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Conserved domains on  [gi|1834198586|ref|NP_001368977|]
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retinal degeneration A, isoform L [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 969-1123 1.06e-76

Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. DAG can be produced from the hydrolysis of phosphatidylinositol 4,5-bisphosphate (PIP2) by a phosphoinositide-specific phospholipase C and by the degradation of phosphatidylcholine (PC) by a phospholipase C or the concerted actions of phospholipase D and phosphatidate phosphohydrolase. This domain might either be an accessory domain or else contribute to the catalytic domain. Bacterial homologues are known.


:

Pssm-ID: 214486  Cd Length: 160  Bit Score: 250.72  E-value: 1.06e-76
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198586   969 VINNYFSFGVDAHIALEFHEAREAHPERFNSRLRNKMYYGQMGGKDLILRQYRNLSQWVTLECDGQDFTGKLrdaGCHAV 1048
Cdd:smart00045    1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLPN---SLEGI 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198586  1049 LFLNIPSYGGGTHPWNDS----FGASKPSIDDGLMEVVGLTTYQLP--MLQAGMHGTCICQCRKAR--IITKRTIPMQVD 1120
Cdd:smart00045   78 AVLNIPSYGGGTNLWGTTdkedLNFSKQSHDDGLLEVVGLTGAMHMaqIRQVGLAGRRIAQCSEVRitIKTSKTIPMQVD 157


                    ...
gi 1834198586  1121 GEA 1123
Cdd:smart00045  158 GEP 160
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 814-942 5.85e-53

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: 181.34  E-value: 5.85e-53
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198586   814 IVFINPKSGGNQGHKLLGKFQHLLNPRQVFDLTQGGPKMGLDMFRKAPN-LRVLACGGDGTVGWVLSVLDQIQPPLqPAP 892
Cdd:smart00046    1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVPDfNRVLVCGGDGTVGWVLNALDKRELPL-PEP 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|
gi 1834198586   893 AVGVLPLGTGNDLARALGWGGsiffqGYTDEPIGKILREIGMSQCVLMDR 942
Cdd:smart00046   80 PVAVLPLGTGNDLARSLGWGG-----GYDGEKLLKTLRDALESDTVKLDR 124
C1_DGK_typeIV_rpt2 cd20855
second protein kinase C conserved region 1 (C1 domain) found in type IV diacylglycerol kinases; ...
 661-727 2.87e-31

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: 117.06  E-value: 2.87e-31
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1834198586  661 HHWVHRKLEKGKCKQCGKFFpmkqavQSKL-FGSKEIVALACAWCHEIYHNKEACFNQAKIGEECRLG 727
Cdd:cd20855      1 HHWVHRRKQEGKCKQCGKSF------QQKLsFSSKEIVAISCSWCKEAYHNKDSCFNMKKIEEPCNLG 62
C1_DGK_typeIV_rpt1 cd20802
first protein kinase C conserved region 1 (C1 domain) found in type IV diacylglycerol kinases; ...
 586-647 3.61e-29

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: 110.85  E-value: 3.61e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1834198586  586 AVQGEHYWKPTSASGDLCCLNE-ECIKSGQRMKCSACQLVAHHNCIPFVNEKStLACKPTYRD 647
Cdd:cd20802      1 AVNGEHLWTDTSASGDLCYVGEqDCLKSGSRKKCSACKIVVHTGCIPQLEKIN-FKCKPTFRE 62
 
Name Accession Description Interval E-value
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 969-1123 1.06e-76

Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. DAG can be produced from the hydrolysis of phosphatidylinositol 4,5-bisphosphate (PIP2) by a phosphoinositide-specific phospholipase C and by the degradation of phosphatidylcholine (PC) by a phospholipase C or the concerted actions of phospholipase D and phosphatidate phosphohydrolase. This domain might either be an accessory domain or else contribute to the catalytic domain. Bacterial homologues are known.


