEPLSKILSH 374
Cdd:pfam00781  80 -TRPPLGIIPLGTGNDFARALGIPGDP-EEALEAILKG 115
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 260-585 9.07e-27

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


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 110.71  E-value: 9.07e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811472993 260 MKPLLVFVNPKSGGNQGNKILQSFMWYLNpRQVFDLSQ---GGPHEGLELYRKVHNLS---ILACGGDGTVGWILSCLde 333
Cdd:COG1597     2 MMRALLIVNPASGRGRAARLLERLVAALR-AAGLEVEVletESPGDATELAREAAAEGadlVVAAGGDGTVNEVANGL-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811472993 334 laLNPQPPVAVLPLGTGNDLARTLNwgggfTDEPLSKILSHVEDGTVVQLDrwnlqvepnhsaGAETDEQqtdklpldVF 413
Cdd:COG1597    79 --AGTGPPLGILPLGTGNDFARALG-----IPLDPEAALEALLTGRTRRID------------LGRVNGR--------YF 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811472993 414 NNYFSLGFDAHVTLEFHESReanpekfnSRFRNKMFYAGTAFSdfLMGSSKdlSKHIKVVCDGTDLTSKVqdlkLQCLVF 493
Cdd:COG1597   132 LNVAGIGFDAEVVERANRAL--------KRRLGKLAYVLAALR--ALLRYR--PFRLRIELDGEEIEGEA----LLVAVG 195

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811472993 494 lNIPRYcagttpwgnpGEHHDFEPQ-RHDDGYIEVIGFT-------MTSLATLQVGGHGERLN----QCREVTLTTTKPL 561
Cdd:COG1597   196 -NGPYY----------GGGLRLAPDaSLDDGLLDVVVVRplsrlrlLRLLPRLLRGRHLRHPGvryfRAREVEIESDRPL 264

                         330       340
                  ....*....|....*....|....
gi 1811472993 562 PVQVDGEPCR*APSViHISLRNQA 585
Cdd:COG1597   265 PVQLDGEPLGLATPL-EFEVLPGA 287
PRK12361 PRK12361
hypothetical protein; Provisional
 261-378 1.57e-07

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 54.24  E-value: 1.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811472993 261 KPLLVFVNPKSGGNQGNKILQSFMWYLNPRqvFDLS--QGGPHEGLELYRKVHNLS----ILACGGDGTVGWILSCLdel 334
Cdd:PRK12361  243 KRAWLIANPVSGGGKWQEYGEQIQRELKAY--FDLTvkLTTPEISAEALAKQARKAgadiVIACGGDGTVTEVASEL--- 317

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1811472993 335 aLNPQPPVAVLPLGTGNDLARTLnWGGGFTDEPLSKILSHVEDG 378
Cdd:PRK12361  318 -VNTDITLGIIPLGTANALSHAL-FGLGSKLIPVEQACDNIIQG 359
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
 138-196 3.65e-07

Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the Protein kinase C conserved region 1 (C1) domain.


Pssm-ID: 395079  Cd Length: 53  Bit Score: 47.05  E-value: 3.65e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811472993 138 HHWVHRR-RQEGKCKQCGKGFqqkfafHSKEIVAISCSWCKQAYHNKvsCFMLQQIEEAC 196
Cdd:pfam00130   1 HHFVHRNfKQPTFCDHCGEFL------WGLGKQGLKCSWCKLNVHKR--CHEKVPPECGC 52
PRK13057 PRK13057
lipid kinase;
264-585 8.06e-06

lipid kinase;


Pssm-ID: 183857 [Multi-domain]  Cd Length: 287  Bit Score: 47.99  E-value: 8.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811472993 264 LVFVNPKSggNQGNKILQSFMWYLNPRQvFDLSQGGPHEGLEL------YRKVHNLSILAcGGDGTVGWILSCLDELALn 337
Cdd:PRK13057    1 LLLVNRHA--RSGRAALAAARAALEAAG-LELVEPPAEDPDDLsevieaYADGVDLVIVG-GGDGTLNAAAPALVETGL- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811472993 338 pqpPVAVLPLGTGNDLARTLnwggGFTDEPlskilshVEDGTVVqldrwnlqvepnhSAGAETdeqqtdklPLDV----- 412
Cdd:PRK13057   76 ---PLGILPLGTANDLARTL----GIPLDL-------EAAARVI-------------ATGQVR--------RIDLgwvng 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811472993 413 --FNNYFSLGFDAHVTLEFHesreanpEKFNSRFrNKMFYAGTAFSdfLMGSSKDLSKHIkvVCDGTDLTSKVqdlkLQC 490
Cdd:PRK13057  121 hyFFNVASLGLSAELARRLT-------KELKRRW-GTLGYAIAALR--VLRRSRPFTAEI--EHDGRTERVKT----LQV 184

