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Conserved domains on  [gi|1039775254|ref|XP_017177119|]
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diacylglycerol kinase iota isoform X10 [Mus musculus]

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 ...
 562-719 3.48e-74

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: 241.09  E-value: 3.48e-74
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775254   562 VFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGAAFSDFLQRSSRDLSKHVKVVCDGTDLTPKIqdlKFQCI 641
Cdd:smart00045    1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLPN---SLEGI 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775254   642 VFLNIPRYCAGTMPWGNPGDH-HDFEPQRHDDGYIEVIGFTMASLAA--LQVGGHGERLHQCREV--MLLTYKSIPMQVD 716
Cdd:smart00045   78 AVLNIPSYGGGTNLWGTTDKEdLNFSKQSHDDGLLEVVGLTGAMHMAqiRQVGLAGRRIAQCSEVriTIKTSKTIPMQVD 157


                    ...
gi 1039775254   717 GEP 719
Cdd:smart00045  158 GEP 160
C1_DGKiota_rpt2 cd20896
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase iota ...
 244-318 8.00e-52

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: 175.66  E-value: 8.00e-52
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039775254  244 VRHHWVHRRRQEGKCKQCGKGFQQKFSFHSKEIVAISCSWCKQAFHNKVTCFMLHHIEEPCSLGAHAAVIVPPTW 318
Cdd:cd20896      1 VRHHWVHRRRQEGKCKQCGKGFQQKFSFHSKEIVAISCSWCKQAFHNKVTCFMLHHIEEPCSLGAHAAVIVPPTW 75
C1_DGKiota_rpt1 cd20850
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase iota (DAG ...
 163-235 4.15e-51

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: 173.67  E-value: 4.15e-51
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039775254  163 DWSENAVNGEHLWLETNVSGDLCYLGEENCQVRFAKSALRRKCAVCKIVVHTACIEQLEKINFRCKPTFREGG 235
Cdd:cd20850      1 DWSENAVNGEHLWLETNVSGDLCYLGEENCQVKFAKSALRRKCAACKIVVHTACIEQLEKINFRCKPTFREGG 73
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 414-535 5.16e-47

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: 164.01  E-value: 5.16e-47
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775254   414 LVFVNPKSGGNQGTKVLQMFMWYLNPRQVFDLSQEGPKDALEMYRKVPN-LRILACGGDGTVGWILSILDELQL-SPQPP 491
Cdd:smart00046    1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVPDfNRVLVCGGDGTVGWVLNALDKRELpLPEPP 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 1039775254   492 VGVLPLGTGNDLARTLNWGGGYTDEPVSKILCQVEDGTIVQLDR 535
Cdd:smart00046   81 VAVLPLGTGNDLARSLGWGGGYDGEKLLKTLRDALESDTVKLDR 124
 
Name Accession Description Interval E-value
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 562-719 3.48e-74

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: 241.09  E-value: 3.48e-74
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775254   562 VFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGAAFSDFLQRSSRDLSKHVKVVCDGTDLTPKIqdlKFQCI 641
Cdd:smart00045    1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLPN---SLEGI 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775254   642 VFLNIPRYCAGTMPWGNPGDH-HDFEPQRHDDGYIEVIGFTMASLAA--LQVGGHGERLHQCREV--MLLTYKSIPMQVD 716
Cdd:smart00045   78 AVLNIPSYGGGTNLWGTTDKEdLNFSKQSHDDGLLEVVGLTGAMHMAqiRQVGLAGRRIAQCSEVriTIKTSKTIPMQVD 157


                    ...
gi 1039775254   717 GEP 719
Cdd:smart00045  158 GEP 160
DAGK_acc pfam00609
Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts ...
 562-719 6.92e-68

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: 224.02  E-value: 6.92e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775254  562 VFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGAAFSDFLQRSSRDLSKHVKVVCDGTDLTPKiqdLKFQCI 641
Cdd:pfam00609    1 VMNNYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDMFQRSCKNLIEKVELEVDGKDLPLP---KSLEGI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775254  642 VFLNIPRYCAGTMPWGNPGDHHD-FEPQRHDDGYIEVIGFT-MASLAALQVGGHGE-RLHQCREVMLLTYKSIPMQVDGE 718
Cdd:pfam00609   78 VVLNIPSYAGGTDLWGNSKEDGLgFAPQSVDDGLLEVVGLTgALHLGQVQVGLGSAkRIAQGGPIRITTKKKIPMQVDGE 157