Pssm-ID: 214486  Cd Length: 160  Bit Score: 250.72  E-value: 1.06e-76
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198586   969 VINNYFSFGVDAHIALEFHEAREAHPERFNSRLRNKMYYGQMGGKDLILRQYRNLSQWVTLECDGQDFTGKLrdaGCHAV 1048
Cdd:smart00045    1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLPN---SLEGI 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198586  1049 LFLNIPSYGGGTHPWNDS----FGASKPSIDDGLMEVVGLTTYQLP--MLQAGMHGTCICQCRKAR--IITKRTIPMQVD 1120
Cdd:smart00045   78 AVLNIPSYGGGTNLWGTTdkedLNFSKQSHDDGLLEVVGLTGAMHMaqIRQVGLAGRRIAQCSEVRitIKTSKTIPMQVD 157


                    ...
gi 1834198586  1121 GEA 1123
Cdd:smart00045  158 GEP 160
DAGK_acc pfam00609
Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts ...
 969-1123 2.41e-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: 223.63  E-value: 2.41e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198586  969 VINNYFSFGVDAHIALEFHEAREAHPERFNSRLRNKMYYGQMGGKDLILRQYRNLSQWVTLECDGQDFtgKLRdAGCHAV 1048
Cdd:pfam00609    1 VMNNYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDMFQRSCKNLIEKVELEVDGKDL--PLP-KSLEGI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198586 1049 LFLNIPSYGGGTHPWNDSF----GASKPSIDDGLMEVVGLT-TYQLPMLQAGMH-GTCICQCRKARIITKRTIPMQVDGE 1122
Cdd:pfam00609   78 VVLNIPSYAGGTDLWGNSKedglGFAPQSVDDGLLEVVGLTgALHLGQVQVGLGsAKRIAQGGPIRITTKKKIPMQVDGE 157


                   .
gi 1834198586 1123 A 1123
Cdd:pfam00609  158 P 158
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 814-942 5.85e-53

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: 181.34  E-value: 5.85e-53
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198586   814 IVFINPKSGGNQGHKLLGKFQHLLNPRQVFDLTQGGPKMGLDMFRKAPN-LRVLACGGDGTVGWVLSVLDQIQPPLqPAP 892
Cdd:smart00046    1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVPDfNRVLVCGGDGTVGWVLNALDKRELPL-PEP 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|
gi 1834198586   893 AVGVLPLGTGNDLARALGWGGsiffqGYTDEPIGKILREIGMSQCVLMDR 942
Cdd:smart00046   80 PVAVLPLGTGNDLARSLGWGG-----GYDGEKLLKTLRDALESDTVKLDR 124
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 812-915 3.11e-36

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


Pssm-ID: 425868 [Multi-domain]  Cd Length: 125  Bit Score: 133.48  E-value: 3.11e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198586  812 PVIVFINPKSGGNQGHKLLGKFQHLLNPRQV-FDLTQ-GGPKMGLDMFRKAPNL---RVLACGGDGTVGWVLSVLDQIQP 886
Cdd:pfam00781    1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVeVELVLtEGPGDALELAREAAEDgydRIVVAGGDGTVNEVLNGLAGLAT 80

                           90       100
                   ....*....|....*....|....*....
gi 1834198586  887 PlqpaPAVGVLPLGTGNDLARALGWGGSI 915
Cdd:pfam00781   81 R----PPLGIIPLGTGNDFARALGIPGDP 105
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 813-1140 5.13e-32

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


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 127.28  E-value: 5.13e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198586  813 VIVFINPKSGGNQGHKLLGKFQHLLNPR----QVFDLTQGGPkmGLDMFRKAPNL---RVLACGGDGTVGWVLSVLDQIQ 885
Cdd:COG1597      5 ALLIVNPASGRGRAARLLERLVAALRAAglevEVLETESPGD--ATELAREAAAEgadLVVAAGGDGTVNEVANGLAGTG 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198586  886 PPLqpapavGVLPLGTGNDLARALGwggsiffqgyTDEPIGKILREIGMSQCVLMDRWRVkvtpnddvtDDHVdrskpnv 965
Cdd:COG1597     83 PPL------GILPLGTGNDFARALG----------IPLDPEAALEALLTGRTRRIDLGRV---------NGRY------- 130

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198586  966 plnVINNyFSFGVDAHIALEFHEAReahperfnSRLRNKMYYGQMGGKdlILRQYRNLSqwVTLECDGQDFTGKlrdagC 1045
Cdd:COG1597    131 ---FLNV-AGIGFDAEVVERANRAL--------KRRLGKLAYVLAALR--ALLRYRPFR--LRIELDGEEIEGE-----A 189

