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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073286  373 IINNYFSIGVDASIAHRFHLMREKYPEKFNSRMKNKLWYFEFATSESIFSTCKKLEESVTVEICGKlLDLSDLSLEGIAV 452
Cdd:smart00045   1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGV-DVDLPNSLEGIAV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073286  453 LNIPSTHGGSNLWGDtkrphgdtceinqalgsaakiiTDPDILKTCVPDMSDKRLEVVGIEGAIEMGQIYtRLKSAGHRL 532
Cdd:smart00045  80 LNIPSYGGGTNLWGT----------------------TDKEDLNFSKQSHDDGLLEVVGLTGAMHMAQIR-QVGLAGRRI 136

                          170       180
                   ....*....|....*....|....
gi 1907073286  533 AKCSE--ITFQTTKTLPMQIDGEP 554
Cdd:smart00045 137 AQCSEvrITIKTSKTIPMQVDGEP 160

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 1907073286 129 HLWVRGGCHSGRCDRCQKKIRTYHSLTGLHCVWCHLEIHDDCLQAVGPECDCGLLRDHILPP 190
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
                  ....*....|....*....|....*....|....*....|..
gi 1907073286   1 MMRVAEYLDWDVSElrPILQEMMREMDQDGSGSVSLDEWVRA 42
Cdd:cd00051    22 LKAALKSLGEGLSE--EEIDEMIREVDKDGDGKIDFEEFLEL 61

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073286  373 IINNYFSIGVDASIAHRFHLMREKYPEKFNSRMKNKLWYFEFATSESIFSTCKKLEESVTVEICGKlLDLSDLSLEGIAV 452
Cdd:smart00045   1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGV-DVDLPNSLEGIAV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073286  453 LNIPSTHGGSNLWGDtkrphgdtceinqalgsaakiiTDPDILKTCVPDMSDKRLEVVGIEGAIEMGQIYtRLKSAGHRL 532
Cdd:smart00045  80 LNIPSYGGGTNLWGT----------------------TDKEDLNFSKQSHDDGLLEVVGLTGAMHMAQIR-QVGLAGRRI 136

                          170       180
                   ....*....|....*....|....
gi 1907073286  533 AKCSE--ITFQTTKTLPMQIDGEP 554
Cdd:smart00045 137 AQCSEvrITIKTSKTIPMQVDGEP 160

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 1907073286  232 LVFINLKSGGKQGQSVLWKFQYILNPRQVFDL-KDGPEPGLRFFKDVPQF-RILVCGGDGTVGWVLETIDKANF-ATVPP 308
Cdd:smart00046   1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLtKKGPAVALVIFRDVPDFnRVLVCGGDGTVGWVLNALDKRELpLPEPP 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1907073286  309 VAVLPLGTGNDLARCLRWGRGYEGENLRKILKDIELSKVVYLDR 352
Cdd:smart00046  81 VAVLPLGTGNDLARSLGWGGGYDGEKLLKTLRDALESDTVKLDR 124

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 1907073286 230 PLLVFINLKSGGKQGQSVLWKFQYILNPRQV-FDLK--DGPEPGLRFFKDVPQ---FRILVCGGDGTVGWVLETIDKanF 303
Cdd:pfam00781   1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVeVELVltEGPGDALELAREAAEdgyDRIVVAGGDGTVNEVLNGLAG--L 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1907073286 304 ATVPPVAVLPLGTGNDLARCLRWGRGYEG--ENLRK-ILKDIELSKV 347
Cdd:pfam00781  79 ATRPPLGIIPLGTGNDFARALGIPGDPEEalEAILKgQTRPVDVGKV 125