                   .
gi 1039775254  719 P 719
Cdd:pfam00609  158 P 158
C1_DGKiota_rpt2 cd20896
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase iota ...
 244-318 8.00e-52

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: 175.66  E-value: 8.00e-52
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039775254  244 VRHHWVHRRRQEGKCKQCGKGFQQKFSFHSKEIVAISCSWCKQAFHNKVTCFMLHHIEEPCSLGAHAAVIVPPTW 318
Cdd:cd20896      1 VRHHWVHRRRQEGKCKQCGKGFQQKFSFHSKEIVAISCSWCKQAFHNKVTCFMLHHIEEPCSLGAHAAVIVPPTW 75
C1_DGKiota_rpt1 cd20850
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase iota (DAG ...
 163-235 4.15e-51

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: 173.67  E-value: 4.15e-51
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039775254  163 DWSENAVNGEHLWLETNVSGDLCYLGEENCQVRFAKSALRRKCAVCKIVVHTACIEQLEKINFRCKPTFREGG 235
Cdd:cd20850      1 DWSENAVNGEHLWLETNVSGDLCYLGEENCQVKFAKSALRRKCAACKIVVHTACIEQLEKINFRCKPTFREGG 73
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 414-535 5.16e-47

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: 164.01  E-value: 5.16e-47
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775254   414 LVFVNPKSGGNQGTKVLQMFMWYLNPRQVFDLSQEGPKDALEMYRKVPN-LRILACGGDGTVGWILSILDELQL-SPQPP 491
Cdd:smart00046    1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVPDfNRVLVCGGDGTVGWVLNALDKRELpLPEPP 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 1039775254   492 VGVLPLGTGNDLARTLNWGGGYTDEPVSKILCQVEDGTIVQLDR 535
Cdd:smart00046   81 VAVLPLGTGNDLARSLGWGGGYDGEKLLKTLRDALESDTVKLDR 124
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 412-511 3.83e-34

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: 126.93  E-value: 3.83e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775254  412 PLLVFVNPKSGGNQGTKVLQMFMWYLNPRQV-FDLSQ-EGPKDALEMYRKVPNL---RILACGGDGTVGWILSILDELql 486
Cdd:pfam00781    1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVeVELVLtEGPGDALELAREAAEDgydRIVVAGGDGTVNEVLNGLAGL-- 78

                           90       100
                   ....*....|....*....|....*
gi 1039775254  487 SPQPPVGVLPLGTGNDLARTLNWGG 511
Cdd:pfam00781   79 ATRPPLGIIPLGTGNDFARALGIPG 103
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 410-729 2.01e-26

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


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 110.33  E-value: 2.01e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775254  410 MKPLLVFVNPKSGGNQGTKVLQMFMWYLNpRQVFDLSQ---EGPKDALEMYRKVPNL---RILACGGDGTVGWILSILde 483
Cdd:COG1597      2 MMRALLIVNPASGRGRAARLLERLVAALR-AAGLEVEVletESPGDATELAREAAAEgadLVVAAGGDGTVNEVANGL-- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775254  484 lqLSPQPPVGVLPLGTGNDLARTLNwgggyTDEPVSKILCQVEDGTIVQLDrwnlhvernpdlppeeledgVCKLPLNVF 563
Cdd:COG1597     79 --AGTGPPLGILPLGTGNDFARALG-----IPLDPEAALEALLTGRTRRID--------------------LGRVNGRYF 131

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775254  564 NNYFSLGFDAHVTLEFHESReanpekfnSRFRNKMFYAGAAFSDFLQRSSRdlskHVKVVCDGTDLTpkiqdLKFQCIVF 643
Cdd:COG1597    132 LNVAGIGFDAEVVERANRAL--------KRRLGKLAYVLAALRALLRYRPF----RLRIELDGEEIE-----GEALLVAV 194

