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Conserved domains on  [gi|528485566|ref|XP_005169094|]
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diacylglycerol kinase zeta isoform X7 [Danio rerio]

Protein Classification

diacylglycerol kinase zeta( domain architecture ID 15336656)

diacylglycerol kinase zeta converts diacylglycerol/DAG into phosphatidic acid/phosphatidate/PA and regulates the respective levels of these two bioactive lipids

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 ...
 455-612 1.39e-73

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: 239.93  E-value: 1.39e-73
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485566    455 VFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGTAFSDFLMGSSKDLAKHIKVVCDGTDLTSKvqdLKLQCL 534
Cdd:smart00045    1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLP---NSLEGI 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485566    535 VFLNIPRYCAGTMPWGNPSEH-HDFEPQRHDDGCIEVIGFTMTSLA--TLQVGGHGERLNQCREV--TLTTFKSIPMQVD 609
Cdd:smart00045   78 AVLNIPSYGGGTNLWGTTDKEdLNFSKQSHDDGLLEVVGLTGAMHMaqIRQVGLAGRRIAQCSEVriTIKTSKTIPMQVD 157


                    ...
gi 528485566    610 GEP 612
Cdd:smart00045  158 GEP 160
C1_DGKzeta_rpt2 cd20895
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta ...
 179-253 3.74e-52

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: 176.81  E-value: 3.74e-52
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528485566  179 VRHHWVHRRRQEGKCKQCGKGFQQKFAFHSKEIVAISCSWCKQAYHNKVTCFMLQQIEEPCSLGAHAAVIVPPTW 253
Cdd:cd20895     1 VRHHWVHRRRQEGKCRQCGKGFQQKFAFHSKEIVAISCSWCKQAYHSKVSCFMLQQIEEPCSLGAHAAVIVPPTW 75
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 306-427 3.98e-51

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: 175.56  E-value: 3.98e-51
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485566    306 LVFVNPKSGGNQGAKIIQTFLWYLNPRQVFDLSQGGPQEGLEMYRKVHN-LRILACGGDGTVGWILSALDQLQL-NPSPA 383
Cdd:smart00046    1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVPDfNRVLVCGGDGTVGWVLNALDKRELpLPEPP 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 528485566    384 VAVLPLGTGNDLARTLNWGGGYTDEPLSKILSHVEDGNIVQLDR 427
Cdd:smart00046   81 VAVLPLGTGNDLARSLGWGGGYDGEKLLKTLRDALESDTVKLDR 124
C1_DGKzeta_rpt1 cd20849
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta (DAG ...
 96-169 4.05e-49

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: 167.81  E-value: 4.05e-49
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528485566   96 DWSESAVYGEHIWFETNVSGDFCYVGEQHCYAKSLQKSVARKKCAACKIVVHSICIEQLEKINFRCKPSFRESG 169
Cdd:cd20849     1 DWSESAVYGEHIWFETNVSGDFCYVGEQNCVAKQLQKSVSRKKCAACKIVVHTPCIEQLEKINFRCKPSFRESG 74
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
882-1027 4.32e-21

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 95.02  E-value: 4.32e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485566  882 VNNANSVSVDSLIECVKKKDHQKLKELHKKGADLCVQDPAGRTLLHYAVEVGSKEIVKYIIDN-APTDILDvtekENGET 960
Cdd:COG0666   113 VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAgADVNARD----NDGET 188

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528485566  961 VLHKAASLCHRTICHYLVEAGASLMKTDLQGDTPKHRAEKAKDAELAAYLENRQHYQMIQREDQETA 1027
Cdd:COG0666   189 PLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTA 255
 
Name Accession Description Interval E-value
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 455-612 1.39e-73

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: 239.93  E-value: 1.39e-73
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485566    455 VFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGTAFSDFLMGSSKDLAKHIKVVCDGTDLTSKvqdLKLQCL 534
Cdd:smart00045    1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLP---NSLEGI 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485566    535 VFLNIPRYCAGTMPWGNPSEH-HDFEPQRHDDGCIEVIGFTMTSLA--TLQVGGHGERLNQCREV--TLTTFKSIPMQVD 609
Cdd:smart00045   78 AVLNIPSYGGGTNLWGTTDKEdLNFSKQSHDDGLLEVVGLTGAMHMaqIRQVGLAGRRIAQCSEVriTIKTSKTIPMQVD 157


                    ...
gi 528485566    610 GEP 612
Cdd:smart00045  158 GEP 160
DAGK_acc pfam00609
Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts ...
 455-612 9.78e-67

Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. This domain is assumed to be an accessory domain: its function is unknown.


