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Conserved domains on  [gi|755498484|ref|XP_011237546|]
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diacylglycerol kinase zeta isoform X14 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
C1_DGKzeta_rpt2 cd20895
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta ...
 365-439 3.20e-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: 166.41  E-value: 3.20e-49
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755498484 365 VRHHWVHRRRQDGKCRHCGKGFQQKFTFHSKEIVAISCSWCKQAYHSKVSCFMMQQIEEPCSLGVHAAVVIPPTW 439
Cdd:cd20895    1 VRHHWVHRRRQEGKCRQCGKGFQQKFAFHSKEIVAISCSWCKQAYHSKVSCFMLQQIEEPCSLGAHAAVIVPPTW 75
C1_DGKzeta_rpt1 cd20849
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta (DAG ...
 282-355 3.90e-47

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: 160.87  E-value: 3.90e-47
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755498484 282 DWSESAVYGEHIWFETNVSGDFCYVGEQHCVAKMLPKSAPRKKCAACKIVVHTQCIKQLEKINFRCKPSFRESG 355
Cdd:cd20849    1 DWSESAVYGEHIWFETNVSGDFCYVGEQNCVAKQLQKSVSRKKCAACKIVVHTPCIEQLEKINFRCKPSFRESG 74
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 492-594 6.20e-45

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: 156.30  E-value: 6.20e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498484   492 LVFVNPKSGGNQGAKIIQSFLWYLNPRQVFDLSQGGPREALEMYRKVHN-LRILACGGDGTVGWILSTLDQLRLKPP-PP 569
Cdd:smart00046   1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVPDfNRVLVCGGDGTVGWVLNALDKRELPLPePP 80

                           90       100
                   ....*....|....*....|....*
gi 755498484   570 VAILPLGTGNDLARTLNWGGSPPTR 594
Cdd:smart00046  81 VAVLPLGTGNDLARSLGWGGGYDGE 105
 
Name Accession Description Interval E-value
C1_DGKzeta_rpt2 cd20895
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta ...
 365-439 3.20e-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: 166.41  E-value: 3.20e-49
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755498484 365 VRHHWVHRRRQDGKCRHCGKGFQQKFTFHSKEIVAISCSWCKQAYHSKVSCFMMQQIEEPCSLGVHAAVVIPPTW 439
Cdd:cd20895    1 VRHHWVHRRRQEGKCRQCGKGFQQKFAFHSKEIVAISCSWCKQAYHSKVSCFMLQQIEEPCSLGAHAAVIVPPTW 75
C1_DGKzeta_rpt1 cd20849
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta (DAG ...
 282-355 3.90e-47

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: 160.87  E-value: 3.90e-47
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755498484 282 DWSESAVYGEHIWFETNVSGDFCYVGEQHCVAKMLPKSAPRKKCAACKIVVHTQCIKQLEKINFRCKPSFRESG 355
Cdd:cd20849    1 DWSESAVYGEHIWFETNVSGDFCYVGEQNCVAKQLQKSVSRKKCAACKIVVHTPCIEQLEKINFRCKPSFRESG 74
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 492-594 6.20e-45

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: 156.30  E-value: 6.20e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498484   492 LVFVNPKSGGNQGAKIIQSFLWYLNPRQVFDLSQGGPREALEMYRKVHN-LRILACGGDGTVGWILSTLDQLRLKPP-PP 569
Cdd:smart00046   1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVPDfNRVLVCGGDGTVGWVLNALDKRELPLPePP 80

                           90       100
                   ....*....|....*....|....*
gi 755498484   570 VAILPLGTGNDLARTLNWGGSPPTR 594
Cdd:smart00046  81 VAVLPLGTGNDLARSLGWGGGYDGE 105
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 490-593 5.67e-36

Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. The catalytic domain is assumed from the finding of bacterial homologs. YegS is the Escherichia coli protein in this family whose crystal structure reveals an active site in the inter-domain cleft formed by four conserved sequence motifs, revealing a novel metal-binding site. The residues of this site are conserved across the family.