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198586 1046 HAVLFLNIPSYGGGTHPwndsfgASKPSIDDGLMEVVGLTT-------YQLPMLQAGMHGTC----ICQCRKARIITKRT 1114
Cdd:COG1597    190 LLVAVGNGPYYGGGLRL------APDASLDDGLLDVVVVRPlsrlrllRLLPRLLRGRHLRHpgvrYFRAREVEIESDRP 263

                          330       340
                   ....*....|....*....|....*.
gi 1834198586 1115 IPMQVDGEACRVKPSViEIELLNKAL 1140
Cdd:COG1597    264 LPVQLDGEPLGLATPL-EFEVLPGAL 288
C1_DGK_typeIV_rpt2 cd20855
second protein kinase C conserved region 1 (C1 domain) found in type IV diacylglycerol kinases; ...
 661-727 2.87e-31

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: 117.06  E-value: 2.87e-31
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1834198586  661 HHWVHRKLEKGKCKQCGKFFpmkqavQSKL-FGSKEIVALACAWCHEIYHNKEACFNQAKIGEECRLG 727
Cdd:cd20855      1 HHWVHRRKQEGKCKQCGKSF------QQKLsFSSKEIVAISCSWCKEAYHNKDSCFNMKKIEEPCNLG 62
C1_DGK_typeIV_rpt1 cd20802
first protein kinase C conserved region 1 (C1 domain) found in type IV diacylglycerol kinases; ...
 586-647 3.61e-29

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: 110.85  E-value: 3.61e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1834198586  586 AVQGEHYWKPTSASGDLCCLNE-ECIKSGQRMKCSACQLVAHHNCIPFVNEKStLACKPTYRD 647
Cdd:cd20802      1 AVNGEHLWTDTSASGDLCYVGEqDCLKSGSRKKCSACKIVVHTGCIPQLEKIN-FKCKPTFRE 62
TIGR00147 TIGR00147
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ...
 817-1133 1.03e-10

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: 64.45  E-value: 1.03e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198586  817 INPKSGGNQGHKLLGKFQHLLNPRQVFDLTQGGPKMGLDMF-----RKAPNLRVLACGGDGTVGWVLSVLDqiqpPLQPA 891
Cdd:TIGR00147    8 LNPTAGKSNDNKPLREVIMLLREEGMEIHVRVTWEKGDAARyveeaRKFGVDTVIAGGGDGTINEVVNALI----QLDDI 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198586  892 PAVGVLPLGTGNDLARALGWGGSIffqgytDEPIGKILREIGMSqcvlmdrwrvkvtpnddvtddhVDRSKPNVPLNVIn 971
Cdd:TIGR00147   84 PALGILPLGTANDFARSLGIPEDL------DKAAKLVIAGDARA----------------------IDMGQVNKQYCFI- 134

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198586  972 NYFSFGVDAHIALEFheareahPERFNSRLRNKMYYgqmggkdliLRQYRNLS--QWVTLECDGQDFTGKLrdagcHAVL 1049
Cdd:TIGR00147  135 NMAGGGFGTEITTET-------PEKLKAALGSLSYI---------LSGLMRMDtlQPFRCEIRGEGEHWQG-----EAVV 193

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198586 1050 FL--NIPSYGGGTHPWNDSfgaskpSIDDGLMEVVGLTTYQL-------PMLQAGMH----GTCICQCRKARIITKRTIP 1116
Cdd:TIGR00147  194 FLvgNGRQAGGGQKLAPDA------SINDGLLDLRIFTNDNLlpalvltLMSDEGKHtdnpNIIYGKASRIDIQTPHKIT 267

                          330
                   ....*....|....*..
gi 1834198586 1117 MQVDGEACRVKPSVIEI 1133
Cdd:TIGR00147  268 FNLDGEPLGGTPFHIEI 284
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
 591-640 2.38e-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: 51.67  E-value: 2.38e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1834198586  591 HYWKPTS-ASGDLCCLNEECI--KSGQRMKCSACQLVAHHNCIPFVNEKSTLA 640
Cdd:pfam00130    1 HHFVHRNfKQPTFCDHCGEFLwgLGKQGLKCSWCKLNVHKRCHEKVPPECGCD 53
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
 661-725 3.23e-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: 3.23e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1834198586  661 HHWVHRKLEK-GKCKQCGKFFPMKqavqsklfgskEIVALACAWCHEIYHNKeaCFNQAKIGEECR 725
Cdd:pfam00130    1 HHFVHRNFKQpTFCDHCGEFLWGL-----------GKQGLKCSWCKLNVHKR--CHEKVPPECGCD 53
PRK13054 PRK13054
lipid kinase; Reviewed
 864-910 8.61e-07