Pssm-ID: 459866  Cd Length: 158  Bit Score: 220.94  E-value: 9.78e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485566   455 VFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGTAFSDFLMGSSKDLAKHIKVVCDGTDLTSKvqdLKLQCL 534
Cdd:pfam00609    1 VMNNYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDMFQRSCKNLIEKVELEVDGKDLPLP---KSLEGI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485566   535 VFLNIPRYCAGTMPWGNPSEHHD-FEPQRHDDGCIEVIGFT-MTSLATLQVGGHGE-RLNQCREVTLTTFKSIPMQVDGE 611
Cdd:pfam00609   78 VVLNIPSYAGGTDLWGNSKEDGLgFAPQSVDDGLLEVVGLTgALHLGQVQVGLGSAkRIAQGGPIRITTKKKIPMQVDGE 157


                   .
gi 528485566   612 P 612
Cdd:pfam00609  158 P 158
C1_DGKzeta_rpt2 cd20895
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta ...
 179-253 3.74e-52

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: 176.81  E-value: 3.74e-52
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528485566  179 VRHHWVHRRRQEGKCKQCGKGFQQKFAFHSKEIVAISCSWCKQAYHNKVTCFMLQQIEEPCSLGAHAAVIVPPTW 253
Cdd:cd20895     1 VRHHWVHRRRQEGKCRQCGKGFQQKFAFHSKEIVAISCSWCKQAYHSKVSCFMLQQIEEPCSLGAHAAVIVPPTW 75
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 306-427 3.98e-51

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: 175.56  E-value: 3.98e-51
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485566    306 LVFVNPKSGGNQGAKIIQTFLWYLNPRQVFDLSQGGPQEGLEMYRKVHN-LRILACGGDGTVGWILSALDQLQL-NPSPA 383
Cdd:smart00046    1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVPDfNRVLVCGGDGTVGWVLNALDKRELpLPEPP 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 528485566    384 VAVLPLGTGNDLARTLNWGGGYTDEPLSKILSHVEDGNIVQLDR 427
Cdd:smart00046   81 VAVLPLGTGNDLARSLGWGGGYDGEKLLKTLRDALESDTVKLDR 124
C1_DGKzeta_rpt1 cd20849
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta (DAG ...
 96-169 4.05e-49

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: 167.81  E-value: 4.05e-49
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528485566   96 DWSESAVYGEHIWFETNVSGDFCYVGEQHCYAKSLQKSVARKKCAACKIVVHSICIEQLEKINFRCKPSFRESG 169
Cdd:cd20849     1 DWSESAVYGEHIWFETNVSGDFCYVGEQNCVAKQLQKSVSRKKCAACKIVVHTPCIEQLEKINFRCKPSFRESG 74
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 304-426 2.83e-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: 127.32  E-value: 2.83e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485566   304 PLLVFVNPKSGGNQGAKIIQTFLWYLNPRQV-FDLSQ-GGPQEGLEMYRKV---HNLRILACGGDGTVGWILSALDQLQl 378
Cdd:pfam00781    1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVeVELVLtEGPGDALELAREAaedGYDRIVVAGGDGTVNEVLNGLAGLA- 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 528485566   379 nPSPAVAVLPLGTGNDLARTLNWGGgytdePLSKILSHVEDGNIVQLD 426
Cdd:pfam00781   80 -TRPPLGIIPLGTGNDFARALGIPG-----DPEEALEAILKGQTRPVD 121
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 302-628 1.63e-25

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


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 108.02  E-value: 1.63e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485566  302 MKPLLVFVNPKSGGNQGAKIIQTFLWYLNpRQVFDLSQ---GGPQEGLEMYRKVHNL---RILACGGDGTVGWILSALdq 375
Cdd:COG1597     2 MMRALLIVNPASGRGRAARLLERLVAALR-AAGLEVEVletESPGDATELAREAAAEgadLVVAAGGDGTVNEVANGL-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485566  376 lqLNPSPAVAVLPLGTGNDLARTLNwgggyTDEPLSKILSHVEDGNIVQLDrwnlvvkpnpeAGpeerdeQVTDKLpldv 455
Cdd:COG1597    79 --AGTGPPLGILPLGTGNDFARALG-----IPLDPEAALEALLTGRTRRID-----------LG------RVNGRY---- 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485566  456 FNNYFSLGFDAHVTLEFHESReanpekfnSRFRNKMFYAGTAFSdfLMGSSKdlAKHIKVVCDGTDLTSKVqdlkLQCLV 535
Cdd:COG1597   131 FLNVAGIGFDAEVVERANRAL--------KRRLGKLAYVLAALR--ALLRYR--PFRLRIELDGEEIEGEA----LLVAV 194