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775254  644 LNIPRYcaGTMPWGNPGDhhdfepqRHDDGYIEVIGFT-------MASLAALQVGGHGE----RLHQCREVMLLTYKSIP 712
Cdd:COG1597    195 GNGPYY--GGGLRLAPDA-------SLDDGLLDVVVVRplsrlrlLRLLPRLLRGRHLRhpgvRYFRAREVEIESDRPLP 265

                          330
                   ....*....|....*...
gi 1039775254  713 MQVDGEPCRLA-PAMIRI 729
Cdd:COG1597    266 VQLDGEPLGLAtPLEFEV 283
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
 246-305 1.00e-09

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: 55.14  E-value: 1.00e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039775254  246 HHWVHRR-RQEGKCKQCGKgfqqkfSFHSKEIVAISCSWCKQAFHNKvtCFMLHHIEEPCS 305
Cdd:pfam00130    1 HHFVHRNfKQPTFCDHCGE------FLWGLGKQGLKCSWCKLNVHKR--CHEKVPPECGCD 53
PRK13057 PRK13057
lipid kinase;
414-508 4.04e-08

lipid kinase;


Pssm-ID: 183857 [Multi-domain]  Cd Length: 287  Bit Score: 55.69  E-value: 4.04e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775254  414 LVFVNPKSggNQGTKVLQMFMWYLNPRQvFDLSQEGPKDA------LEMYRKVPNLRILAcGGDGTVGWILSILDELQLs 487
Cdd:PRK13057     1 LLLVNRHA--RSGRAALAAARAALEAAG-LELVEPPAEDPddlsevIEAYADGVDLVIVG-GGDGTLNAAAPALVETGL- 75

                           90       100
                   ....*....|....*....|.
gi 1039775254  488 pqpPVGVLPLGTGNDLARTLN 508
Cdd:PRK13057    76 ---PLGILPLGTANDLARTLG 93
TIGR00147 TIGR00147
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ...
 464-507 1.13e-03

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: 1.13e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1039775254  464 RILACGGDGTVGWILSILdeLQLSPQPPVGVLPLGTGNDLARTL 507
Cdd:TIGR00147   60 TVIAGGGDGTINEVVNAL--IQLDDIPALGILPLGTANDFARSL 101
 
Name Accession Description Interval E-value
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 562-719 3.48e-74

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: 241.09  E-value: 3.48e-74
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775254   562 VFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGAAFSDFLQRSSRDLSKHVKVVCDGTDLTPKIqdlKFQCI 641
Cdd:smart00045    1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLPN---SLEGI 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775254   642 VFLNIPRYCAGTMPWGNPGDH-HDFEPQRHDDGYIEVIGFTMASLAA--LQVGGHGERLHQCREV--MLLTYKSIPMQVD 716
Cdd:smart00045   78 AVLNIPSYGGGTNLWGTTDKEdLNFSKQSHDDGLLEVVGLTGAMHMAqiRQVGLAGRRIAQCSEVriTIKTSKTIPMQVD 157


                    ...
gi 1039775254   717 GEP 719
Cdd:smart00045  158 GEP 160
DAGK_acc pfam00609
Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts ...
 562-719 6.92e-68

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: 224.02  E-value: 6.92e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775254  562 VFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGAAFSDFLQRSSRDLSKHVKVVCDGTDLTPKiqdLKFQCI 641
Cdd:pfam00609    1 VMNNYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDMFQRSCKNLIEKVELEVDGKDLPLP---KSLEGI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775254  642 VFLNIPRYCAGTMPWGNPGDHHD-FEPQRHDDGYIEVIGFT-MASLAALQVGGHGE-RLHQCREVMLLTYKSIPMQVDGE 718
Cdd:pfam00609   78 VVLNIPSYAGGTDLWGNSKEDGLgFAPQSVDDGLLEVVGLTgALHLGQVQVGLGSAkRIAQGGPIRITTKKKIPMQVDGE 157


                   .
gi 1039775254  719 P 719
Cdd:pfam00609  158 P 158
C1_DGKiota_rpt2 cd20896
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase iota ...
 244-318 8.00e-52