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811472993 491 LVflniprycagttpwGNpGEHHD-----FEPQRHDDGYIEVIGFTMTSLATL-------QVGGHGERLN----QCREVT 554
Cdd:PRK13057  185 AV--------------GN-GRYYGggmtvAHDATIDDGRLDLYSLEVAHWWRLlallpalRRGRHGEWPDvrafRTTELE 249

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1811472993 555 LTTTKPLPVQVDGEPCR*APSviHISLRNQA 585
Cdd:PRK13057  250 LRTRKPRPINTDGELTTYTPA--HFRVLPKA 278
TIGR00147 TIGR00147
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ...
 260-357 7.22e-04

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: 42.11  E-value: 7.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811472993 260 MKPLLVFVNPKSGGNQGNKILQSFMWYLNPRQVFDLSQGGPHEGLELY-----RKVHNLSILACGGDGTVGWILSCLdeL 334
Cdd:TIGR00147   1 MAEAPAILNPTAGKSNDNKPLREVIMLLREEGMEIHVRVTWEKGDAARyveeaRKFGVDTVIAGGGDGTINEVVNAL--I 78

                          90       100
                  ....*....|....*....|...
gi 1811472993 335 ALNPQPPVAVLPLGTGNDLARTL 357
Cdd:TIGR00147  79 QLDDIPALGILPLGTANDFARSL 101
 
Name Accession Description Interval E-value
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 412-569 3.69e-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: 240.31  E-value: 3.69e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811472993  412 VFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGTAFSDFLMGSSKDLSKHIKVVCDGTDLTSKvqdLKLQCL 491
Cdd:smart00045   1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLP---NSLEGI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811472993  492 VFLNIPRYCAGTTPWGNPGEH-HDFEPQRHDDGYIEVIGFTMTSLA--TLQVGGHGERLNQCREV--TLTTTKPLPVQVD 566
Cdd:smart00045  78 AVLNIPSYGGGTNLWGTTDKEdLNFSKQSHDDGLLEVVGLTGAMHMaqIRQVGLAGRRIAQCSEVriTIKTSKTIPMQVD 157


                   ...
gi 1811472993  567 GEP 569
Cdd:smart00045 158 GEP 160
DAGK_acc pfam00609
Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts ...
 412-569 8.02e-69

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: 220.94  E-value: 8.02e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811472993 412 VFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGTAFSDFLMGSSKDLSKHIKVVCDGTDLTSKvqdLKLQCL 491
Cdd:pfam00609   1 VMNNYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDMFQRSCKNLIEKVELEVDGKDLPLP---KSLEGI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811472993 492 VFLNIPRYCAGTTPWGNPGEHHD-FEPQRHDDGYIEVIGFT-MTSLATLQVGGHGE-RLNQCREVTLTTTKPLPVQVDGE 568
Cdd:pfam00609  78 VVLNIPSYAGGTDLWGNSKEDGLgFAPQSVDDGLLEVVGLTgALHLGQVQVGLGSAkRIAQGGPIRITTKKKIPMQVDGE 157


                  .
gi 1811472993 569 P 569
Cdd:pfam00609 158 P 158
C1_DGKzeta_rpt2 cd20895
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta ...
 136-210 1.46e-49

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: 166.80  E-value: 1.46e-49
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1811472993 136 VRHHWVHRRRQEGKCKQCGKGFQQKFAFHSKEIVAISCSWCKQAYHNKVSCFMLQQIEEACPIGAHAALIVPPTW 210
Cdd:cd20895     1 VRHHWVHRRRQEGKCRQCGKGFQQKFAFHSKEIVAISCSWCKQAYHSKVSCFMLQQIEEPCSLGAHAAVIVPPTW 75
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 264-385 8.04e-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: 166.32  E-value: 8.04e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811472993  264 LVFVNPKSGGNQGNKILQSFMWYLNPRQVFDLSQGGPHEGLELYRKVHNLS-ILACGGDGTVGWILSCLDELALNPQ-PP 341
Cdd:smart00046   1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVPDFNrVLVCGGDGTVGWVLNALDKRELPLPePP 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1811472993  342 VAVLPLGTGNDLARTLNWGGGFTDEPLSKILSHVEDGTVVQLDR 385
Cdd:smart00046  81 VAVLPLGTGNDLARSLGWGGGYDGEKLLKTLRDALESDTVKLDR 124
C1_DGKiota_rpt2 cd20896
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase iota ...
 136-210 9.14e-47