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485566  536 FlNIPRYcaGTMPWGNPSEhhdfepqRHDDGCIEVIGFT-------MTSLATLQVGGHGERLN----QCREVTLTTFKSI 604
Cdd:COG1597   195 G-NGPYY--GGGLRLAPDA-------SLDDGLLDVVVVRplsrlrlLRLLPRLLRGRHLRHPGvryfRAREVEIESDRPL 264

                         330       340
                  ....*....|....*....|....
gi 528485566  605 PMQVDGEPCKLAPSViHISLRNQA 628
Cdd:COG1597   265 PVQLDGEPLGLATPL-EFEVLPGA 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
882-1027 4.32e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 95.02  E-value: 4.32e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485566  882 VNNANSVSVDSLIECVKKKDHQKLKELHKKGADLCVQDPAGRTLLHYAVEVGSKEIVKYIIDN-APTDILDvtekENGET 960
Cdd:COG0666   113 VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAgADVNARD----NDGET 188

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528485566  961 VLHKAASLCHRTICHYLVEAGASLMKTDLQGDTPKHRAEKAKDAELAAYLENRQHYQMIQREDQETA 1027
Cdd:COG0666   189 PLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTA 255
Ank_2 pfam12796
Ankyrin repeats (3 copies);
893-988 1.61e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.32  E-value: 1.61e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485566   893 LIECVKKKDHQKLKELHKKGADLCVQDPAGRTLLHYAVEVGSKEIVKYIIDNAptdilDVTEKENGETVLHKAASLCHRT 972
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-----DVNLKDNGRTALHYAARSGHLE 75

                           90
                   ....*....|....*.
gi 528485566   973 ICHYLVEAGASLMKTD 988
Cdd:pfam12796   76 IVKLLLEKGADINVKD 91
PRK12361 PRK12361
hypothetical protein; Provisional
 303-426 2.06e-08

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 58.09  E-value: 2.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485566  303 KPLLVFVNPKSGGNQGAKIIQTFLWYLNPRqvFDLS--QGGPQEGLEMYRKVHNLR----ILACGGDGTVGWILSALdql 376
Cdd:PRK12361  243 KRAWLIANPVSGGGKWQEYGEQIQRELKAY--FDLTvkLTTPEISAEALAKQARKAgadiVIACGGDGTVTEVASEL--- 317

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 528485566  377 qLNPSPAVAVLPLGTGNDLARTLnWGGGYTDEPLSKILSHVEDGNIVQLD 426
Cdd:PRK12361  318 -VNTDITLGIIPLGTANALSHAL-FGLGSKLIPVEQACDNIIQGHTQRID 365
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
 181-240 2.12e-08

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: 51.29  E-value: 2.12e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528485566   181 HHWVHRR-RQEGKCKQCGKGFqqkfafHSKEIVAISCSWCKQAYHNKvtCFMLQQIEEPCS 240
Cdd:pfam00130    1 HHFVHRNfKQPTFCDHCGEFL------WGLGKQGLKCSWCKLNVHKR--CHEKVPPECGCD 53
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 882-998 7.28e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 52.75  E-value: 7.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485566  882 VNNANSVSVDSLIECV-KKKDHQKL-KELHKKGADLCVQDPAGRTLLHYAVEVGS--KEIVKYIIDN------------- 944
Cdd:PHA03100   99 VNAPDNNGITPLLYAIsKKSNSYSIvEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKgvdinaknrvnyl 178

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 528485566  945 ----APTDILDvtekENGETVLHKAASLCHRTICHYLVEAGASLMKTDLQGDTPKHRA 998
Cdd:PHA03100  179 lsygVPINIKD----VYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIA 232
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 893-986 1.12e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 46.16  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485566  893 LIECVKKKDHQKLKELHK-KGADLCVQDPAGRTLLHYAVEVGSKEIVKYIIDNAPTDI-LDVT-EKENGETVLHKAASLC 969
Cdd:cd22192    21 LLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVnEPMTsDLYQGETALHIAVVNQ 100

                          90
                  ....*....|....*..
gi 528485566  970 HRTICHYLVEAGASLMK 986
Cdd:cd22192   101 NLNLVRELIARGADVVS 117
TIGR00147 TIGR00147
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ...
 356-399 1.65e-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: 44.80  E-value: 1.65e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 528485566   356 RILACGGDGTVGWILSALdqLQLNPSPAVAVLPLGTGNDLARTL 399
Cdd:TIGR00147   60 TVIAGGGDGTINEVVNAL--IQLDDIPALGILPLGTANDFARSL 101
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 922-944 1.86e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.80  E-value: 1.86e-03
                            10        20
                    ....*....|....*....|...
gi 528485566    922 GRTLLHYAVEVGSKEIVKYIIDN 944
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDK 24
 
Name Accession Description Interval E-value
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 455-612 1.39e-73

