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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990601   203 PIMVIVNPKSGSGAGKQLLRNFRAHLHPAQV-VDVLKSNIAAS----LRWIDEHpNVDvRILIAGGDGTICSALDQIDTL 277
Cdd:pfam00781   1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVeVELVLTEGPGDalelAREAAED-GYD-RIVVAGGDGTVNEVLNGLAGL 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 71990601   278 SRRIPVAVLPLGTGNDLSRLLKWGKKCDGDIDVIkLMEDIQEAEVTLV 325
Cdd:pfam00781  79 ATRPPLGIIPLGTGNDFARALGIPGDPEEALEAI-LKGQTRPVDVGKV 125

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

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 71990601  44 KSGHYWSSINYSEQHNYCSGCKEHIVSGYECDNCLLKVDNiNCLRAVSTKIQCKV 98
Cdd:cd20801   1 SKGHHWVSTDLFSKPTYCSVCETLILSGAFCDCCGLCVDE-GCLRKADKRFPCKA 54

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990601   350 MTNYVSVGVDACVTLGMQNTRESIPRAMSSRLLNKFLFFTFGTKDVFERVCKGLNERIDLYLDDVHVNLP-DIEGLIFLN 428
Cdd:pfam00609   2 MNNYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDMFQRSCKNLIEKVELEVDGKDLPLPkSLEGIVVLN 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71990601   429 IPYWGAGVKPWAT----YNDSHRQECDDEMIEVFAVTSSFHIAQMQIGLASPLCIGQAKHAKLVFKGNhsFPMQSDGEA 503
Cdd:pfam00609  82 IPSYAGGTDLWGNskedGLGFAPQSVDDGLLEVVGLTGALHLGQVQVGLGSAKRIAQGGPIRITTKKK--IPMQVDGEP 158

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990601    206 VIVNPKSGSGAGKQLLRNFRAHLHPAQVVDVLKSNIAASLRWIDEHPNvDVRILIAGGDGTI---CSALDQIDTLSRRIP 282
Cdd:smart00046   2 VFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVPD-FNRVLVCGGDGTVgwvLNALDKRELPLPEPP 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 71990601    283 VAVLPLGTGNDLSRLLKWGKKCDGDIDVIKLMEDIqEAEVTLVDR 327
Cdd:smart00046  81 VAVLPLGTGNDLARSLGWGGGYDGEKLLKTLRDAL-ESDTVKLDR 124

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990601 202 RPIMVIVNPKSGSGAGKQLLRNFRAHLHPAQV-VDVLKSNIAASL-RWIDEH--PNVDVrILIAGGDGTICSALDQIdtL 277
Cdd:COG1597   3 MRALLIVNPASGRGRAARLLERLVAALRAAGLeVEVLETESPGDAtELAREAaaEGADL-VVAAGGDGTVNEVANGL--A 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990601 278 SRRIPVAVLPLGTGNDLSRLLKWgkkcdgDIDVIKLMEDIQEAEVTLVDrwtidaesqkkLGV---RLqsnktlsMTNYV 354
Cdd:COG1597  80 GTGPPLGILPLGTGNDFARALGI------PLDPEAALEALLTGRTRRID-----------LGRvngRY-------FLNVA 135

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990601 355 SVGVDACVTLGMQntresiprAMSSRLLNKFLFFTFGTKDVFERvcKGLneRIDLYLDDVHVnlpDIEGLIFL--NIPYW 432
Cdd:COG1597 136 GIGFDAEVVERAN--------RALKRRLGKLAYVLAALRALLRY--RPF--RLRIELDGEEI---EGEALLVAvgNGPYY 200

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71990601 433 GAGVKPwatyndSHRQECDDEMIEVFAVTsSFHIAQMqIGLASPLCIGQAKHA---------KLVFKGNHSFPMQSDGE 502
Cdd:COG1597 201 GGGLRL------APDASLDDGLLDVVVVR-PLSRLRL-LRLLPRLLRGRHLRHpgvryfrarEVEIESDRPLPVQLDGE 271

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

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 71990601    110 HHWICGNIGADLFCEVCEELCGGVGLQDFRCSWCWRVVHTKCKPKFTKHC 159
Cdd:smart00109   1 HKHVFRTFTKPTFCCVCRKSIWGSFKQGLRCSECKVKCHKKCADKVPKAC 50