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: 159.10  E-value: 9.14e-47
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1811472993 136 VRHHWVHRRRQEGKCKQCGKGFQQKFAFHSKEIVAISCSWCKQAYHNKVSCFMLQQIEEACPIGAHAALIVPPTW 210
Cdd:cd20896     1 VRHHWVHRRRQEGKCKQCGKGFQQKFSFHSKEIVAISCSWCKQAFHNKVTCFMLHHIEEPCSLGAHAAVIVPPTW 75
C1_DGK_typeIV_rpt2 cd20855
second protein kinase C conserved region 1 (C1 domain) found in type IV diacylglycerol kinases; ...
 138-199 2.73e-39

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: 138.25  E-value: 2.73e-39
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1811472993 138 HHWVHRRRQEGKCKQCGKGFQQKFAFHSKEIVAISCSWCKQAYHNKVSCFMLQQIEEACPIG 199
Cdd:cd20855     1 HHWVHRRKQEGKCKQCGKSFQQKLSFSSKEIVAISCSWCKEAYHNKDSCFNMKKIEEPCNLG 62
C1_DGKzeta_rpt1 cd20849
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta (DAG ...
 32-126 4.40e-39

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: 138.15  E-value: 4.40e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811472993  32 DWTDSAVYGDHIWFETNVSGDYCYVGETTLYCQALQKSVSRRKCAACKIVAHTICIEQLEKfpssrailldatlplndpn 111
Cdd:cd20849     1 DWSESAVYGEHIWFETNVSGDFCYVGEQNCVAKQLQKSVSRKKCAACKIVVHTPCIEQLEK------------------- 61

                          90
                  ....*....|....*
gi 1811472993 112 frINFRCKPSFRESG 126
Cdd:cd20849    62 --INFRCKPSFRESG 74
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 262-374 2.63e-35

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: 129.24  E-value: 2.63e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811472993 262 PLLVFVNPKSGGNQGNKILQSFMWYLNPRQV-FDLSQ-GGPHEGLELYRKVHNLS---ILACGGDGTVGWILSCLDELAl 336
Cdd:pfam00781   1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVeVELVLtEGPGDALELAREAAEDGydrIVVAGGDGTVNEVLNGLAGLA- 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1811472993 337 nPQPPVAVLPLGTGNDLARTLNWGGGFtDEPLSKILSH 374
Cdd:pfam00781  80 -TRPPLGIIPLGTGNDFARALGIPGDP-EEALEAILKG 115
C1_DGKiota_rpt1 cd20850
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase iota (DAG ...
 32-126 1.28e-30

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: 114.35  E-value: 1.28e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811472993  32 DWTDSAVYGDHIWFETNVSGDYCYVGETTlyCQA-LQKSVSRRKCAACKIVAHTICIEQLEKfpssrailldatlplndp 110
Cdd:cd20850     1 DWSENAVNGEHLWLETNVSGDLCYLGEEN--CQVkFAKSALRRKCAACKIVVHTACIEQLEK------------------ 60

                          90
                  ....*....|....*.
gi 1811472993 111 nfrINFRCKPSFRESG 126
Cdd:cd20850    61 ---INFRCKPTFREGG 73
C1_DGK_typeIV_rpt1 cd20802
first protein kinase C conserved region 1 (C1 domain) found in type IV diacylglycerol kinases; ...
 37-124 4.86e-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: 103.91  E-value: 4.86e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811472993  37 AVYGDHIWFETNVSGDYCYVGETtlYCQalqKSVSRRKCAACKIVAHTICIEQLEkfpssrailldatlplndpnfRINF 116
Cdd:cd20802     1 AVNGEHLWTDTSASGDLCYVGEQ--DCL---KSGSRKKCSACKIVVHTGCIPQLE---------------------KINF 54


                  ....*...
gi 1811472993 117 RCKPSFRE 124
Cdd:cd20802    55 KCKPTFRE 62
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 260-585 9.07e-27