lipid kinase; Reviewed


Pssm-ID: 237281 [Multi-domain]  Cd Length: 300  Bit Score: 52.57  E-value: 8.61e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1834198586  864 RVLACGGDGTVGWVLSVLDQIQPPLQpaPAVGVLPLGTGNDLARALG 910
Cdd:PRK13054    59 TVIAGGGDGTINEVATALAQLEGDAR--PALGILPLGTANDFATAAG 103
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
 590-635 1.04e-06

Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.


Pssm-ID: 197519  Cd Length: 50  Bit Score: 46.69  E-value: 1.04e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1834198586   590 EHYWKPTSASGDLCCLNEECIKSG--QRMKCSACQLVAHHNCIPFVNE 635
Cdd:smart00109    1 HKHVFRTFTKPTFCCVCRKSIWGSfkQGLRCSECKVKCHKKCADKVPK 48
 
Name Accession Description Interval E-value
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 969-1123 1.06e-76

Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. DAG can be produced from the hydrolysis of phosphatidylinositol 4,5-bisphosphate (PIP2) by a phosphoinositide-specific phospholipase C and by the degradation of phosphatidylcholine (PC) by a phospholipase C or the concerted actions of phospholipase D and phosphatidate phosphohydrolase. This domain might either be an accessory domain or else contribute to the catalytic domain. Bacterial homologues are known.


Pssm-ID: 214486  Cd Length: 160  Bit Score: 250.72  E-value: 1.06e-76
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198586   969 VINNYFSFGVDAHIALEFHEAREAHPERFNSRLRNKMYYGQMGGKDLILRQYRNLSQWVTLECDGQDFTGKLrdaGCHAV 1048
Cdd:smart00045    1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLPN---SLEGI 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198586  1049 LFLNIPSYGGGTHPWNDS----FGASKPSIDDGLMEVVGLTTYQLP--MLQAGMHGTCICQCRKAR--IITKRTIPMQVD 1120
Cdd:smart00045   78 AVLNIPSYGGGTNLWGTTdkedLNFSKQSHDDGLLEVVGLTGAMHMaqIRQVGLAGRRIAQCSEVRitIKTSKTIPMQVD 157


                    ...
gi 1834198586  1121 GEA 1123
Cdd:smart00045  158 GEP 160
DAGK_acc pfam00609
Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts ...
 969-1123 2.41e-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: 223.63  E-value: 2.41e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198586  969 VINNYFSFGVDAHIALEFHEAREAHPERFNSRLRNKMYYGQMGGKDLILRQYRNLSQWVTLECDGQDFtgKLRdAGCHAV 1048
Cdd:pfam00609    1 VMNNYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDMFQRSCKNLIEKVELEVDGKDL--PLP-KSLEGI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198586 1049 LFLNIPSYGGGTHPWNDSF----GASKPSIDDGLMEVVGLT-TYQLPMLQAGMH-GTCICQCRKARIITKRTIPMQVDGE 1122
Cdd:pfam00609   78 VVLNIPSYAGGTDLWGNSKedglGFAPQSVDDGLLEVVGLTgALHLGQVQVGLGsAKRIAQGGPIRITTKKKIPMQVDGE 157


                   .
gi 1834198586 1123 A 1123
Cdd:pfam00609  158 P 158
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 814-942 5.85e-53

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: 181.34  E-value: 5.85e-53
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198586   814 IVFINPKSGGNQGHKLLGKFQHLLNPRQVFDLTQGGPKMGLDMFRKAPN-LRVLACGGDGTVGWVLSVLDQIQPPLqPAP 892
Cdd:smart00046    1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVPDfNRVLVCGGDGTVGWVLNALDKRELPL-PEP 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|
gi 1834198586   893 AVGVLPLGTGNDLARALGWGGsiffqGYTDEPIGKILREIGMSQCVLMDR 942
Cdd:smart00046   80 PVAVLPLGTGNDLARSLGWGG-----GYDGEKLLKTLRDALESDTVKLDR 124
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 812-915 3.11e-36