Pssm-ID: 425868 [Multi-domain]  Cd Length: 125  Bit Score: 131.55  E-value: 5.67e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498484  490 PLLVFVNPKSGGNQGAKIIQSFLWYLNPRQV-FDLSQGGPRE-ALEMYRKV---HNLRILACGGDGTVGWILSTLDqlRL 564
Cdd:pfam00781   1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVeVELVLTEGPGdALELAREAaedGYDRIVVAGGDGTVNEVLNGLA--GL 78

                          90       100
                  ....*....|....*....|....*....
gi 755498484  565 KPPPPVAILPLGTGNDLARTLNWGGSPPT 593
Cdd:pfam00781  79 ATRPPLGIIPLGTGNDFARALGIPGDPEE 107
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 488-586 9.98e-15

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


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 75.27  E-value: 9.98e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498484 488 MKPLLVFVNPKSGGNQGAKIIQSFLWYLNPR----QVFDLSQGGP-----REALEmyRKVHnlRILACGGDGTVGWILST 558
Cdd:COG1597    2 MMRALLIVNPASGRGRAARLLERLVAALRAAglevEVLETESPGDatelaREAAA--EGAD--LVVAAGGDGTVNEVANG 77

                         90       100
                 ....*....|....*....|....*...
gi 755498484 559 LdqlrLKPPPPVAILPLGTGNDLARTLN 586
Cdd:COG1597   78 L----AGTGPPLGILPLGTGNDFARALG 101
PRK13054 PRK13054
lipid kinase; Reviewed
 542-583 5.80e-07

lipid kinase; Reviewed


Pssm-ID: 237281 [Multi-domain]  Cd Length: 300  Bit Score: 51.80  E-value: 5.80e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 755498484 542 RILACGGDGTVGWILSTLDQLRLKPPPPVAILPLGTGNDLAR 583
Cdd:PRK13054  59 TVIAGGGDGTINEVATALAQLEGDARPALGILPLGTANDFAT 100
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
 367-426 1.51e-06

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: 45.51  E-value: 1.51e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755498484  367 HHWVHRR-RQDGKCRHCGKgfqqkfTFHSKEIVAISCSWCKQAYHSKvsCFMMQQIEEPCS 426
Cdd:pfam00130   1 HHFVHRNfKQPTFCDHCGE------FLWGLGKQGLKCSWCKLNVHKR--CHEKVPPECGCD 53
TIGR00147 TIGR00147
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ...
 542-585 1.26e-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: 41.34  E-value: 1.26e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 755498484  542 RILACGGDGTVGWILSTLDQLRLKPPppVAILPLGTGNDLARTL 585
Cdd:TIGR00147  60 TVIAGGGDGTINEVVNALIQLDDIPA--LGILPLGTANDFARSL 101
 
Name Accession Description Interval E-value
C1_DGKzeta_rpt2 cd20895
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta ...
 365-439 3.20e-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: 166.41  E-value: 3.20e-49
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755498484 365 VRHHWVHRRRQDGKCRHCGKGFQQKFTFHSKEIVAISCSWCKQAYHSKVSCFMMQQIEEPCSLGVHAAVVIPPTW 439
Cdd:cd20895    1 VRHHWVHRRRQEGKCRQCGKGFQQKFAFHSKEIVAISCSWCKQAYHSKVSCFMLQQIEEPCSLGAHAAVIVPPTW 75
C1_DGKzeta_rpt1 cd20849
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta (DAG ...
 282-355 3.90e-47

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: 160.87  E-value: 3.90e-47
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755498484 282 DWSESAVYGEHIWFETNVSGDFCYVGEQHCVAKMLPKSAPRKKCAACKIVVHTQCIKQLEKINFRCKPSFRESG 355
Cdd:cd20849    1 DWSESAVYGEHIWFETNVSGDFCYVGEQNCVAKQLQKSVSRKKCAACKIVVHTPCIEQLEKINFRCKPSFRESG 74
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 492-594 6.20e-45

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: 156.30  E-value: 6.20e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498484   492 LVFVNPKSGGNQGAKIIQSFLWYLNPRQVFDLSQGGPREALEMYRKVHN-LRILACGGDGTVGWILSTLDQLRLKPP-PP 569
Cdd:smart00046   1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVPDfNRVLVCGGDGTVGWVLNALDKRELPLPePP 80

                           90       100
                   ....*....|....*....|....*
gi 755498484   570 VAILPLGTGNDLARTLNWGGSPPTR 594
Cdd:smart00046  81 VAVLPLGTGNDLARSLGWGGGYDGE 105
C1_DGKiota_rpt2 cd20896
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase iota ...
 365-439 5.08e-44