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


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 110.71  E-value: 9.07e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811472993 260 MKPLLVFVNPKSGGNQGNKILQSFMWYLNpRQVFDLSQ---GGPHEGLELYRKVHNLS---ILACGGDGTVGWILSCLde 333
Cdd:COG1597     2 MMRALLIVNPASGRGRAARLLERLVAALR-AAGLEVEVletESPGDATELAREAAAEGadlVVAAGGDGTVNEVANGL-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811472993 334 laLNPQPPVAVLPLGTGNDLARTLNwgggfTDEPLSKILSHVEDGTVVQLDrwnlqvepnhsaGAETDEQqtdklpldVF 413
Cdd:COG1597    79 --AGTGPPLGILPLGTGNDFARALG-----IPLDPEAALEALLTGRTRRID------------LGRVNGR--------YF 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811472993 414 NNYFSLGFDAHVTLEFHESReanpekfnSRFRNKMFYAGTAFSdfLMGSSKdlSKHIKVVCDGTDLTSKVqdlkLQCLVF 493
Cdd:COG1597   132 LNVAGIGFDAEVVERANRAL--------KRRLGKLAYVLAALR--ALLRYR--PFRLRIELDGEEIEGEA----LLVAVG 195

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811472993 494 lNIPRYcagttpwgnpGEHHDFEPQ-RHDDGYIEVIGFT-------MTSLATLQVGGHGERLN----QCREVTLTTTKPL 561
Cdd:COG1597   196 -NGPYY----------GGGLRLAPDaSLDDGLLDVVVVRplsrlrlLRLLPRLLRGRHLRHPGvryfRAREVEIESDRPL 264

                         330       340
                  ....*....|....*....|....
gi 1811472993 562 PVQVDGEPCR*APSViHISLRNQA 585
Cdd:COG1597   265 PVQLDGEPLGLATPL-EFEVLPGA 287
C1_DGK_rpt2 cd20805
second protein kinase C conserved region 1 (C1 domain) found in the diacylglycerol kinase ...
 138-194 1.83e-08

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: 50.91  E-value: 1.83e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1811472993 138 HHWVHRRRQ-EGKCKQCGKGFQQKFAFHSKeivaiSCSWCKQAYHNkvSCFMLQQIEE 194
Cdd:cd20805     1 HHWVEGNLPsGAKCSVCGKKCGSSFGLAGY-----RCSWCKRTVHS--ECIDKLGPEE 51
PRK12361 PRK12361
hypothetical protein; Provisional
 261-378 1.57e-07

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 54.24  E-value: 1.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811472993 261 KPLLVFVNPKSGGNQGNKILQSFMWYLNPRqvFDLS--QGGPHEGLELYRKVHNLS----ILACGGDGTVGWILSCLdel 334
Cdd:PRK12361  243 KRAWLIANPVSGGGKWQEYGEQIQRELKAY--FDLTvkLTTPEISAEALAKQARKAgadiVIACGGDGTVTEVASEL--- 317

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1811472993 335 aLNPQPPVAVLPLGTGNDLARTLnWGGGFTDEPLSKILSHVEDG 378
Cdd:PRK12361  318 -VNTDITLGIIPLGTANALSHAL-FGLGSKLIPVEQACDNIIQG 359
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
 138-196 3.65e-07

Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the Protein kinase C conserved region 1 (C1) domain.


Pssm-ID: 395079  Cd Length: 53  Bit Score: 47.05  E-value: 3.65e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811472993 138 HHWVHRR-RQEGKCKQCGKGFqqkfafHSKEIVAISCSWCKQAYHNKvsCFMLQQIEEAC 196
Cdd:pfam00130   1 HHFVHRNfKQPTFCDHCGEFL------WGLGKQGLKCSWCKLNVHKR--CHEKVPPECGC 52
PRK13059 PRK13059
putative lipid kinase; Reviewed
 260-358 6.90e-06

putative lipid kinase; Reviewed


Pssm-ID: 183858  Cd Length: 295  Bit Score: 48.49  E-value: 6.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811472993 260 MKPLLVFVNPKSGGN----QGNKILQSFMWYLNPRQVFDLSQGGP-HEGLELYRKVHNLsILACGGDGTVGWILSCLDEL 334
Cdd:PRK13059    1 MKKVKFIYNPYSGENaiisELDKVIRIHQEKGYLVVPYRISLEYDlKNAFKDIDESYKY-ILIAGGDGTVDNVVNAMKKL 79

                          90       100
                  ....*....|....*....|....
gi 1811472993 335 ALNPqpPVAVLPLGTGNDLARTLN 358
Cdd:PRK13059   80 NIDL--PIGILPVGTANDFAKFLG 101
PRK13057 PRK13057
lipid kinase;
264-585 8.06e-06

lipid kinase;