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


Pssm-ID: 425868 [Multi-domain]  Cd Length: 125  Bit Score: 133.48  E-value: 3.11e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198586  812 PVIVFINPKSGGNQGHKLLGKFQHLLNPRQV-FDLTQ-GGPKMGLDMFRKAPNL---RVLACGGDGTVGWVLSVLDQIQP 886
Cdd:pfam00781    1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVeVELVLtEGPGDALELAREAAEDgydRIVVAGGDGTVNEVLNGLAGLAT 80

                           90       100
                   ....*....|....*....|....*....
gi 1834198586  887 PlqpaPAVGVLPLGTGNDLARALGWGGSI 915
Cdd:pfam00781   81 R----PPLGIIPLGTGNDFARALGIPGDP 105
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 813-1140 5.13e-32

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


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 127.28  E-value: 5.13e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198586  813 VIVFINPKSGGNQGHKLLGKFQHLLNPR----QVFDLTQGGPkmGLDMFRKAPNL---RVLACGGDGTVGWVLSVLDQIQ 885
Cdd:COG1597      5 ALLIVNPASGRGRAARLLERLVAALRAAglevEVLETESPGD--ATELAREAAAEgadLVVAAGGDGTVNEVANGLAGTG 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198586  886 PPLqpapavGVLPLGTGNDLARALGwggsiffqgyTDEPIGKILREIGMSQCVLMDRWRVkvtpnddvtDDHVdrskpnv 965
Cdd:COG1597     83 PPL------GILPLGTGNDFARALG----------IPLDPEAALEALLTGRTRRIDLGRV---------NGRY------- 130

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198586  966 plnVINNyFSFGVDAHIALEFHEAReahperfnSRLRNKMYYGQMGGKdlILRQYRNLSqwVTLECDGQDFTGKlrdagC 1045
Cdd:COG1597    131 ---FLNV-AGIGFDAEVVERANRAL--------KRRLGKLAYVLAALR--ALLRYRPFR--LRIELDGEEIEGE-----A 189

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198586 1046 HAVLFLNIPSYGGGTHPwndsfgASKPSIDDGLMEVVGLTT-------YQLPMLQAGMHGTC----ICQCRKARIITKRT 1114
Cdd:COG1597    190 LLVAVGNGPYYGGGLRL------APDASLDDGLLDVVVVRPlsrlrllRLLPRLLRGRHLRHpgvrYFRAREVEIESDRP 263

                          330       340
                   ....*....|....*....|....*.
gi 1834198586 1115 IPMQVDGEACRVKPSViEIELLNKAL 1140
Cdd:COG1597    264 LPVQLDGEPLGLATPL-EFEVLPGAL 288
C1_DGK_typeIV_rpt2 cd20855
second protein kinase C conserved region 1 (C1 domain) found in type IV diacylglycerol kinases; ...
 661-727 2.87e-31

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: 117.06  E-value: 2.87e-31
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1834198586  661 HHWVHRKLEKGKCKQCGKFFpmkqavQSKL-FGSKEIVALACAWCHEIYHNKEACFNQAKIGEECRLG 727
Cdd:cd20855      1 HHWVHRRKQEGKCKQCGKSF------QQKLsFSSKEIVAISCSWCKEAYHNKDSCFNMKKIEEPCNLG 62
C1_DGK_typeIV_rpt1 cd20802
first protein kinase C conserved region 1 (C1 domain) found in type IV diacylglycerol kinases; ...
 586-647 3.61e-29

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: 110.85  E-value: 3.61e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1834198586  586 AVQGEHYWKPTSASGDLCCLNE-ECIKSGQRMKCSACQLVAHHNCIPFVNEKStLACKPTYRD 647
Cdd:cd20802      1 AVNGEHLWTDTSASGDLCYVGEqDCLKSGSRKKCSACKIVVHTGCIPQLEKIN-FKCKPTFRE 62
C1_DGKiota_rpt2 cd20896
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase iota ...
 661-738 1.77e-26

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: 103.63  E-value: 1.77e-26
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1834198586  661 HHWVHRKLEKGKCKQCGKFFPMKQAvqsklFGSKEIVALACAWCHEIYHNKEACFNQAKIGEECRLGNYAPIIVPPSW 738
Cdd:cd20896      3 HHWVHRRRQEGKCKQCGKGFQQKFS-----FHSKEIVAISCSWCKQAFHNKVTCFMLHHIEEPCSLGAHAAVIVPPTW 75
C1_DGKzeta_rpt2 cd20895
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta ...
 661-738 4.15e-26