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

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 71990601   110 HHWICGNIGADLFCEVCEELCGGVGLQDFRCSWCWRVVHTKCKPKFTKHCDFG 162
Cdd:pfam00130   1 HHFVHRNFKQPTFCDHCGEFLWGLGKQGLKCSWCKLNVHKRCHEKVPPECGCD 53

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990601   350 MTNYVSVGVDACVTLGMQNTRESIPRAMSSRLLNKFLFFTFGTKDVFERVCKGLNERIDLYLDDVHVNLP-DIEGLIFLN 428
Cdd:pfam00609   2 MNNYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDMFQRSCKNLIEKVELEVDGKDLPLPkSLEGIVVLN 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71990601   429 IPYWGAGVKPWAT----YNDSHRQECDDEMIEVFAVTSSFHIAQMQIGLASPLCIGQAKHAKLVFKGNhsFPMQSDGEA 503
Cdd:pfam00609  82 IPSYAGGTDLWGNskedGLGFAPQSVDDGLLEVVGLTGALHLGQVQVGLGSAKRIAQGGPIRITTKKK--IPMQVDGEP 158

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990601    206 VIVNPKSGSGAGKQLLRNFRAHLHPAQVVDVLKSNIAASLRWIDEHPNvDVRILIAGGDGTI---CSALDQIDTLSRRIP 282
Cdd:smart00046   2 VFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVPD-FNRVLVCGGDGTVgwvLNALDKRELPLPEPP 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 71990601    283 VAVLPLGTGNDLSRLLKWGKKCDGDIDVIKLMEDIqEAEVTLVDR 327
Cdd:smart00046  81 VAVLPLGTGNDLARSLGWGGGYDGEKLLKTLRDAL-ESDTVKLDR 124

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990601 202 RPIMVIVNPKSGSGAGKQLLRNFRAHLHPAQV-VDVLKSNIAASL-RWIDEH--PNVDVrILIAGGDGTICSALDQIdtL 277
Cdd:COG1597   3 MRALLIVNPASGRGRAARLLERLVAALRAAGLeVEVLETESPGDAtELAREAaaEGADL-VVAAGGDGTVNEVANGL--A 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990601 278 SRRIPVAVLPLGTGNDLSRLLKWgkkcdgDIDVIKLMEDIQEAEVTLVDrwtidaesqkkLGV---RLqsnktlsMTNYV 354
Cdd:COG1597  80 GTGPPLGILPLGTGNDFARALGI------PLDPEAALEALLTGRTRRID-----------LGRvngRY-------FLNVA 135

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990601 355 SVGVDACVTLGMQntresiprAMSSRLLNKFLFFTFGTKDVFERvcKGLneRIDLYLDDVHVnlpDIEGLIFL--NIPYW 432
Cdd:COG1597 136 GIGFDAEVVERAN--------RALKRRLGKLAYVLAALRALLRY--RPF--RLRIELDGEEI---EGEALLVAvgNGPYY 200

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71990601 433 GAGVKPwatyndSHRQECDDEMIEVFAVTsSFHIAQMqIGLASPLCIGQAKHA---------KLVFKGNHSFPMQSDGE 502
Cdd:COG1597 201 GGGLRL------APDASLDDGLLDVVVVR-PLSRLRL-LRLLPRLLRGRHLRHpgvryfrarEVEIESDRPLPVQLDGE 271

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.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 71990601 110 HHWICGNIGADLFCEVCEELCGGV-GLQDFRCSWCWRVVHTKCKPKFTKH-CDFG 162
Cdd:cd20805   1 HHWVEGNLPSGAKCSVCGKKCGSSfGLAGYRCSWCKRTVHSECIDKLGPEeCDLG 55

