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 1622845375  477 LVFVNPKSGGKQGQRVLWKFQYILNPRQVFNLLKDGPEIGLRLFKDVP-DGRILVCGGDGTVGWILETIDKANLPVL-PP 554
Cdd:smart00046   1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVPdFNRVLVCGGDGTVGWVLNALDKRELPLPePP 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1622845375  555 VAVLPLGTGNDLARCLRWGGGYEGQNLAKILKDLETSKVVHMDR 598
Cdd:smart00046  81 VAVLPLGTGNDLARSLGWGGGYDGEKLLKTLRDALESDTVKLDR 124

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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622845375 369 HVWVRGGCESGRCDRCQKKIRIYHSLTGLHCVWCHLEIHDDCLQAVGHECDCGLLRDHILPP 430
Cdd:cd20890     1 HVWVSGGCESSKCDKCQKKIKSFQSLTGLHCVWCHLKRHDECLSSVPSTCDCGPLRDHILPP 62

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845375 167 KLEFTFKLYDTDRNGILDssvswgpcmlgkgicvhlsapscpyfsrvlrnrrgwgerlspvglnLKEvdkiilqMMRVAE 246
Cdd:cd00051     1 ELREAFRLFDKDGDGTIS----------------------------------------------ADE-------LKAALK 27

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1622845375 247 YLDWDVSElrPILQEMMKEIDYDGSGSVSQAEWVRA 282
Cdd:cd00051    28 SLGEGLSE--EEIDEMIREVDKDGDGKIDFEEFLEL 61

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 1622845375 619 IINNYFSIGVDASIAHRFHIMREKYPEKFNSRMKNKLWYFEFATSESIFSTCKKLEESLTVEICGKPLDLSnLSLEGIAV 698
Cdd:pfam00609   1 VMNNYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDMFQRSCKNLIEKVELEVDGKDLPLP-KSLEGIVV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845375 699 LNIPSMHGGSNLWGDTRKPHgdiyginqalgatakvitdpdiLKTCVPDLSDKRLEVVGLEGAIEMGQIYTKLKNAgRRL 778
Cdd:pfam00609  80 LNIPSYAGGTDLWGNSKEDG----------------------LGFAPQSVDDGLLEVVGLTGALHLGQVQVGLGSA-KRI 136

                         170       180
                  ....*....|....*....|..
gi 1622845375 779 AKCSEITFHTTKTLPMQIDGEP 800
Cdd:pfam00609 137 AQGGPIRITTKKKIPMQVDGEP 158

Diacylglycerol kinase N-terminus; This domain is found at the N-terminus of diacylglycerol kinases.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845375   4 ERGLISPSDFAQLQKYMESssvalssvllrcahdwereeremgrcarsrlsthlrctwtacsssqrrgvksdSTKKVSDV 83
Cdd:pfam14513   1 EWVSLSPEEFAQLQKYAEY-----------------------------------------------------SSKKLKDV 27

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845375  84 LKLF-EDGEMAKYVQGDAIGYEGFQQFLKIYLEVDnVPRHLSLALFQSFKTDHCLNEANVTK------------------ 144
Cdd:pfam14513  28 LEEFnEDGVLAKYNPEEPIDYEGFKLFMKTYLEVD-LPEDLCQHLFLSFQTKPSQESPDSPKegasssvkagfdknpssl 106

                         170       180
                  ....*....|....*....|....*....
gi 1622845375 145 ----------DVVCLNDVSCYFSLLEGGR 163
Cdd:pfam14513 107 ppapsspsasPVVYLKDVSCYLSLLEGGR 135

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 1622845375 475 PLLVFVNPKSGGKQGQRVLWKFQYILNPRQV-FNLLK-DGPEIGLRLFKDVPDG---RILVCGGDGTVGWILETIDKANL 549
Cdd:pfam00781   1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVeVELVLtEGPGDALELAREAAEDgydRIVVAGGDGTVNEVLNGLAGLAT 80

                          90       100
                  ....*....|....*....|....*
gi 1622845375 550 PvlPPVAVLPLGTGNDLARCLRWGG 574
Cdd:pfam00781  81 R--PPLGIIPLGTGNDFARALGIPG 103