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: 102.85  E-value: 4.15e-26
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1834198586  661 HHWVHRKLEKGKCKQCGKFFPMKQAvqsklFGSKEIVALACAWCHEIYHNKEACFNQAKIGEECRLGNYAPIIVPPSW 738
Cdd:cd20895      3 HHWVHRRRQEGKCRQCGKGFQQKFA-----FHSKEIVAISCSWCKQAYHSKVSCFMLQQIEEPCSLGAHAAVIVPPTW 75
C1_DGKiota_rpt1 cd20850
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase iota (DAG ...
 581-649 5.92e-20

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: 85.08  E-value: 5.92e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1834198586  581 DWTENAVQGEHYWKPTSASGDLCCLNEE-CI----KSGQRMKCSACQLVAHHNCIPFVnEKSTLACKPTYRDVG 649
Cdd:cd20850      1 DWSENAVNGEHLWLETNVSGDLCYLGEEnCQvkfaKSALRRKCAACKIVVHTACIEQL-EKINFRCKPTFREGG 73
C1_DGKzeta_rpt1 cd20849
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta (DAG ...
 581-649 8.15e-16

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: 73.43  E-value: 8.15e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1834198586  581 DWTENAVQGEHYWKPTSASGDLCCLNEE-CI-----KSGQRMKCSACQLVAHHNCIPFVnEKSTLACKPTYRDVG 649
Cdd:cd20849      1 DWSESAVYGEHIWFETNVSGDFCYVGEQnCVakqlqKSVSRKKCAACKIVVHTPCIEQL-EKINFRCKPSFRESG 74
TIGR00147 TIGR00147
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ...
 817-1133 1.03e-10

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: 64.45  E-value: 1.03e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198586  817 INPKSGGNQGHKLLGKFQHLLNPRQVFDLTQGGPKMGLDMF-----RKAPNLRVLACGGDGTVGWVLSVLDqiqpPLQPA 891
Cdd:TIGR00147    8 LNPTAGKSNDNKPLREVIMLLREEGMEIHVRVTWEKGDAARyveeaRKFGVDTVIAGGGDGTINEVVNALI----QLDDI 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198586  892 PAVGVLPLGTGNDLARALGWGGSIffqgytDEPIGKILREIGMSqcvlmdrwrvkvtpnddvtddhVDRSKPNVPLNVIn 971
Cdd:TIGR00147   84 PALGILPLGTANDFARSLGIPEDL------DKAAKLVIAGDARA----------------------IDMGQVNKQYCFI- 134

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198586  972 NYFSFGVDAHIALEFheareahPERFNSRLRNKMYYgqmggkdliLRQYRNLS--QWVTLECDGQDFTGKLrdagcHAVL 1049
Cdd:TIGR00147  135 NMAGGGFGTEITTET-------PEKLKAALGSLSYI---------LSGLMRMDtlQPFRCEIRGEGEHWQG-----EAVV 193

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198586 1050 FL--NIPSYGGGTHPWNDSfgaskpSIDDGLMEVVGLTTYQL-------PMLQAGMH----GTCICQCRKARIITKRTIP 1116
Cdd:TIGR00147  194 FLvgNGRQAGGGQKLAPDA------SINDGLLDLRIFTNDNLlpalvltLMSDEGKHtdnpNIIYGKASRIDIQTPHKIT 267

                          330
                   ....*....|....*..
gi 1834198586 1117 MQVDGEACRVKPSVIEI 1133
Cdd:TIGR00147  268 FNLDGEPLGGTPFHIEI 284
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
 591-640 2.38e-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: 51.67  E-value: 2.38e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1834198586  591 HYWKPTS-ASGDLCCLNEECI--KSGQRMKCSACQLVAHHNCIPFVNEKSTLA 640
Cdd:pfam00130    1 HHFVHRNfKQPTFCDHCGEFLwgLGKQGLKCSWCKLNVHKRCHEKVPPECGCD 53
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
 661-725 3.23e-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: 3.23e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1834198586  661 HHWVHRKLEK-GKCKQCGKFFPMKqavqsklfgskEIVALACAWCHEIYHNKeaCFNQAKIGEECR 725
Cdd:pfam00130    1 HHFVHRNFKQpTFCDHCGEFLWGL-----------GKQGLKCSWCKLNVHKR--CHEKVPPECGCD 53
C1_DGK_rpt2 cd20805
second protein kinase C conserved region 1 (C1 domain) found in the diacylglycerol kinase ...
 661-727 1.56e-07