second protein kinase C conserved region 1 (C1 domain) found in type II diacylglycerol kinases; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. Type II DAG kinases (DGKs) contain pleckstrin homology (PH) and sterile alpha motifs (SAM) domains, in addition to C1 and catalytic domains that are present in all DGKs. The SAM domain mediates oligomerization of type II DGKs. Three DGK isozymes (delta, eta and kappa) are classified as type II. DAG kinase delta, also called 130 kDa DAG kinase, or diglyceride kinase delta (DGK-delta), is a residential lipid kinase in the endoplasmic reticulum. It promotes lipogenesis and is involved in triglyceride biosynthesis. DAG kinase eta, also called diglyceride kinase eta (DGK-eta), plays a key role in promoting cell growth. The DAG kinase eta gene, DGKH, is a replicated risk gene of bipolar disorder (BPD). DAG kinase kappa is also called diglyceride kinase kappa (DGK-kappa) or 142 kDa DAG kinase. 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.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 71990601 110 HHWICGNIGADLFCEVCEELCGGV-GLQDFRCSWCWRVVHTKCKPKFTKHCDFG 162
Cdd:cd20852   1 HQWLEGNLPVSSKCAVCDKTCGSVlRLQDWRCLWCGATVHTACKDSLPTKCSLG 54

second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase eta (DAG kinase eta) and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase eta, also called diglyceride kinase eta (DGK-eta), plays a key role in promoting cell growth. It is classified as a type II DAG kinase (DGK), containing pleckstrin homology (PH) and sterile alpha motifs (SAM) domains, in addition to C1 and catalytic domains that are present in all DGKs. The SAM domain mediates oligomerization of type II DGKs. The diacylglycerol kinase eta gene, DGKH, is a replicated risk gene of bipolar disorder (BPD). DAG kinase eta 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.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 71990601 110 HHWICGNIGADLFCEVCEELCGGV-GLQDFRCSWCWRVVHTKCKPKFTKHCDFG 162
Cdd:cd20894   6 HQWLEGNLPVSAKCSVCDKTCGSVlRLQDWRCLWCKAMVHTACKDQYPRKCPLG 59

lipid kinase;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990601  205 MVIVNPKSGSGagKQLLRNFRAHLHPAQVVDVLKSNIAAS--LRWIDEHPN-VDvRILIAGGDGTICSALDQIdtLSRRI 281
Cdd:PRK13057   1 LLLVNRHARSG--RAALAAARAALEAAGLELVEPPAEDPDdlSEVIEAYADgVD-LVIVGGGDGTLNAAAPAL--VETGL 75

                         90
                 ....*....|....*..
gi 71990601  282 PVAVLPLGTGNDLSRLL 298
Cdd:PRK13057  76 PLGILPLGTANDLARTL 92

protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains. It contains the motif HX12CX2CXnCX2CX4HX2CX7C, where C and H are cysteine and histidine, respectively; X represents other residues; and n is either 13 or 14. C1 has a globular fold with two separate Zn(2+)-binding sites. It was originally discovered as lipid-binding modules in protein kinase C (PKC) isoforms. C1 domains that bind and respond to phorbol esters (PE) and diacylglycerol (DAG) are referred to as typical, and those that do not respond to PE and DAG are deemed atypical. A C1 domain may also be referred to as PKC or non-PKC C1, based on the parent protein's activity. Most C1 domain-containing non-PKC proteins act as lipid kinases and scaffolds, except PKD which acts as a protein kinase. PKC C1 domains play roles in membrane translocation and activation of the enzyme.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 71990601 110 HHWICGNIGADLFCEVCEELCGGVGLQDFRCSWCWRVVHTKCKPKFTKHC 159
Cdd:cd00029   1 HRFVPTTFSSPTFCDVCGKLIWGLFKQGLKCSDCGLVCHKKCLDKAPSPC 50

putative lipid kinase; Reviewed

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 71990601  258 ILIAGGDGTICSALDQIDTLSRRIPVAVLPLGTGNDLSRLL 298
Cdd:PRK13059  60 ILIAGGDGTVDNVVNAMKKLNIDLPIGILPVGTANDFAKFL 100

lipid kinase; Reviewed

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990601  202 RPIMVIVNPKSgsgAGKQLLR----NFRAHLHPAQV-VDVLKSNIAaslRWIDE--HPNVDvRILIAGGDGTI---CSAL 271
Cdd:PRK13054   4 PKSLLILNGKS---AGNEELReavgLLREEGHTLHVrVTWEKGDAA---RYVEEalALGVA-TVIAGGGDGTInevATAL 76