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: 152.17  E-value: 5.08e-44
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755498484 365 VRHHWVHRRRQDGKCRHCGKGFQQKFTFHSKEIVAISCSWCKQAYHSKVSCFMMQQIEEPCSLGVHAAVVIPPTW 439
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; ...
 367-428 3.94e-40

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: 140.94  E-value: 3.94e-40
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755498484 367 HHWVHRRRQDGKCRHCGKGFQQKFTFHSKEIVAISCSWCKQAYHSKVSCFMMQQIEEPCSLG 428
Cdd:cd20855    1 HHWVHRRKQEGKCKQCGKSFQQKLSFSSKEIVAISCSWCKEAYHNKDSCFNMKKIEEPCNLG 62
C1_DGKiota_rpt1 cd20850
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase iota (DAG ...
 282-355 1.42e-38

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: 137.08  E-value: 1.42e-38
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755498484 282 DWSESAVYGEHIWFETNVSGDFCYVGEQHCVAKmLPKSAPRKKCAACKIVVHTQCIKQLEKINFRCKPSFRESG 355
Cdd:cd20850    1 DWSENAVNGEHLWLETNVSGDLCYLGEENCQVK-FAKSALRRKCAACKIVVHTACIEQLEKINFRCKPTFREGG 73
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 490-593 5.67e-36

Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. The catalytic domain is assumed from the finding of bacterial homologs. YegS is the Escherichia coli protein in this family whose crystal structure reveals an active site in the inter-domain cleft formed by four conserved sequence motifs, revealing a novel metal-binding site. The residues of this site are conserved across the family.


Pssm-ID: 425868 [Multi-domain]  Cd Length: 125  Bit Score: 131.55  E-value: 5.67e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498484  490 PLLVFVNPKSGGNQGAKIIQSFLWYLNPRQV-FDLSQGGPRE-ALEMYRKV---HNLRILACGGDGTVGWILSTLDqlRL 564
Cdd:pfam00781   1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVeVELVLTEGPGdALELAREAaedGYDRIVVAGGDGTVNEVLNGLA--GL 78

                          90       100
                  ....*....|....*....|....*....
gi 755498484  565 KPPPPVAILPLGTGNDLARTLNWGGSPPT 593
Cdd:pfam00781  79 ATRPPLGIIPLGTGNDFARALGIPGDPEE 107
C1_DGK_typeIV_rpt1 cd20802
first protein kinase C conserved region 1 (C1 domain) found in type IV diacylglycerol kinases; ...
 287-353 5.40e-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: 126.64  E-value: 5.40e-35
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755498484 287 AVYGEHIWFETNVSGDFCYVGEQHCVakmlpKSAPRKKCAACKIVVHTQCIKQLEKINFRCKPSFRE 353
Cdd:cd20802    1 AVNGEHLWTDTSASGDLCYVGEQDCL-----KSGSRKKCSACKIVVHTGCIPQLEKINFKCKPTFRE 62
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 488-586 9.98e-15

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


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 75.27  E-value: 9.98e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498484 488 MKPLLVFVNPKSGGNQGAKIIQSFLWYLNPR----QVFDLSQGGP-----REALEmyRKVHnlRILACGGDGTVGWILST 558
Cdd:COG1597    2 MMRALLIVNPASGRGRAARLLERLVAALRAAglevEVLETESPGDatelaREAAA--EGAD--LVVAAGGDGTVNEVANG 77

                         90       100
                 ....*....|....*....|....*...
gi 755498484 559 LdqlrLKPPPPVAILPLGTGNDLARTLN 586
Cdd:COG1597   78 L----AGTGPPLGILPLGTGNDFARALG 101
C1_DGK_rpt2 cd20805
second protein kinase C conserved region 1 (C1 domain) found in the diacylglycerol kinase ...
 367-428 5.85e-11

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: 58.23  E-value: 5.85e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755498484 367 HHWVHRRRQ-DGKCRHCGKGFQQKFTFHSKeivaiSCSWCKQAYHSkvSCFMMQQIEEpCSLG 428
Cdd:cd20805    1 HHWVEGNLPsGAKCSVCGKKCGSSFGLAGY-----RCSWCKRTVHS--ECIDKLGPEE-CDLG 55
PRK13054 PRK13054
lipid kinase; Reviewed
 542-583 5.80e-07

lipid kinase; Reviewed


Pssm-ID: 237281 [Multi-domain]  Cd Length: 300  Bit Score: 51.80  E-value: 5.80e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 755498484 542 RILACGGDGTVGWILSTLDQLRLKPPPPVAILPLGTGNDLAR 583
Cdd:PRK13054  59 TVIAGGGDGTINEVATALAQLEGDARPALGILPLGTANDFAT 100
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
 367-426 1.51e-06