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: 49.37  E-value: 1.56e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1834198586  661 HHWVHRKLEKG-KCKQCGKffpmkqavqsKLFGSKEIVALACAWCHEIYHNKeaCFNQAKIgEECRLG 727
Cdd:cd20805      1 HHWVEGNLPSGaKCSVCGK----------KCGSSFGLAGYRCSWCKRTVHSE--CIDKLGP-EECDLG 55
PRK13054 PRK13054
lipid kinase; Reviewed
 864-910 8.61e-07

lipid kinase; Reviewed


Pssm-ID: 237281 [Multi-domain]  Cd Length: 300  Bit Score: 52.57  E-value: 8.61e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1834198586  864 RVLACGGDGTVGWVLSVLDQIQPPLQpaPAVGVLPLGTGNDLARALG 910
Cdd:PRK13054    59 TVIAGGGDGTINEVATALAQLEGDAR--PALGILPLGTANDFATAAG 103
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
 590-635 1.04e-06

Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.


Pssm-ID: 197519  Cd Length: 50  Bit Score: 46.69  E-value: 1.04e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1834198586   590 EHYWKPTSASGDLCCLNEECIKSG--QRMKCSACQLVAHHNCIPFVNE 635
Cdd:smart00109    1 HKHVFRTFTKPTFCCVCRKSIWGSfkQGLRCSECKVKCHKKCADKVPK 48
PRK12361 PRK12361
hypothetical protein; Provisional
 815-916 2.50e-06

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 51.93  E-value: 2.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198586  815 VFINPKSGGNQGHKLLGKFQHLLNPRqvFDLT--QGGPKMGLDMFRKAPNLR----VLACGGDGTVGWVLSVLDQIQPPL 888
Cdd:PRK12361   247 LIANPVSGGGKWQEYGEQIQRELKAY--FDLTvkLTTPEISAEALAKQARKAgadiVIACGGDGTVTEVASELVNTDITL 324

                           90       100
                   ....*....|....*....|....*....
gi 1834198586  889 qpapavGVLPLGTGNDLARAL-GWGGSIF 916
Cdd:PRK12361   325 ------GIIPLGTANALSHALfGLGSKLI 347
PRK13057 PRK13057
lipid kinase;
864-910 5.08e-06

lipid kinase;


Pssm-ID: 183857 [Multi-domain]  Cd Length: 287  Bit Score: 49.92  E-value: 5.08e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1834198586  864 RVLACGGDGTVGWVLSVLDQIQPPLqpapavGVLPLGTGNDLARALG 910
Cdd:PRK13057    53 LVIVGGGDGTLNAAAPALVETGLPL------GILPLGTANDLARTLG 93
C1_DGKepsilon_typeIII_rpt2 cd20853
second protein kinase C conserved region 1 (C1 domain) found in type III diacylglycerol kinase, ...
 661-736 9.68e-05

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: 41.49  E-value: 9.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198586  661 HHWVHRKLEKG-KC----KQCGkffpmkqaVQSKLfgskeiVALACAWCHEIYHNKeaCFnqAKIGEECRLGNYAPIIVP 735
Cdd:cd20853      1 HHWVRGNLPLCsVCcvcnEQCG--------NQPGL------CDYRCCWCQRTVHDD--CL--AKLPKECDLGAFRNFIVP 62


                   .
gi 1834198586  736 P 736
Cdd:cd20853     63 P 63
PRK13055 PRK13055
putative lipid kinase; Reviewed
 865-909 1.85e-04

putative lipid kinase; Reviewed


Pssm-ID: 237282 [Multi-domain]  Cd Length: 334  Bit Score: 45.37  E-value: 1.85e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1834198586  865 VLACGGDGTVGWVLSVLdqiqPPLQPAPAVGVLPLGTGNDLARAL 909
Cdd:PRK13055    63 IIAAGGDGTINEVVNGI----APLEKRPKMAIIPAGTTNDYARAL 103
PRK00861 PRK00861
putative lipid kinase; Reviewed
 818-910 1.17e-03

putative lipid kinase; Reviewed


Pssm-ID: 234850 [Multi-domain]  Cd Length: 300  Bit Score: 42.69  E-value: 1.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198586  818 NPKSGGNQGHKLLGKFQHLLNPRQVFDLTQGGPKMGLDMFRKAPNLR----VLACGGDGTVGWVLSVLDQIQPPLqpapa 893
Cdd:PRK00861    10 NPVAGQGNPEVDLALIRAILEPEMDLDIYLTTPEIGADQLAQEAIERgaelIIASGGDGTLSAVAGALIGTDIPL----- 84