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845375 476 LLVFVNPKSGGKQGQRVLWKFQYILNpRQVFNLL-------KDGPEIGLRLFKDVPDgRILVCGGDGTVGWILETIDKAN 548
Cdd:COG1597     5 ALLIVNPASGRGRAARLLERLVAALR-AAGLEVEvletespGDATELAREAAAEGAD-LVVAAGGDGTVNEVANGLAGTG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845375 549 lpvlPPVAVLPLGTGNDLARCLRWgggyeGQNLAKILKDLETSKVVHMDrwsveVIpqqteeKSDPVPFqiINNyFSIGV 628
Cdd:COG1597    83 ----PPLGILPLGTGNDFARALGI-----PLDPEAALEALLTGRTRRID-----LG------RVNGRYF--LNV-AGIGF 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845375 629 DASIAHRfhimrekypekFNSRMKNKL-W--YFeFATSESIFSTcKKLEesLTVEICGKPLDLSNLSlegIAVLNIPSMH 705
Cdd:COG1597   140 DAEVVER-----------ANRALKRRLgKlaYV-LAALRALLRY-RPFR--LRIELDGEEIEGEALL---VAVGNGPYYG 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845375 706 GGSNLWGDtrkphgdiyginqalgatakvitdpdilktcvPDLSDKRLEVVGLE--GAIEMGQIYTKLKNaGR------- 776
Cdd:COG1597   202 GGLRLAPD--------------------------------ASLDDGLLDVVVVRplSRLRLLRLLPRLLR-GRhlrhpgv 248

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1622845375 777 RLAKCSEITFHTTKTLPMQIDGEP-WMQTPCTIKITHK 813
Cdd:COG1597   249 RYFRAREVEIESDRPLPVQLDGEPlGLATPLEFEVLPG 286

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 1622845375 369 HVWVRGG-CESGRCDRCQKKIRiYHSLTGLHCVWCHLEIHDDCLQAVGHECDCG 421
Cdd:pfam00130   1 HHFVHRNfKQPTFCDHCGEFLW-GLGKQGLKCSWCKLNVHKRCHEKVPPECGCD 53

putative lipid kinase; Reviewed

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845375 481 NPKSGGKqgqRVLWKFQYILNPRQVFNLL------KDGPEIGLrLFKDVPDGR--ILVCGGDGTVGWILETIDKANLPVl 552
Cdd:PRK13059    9 NPYSGEN---AIISELDKVIRIHQEKGYLvvpyriSLEYDLKN-AFKDIDESYkyILIAGGDGTVDNVVNAMKKLNIDL- 83

                          90
                  ....*....|....*...
gi 1622845375 553 pPVAVLPLGTGNDLARCL 570
Cdd:PRK13059   84 -PIGILPVGTANDFAKFL 100

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 1622845375  367 QSHVWVRGGcESGRCDRCQKKIRIYHsLTGLHCVWCHLEIHDDCLQAVGHEC 418
Cdd:smart00109   1 HKHVFRTFT-KPTFCCVCRKSIWGSF-KQGLRCSECKVKCHKKCADKVPKAC 50

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 1622845375 619 IINNYFSIGVDASIAHRFHIMREKYPEKFNSRMKNKLWYFEFATSESIFSTCKKLEESLTVEICGKPLDLSnLSLEGIAV 698
Cdd:pfam00609   1 VMNNYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDMFQRSCKNLIEKVELEVDGKDLPLP-KSLEGIVV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845375 699 LNIPSMHGGSNLWGDTRKPHgdiyginqalgatakvitdpdiLKTCVPDLSDKRLEVVGLEGAIEMGQIYTKLKNAgRRL 778
Cdd:pfam00609  80 LNIPSYAGGTDLWGNSKEDG----------------------LGFAPQSVDDGLLEVVGLTGALHLGQVQVGLGSA-KRI 136

                         170       180
                  ....*....|....*....|..
gi 1622845375 779 AKCSEITFHTTKTLPMQIDGEP 800
Cdd:pfam00609 137 AQGGPIRITTKKKIPMQVDGEP 158

Diacylglycerol kinase N-terminus; This domain is found at the N-terminus of diacylglycerol kinases.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845375   4 ERGLISPSDFAQLQKYMESssvalssvllrcahdwereeremgrcarsrlsthlrctwtacsssqrrgvksdSTKKVSDV 83
Cdd:pfam14513   1 EWVSLSPEEFAQLQKYAEY-----------------------------------------------------SSKKLKDV 27