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073286 231 LLVFINLKSGGKQGQSVLWKFQYILNpRQVFDLK----DGPEPGLRFFKDV--PQFRILV-CGGDGTVGWVLETIdkanF 303
Cdd:COG1597     5 ALLIVNPASGRGRAARLLERLVAALR-AAGLEVEvletESPGDATELAREAaaEGADLVVaAGGDGTVNEVANGL----A 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073286 304 ATVPPVAVLPLGTGNDLARCLRWGRgyegeNLRKILKDIELSKVVYLD------RWFLEVipqqngeksdpvpsqiinny 377
Cdd:COG1597    80 GTGPPLGILPLGTGNDFARALGIPL-----DPEAALEALLTGRTRRIDlgrvngRYFLNV-------------------- 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073286 378 FSIGVDASIAHRfhlmrekypekFNSRMKNKL-W--YFeFATSESIFSTcKKLEesVTVEICGKLLDLSDLSlegIAVLN 454
Cdd:COG1597   135 AGIGFDAEVVER-----------ANRALKRRLgKlaYV-LAALRALLRY-RPFR--LRIELDGEEIEGEALL---VAVGN 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073286 455 IPSTHGGSNLWGDtkrphgdtceinqalgsaakiitdpdilktcvPDMSDKRLEVVGIE--GAIEMGQIYTRLKSAGH-- 530
Cdd:COG1597   197 GPYYGGGLRLAPD--------------------------------ASLDDGLLDVVVVRplSRLRLLRLLPRLLRGRHlr 244

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1907073286 531 ----RLAKCSEITFQTTKTLPMQIDGEP-WMQAPCTIKITHK 567
Cdd:COG1597   245 hpgvRYFRAREVEIESDRPLPVQLDGEPlGLATPLEFEVLPG 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 1907073286  65 HIWRPKRFTRLVYCNLCEQSIS-LGKQGLSCNFCKYIVHDHCAMKAQPCE 113
Cdd:pfam00130   1 HHFVHRNFKQPTFCDHCGEFLWgLGKQGLKCSWCKLNVHKRCHEKVPPEC 50

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
                  ....*....|....*....|....*....|....*....|..
gi 1907073286   1 MMRVAEYLDWDVSElrPILQEMMREMDQDGSGSVSLDEWVRA 42
Cdd:cd00051    22 LKAALKSLGEGLSE--EEIDEMIREVDKDGDGKIDFEEFLEL 61

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.

                           10        20
                   ....*....|....*....|....
gi 1907073286   19 LQEMMREMDQDGSGSVSLDEWVRA 42
Cdd:smart00054   2 LKEAFRLFDKDGDGKIDFEEFKDL 25

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 1907073286  129 HLWVRGGCHSG-RCDRCQKKIRTYHsLTGLHCVWCHLEIHDDCLQAVGPEC 178
Cdd:smart00109   1 HKHVFRTFTKPtFCCVCRKSIWGSF-KQGLRCSECKVKCHKKCADKVPKAC 50

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073286  373 IINNYFSIGVDASIAHRFHLMREKYPEKFNSRMKNKLWYFEFATSESIFSTCKKLEESVTVEICGKlLDLSDLSLEGIAV 452
Cdd:smart00045   1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGV-DVDLPNSLEGIAV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073286  453 LNIPSTHGGSNLWGDtkrphgdtceinqalgsaakiiTDPDILKTCVPDMSDKRLEVVGIEGAIEMGQIYtRLKSAGHRL 532
Cdd:smart00045  80 LNIPSYGGGTNLWGT----------------------TDKEDLNFSKQSHDDGLLEVVGLTGAMHMAQIR-QVGLAGRRI 136

                          170       180
                   ....*....|....*....|....
gi 1907073286  533 AKCSE--ITFQTTKTLPMQIDGEP 554
Cdd:smart00045 137 AQCSEvrITIKTSKTIPMQVDGEP 160

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 1907073286  232 LVFINLKSGGKQGQSVLWKFQYILNPRQVFDL-KDGPEPGLRFFKDVPQF-RILVCGGDGTVGWVLETIDKANF-ATVPP 308
Cdd:smart00046   1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLtKKGPAVALVIFRDVPDFnRVLVCGGDGTVGWVLNALDKRELpLPEPP 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1907073286  309 VAVLPLGTGNDLARCLRWGRGYEGENLRKILKDIELSKVVYLDR 352
Cdd:smart00046  81 VAVLPLGTGNDLARSLGWGGGYDGEKLLKTLRDALESDTVKLDR 124

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 1907073286 230 PLLVFINLKSGGKQGQSVLWKFQYILNPRQV-FDLK--DGPEPGLRFFKDVPQ---FRILVCGGDGTVGWVLETIDKanF 303
Cdd:pfam00781   1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVeVELVltEGPGDALELAREAAEdgyDRIVVAGGDGTVNEVLNGLAG--L 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1907073286 304 ATVPPVAVLPLGTGNDLARCLRWGRGYEG--ENLRK-ILKDIELSKV 347
Cdd:pfam00781  79 ATRPPLGIIPLGTGNDFARALGIPGDPEEalEAILKgQTRPVDVGKV 125