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: 239.93  E-value: 1.39e-73
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485566    455 VFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGTAFSDFLMGSSKDLAKHIKVVCDGTDLTSKvqdLKLQCL 534
Cdd:smart00045    1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLP---NSLEGI 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485566    535 VFLNIPRYCAGTMPWGNPSEH-HDFEPQRHDDGCIEVIGFTMTSLA--TLQVGGHGERLNQCREV--TLTTFKSIPMQVD 609
Cdd:smart00045   78 AVLNIPSYGGGTNLWGTTDKEdLNFSKQSHDDGLLEVVGLTGAMHMaqIRQVGLAGRRIAQCSEVriTIKTSKTIPMQVD 157


                    ...
gi 528485566    610 GEP 612
Cdd:smart00045  158 GEP 160
DAGK_acc pfam00609
Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts ...
 455-612 9.78e-67

Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. This domain is assumed to be an accessory domain: its function is unknown.


Pssm-ID: 459866  Cd Length: 158  Bit Score: 220.94  E-value: 9.78e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485566   455 VFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGTAFSDFLMGSSKDLAKHIKVVCDGTDLTSKvqdLKLQCL 534
Cdd:pfam00609    1 VMNNYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDMFQRSCKNLIEKVELEVDGKDLPLP---KSLEGI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485566   535 VFLNIPRYCAGTMPWGNPSEHHD-FEPQRHDDGCIEVIGFT-MTSLATLQVGGHGE-RLNQCREVTLTTFKSIPMQVDGE 611
Cdd:pfam00609   78 VVLNIPSYAGGTDLWGNSKEDGLgFAPQSVDDGLLEVVGLTgALHLGQVQVGLGSAkRIAQGGPIRITTKKKIPMQVDGE 157


                   .
gi 528485566   612 P 612
Cdd:pfam00609  158 P 158
C1_DGKzeta_rpt2 cd20895
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta ...
 179-253 3.74e-52

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: 176.81  E-value: 3.74e-52
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528485566  179 VRHHWVHRRRQEGKCKQCGKGFQQKFAFHSKEIVAISCSWCKQAYHNKVTCFMLQQIEEPCSLGAHAAVIVPPTW 253
Cdd:cd20895     1 VRHHWVHRRRQEGKCRQCGKGFQQKFAFHSKEIVAISCSWCKQAYHSKVSCFMLQQIEEPCSLGAHAAVIVPPTW 75
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 306-427 3.98e-51

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: 175.56  E-value: 3.98e-51
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485566    306 LVFVNPKSGGNQGAKIIQTFLWYLNPRQVFDLSQGGPQEGLEMYRKVHN-LRILACGGDGTVGWILSALDQLQL-NPSPA 383
Cdd:smart00046    1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVPDfNRVLVCGGDGTVGWVLNALDKRELpLPEPP 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 528485566    384 VAVLPLGTGNDLARTLNWGGGYTDEPLSKILSHVEDGNIVQLDR 427
Cdd:smart00046   81 VAVLPLGTGNDLARSLGWGGGYDGEKLLKTLRDALESDTVKLDR 124
C1_DGKiota_rpt2 cd20896
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase iota ...
 179-253 4.58e-50

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: 170.66  E-value: 4.58e-50
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528485566  179 VRHHWVHRRRQEGKCKQCGKGFQQKFAFHSKEIVAISCSWCKQAYHNKVTCFMLQQIEEPCSLGAHAAVIVPPTW 253
Cdd:cd20896     1 VRHHWVHRRRQEGKCKQCGKGFQQKFSFHSKEIVAISCSWCKQAFHNKVTCFMLHHIEEPCSLGAHAAVIVPPTW 75
C1_DGKzeta_rpt1 cd20849
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta (DAG ...
 96-169 4.05e-49

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: 167.81  E-value: 4.05e-49
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528485566   96 DWSESAVYGEHIWFETNVSGDFCYVGEQHCYAKSLQKSVARKKCAACKIVVHSICIEQLEKINFRCKPSFRESG 169
Cdd:cd20849     1 DWSESAVYGEHIWFETNVSGDFCYVGEQNCVAKQLQKSVSRKKCAACKIVVHTPCIEQLEKINFRCKPSFRESG 74
C1_DGK_typeIV_rpt2 cd20855
second protein kinase C conserved region 1 (C1 domain) found in type IV diacylglycerol kinases; ...
 181-242 3.62e-42

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: 147.88  E-value: 3.62e-42
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528485566  181 HHWVHRRRQEGKCKQCGKGFQQKFAFHSKEIVAISCSWCKQAYHNKVTCFMLQQIEEPCSLG 242
Cdd:cd20855     1 HHWVHRRKQEGKCKQCGKSFQQKLSFSSKEIVAISCSWCKEAYHNKDSCFNMKKIEEPCNLG 62
C1_DGKiota_rpt1 cd20850
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase iota (DAG ...
 96-169 6.35e-37