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845375  84 LKLF-EDGEMAKYVQGDAIGYEGFQQFLKIYLEVDnVPRHLSLALFQSFKTDHCLNEANVTK------------------ 144
Cdd:pfam14513  28 LEEFnEDGVLAKYNPEEPIDYEGFKLFMKTYLEVD-LPEDLCQHLFLSFQTKPSQESPDSPKegasssvkagfdknpssl 106

                         170       180
                  ....*....|....*....|....*....
gi 1622845375 145 ----------DVVCLNDVSCYFSLLEGGR 163
Cdd:pfam14513 107 ppapsspsasPVVYLKDVSCYLSLLEGGR 135

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 1622845375 475 PLLVFVNPKSGGKQGQRVLWKFQYILNPRQV-FNLLK-DGPEIGLRLFKDVPDG---RILVCGGDGTVGWILETIDKANL 549
Cdd:pfam00781   1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVeVELVLtEGPGDALELAREAAEDgydRIVVAGGDGTVNEVLNGLAGLAT 80

                          90       100
                  ....*....|....*....|....*
gi 1622845375 550 PvlPPVAVLPLGTGNDLARCLRWGG 574
Cdd:pfam00781  81 R--PPLGIIPLGTGNDFARALGIPG 103

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 1622845375 369 HVWVRGGCEsGRCDRCQKKIRIYHSLTGLHCVWCHLEIHDDCLQAVGHECDCG 421
Cdd:cd20851     1 HHWVEGNCP-GKCDKCHKSIKSYQGLTGLHCVWCHITLHNKCASHVKPECDLG 52

first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase beta (DAG kinase beta) and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase beta, also called 90 kDa diacylglycerol kinase, or diglyceride kinase beta (DGK-beta), exhibits high phosphorylation activity for long-chain diacylglycerols. 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 beta contains two copies of the C1 domain. This model corresponds to the first one. DGK-beta contains 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        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622845375 298 TLKDDGQHMWRPKRFPRPVYCNLCESS-IGLGKQGLSCNLCKYTVHDQCAMKALPCEVSTYAKSRK 362
Cdd:cd20845     1 NVKDDGQHVWRLKHFNKPAYCNLCLNMlVGLGKQGLCCSFCKYTVHERCVQRAPASCIKTYVKSKK 66

second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase beta (DAG kinase beta) and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase beta, also called 90 kDa diacylglycerol kinase, or diglyceride kinase beta (DGK-beta), exhibits high phosphorylation activity for long-chain diacylglycerols. 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 beta contains two copies of the C1 domain. This model corresponds to the second one. DGK-beta contains 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 1622845375 369 HVWVRGGCESgRCDRCQKKIRIYHSLTGLHCVWCHLEIHDDCLQAVGHECDCGLLRDH 426
Cdd:cd20891     3 HFWVEGNCPT-KCDKCHKTIKCYQGLTGLHCVWCQITLHNKCASHVKPECDCGPLKDH 59

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 1622845375 369 HVWVRGGCESG-RCDRCQKKIRIYHSLTGLHCVWCHLEIHDDCLQAVGH-ECDCG 421
Cdd:cd20805     1 HHWVEGNLPSGaKCSVCGKKCGSSFGLAGYRCSWCKRTVHSECIDKLGPeECDLG 55

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        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845375 301 DDGQHMWRPKRFPRPVYCNLCESSI-GLGKQGLSCNLCKYTVHDQCAMKAL-PCEVSTYA 358
Cdd:cd20800     1 LSGSHNWYACSHARPTYCNVCREALsGVTSHGLSCEVCKFKAHKRCAVKAPnNCKWTTLA 60