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        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907073286  60 KDDGNHIWRPKRFTRLVYCNLCEQSI-SLGKQGLSCNFCKYIVHDHCAMKAQPCEVSTYAKS 120
Cdd:cd20799     1 KDDGQHVWRLKHFNKPAYCNVCENMLvGLRKQGLCCTFCKYTVHERCVSRAPASCIRTYVKS 62

first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase gamma (DAG kinase gamma) and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase gamma, also called diglyceride kinase gamma (DGK-gamma), reverses the normal flow of glycerolipid biosynthesis by phosphorylating diacylglycerol back to phosphatidic acid. 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. DGK-gamma contains two copies of the C1 domain. This model corresponds to the first one. DGK-gamma 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        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907073286  49 LLVLLGMDVTMKDDGNHIWRPKRFTRLVYCNLCEQSI-SLGKQGLSCNFCKYIVHDHCAMKAQPCEVSTYAKS 120
Cdd:cd20846     1 LLVLLGMETNVKDDGQHAWRLKHFKKPAYCNFCHTMLlGVRKQGLCCSFCKYTVHERCVSKDIASCISTYVKS 73

second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase gamma (DAG kinase gamma) and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase gamma, also called diglyceride kinase gamma (DGK-gamma), reverses the normal flow of glycerolipid biosynthesis by phosphorylating diacylglycerol back to phosphatidic acid. 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. DGK-gamma contains two copies of the C1 domain. This model corresponds to the second one. DGK-gamma 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 1907073286 129 HLWVRGGcHSGRCDRCQKKIRTYHSLTGLHCVWCHLEIHDDCLQAVGPECDCGLLRDHILPP 190
Cdd:cd20892     1 HVWVEGN-SPVKCDRCHKSIKCYQGLTGLHCVWCQITLHNKCASHVSPECDGGQLKDHILLP 61

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 1907073286 129 HLWVRGGCHSG-RCDRCQKKIRTYHSLTGLHCVWCHLEIHDDCLQAVGP-ECDCG 181
Cdd:cd20805     1 HHWVEGNLPSGaKCSVCGKKCGSSFGLAGYRCSWCKRTVHSECIDKLGPeECDLG 55

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 1907073286  65 HIWRPKRFTRLVYCNLCEQSIS-LGKQGLSCNFCKYIVHDHCAMKAQPCE 113
Cdd:pfam00130   1 HHFVHRNFKQPTFCDHCGEFLWgLGKQGLKCSWCKLNVHKRCHEKVPPEC 50

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 1907073286  65 HIWRPKRFTRLVYCNLCEQSI-SLGKQGLSCNFCKYIVHDHCAMKA-QPC 112
Cdd:cd00029     1 HRFVPTTFSSPTFCDVCGKLIwGLFKQGLKCSDCGLVCHKKCLDKApSPC 50

third 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 third 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 1907073286 129 HLWVRGGCHSG-RCDRCQKKIRTYHSLTGLHCVWCHLEIHDDCLQAVGPECDCGLLRDHILPP 190
Cdd:cd20854     1 HHWREGNLPSNsKCEVCKKSCGSSECLAGMRCEWCGITAHASCYKSLPKECNFGRLRNIILPP 63

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 1907073286  65 HIWRPKRFTRLVYCNLCEQSI-SLGKQGLSCNFCKYIVHDHCAMKAQP 111
Cdd:cd20824     2 HNFKPHSFSIPTKCDYCGEKIwGLSKKGLSCKDCGFNCHIKCELKVPP 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.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1907073286  65 HIWRPKRFTRLVYCNLCEQSI-SLGKQGLSCNFCKYIVHDHC 105
Cdd:cd20794     3 HLFQAKRFNRRAVCAYCSDRIwGLGRQGYKCINCKLLVHKKC 44