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: 133.23  E-value: 6.35e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528485566   96 DWSESAVYGEHIWFETNVSGDFCYVGEQHCYAKsLQKSVARKKCAACKIVVHSICIEQLEKINFRCKPSFRESG 169
Cdd:cd20850     1 DWSENAVNGEHLWLETNVSGDLCYLGEENCQVK-FAKSALRRKCAACKIVVHTACIEQLEKINFRCKPTFREGG 73
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 304-426 2.83e-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: 127.32  E-value: 2.83e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485566   304 PLLVFVNPKSGGNQGAKIIQTFLWYLNPRQV-FDLSQ-GGPQEGLEMYRKV---HNLRILACGGDGTVGWILSALDQLQl 378
Cdd:pfam00781    1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVeVELVLtEGPGDALELAREAaedGYDRIVVAGGDGTVNEVLNGLAGLA- 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 528485566   379 nPSPAVAVLPLGTGNDLARTLNWGGgytdePLSKILSHVEDGNIVQLD 426
Cdd:pfam00781   80 -TRPPLGIIPLGTGNDFARALGIPG-----DPEEALEAILKGQTRPVD 121
C1_DGK_typeIV_rpt1 cd20802
first protein kinase C conserved region 1 (C1 domain) found in type IV diacylglycerol kinases; ...
 101-167 1.26e-33

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: 123.17  E-value: 1.26e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528485566  101 AVYGEHIWFETNVSGDFCYVGEQHCyakslQKSVARKKCAACKIVVHSICIEQLEKINFRCKPSFRE 167
Cdd:cd20802     1 AVNGEHLWTDTSASGDLCYVGEQDC-----LKSGSRKKCSACKIVVHTGCIPQLEKINFKCKPTFRE 62
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 302-628 1.63e-25

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


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 108.02  E-value: 1.63e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485566  302 MKPLLVFVNPKSGGNQGAKIIQTFLWYLNpRQVFDLSQ---GGPQEGLEMYRKVHNL---RILACGGDGTVGWILSALdq 375
Cdd:COG1597     2 MMRALLIVNPASGRGRAARLLERLVAALR-AAGLEVEVletESPGDATELAREAAAEgadLVVAAGGDGTVNEVANGL-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485566  376 lqLNPSPAVAVLPLGTGNDLARTLNwgggyTDEPLSKILSHVEDGNIVQLDrwnlvvkpnpeAGpeerdeQVTDKLpldv 455
Cdd:COG1597    79 --AGTGPPLGILPLGTGNDFARALG-----IPLDPEAALEALLTGRTRRID-----------LG------RVNGRY---- 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485566  456 FNNYFSLGFDAHVTLEFHESReanpekfnSRFRNKMFYAGTAFSdfLMGSSKdlAKHIKVVCDGTDLTSKVqdlkLQCLV 535
Cdd:COG1597   131 FLNVAGIGFDAEVVERANRAL--------KRRLGKLAYVLAALR--ALLRYR--PFRLRIELDGEEIEGEA----LLVAV 194

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485566  536 FlNIPRYcaGTMPWGNPSEhhdfepqRHDDGCIEVIGFT-------MTSLATLQVGGHGERLN----QCREVTLTTFKSI 604
Cdd:COG1597   195 G-NGPYY--GGGLRLAPDA-------SLDDGLLDVVVVRplsrlrlLRLLPRLLRGRHLRHPGvryfRAREVEIESDRPL 264

                         330       340
                  ....*....|....*....|....
gi 528485566  605 PMQVDGEPCKLAPSViHISLRNQA 628
Cdd:COG1597   265 PVQLDGEPLGLATPL-EFEVLPGA 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
882-1027 4.32e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 95.02  E-value: 4.32e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485566  882 VNNANSVSVDSLIECVKKKDHQKLKELHKKGADLCVQDPAGRTLLHYAVEVGSKEIVKYIIDN-APTDILDvtekENGET 960
Cdd:COG0666   113 VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAgADVNARD----NDGET 188

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528485566  961 VLHKAASLCHRTICHYLVEAGASLMKTDLQGDTPKHRAEKAKDAELAAYLENRQHYQMIQREDQETA 1027
Cdd:COG0666   189 PLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTA 255
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
881-1010 1.61e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 90.01  E-value: 1.61e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485566  881 AVNNANSVSVDSLIECVKKKDHQKLKELHKKGADLCVQDPAGRTLLHYAVEVGSKEIVKYIIDN-APTDILDvtekENGE 959
Cdd:COG0666    79 DINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAgADVNAQD----NDGN 154