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: 175.66  E-value: 8.00e-52
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039775254  244 VRHHWVHRRRQEGKCKQCGKGFQQKFSFHSKEIVAISCSWCKQAFHNKVTCFMLHHIEEPCSLGAHAAVIVPPTW 318
Cdd:cd20896      1 VRHHWVHRRRQEGKCKQCGKGFQQKFSFHSKEIVAISCSWCKQAFHNKVTCFMLHHIEEPCSLGAHAAVIVPPTW 75
C1_DGKiota_rpt1 cd20850
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase iota (DAG ...
 163-235 4.15e-51

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: 173.67  E-value: 4.15e-51
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039775254  163 DWSENAVNGEHLWLETNVSGDLCYLGEENCQVRFAKSALRRKCAVCKIVVHTACIEQLEKINFRCKPTFREGG 235
Cdd:cd20850      1 DWSENAVNGEHLWLETNVSGDLCYLGEENCQVKFAKSALRRKCAACKIVVHTACIEQLEKINFRCKPTFREGG 73
C1_DGKzeta_rpt2 cd20895
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta ...
 244-318 5.71e-51

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: 173.35  E-value: 5.71e-51
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039775254  244 VRHHWVHRRRQEGKCKQCGKGFQQKFSFHSKEIVAISCSWCKQAFHNKVTCFMLHHIEEPCSLGAHAAVIVPPTW 318
Cdd:cd20895      1 VRHHWVHRRRQEGKCRQCGKGFQQKFAFHSKEIVAISCSWCKQAYHSKVSCFMLQQIEEPCSLGAHAAVIVPPTW 75
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 414-535 5.16e-47

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: 164.01  E-value: 5.16e-47
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775254   414 LVFVNPKSGGNQGTKVLQMFMWYLNPRQVFDLSQEGPKDALEMYRKVPN-LRILACGGDGTVGWILSILDELQL-SPQPP 491
Cdd:smart00046    1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVPDfNRVLVCGGDGTVGWVLNALDKRELpLPEPP 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 1039775254   492 VGVLPLGTGNDLARTLNWGGGYTDEPVSKILCQVEDGTIVQLDR 535
Cdd:smart00046   81 VAVLPLGTGNDLARSLGWGGGYDGEKLLKTLRDALESDTVKLDR 124
C1_DGK_typeIV_rpt2 cd20855
second protein kinase C conserved region 1 (C1 domain) found in type IV diacylglycerol kinases; ...
 246-307 5.21e-41

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: 144.41  E-value: 5.21e-41
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039775254  246 HHWVHRRRQEGKCKQCGKGFQQKFSFHSKEIVAISCSWCKQAFHNKVTCFMLHHIEEPCSLG 307
Cdd:cd20855      1 HHWVHRRKQEGKCKQCGKSFQQKLSFSSKEIVAISCSWCKEAYHNKDSCFNMKKIEEPCNLG 62
C1_DGKzeta_rpt1 cd20849
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta (DAG ...
 163-235 4.88e-38

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: 136.22  E-value: 4.88e-38
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039775254  163 DWSENAVNGEHLWLETNVSGDLCYLGEENCQVR-FAKSALRRKCAVCKIVVHTACIEQLEKINFRCKPTFREGG 235
Cdd:cd20849      1 DWSESAVYGEHIWFETNVSGDFCYVGEQNCVAKqLQKSVSRKKCAACKIVVHTPCIEQLEKINFRCKPSFRESG 74
C1_DGK_typeIV_rpt1 cd20802
first protein kinase C conserved region 1 (C1 domain) found in type IV diacylglycerol kinases; ...
 168-233 7.12e-35

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: 127.03  E-value: 7.12e-35
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039775254  168 AVNGEHLWLETNVSGDLCYLGEENCQvrfaKSALRRKCAVCKIVVHTACIEQLEKINFRCKPTFRE 233
Cdd:cd20802      1 AVNGEHLWTDTSASGDLCYVGEQDCL----KSGSRKKCSACKIVVHTGCIPQLEKINFKCKPTFRE 62
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 412-511 3.83e-34

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: 126.93  E-value: 3.83e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775254  412 PLLVFVNPKSGGNQGTKVLQMFMWYLNPRQV-FDLSQ-EGPKDALEMYRKVPNL---RILACGGDGTVGWILSILDELql 486
Cdd:pfam00781    1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVeVELVLtEGPGDALELAREAAEDgydRIVVAGGDGTVNEVLNGLAGL-- 78