protein kinase C conserved region 1 (C1 domain) found in Drosophila melanogaster GM13116p and similar proteins; This group contains uncharacterized proteins including Drosophila melanogaster GM13116p and Caenorhabditis elegans hypothetical protein R11G1.4, both of which contain C2 (a calcium-binding domain) and C1 domains. This model describes the C1 domain, 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 1907073286  64 NHIWRPKRFTRLVYCNLCEQSI--SLGKQGLSCNFCKYIVHDHCAMKA-QPC 112
Cdd:cd20831     5 DHTFVATHFKGGPSCAVCNKLIpgRFGKQGYQCRDCGLICHKRCHVKVeTHC 56

protein kinase C conserved region 1 (C1 domain) found in the atypical protein kinase C (aPKC) zeta type; 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. Members of this family contain C1 domain found in aPKC isoform zeta. 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 1907073286  65 HIWRPKRFTRLVYCNLCEQSI-SLGKQGLSCNFCKYIVHDHC 105
Cdd:cd21095     3 HLFQAKRFNRRAYCGQCSERIwGLGRQGYKCINCKLLVHKRC 44

protein kinase C conserved region 1 (C1 domain) found in tensin-2 like (TNS2-like) proteins; The TNS2-like group includes TNS2, and variants of TNS1 and TNS3. Tensin-2 (TNS2), also called C1 domain-containing phosphatase and tensin (C1-TEN), or tensin-like C1 domain-containing phosphatase (TENC1), is an essential component for the maintenance of glomerular basement membrane (GBM) structures. It regulates cell motility and proliferation. It may have phosphatase activity. TNS2 reduces AKT1 phosphorylation, lowers AKT1 kinase activity and interferes with AKT1 signaling. Tensin-1 (TNS1) plays a role in fibrillar adhesion formation. It may be involved in cell migration, cartilage development and in linking signal transduction pathways to the cytoskeleton. 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. Typical TNS1 and TNS3 do not contain C1 domains, but some isoforms/variants do. Members of this family contain an N-terminal region with a zinc finger (C1 domain), a protein tyrosine phosphatase (PTP)-like domain and a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains. This model corresponds to 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 1907073286  65 HIWRPKRFTRLVYCNLCEQSISlgKQGLSCNFCKYIVHDHC-AMKAQPCEVS 115
Cdd:cd20826     3 HSFKEKSFRKPRTCDVCKQIIW--NEGSSCRVCKYACHRKCePKVTAACSPS 52

putative lipid kinase; Reviewed

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073286 282 ILVCGGDGTVGWVLETIdkANFATVPPVAVLPLGTGNDLARCLRWGRGYEGENLRKILKD 341
Cdd:PRK13055   63 IIAAGGDGTINEVVNGI--APLEKRPKMAIIPAGTTNDYARALKIPRDNPVEAAKVILKN 120

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.

                           10        20
                   ....*....|....*....|....
gi 1907073286   19 LQEMMREMDQDGSGSVSLDEWVRA 42
Cdd:smart00054   2 LKEAFRLFDKDGDGKIDFEEFKDL 25

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.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1907073286  65 HIWRPKRFTRLVYCNLCEQSIslGKQGLSCNFCKYIVHDHCAMK-AQPC 112
Cdd:cd20889     3 HTFKNKTFKKPKVCSICKQVI--DSQGISCRVCKYACHKKCEAKvVTPC 49

protein kinase C conserved region 1 (C1 domain) found in PDZ domain-containing protein 8 (PDZD8) and similar proteins; PDZD8, also called Sarcoma antigen NY-SAR-84/NY-SAR-104, is a molecular tethering protein that connects endoplasmic reticulum (ER) and mitochondrial membranes. PDZD8-dependent ER-mitochondria membrane tethering is essential for ER-mitochondria Ca2+ transfer. In neurons, it is involved in the regulation of dendritic Ca2+ dynamics by regulating mitochondrial Ca2+ uptake. PDZD8 also plays an indirect role in the regulation of cell morphology and cytoskeletal organization. It contains a PDZ domain and a C1 domain. This model describes the C1 domain, 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 1907073286  62 DGNHIWRPKRFTRLVYCNLCEQSISLgKQGLSCNFCKYIVHDHCAMKAQ 110
Cdd:cd20825     1 EGKHDFVLTQFQNATYCDFCKKKIWL-KEAFQCRLCGMICHKKCLDKCQ 48

EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering/transport proteins. The first group is the largest and includes the most well-known members of the family such as calmodulin, troponin C and S100B. These proteins typically undergo a calcium-dependent conformational change which opens a target binding site. The latter group is represented by calbindin D9k and do not undergo calcium dependent conformational changes.