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 1622845375 305 HMWRPKRFPRPVYCNLCESSI-GLGKQGLSCNLCKYTVHDQCAMKA-LPC 352
Cdd:cd00029     1 HRFVPTTFSSPTFCDVCGKLIwGLFKQGLKCSDCGLVCHKKCLDKApSPC 50

protein kinase C conserved region 1 (C1 domain) found in Schizosaccharomyces pombe protein BZZ1 and similar proteins; BZZ1 is a syndapin-like F-BAR protein that plays a role in endocytosis and trafficking to the vacuole. It functions with type I myosins to restore polarity of the actin cytoskeleton after NaCl stress. BZZ1 contains an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs), a central coiled-coil, and two C-terminal SH3 domains. Schizosaccharomyces pombe BZZ1 also harbors a C1 domain, but Saccharomyces cerevisiae BZZ1 doesn't have any. 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
                  ....*....|....*....|....*....|....*....|....*....
gi 1622845375 304 QHMWRPKRFPRPVYCNLCESSI-GLGKQGLSCNLCKYTVHDQCAMKALP 351
Cdd:cd20824     1 PHNFKPHSFSIPTKCDYCGEKIwGLSKKGLSCKDCGFNCHIKCELKVPP 49

first 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 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 1622845375 303 GQHMWRPKRFPRPVYCNLCESSI-GLGKQGLSCNLCKYTVHDQCAMKAL-PCEVSTYA 358
Cdd:cd20848    28 GMHNWYACSHARPTFCNVCRESLsGVTSHGLSCEVCKFKAHKRCAVRATnNCKWTTLA 85

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        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1622845375 305 HMWRPKRFPRPVYCNLCESSI-GLGKQGLSCNLCKYTVHDQCAMKAL 350
Cdd:cd20834     8 HEFIAKFFRQPTFCSVCKEFLwGFNKQGYQCRQCNAAVHKKCHDKIL 54

protein kinase C conserved region 1 (C1 domain) found in myotonic dystrophy kinase-related Cdc42-binding kinase gamma (MRCK gamma) and similar proteins; MRCK gamma (MRCKG), also called Cdc42-binding protein kinase gamma, DMPK-like gamma, myotonic dystrophy protein kinase-like gamma, or myotonic dystrophy protein kinase-like alpha, is a serine/threonine-protein kinase expressed in heart and skeletal muscles. It may act as a downstream effector of Cdc42 in cytoskeletal reorganization and contributes to the actomyosin contractility required for cell invasion, through the regulation of MYPT1 and thus MLC2 phosphorylation. 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.

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                  ....*....|....*....|....*....|....*....|....*....
gi 1622845375 305 HMWRPKRFPRPVYCNLCES-SIGLGKQGLSCNLCKYTVHDQCAMKALPC 352
Cdd:cd20866     1 HTFKPKTFTSPTKCLRCTSlMVGLVRQGLACEACNYVCHVSCAEGAPIC 49

protein kinase C conserved region 1 (C1 domain) found in the atypical protein kinase C (aPKC) family; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. They contain a C2-like region, instead of a calcium-binding (C2) region found in classical PKCs, in their regulatory domain. There are two aPKC isoforms, zeta and iota. aPKCs are involved in many cellular functions including proliferation, migration, apoptosis, polarity maintenance and cytoskeletal regulation. They also play a critical role in the regulation of glucose metabolism and in the pathogenesis of type 2 diabetes. PKC-zeta plays a critical role in activating the glucose transport response. It is activated by glucose, insulin, and exercise through diverse pathways. PKC-zeta also plays a central role in maintaining cell polarity in yeast and mammalian cells. In addition, it affects actin remodeling in muscle cells. PKC-iota is directly implicated in carcinogenesis. It is critical to oncogenic signaling mediated by Ras and Bcr-Abl. The PKC-iota gene is the target of tumor-specific gene amplification in many human cancers, and has been identified as a human oncogene. In addition to its role in transformed growth, PKC-iota also promotes invasion, chemoresistance, and tumor cell survival. Expression profiling of PKC-iota is a prognostic marker of poor clinical outcome in several human cancers. PKC-iota also plays a role in establishing cell polarity, and has critical embryonic functions. Members of this family contain one 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.