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 528485566  960 TVLHKAASLCHRTICHYLVEAGASLMKTDLQGDTPKHRAEKAKDAELAAYL 1010
Cdd:COG0666   155 TPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
Ank_2 pfam12796
Ankyrin repeats (3 copies);
893-988 1.61e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.32  E-value: 1.61e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485566   893 LIECVKKKDHQKLKELHKKGADLCVQDPAGRTLLHYAVEVGSKEIVKYIIDNAptdilDVTEKENGETVLHKAASLCHRT 972
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-----DVNLKDNGRTALHYAARSGHLE 75

                           90
                   ....*....|....*.
gi 528485566   973 ICHYLVEAGASLMKTD 988
Cdd:pfam12796   76 IVKLLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
881-1010 1.09e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 69.98  E-value: 1.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485566  881 AVNNANSVSVDSLIECVKKKDHQKLKELHKKGADLCVQDPAGRTLLHYAVEVGSKEIVKYIIDN-APTDILDvtekENGE 959
Cdd:COG0666    46 ALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAgADVNARD----KDGE 121

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 528485566  960 TVLHKAASLCHRTICHYLVEAGASLMKTDLQGDTPKHRAEKAKDAELAAYL 1010
Cdd:COG0666   122 TPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172
C1_DGK_rpt2 cd20805
second protein kinase C conserved region 1 (C1 domain) found in the diacylglycerol kinase ...
 181-242 1.30e-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: 57.46  E-value: 1.30e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528485566  181 HHWVHRRRQ-EGKCKQCGKGFQQKFAFHSKeivaiSCSWCKQAYHNKvtCFMLQQIEEpCSLG 242
Cdd:cd20805     1 HHWVEGNLPsGAKCSVCGKKCGSSFGLAGY-----RCSWCKRTVHSE--CIDKLGPEE-CDLG 55
PRK12361 PRK12361
hypothetical protein; Provisional
 303-426 2.06e-08

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 58.09  E-value: 2.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485566  303 KPLLVFVNPKSGGNQGAKIIQTFLWYLNPRqvFDLS--QGGPQEGLEMYRKVHNLR----ILACGGDGTVGWILSALdql 376
Cdd:PRK12361  243 KRAWLIANPVSGGGKWQEYGEQIQRELKAY--FDLTvkLTTPEISAEALAKQARKAgadiVIACGGDGTVTEVASEL--- 317

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 528485566  377 qLNPSPAVAVLPLGTGNDLARTLnWGGGYTDEPLSKILSHVEDGNIVQLD 426
Cdd:PRK12361  318 -VNTDITLGIIPLGTANALSHAL-FGLGSKLIPVEQACDNIIQGHTQRID 365
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
 181-240 2.12e-08

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: 51.29  E-value: 2.12e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528485566   181 HHWVHRR-RQEGKCKQCGKGFqqkfafHSKEIVAISCSWCKQAYHNKvtCFMLQQIEEPCS 240
Cdd:pfam00130    1 HHFVHRNfKQPTFCDHCGEFL------WGLGKQGLKCSWCKLNVHKR--CHEKVPPECGCD 53
PRK13054 PRK13054
lipid kinase; Reviewed
 356-397 1.72e-07

lipid kinase; Reviewed


Pssm-ID: 237281 [Multi-domain]  Cd Length: 300  Bit Score: 54.11  E-value: 1.72e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 528485566  356 RILACGGDGTVGWILSALDQLQLNPSPAVAVLPLGTGNDLAR 397
Cdd:PRK13054   59 TVIAGGGDGTINEVATALAQLEGDARPALGILPLGTANDFAT 100
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 882-998 7.28e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 52.75  E-value: 7.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485566  882 VNNANSVSVDSLIECV-KKKDHQKL-KELHKKGADLCVQDPAGRTLLHYAVEVGS--KEIVKYIIDN------------- 944
Cdd:PHA03100   99 VNAPDNNGITPLLYAIsKKSNSYSIvEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKgvdinaknrvnyl 178

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 528485566  945 ----APTDILDvtekENGETVLHKAASLCHRTICHYLVEAGASLMKTDLQGDTPKHRA 998
Cdd:PHA03100  179 lsygVPINIKD----VYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIA 232
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 897-998 2.08e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 51.50  E-value: 2.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485566  897 VKKKDHQKLKELHKKGADLCVQDPAGRTLLHYAVEVGSKEIVKYIIDNAPtdilDVTEK-ENGETVLHKAAsLCHRTICH 975
Cdd:PHA02874  165 IKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGN----HIMNKcKNGFTPLHNAI-IHNRSAIE 239