                          10        20
                  ....*....|....*....|....*
gi 1907073286  18 ILQEMMREMDQDGSGSVSLDEWVRA 42
Cdd:pfam00036   1 ELKEIFRLFDKDGDGKIDFEEFKEL 25

protein kinase C conserved region 1 (C1 domain) found in tensin-1 (TNS1) variant and similar proteins; Tensin-1 (TNS1) plays a role in fibrillar adhesion formation. It may be involved in cell migration, cartilage development and in linking signal transduction pathways to the cytoskeleton. This model corresponds to the C1 domain found in TNS1 variant. Typical TNS1 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.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1907073286  65 HIWRPKRFTRLVYCNLCEQSISlgKQGLSCNFCKYIVHDHCAMK-AQPC 112
Cdd:cd20888     6 HTFKVKTFKKVKSCGICKQAIT--REGSTCRVCKLSCHKKCEAKvATPC 52

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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907073286  65 HIWRPKRFTRLVYCNLCEQSI-SLGKQGLSCNFCKYIVHDHCAMKA--QPC 112
Cdd:cd20881     6 HSFQEHVFKKPSPCELCHQMIvGNSKQGLRCKMCKVSVHLWCSEEVshQQC 56

protein kinase C conserved region 1 (C1 domain) found in tensin-2 and similar proteins; Tensin-2 (TNS2), also called C1 domain-containing phosphatase and tensin (C1-TEN), or tensin-like C1 domain-containing phosphatase (TENC1), is an essential component for the maintenance of glomerular basement membrane (GBM) structures. It regulates cell motility and proliferation. It may have phosphatase activity. TNS2 reduces AKT1 phosphorylation, lowers AKT1 kinase activity, and interferes with AKT1 signaling. It contains an N-terminal region with a zinc finger (C1 domain), a protein tyrosine phosphatase (PTP)-like domain and a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains. 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 1907073286  65 HIWRPKRFTRLVYCNLCEQSIslGKQGLSCNFCKYIVHDHCAMKAQP 111
Cdd:cd20887     3 HSFKEKTFKKKRACAVCREPV--GGQGLVCRVCKVASHKKCEAKVTS 47

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.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1907073286  64 NHIWRPKRFTRLVYCNLCEQSI-SLGKQGLSCNFCKYIVHDHC 105
Cdd:cd20833     2 DHKFIARFFKQPTFCSHCTDFIwGFGKQGFQCQVCSFVVHKRC 44

hypothetical protein; Provisional

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1907073286 282 ILVCGGDGTVGWVLETIdkANFATVppVAVLPLGTGNDLARCL 324
Cdd:PRK12361  301 VIACGGDGTVTEVASEL--VNTDIT--LGIIPLGTANALSHAL 339

protein kinase C conserved region 1 (C1 domain) found in the Raf (Rapidly Accelerated Fibrosarcoma) kinase family; Raf kinases are serine/threonine kinases (STKs) that catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. They act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. Aberrant expression or activation of components in this pathway are associated with tumor initiation, progression, and metastasis. Raf proteins contain a Ras binding domain, a zinc finger cysteine-rich domain (C1), and a catalytic kinase domain. Vertebrates have three Raf isoforms (A-, B-, and C-Raf) with different expression profiles, modes of regulation, and abilities to function in the ERK cascade, depending on cellular context and stimuli. They have essential and non-overlapping roles during embryo- and organogenesis. Knockout of each isoform results in a lethal phenotype or abnormality in most mouse strains. This model describes 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 1907073286  64 NHIWRPKRFTRLVYCNLCEQSISlgkQGLSCNFCKYIVHDHCAMKAQP-CE 113
Cdd:cd20811     2 SHNFVRKTFFTLAFCDVCRKLLF---QGFRCQTCGFKFHQRCSDQVPAlCE 49

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];

                          10        20        30
                  ....*....|....*....|....*....|....
gi 1907073286   9 DWDVSElrPILQEMMREMDQDGSGSVSLDEWVRA 42
Cdd:COG5126    97 ALGVSE--EEADELFARLDTDGDGKISFEEFVAA 128