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: 45.51  E-value: 1.51e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755498484  367 HHWVHRR-RQDGKCRHCGKgfqqkfTFHSKEIVAISCSWCKQAYHSKvsCFMMQQIEEPCS 426
Cdd:pfam00130   1 HHFVHRNfKQPTFCDHCGE------FLWGLGKQGLKCSWCKLNVHKR--CHEKVPPECGCD 53
PRK13057 PRK13057
lipid kinase;
529-586 4.53e-06

lipid kinase;


Pssm-ID: 183857 [Multi-domain]  Cd Length: 287  Bit Score: 48.76  E-value: 4.53e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 755498484 529 REALEMYRKVHNLRILAcGGDGTVGWILSTLDQLRLkpppPVAILPLGTGNDLARTLN 586
Cdd:PRK13057  41 SEVIEAYADGVDLVIVG-GGDGTLNAAAPALVETGL----PLGILPLGTANDLARTLG 93
PRK13059 PRK13059
putative lipid kinase; Reviewed
 488-586 1.09e-05

putative lipid kinase; Reviewed


Pssm-ID: 183858  Cd Length: 295  Bit Score: 47.72  E-value: 1.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498484 488 MKPLLVFVNPKSGGNQGA----KIIQSFLWYLNPRQVFDLSQGGP-REALEMYRKVHNLrILACGGDGTVGWILSTLDQL 562
Cdd:PRK13059   1 MKKVKFIYNPYSGENAIIseldKVIRIHQEKGYLVVPYRISLEYDlKNAFKDIDESYKY-ILIAGGDGTVDNVVNAMKKL 79

                         90       100
                 ....*....|....*....|....
gi 755498484 563 RLKPPppVAILPLGTGNDLARTLN 586
Cdd:PRK13059  80 NIDLP--IGILPVGTANDFAKFLG 101
PRK13055 PRK13055
putative lipid kinase; Reviewed
 543-586 1.87e-05

putative lipid kinase; Reviewed


Pssm-ID: 237282 [Multi-domain]  Cd Length: 334  Bit Score: 47.29  E-value: 1.87e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 755498484 543 ILACGGDGTVGWILSTLDQlrLKPPPPVAILPLGTGNDLARTLN 586
Cdd:PRK13055  63 IIAAGGDGTINEVVNGIAP--LEKRPKMAIIPAGTTNDYARALK 104
PRK12361 PRK12361
hypothetical protein; Provisional
 489-585 4.00e-05

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 46.92  E-value: 4.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498484 489 KPLLVFVNPKSGGNQGAKIIQSFLWYLNPRqvFDLS-------QGGPREALEMYRKVHNLrILACGGDGTVGWILSTL-- 559
Cdd:PRK12361 243 KRAWLIANPVSGGGKWQEYGEQIQRELKAY--FDLTvklttpeISAEALAKQARKAGADI-VIACGGDGTVTEVASELvn 319

                         90       100
                 ....*....|....*....|....*.
gi 755498484 560 DQLRLkppppvAILPLGTGNDLARTL 585
Cdd:PRK12361 320 TDITL------GIIPLGTANALSHAL 339
TIGR00147 TIGR00147
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ...
 542-585 1.26e-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: 41.34  E-value: 1.26e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 755498484  542 RILACGGDGTVGWILSTLDQLRLKPPppVAILPLGTGNDLARTL 585
Cdd:TIGR00147  60 TVIAGGGDGTINEVVNALIQLDDIPA--LGILPLGTANDFARSL 101
C1_DGKepsilon_typeIII_rpt1 cd20801
first protein kinase C conserved region 1 (C1 domain) found in type III diacylglycerol kinase, ...
 292-348 9.49e-03

first 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 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: 410351  Cd Length: 54  Bit Score: 34.99  E-value: 9.49e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 755498484 292 HIWFETNVSGD--FCYVGEQHCVAKMlpksaprkKCAACKIVVHTQCIKQLEKInFRCK 348
Cdd:cd20801    4 HHWVSTDLFSKptYCSVCETLILSGA--------FCDCCGLCVDEGCLRKADKR-FPCK 53
 
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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