Pssm-ID: 183857 [Multi-domain]  Cd Length: 287  Bit Score: 47.99  E-value: 8.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811472993 264 LVFVNPKSggNQGNKILQSFMWYLNPRQvFDLSQGGPHEGLEL------YRKVHNLSILAcGGDGTVGWILSCLDELALn 337
Cdd:PRK13057    1 LLLVNRHA--RSGRAALAAARAALEAAG-LELVEPPAEDPDDLsevieaYADGVDLVIVG-GGDGTLNAAAPALVETGL- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811472993 338 pqpPVAVLPLGTGNDLARTLnwggGFTDEPlskilshVEDGTVVqldrwnlqvepnhSAGAETdeqqtdklPLDV----- 412
Cdd:PRK13057   76 ---PLGILPLGTANDLARTL----GIPLDL-------EAAARVI-------------ATGQVR--------RIDLgwvng 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811472993 413 --FNNYFSLGFDAHVTLEFHesreanpEKFNSRFrNKMFYAGTAFSdfLMGSSKDLSKHIkvVCDGTDLTSKVqdlkLQC 490
Cdd:PRK13057  121 hyFFNVASLGLSAELARRLT-------KELKRRW-GTLGYAIAALR--VLRRSRPFTAEI--EHDGRTERVKT----LQV 184

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811472993 491 LVflniprycagttpwGNpGEHHD-----FEPQRHDDGYIEVIGFTMTSLATL-------QVGGHGERLN----QCREVT 554
Cdd:PRK13057  185 AV--------------GN-GRYYGggmtvAHDATIDDGRLDLYSLEVAHWWRLlallpalRRGRHGEWPDvrafRTTELE 249

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1811472993 555 LTTTKPLPVQVDGEPCR*APSviHISLRNQA 585
Cdd:PRK13057  250 LRTRKPRPINTDGELTTYTPA--HFRVLPKA 278
PRK13054 PRK13054
lipid kinase; Reviewed
 315-355 7.35e-05

lipid kinase; Reviewed


Pssm-ID: 237281 [Multi-domain]  Cd Length: 300  Bit Score: 45.25  E-value: 7.35e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1811472993 315 ILACGGDGTVGWILSCLDELALNPQPPVAVLPLGTGNDLAR 355
Cdd:PRK13054   60 VIAGGGDGTINEVATALAQLEGDARPALGILPLGTANDFAT 100
PRK13055 PRK13055
putative lipid kinase; Reviewed
 315-358 6.66e-04

putative lipid kinase; Reviewed


Pssm-ID: 237282 [Multi-domain]  Cd Length: 334  Bit Score: 42.28  E-value: 6.66e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1811472993 315 ILACGGDGTVGWILSCLDELALNPQppVAVLPLGTGNDLARTLN 358
Cdd:PRK13055   63 IIAAGGDGTINEVVNGIAPLEKRPK--MAIIPAGTTNDYARALK 104
TIGR00147 TIGR00147
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ...
 260-357 7.22e-04

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: 42.11  E-value: 7.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811472993 260 MKPLLVFVNPKSGGNQGNKILQSFMWYLNPRQVFDLSQGGPHEGLELY-----RKVHNLSILACGGDGTVGWILSCLdeL 334
Cdd:TIGR00147   1 MAEAPAILNPTAGKSNDNKPLREVIMLLREEGMEIHVRVTWEKGDAARyveeaRKFGVDTVIAGGGDGTINEVVNAL--I 78

                          90       100
                  ....*....|....*....|...
gi 1811472993 335 ALNPQPPVAVLPLGTGNDLARTL 357
Cdd:TIGR00147  79 QLDDIPALGILPLGTANDFARSL 101
C1_DGKepsilon_typeIII_rpt2 cd20853
second protein kinase C conserved region 1 (C1 domain) found in type III diacylglycerol kinase, ...
 138-208 5.97e-03

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: 35.72  E-value: 5.97e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1811472993 138 HHWVHrrrqeG------KCKQCGK--GFQQKFAFHSkeivaisCSWCKQAYHNKvsCfmLQQIEEACPIGAHAALIVPP 208
Cdd:cd20853     1 HHWVR-----GnlplcsVCCVCNEqcGNQPGLCDYR-------CCWCQRTVHDD--C--LAKLPKECDLGAFRNFIVPP 63
 
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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