                           90       100
                   ....*....|....*....|....*
gi 1039775254  487 SPQPPVGVLPLGTGNDLARTLNWGG 511
Cdd:pfam00781   79 ATRPPLGIIPLGTGNDFARALGIPG 103
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 410-729 2.01e-26

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


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 110.33  E-value: 2.01e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775254  410 MKPLLVFVNPKSGGNQGTKVLQMFMWYLNpRQVFDLSQ---EGPKDALEMYRKVPNL---RILACGGDGTVGWILSILde 483
Cdd:COG1597      2 MMRALLIVNPASGRGRAARLLERLVAALR-AAGLEVEVletESPGDATELAREAAAEgadLVVAAGGDGTVNEVANGL-- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775254  484 lqLSPQPPVGVLPLGTGNDLARTLNwgggyTDEPVSKILCQVEDGTIVQLDrwnlhvernpdlppeeledgVCKLPLNVF 563
Cdd:COG1597     79 --AGTGPPLGILPLGTGNDFARALG-----IPLDPEAALEALLTGRTRRID--------------------LGRVNGRYF 131

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775254  564 NNYFSLGFDAHVTLEFHESReanpekfnSRFRNKMFYAGAAFSDFLQRSSRdlskHVKVVCDGTDLTpkiqdLKFQCIVF 643
Cdd:COG1597    132 LNVAGIGFDAEVVERANRAL--------KRRLGKLAYVLAALRALLRYRPF----RLRIELDGEEIE-----GEALLVAV 194

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775254  644 LNIPRYcaGTMPWGNPGDhhdfepqRHDDGYIEVIGFT-------MASLAALQVGGHGE----RLHQCREVMLLTYKSIP 712
Cdd:COG1597    195 GNGPYY--GGGLRLAPDA-------SLDDGLLDVVVVRplsrlrlLRLLPRLLRGRHLRhpgvRYFRAREVEIESDRPLP 265

                          330
                   ....*....|....*...
gi 1039775254  713 MQVDGEPCRLA-PAMIRI 729
Cdd:COG1597    266 VQLDGEPLGLAtPLEFEV 283
C1_DGK_rpt2 cd20805
second protein kinase C conserved region 1 (C1 domain) found in the diacylglycerol kinase ...
 246-307 5.57e-10

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: 55.92  E-value: 5.57e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039775254  246 HHWVHRRRQ-EGKCKQCGKGFQQKFSFHSKeivaiSCSWCKQAFHNKvtCFMLHHIEEpCSLG 307
Cdd:cd20805      1 HHWVEGNLPsGAKCSVCGKKCGSSFGLAGY-----RCSWCKRTVHSE--CIDKLGPEE-CDLG 55
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
 246-305 1.00e-09

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: 55.14  E-value: 1.00e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039775254  246 HHWVHRR-RQEGKCKQCGKgfqqkfSFHSKEIVAISCSWCKQAFHNKvtCFMLHHIEEPCS 305
Cdd:pfam00130    1 HHFVHRNfKQPTFCDHCGE------FLWGLGKQGLKCSWCKLNVHKR--CHEKVPPECGCD 53
PRK13057 PRK13057
lipid kinase;
414-508 4.04e-08

lipid kinase;


Pssm-ID: 183857 [Multi-domain]  Cd Length: 287  Bit Score: 55.69  E-value: 4.04e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775254  414 LVFVNPKSggNQGTKVLQMFMWYLNPRQvFDLSQEGPKDA------LEMYRKVPNLRILAcGGDGTVGWILSILDELQLs 487
Cdd:PRK13057     1 LLLVNRHA--RSGRAALAAARAALEAAG-LELVEPPAEDPddlsevIEAYADGVDLVIVG-GGDGTLNAAAPALVETGL- 75

                           90       100
                   ....*....|....*....|.
gi 1039775254  488 pqpPVGVLPLGTGNDLARTLN 508
Cdd:PRK13057    76 ---PLGILPLGTANDLARTLG 93
PRK12361 PRK12361
hypothetical protein; Provisional
 411-528 2.55e-07