                           90
                   ....*....|....*..
gi 1834198586  894 vGVLPLGTGNDLARALG 910
Cdd:PRK00861    85 -GIIPRGTANAFAAALG 100
C1_DGK_typeI_like_rpt2 cd20851
second protein kinase C conserved region 1 (C1 domain) found in type I diacylglycerol kinases; ...
 661-727 1.39e-03

second protein kinase C conserved region 1 (C1 domain) found in type I diacylglycerol kinases; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. Type I DAG kinases (DGKs) contain EF-hand structures that bind Ca(2+) and recoverin homology domains, in addition to C1 and catalytic domains that are present in all DGKs. Type I DGKs, regulated by calcium binding, include three DGK isozymes (alpha, beta and gamma). DAG kinase alpha, also called 80 kDa DAG kinase, or diglyceride kinase alpha (DGK-alpha), is active upon cell stimulation, initiating the resynthesis of phosphatidylinositols and attenuating protein kinase C activity. DAG kinase beta, also called 90 kDa DAG kinase, or diglyceride kinase beta (DGK-beta), exhibits high phosphorylation activity for long-chain diacylglycerols. DAG kinase gamma, also called diglyceride kinase gamma (DGK-gamma), reverses the normal flow of glycerolipid biosynthesis by phosphorylating diacylglycerol back to phosphatidic acid. Members of this family contain two copies of the C1 domain. This model corresponds to the second one. DGK-alpha contains atypical C1 domains, while DGK-beta and DGK-gamma contain typical C1 domains that bind DAG and phorbol esters. 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: 410401  Cd Length: 52  Bit Score: 38.10  E-value: 1.39e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1834198586  661 HHWVHRKLEkGKCKQCGKFFPMKQAVQsklfgskeivALACAWCHEIYHNKeaCFNQakIGEECRLG 727
Cdd:cd20851      1 HHWVEGNCP-GKCDKCHKSIKSYQGLT----------GLHCVWCHITLHNK--CASH--VKPECDLG 52
PRK13059 PRK13059
putative lipid kinase; Reviewed
 865-915 6.52e-03

putative lipid kinase; Reviewed


Pssm-ID: 183858  Cd Length: 295  Bit Score: 40.41  E-value: 6.52e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1834198586  865 VLACGGDGTVGWVLSVLDQ--IQPPLqpapavGVLPLGTGNDLARALGWGGSI 915
Cdd:PRK13059    60 ILIAGGDGTVDNVVNAMKKlnIDLPI------GILPVGTANDFAKFLGMPTDI 106
C1_DGKalpha_rpt2 cd20890
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase alpha ...
 661-736 9.57e-03

second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase alpha (DAG kinase alpha) and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase alpha, also called 80 kDa diacylglycerol kinase, or diglyceride kinase alpha (DGK-alpha), converts the second messenger diacylglycerol into phosphatidate upon cell stimulation, initiating the resynthesis of phosphatidylinositols and attenuating protein kinase C activity. It is classified as a type I DAG kinase (DGK), containing EF-hand structures that bind Ca(2+) and a recoverin homology domain, in addition to C1 and catalytic domains that are present in all DGKs. As a type I DGK, it is regulated by calcium binding. DAG kinase alpha 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: 410440  Cd Length: 62  Bit Score: 35.98  E-value: 9.57e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1834198586  661 HHWVHRKLEKGKCKQCgkffpmkqavQSKLFGSKEIVALACAWCHEIYHNkeACFNQakIGEECRLGNYAPIIVPP 736
Cdd:cd20890      1 HVWVSGGCESSKCDKC----------QKKIKSFQSLTGLHCVWCHLKRHD--ECLSS--VPSTCDCGPLRDHILPP 62
 
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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