                          90       100
                  ....*....|....*....|...
gi 528485566  976 YLVEaGASLMKTDLQGDTPKHRA 998
Cdd:PHA02874  240 LLIN-NASINDQDIDGSTPLHHA 261
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 882-998 4.91e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 50.35  E-value: 4.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485566  882 VNNANSVSVDSLIECVKKKDHQKLKELHKKGADLCVQDPAGRTLLHYAVEVGSKEIVKYIIDNAPtdILDVTEKeNGETV 961
Cdd:PHA02874  117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGA--YANVKDN-NGESP 193

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 528485566  962 LHKAASLCHRTICHYLVEAGASLMKTDLQGDTPKHRA 998
Cdd:PHA02874  194 LHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA 230
PRK13057 PRK13057
lipid kinase;
306-400 6.97e-06

lipid kinase;


Pssm-ID: 183857 [Multi-domain]  Cd Length: 287  Bit Score: 49.15  E-value: 6.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485566  306 LVFVNPKS--GGNQGAKIIQTF------LWYLNPRQVFDLSqggpqEGLEMYRKVHNLRILAcGGDGTVGWILSALDQLQ 377
Cdd:PRK13057    1 LLLVNRHArsGRAALAAARAALeaagleLVEPPAEDPDDLS-----EVIEAYADGVDLVIVG-GGDGTLNAAAPALVETG 74

                          90       100
                  ....*....|....*....|...
gi 528485566  378 LnpspAVAVLPLGTGNDLARTLN 400
Cdd:PRK13057   75 L----PLGILPLGTANDLARTLG 93
Ank_4 pfam13637
Ankyrin repeats (many copies);
893-942 2.68e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.65  E-value: 2.68e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 528485566   893 LIECVKKKDHQKLKELHKKGADLCVQDPAGRTLLHYAVEVGSKEIVKYII 942
Cdd:pfam13637    5 LHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 899-994 3.36e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 47.71  E-value: 3.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485566  899 KKDHQKLKELHKKGADLCVQDPAGRTLLHYAVEVGSKE---IVKYIIDNAPTDILDVtekeNGETVLHKAASLCHRTICH 975
Cdd:PHA03095  199 KPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrslVLPLLIAGISINARNR----YGQTPLHYAAVFNNPRACR 274

                          90
                  ....*....|....*....
gi 528485566  976 YLVEAGASLMKTDLQGDTP 994
Cdd:PHA03095  275 RLIALGADINAVSSDGNTP 293
Ank_4 pfam13637
Ankyrin repeats (many copies);
922-978 3.50e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.26  E-value: 3.50e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 528485566   922 GRTLLHYAVEVGSKEIVKYIIDNaPTDILDVTekENGETVLHKAASLCHRTICHYLV 978
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEK-GADINAVD--GNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 905-1010 3.51e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 47.71  E-value: 3.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485566  905 LKELHKKGADLCVQDPAGRTLLHYAVEV--GSKEIVKYII----DNAPTDILdvtekenGETVLHKAA--SLCHRTICHY 976
Cdd:PHA03095  170 LRLLIDAGADVYAVDDRFRSLLHHHLQSfkPRARIVRELIragcDPAATDML-------GNTPLHSMAtgSSCKRSLVLP 242

                          90       100       110
                  ....*....|....*....|....*....|....
gi 528485566  977 LVEAGASLMKTDLQGDTPKHRAEKAKDAELAAYL 1010
Cdd:PHA03095  243 LLIAGISINARNRYGQTPLHYAAVFNNPRACRRL 276
Ank_4 pfam13637
Ankyrin repeats (many copies);
960-1010 6.12e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.49  E-value: 6.12e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 528485566   960 TVLHKAASLCHRTICHYLVEAGASLMKTDLQGDTPKHRAEKAKDAELAAYL 1010
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 890-1010 1.03e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.11  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485566  890 VDSLIECVKKKDHQKLKELHKKGADLCVQDPAGRTLLHYAVEVGSKEIVKYIID-NAPTDILDVtekeNGETVLHKAASL 968
Cdd:PHA02874   92 VDTSILPIPCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEyGADVNIEDD----NGCYPIHIAIKH 167

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 528485566  969 CHRTICHYLVEAGASLMKTDLQGDTPKHRAEKAKDAELAAYL 1010
Cdd:PHA02874  168 NFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLL 209
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 893-986 1.12e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 46.16  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485566  893 LIECVKKKDHQKLKELHK-KGADLCVQDPAGRTLLHYAVEVGSKEIVKYIIDNAPTDI-LDVT-EKENGETVLHKAASLC 969
Cdd:cd22192    21 LLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVnEPMTsDLYQGETALHIAVVNQ 100

                          90
                  ....*....|....*..
gi 528485566  970 HRTICHYLVEAGASLMK 986
Cdd:cd22192   101 NLNLVRELIARGADVVS 117
C1_DGKepsilon_typeIII_rpt2 cd20853
second protein kinase C conserved region 1 (C1 domain) found in type III diacylglycerol kinase, ...
 181-251 1.52e-04