                         90       100
                 ....*....|....*....|....*.
gi 71990601  272 DQIDTLSRriPV-AVLPLGTGNDLSR 296
Cdd:PRK13054  77 AQLEGDAR--PAlGILPLGTANDFAT 100

first protein kinase C conserved region 1 (C1 domain) found in type II diacylglycerol kinases; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. Type II DAG kinases (DGKs) contain pleckstrin homology (PH) and sterile alpha motifs (SAM) domains, in addition to C1 and catalytic domains that are present in all DGKs. The SAM domain mediates oligomerization of type II DGKs. Three DGK isozymes (delta, eta and kappa) are classified as type II. DAG kinase delta, also called 130 kDa DAG kinase, or diglyceride kinase delta (DGK-delta), is a residential lipid kinase in the endoplasmic reticulum. It promotes lipogenesis and is involved in triglyceride biosynthesis. DAG kinase eta, also called diglyceride kinase eta (DGK-eta), plays a key role in promoting cell growth. The DAG kinase eta gene, DGKH, is a replicated risk gene of bipolar disorder (BPD). DAG kinase kappa is also called diglyceride kinase kappa (DGK-kappa) or 142 kDa DAG kinase. 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.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 71990601 110 HHWICGNIGADLFCEVCEELCGGVGLQDFRCSWCWRVVHTKCKPKFTKHC 159
Cdd:cd20800   5 HNWYACSHARPTYCNVCREALSGVTSHGLSCEVCKFKAHKRCAVKAPNNC 54

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.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 71990601 110 HHWICGNIGADlfCEVCEELCG-GVGLQDFRCSWCWRVVHTKCKPKFTKHCDFG 162
Cdd:cd20851   1 HHWVEGNCPGK--CDKCHKSIKsYQGLTGLHCVWCHITLHNKCASHVKPECDLG 52

first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) theta, delta, and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domains. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. 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.

                        10        20        30
                ....*....|....*....|....*....|....*...
gi 71990601 122 FCEVCEELCGGVGLQDFRCSWCWRVVHTKCKPKFTKHC 159
Cdd:cd20834  20 FCSVCKEFLWGFNKQGYQCRQCNAAVHKKCHDKILGKC 57

first protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) protein kinase C (cPKC), novel protein kinase C (nPKC), and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domains. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. nPKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs (aPKCs) only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. This family includes classical PKCs (cPKCs) and novel PKCs (nPKCs). There are four cPKC isoforms (named alpha, betaI, betaII, and gamma) and four nPKC isoforms (delta, epsilon, eta, and theta). 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.

                        10        20        30
                ....*....|....*....|....*....|....*...
gi 71990601 122 FCEVCEELCGGVGLQDFRCSWCWRVVHTKCKPKFTKHC 159
Cdd:cd20792  14 FCSHCKDFIWGLGKQGYQCQVCRFVVHKRCHEYVVFKC 51

protein kinase C conserved region 1 (C1 domain) found in uncharacterized proteins similar to myotubularin-related proteins; The family includes a group of uncharacterized proteins that show high sequence similarity to vertebrate myotubularin-related proteins (MTMRs), such as MTMR5 and MTMR13. MTMRs may function as guanine nucleotide exchange factors (GEFs). Vertebrate MTMR5 and MTMR13 contain an N-terminal DENN domain, a PH-GRAM domain, an inactive PTP domain, a SET interaction domain, a coiled-coil domain, and a C-terminal PH domain. Members of this family contain these domains and have an additional C1 domain. This model corresponds to the C1 domain. 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.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 71990601 107 TFDHHWICGNIGADLFCEVCEELCGGVGLQDFRCSWCWRVVHTKCKPKFTKHC 159
Cdd:cd20828   3 TQPHNFEPHSFVTPTNCDYCLQILWGIVKKGMKCSECGYNCHEKCQPQVPKQC 55

first 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 first 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.

                        10        20        30
                ....*....|....*....|....*....|....*...
gi 71990601 122 FCEVCEELCGGVGLQDFRCSWCWRVVHTKCKPKFTKHC 159
Cdd:cd20799  18 YCNVCENMLVGLRKQGLCCTFCKYTVHERCVSRAPASC 55