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                  ....*....|....*....|....*....|....*....|..
gi 1622845375 305 HMWRPKRFPRPVYCNLCESSI-GLGKQGLSCNLCKYTVHDQC 345
Cdd:cd20794     3 HLFQAKRFNRRAVCAYCSDRIwGLGRQGYKCINCKLLVHKKC 44

protein kinase C conserved region 1 (C1 domain) found in tensin-3 (TNS3) variant and similar proteins; Tensin-3 (TNS3), also called tensin-like SH2 domain-containing protein 1 (TENS1), or tumor endothelial marker 6 (TEM6), may play a role in actin remodeling. It is involved in the dissociation of the integrin-tensin-actin complex. This model corresponds to the C1 domain found in TNS3 variant. Typical TNS3 does not contain 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.

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                  ....*....|....*....|....*....|....*....|....*....
gi 1622845375 305 HMWRPKRFPRPVYCNLCESSIGlgKQGLSCNLCKYTVHDQCAMKAL-PC 352
Cdd:cd20889     3 HTFKNKTFKKPKVCSICKQVID--SQGISCRVCKYACHKKCEAKVVtPC 49

first protein kinase C conserved region 1 (C1 domain) found in the classical (or conventional) protein kinase C (cPKC) family; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domains. cPKCs are potent kinases for histones, myelin basic protein, and protamine. They depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. PKC-alpha is expressed in many tissues and is associated with cell proliferation, apoptosis, and cell motility. It plays a role in the signaling of the growth factors PDGF, VEGF, EGF, and FGF. Abnormal levels of PKC-alpha have been detected in many transformed cell lines and several human tumors. In addition, PKC-alpha is required for HER2 dependent breast cancer invasion. The PKC beta isoforms (I and II), generated by alternative splicing of a single gene, are preferentially activated by hyperglycemia-induced DAG (1,2-diacylglycerol) in retinal tissues. This is implicated in diabetic microangiopathy such as ischemia, neovascularization, and abnormal vasodilator function. PKC-beta also plays an important role in VEGF signaling. In addition, glucose regulates proliferation in retinal endothelial cells via PKC-betaI. PKC-beta is also being explored as a therapeutic target in cancer. It contributes to tumor formation and is involved in the tumor host mechanisms of inflammation and angiogenesis. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia. 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.

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                  ....*....|....*....|....*....|....*....|..
gi 1622845375 305 HMWRPKRFPRPVYCNLCESSI-GLGKQGLSCNLCKYTVHDQC 345
Cdd:cd20833     3 HKFIARFFKQPTFCSHCTDFIwGFGKQGFQCQVCSFVVHKRC 44

protein kinase C conserved region 1 (C1 domain) found in SH3 and cysteine-rich domain-containing protein 2 (Stac2) and similar proteins; Stac2, also called 24b2/Stac2, or Src homology 3 and cysteine-rich domain-containing protein 2, plays a redundant role in promoting the expression of calcium channel CACNA1S at the cell membrane, and thereby contributes to increased channel activity. It slows down the inactivation rate of the calcium channel CACNA1C. Stac2 contains a cysteine-rich C1 domain and one SH3 domain at the C-terminus. 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.

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                  ....*....|....*....|....*....|....*....|...
gi 1622845375 305 HMWRPKRFPRPVYCNLCESSI-GLGKQGLSCNLCKYTVHDQCA 346
Cdd:cd20881     6 HSFQEHVFKKPSPCELCHQMIvGNSKQGLRCKMCKVSVHLWCS 48

protein kinase C conserved region 1 (C1 domain) found in myotonic dystrophy kinase-related Cdc42-binding kinase alpha (MRCK alpha) and similar proteins; MRCK alpha, also called Cdc42-binding protein kinase alpha, DMPK-like alpha, or myotonic dystrophy protein kinase-like alpha, is a serine/threonine-protein kinase expressed ubiquitously in many tissues. It plays a role in the regulation of peripheral actin reorganization and neurite outgrowth. It may also play a role in the transferrin iron uptake pathway. MRCK alpha is an important downstream effector of Cdc42 and plays a role in the regulation of cytoskeleton reorganization and cell migration. 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.