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


Pssm-ID: 410403  Cd Length: 63  Bit Score: 40.72  E-value: 1.52e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528485566  181 HHWVHrrrqeG------KCKQCGK--GFQQKFAFHSkeivaisCSWCKQAYHNKvtCfmLQQIEEPCSLGAHAAVIVPP 251
Cdd:cd20853     1 HHWVR-----GnlplcsVCCVCNEqcGNQPGLCDYR-------CCWCQRTVHDD--C--LAKLPKECDLGAFRNFIVPP 63
TIGR00147 TIGR00147
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ...
 356-399 1.65e-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: 44.80  E-value: 1.65e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 528485566   356 RILACGGDGTVGWILSALdqLQLNPSPAVAVLPLGTGNDLARTL 399
Cdd:TIGR00147   60 TVIAGGGDGTINEVVNAL--IQLDDIPALGILPLGTANDFARSL 101
PRK13055 PRK13055
putative lipid kinase; Reviewed
 357-400 1.98e-04

putative lipid kinase; Reviewed


Pssm-ID: 237282 [Multi-domain]  Cd Length: 334  Bit Score: 44.60  E-value: 1.98e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 528485566  357 ILACGGDGTVGWILSALdqLQLNPSPAVAVLPLGTGNDLARTLN 400
Cdd:PRK13055   63 IIAAGGDGTINEVVNGI--APLEKRPKMAIIPAGTTNDYARALK 104
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 880-998 6.41e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 43.50  E-value: 6.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485566  880 SAVNNANSVSVDSLIECVKKKDHQKLKELHKKGADLCVQDPAGRTLLHYAV--EVGSKEIVKYIIDNApTDILDVTekEN 957
Cdd:PHA03100   64 STKNNSTPLHYLSNIKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNG-ANVNIKN--SD 140

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 528485566  958 GETVLHKAASLCHRT-------ICH-----------YLVEAGASLMKTDLQGDTPKHRA 998
Cdd:PHA03100  141 GENLLHLYLESNKIDlkilkllIDKgvdinaknrvnYLLSYGVPINIKDVYGFTPLHYA 199
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 901-996 7.10e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 43.33  E-value: 7.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485566  901 DHQKLKELHKKGADLCVQDP-AGRTLLHYAVEVGSKEIVKY-IIDNAPTDILDVTEKengeTVLHKAASLCHRTICHYLV 978
Cdd:PHA02878  146 EAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELlLSYGANVNIPDKTNN----SPLHHAVKHYNKPIVHILL 221

                          90
                  ....*....|....*...
gi 528485566  979 EAGASLMKTDLQGDTPKH 996
Cdd:PHA02878  222 ENGASTDARDKCGNTPLH 239
PRK13059 PRK13059
putative lipid kinase; Reviewed
 302-400 7.99e-04

putative lipid kinase; Reviewed


Pssm-ID: 183858  Cd Length: 295  Bit Score: 42.72  E-value: 7.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485566  302 MKPLLVFVNPKSGGNQGA----KIIQTFLWYLNPRQVFDLSQGGP-QEGLEMYRKVHNLrILACGGDGTVGWILSALdqL 376
Cdd:PRK13059    1 MKKVKFIYNPYSGENAIIseldKVIRIHQEKGYLVVPYRISLEYDlKNAFKDIDESYKY-ILIAGGDGTVDNVVNAM--K 77

                          90       100
                  ....*....|....*....|....
gi 528485566  377 QLNPSPAVAVLPLGTGNDLARTLN 400
Cdd:PRK13059   78 KLNIDLPIGILPVGTANDFAKFLG 101
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 897-983 1.41e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 42.34  E-value: 1.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485566  897 VKKKDhqKLKELHKKGADLCVQDPAGRTLLHYAVEVGSKEIVKYIIDNApTDILDVTekENGETVLHKAASLCHRTICHY 976
Cdd:PHA03100  169 INAKN--RVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLG-ANPNLVN--KYGDTPLHIAILNNNKEIFKL 243


                  ....*..
gi 528485566  977 LVEAGAS 983
Cdd:PHA03100  244 LLNNGPS 250
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 922-944 1.86e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.80  E-value: 1.86e-03
                            10        20
                    ....*....|....*....|...
gi 528485566    922 GRTLLHYAVEVGSKEIVKYIIDN 944
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDK 24
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 922-944 2.09e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.47  E-value: 2.09e-03
                           10        20
                   ....*....|....*....|...
gi 528485566   922 GRTLLHYAVEVGSKEIVKYIIDN 944
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLEN 24
 
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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