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 54.63  E-value: 2.55e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775254  411 KPLLVFVNPKSGGNQGTKVLQMFMWYLNPRqvFDLS-QEGPKD------ALEMYRKVPNLrILACGGDGTVGWILSIL-- 481
Cdd:PRK12361   243 KRAWLIANPVSGGGKWQEYGEQIQRELKAY--FDLTvKLTTPEisaealAKQARKAGADI-VIACGGDGTVTEVASELvn 319

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1039775254  482 DELQLspqppvGVLPLGTGNDLARTLnWGGGYTDEPVSKILCQVEDG 528
Cdd:PRK12361   320 TDITL------GIIPLGTANALSHAL-FGLGSKLIPVEQACDNIIQG 359
PRK13054 PRK13054
lipid kinase; Reviewed
 464-505 1.29e-05

lipid kinase; Reviewed


Pssm-ID: 237281 [Multi-domain]  Cd Length: 300  Bit Score: 48.33  E-value: 1.29e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1039775254  464 RILACGGDGTVGWILSILDELQLSPQPPVGVLPLGTGNDLAR 505
Cdd:PRK13054    59 TVIAGGGDGTINEVATALAQLEGDARPALGILPLGTANDFAT 100
PRK13059 PRK13059
putative lipid kinase; Reviewed
 410-508 1.87e-05

putative lipid kinase; Reviewed


Pssm-ID: 183858  Cd Length: 295  Bit Score: 47.72  E-value: 1.87e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775254  410 MKPLLVFVNPKSGGN----QGTKVLQMFMWYLNPRQVFDLSQEGP-KDALEMYRKVPNLrILACGGDGTVGWILSILDEL 484
Cdd:PRK13059     1 MKKVKFIYNPYSGENaiisELDKVIRIHQEKGYLVVPYRISLEYDlKNAFKDIDESYKY-ILIAGGDGTVDNVVNAMKKL 79

                           90       100
                   ....*....|....*....|....
gi 1039775254  485 QLSPqpPVGVLPLGTGNDLARTLN 508
Cdd:PRK13059    80 NIDL--PIGILPVGTANDFAKFLG 101
C1_DGKepsilon_typeIII_rpt2 cd20853
second protein kinase C conserved region 1 (C1 domain) found in type III diacylglycerol kinase, ...
 246-316 8.03e-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: 38.80  E-value: 8.03e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039775254  246 HHWVHrrrqeG------KCKQCGK--GFQQKFSFHSkeivaisCSWCKQAFHNKvtCfmLHHIEEPCSLGAHAAVIVPP 316
Cdd:cd20853      1 HHWVR-----GnlplcsVCCVCNEqcGNQPGLCDYR-------CCWCQRTVHDD--C--LAKLPKECDLGAFRNFIVPP 63
PRK13055 PRK13055
putative lipid kinase; Reviewed
 465-508 1.08e-03

putative lipid kinase; Reviewed


Pssm-ID: 237282 [Multi-domain]  Cd Length: 334  Bit Score: 42.28  E-value: 1.08e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1039775254  465 ILACGGDGTVGWILSILdeLQLSPQPPVGVLPLGTGNDLARTLN 508
Cdd:PRK13055    63 IIAAGGDGTINEVVNGI--APLEKRPKMAIIPAGTTNDYARALK 104
TIGR00147 TIGR00147
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ...
 464-507 1.13e-03

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: 1.13e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1039775254  464 RILACGGDGTVGWILSILdeLQLSPQPPVGVLPLGTGNDLARTL 507
Cdd:TIGR00147   60 TVIAGGGDGTINEVVNAL--IQLDDIPALGILPLGTANDFARSL 101
C1_DGK_rpt2 cd20805
second protein kinase C conserved region 1 (C1 domain) found in the diacylglycerol kinase ...
 173-220 9.19e-03

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: 35.50  E-value: 9.19e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1039775254  173 HLWLETNV-SGDLCYLGEENCQVRFAKSALRrkCAVCKIVVHTACIEQL 220
Cdd:cd20805      1 HHWVEGNLpSGAKCSVCGKKCGSSFGLAGYR--CSWCKRTVHSECIDKL 47
 
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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