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                  ....*....|....*....|....*....|....*....|....*.
gi 1622845375 305 HMWRPKRFPRPVYCNLCES-SIGLGKQGLSCNLCKYTVHDQCAMKA 349
Cdd:cd20864     3 HQFVVKSFTTPTKCNQCTSlMVGLIRQGCTCEVCGFSCHVTCADKA 48

second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) epsilon, eta, 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 domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. PKC-epsilon has been shown to behave as an oncoprotein. Its overexpression contributes to neoplastic transformation depending on the cell type. It contributes to oncogenesis by inducing disordered cell growth and inhibiting cell death. It also plays a role in tumor invasion and metastasis. PKC-epsilon has also been found to confer cardioprotection against ischemia and reperfusion-mediated damage. Other cellular functions include the regulation of gene expression, cell adhesion, and cell motility. PKC-eta is predominantly expressed in squamous epithelia, where it plays a crucial role in the signaling of cell-type specific differentiation. It is also expressed in pro-B cells and early-stage thymocytes, and acts as a key regulator in early B-cell development. PKC-eta increases glioblastoma multiforme (GBM) proliferation and resistance to radiation, and is being developed as a therapeutic target for the management of GBM. Members of this family contain two copies of 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.

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                  ....*....|....*....|....*....|....*....|..
gi 1622845375 305 HMWRPKRFPRPVYCNLCESSI-GLGKQGLSCNLCKYTVHDQC 345
Cdd:cd20838     3 HRFSVHNYKRPTFCDHCGSLLyGLYKQGLQCKVCKMNVHKRC 44

second 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 domain. 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 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
                  ....*....|....*....|....*....|....*....|..
gi 1622845375 305 HMWRPKRFPRPVYCNLCESSI-GLGKQGLSCNLCKYTVHDQC 345
Cdd:cd20793     1 HKFKVHTYYSPTFCDHCGSLLyGLVRQGLKCKDCGMNVHHRC 42

protein kinase C conserved region 1 (C1 domain) found in the SH3 and cysteine-rich domain-containing protein (Stac) family; Stac proteins are putative adaptor proteins that are important for neuronal function. There are three mammalian members (Stac1, Stac2 and Stac3) of this family. Stac1 and Stac3 contain two SH3 domains while Stac2 contains a single SH3 domain at the C-terminus. Stac1 and Stac2 have been found to be expressed differently in mature dorsal root ganglia (DRG) neurons. Stac1 is mainly expressed in peptidergic neurons while Stac2 is found in a subset of nonpeptidergic and all trkB+ neurons. Stac proteins contain a cysteine-rich C1 domain and one or two SH3 domains at the C-terminus. 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.

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                  ....*....|....*....|....*....|....*....|..
gi 1622845375 312 FPRPVYCNLCESSI-GLGKQGLSCNLCKYTVHDQCAMKALPC 352
Cdd:cd20817     8 FKKPTFCDVCKELLvGLSKQGLRCKNCKMNVHHKCQEGVPDC 49

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.

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                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845375 167 KLEFTFKLYDTDRNGILDssvswgpcmlgkgicvhlsapscpyfsrvlrnrrgwgerlspvglnLKEvdkiilqMMRVAE 246
Cdd:cd00051     1 ELREAFRLFDKDGDGTIS----------------------------------------------ADE-------LKAALK 27

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1622845375 247 YLDWDVSElrPILQEMMKEIDYDGSGSVSQAEWVRA 282
Cdd:cd00051    28 SLGEGLSE--EEIDEMIREVDKDGDGKIDFEEFLEL 61

first protein kinase C conserved region 1 (C1 domain) found in type V diacylglycerol kinase, DAG kinase theta, and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase theta, also called diglyceride kinase theta (DGK-theta), is the only isoform classified as type V; it contains a pleckstrin homology (PH)-like domain and an additional C1 domain, compared to other DGKs. It may regulate the activity of protein kinase C by controlling the balance between the two signaling lipids, diacylglycerol and phosphatidic acid. DAG kinase theta contains three 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 1622845375 305 HMWRPKRFPRPVYCNLCESSI-GLGKQGLSCNLCKYTVHDQCAMKAL-PC 352
Cdd:cd20803     2 HSFRKKTFHKPTYCHHCTDLLwGLLNQGYQCEVCNFVSHERCLKTVVtPC 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.

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                  ....*....|....*....|....*....|....*....|....
gi 1622845375 304 QHMWRPKRFPRPVYCNLCESSI-GLGKQGLSCNLCKYTVHDQCA 346
Cdd:cd20828     5 PHNFEPHSFVTPTNCDYCLQILwGIVKKGMKCSECGYNCHEKCQ 48