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 1622845385  566 IINNYFSIGVDASIAHRFHIMREKYPEKFNSRMKNKLWYFEFATSESIFSTCKKLEESLTVEICGKPLDLSNlSLEGIAV 645
Cdd:smart00045   1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLPN-SLEGIAV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845385  646 LNIPSMHGGSNLWGDtrkphgdiyginqalgatakviTDPDILKTCVPDLSDKRLEVVGLEGAIEMGQIYtKLKNAGRRL 725
Cdd:smart00045  80 LNIPSYGGGTNLWGT----------------------TDKEDLNFSKQSHDDGLLEVVGLTGAMHMAQIR-QVGLAGRRI 136

                          170       180
                   ....*....|....*....|....
gi 1622845385  726 AKCSE--ITFHTTKTLPMQIDGEP 747
Cdd:smart00045 137 AQCSEvrITIKTSKTIPMQVDGEP 160

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845385   4 ERGLISPSDFAQLQKYMEYSTKKVSDVLKLF-EDGEMAKYVQGDAIGYEGFQQFLKIYLEVDnVPRHLSLALFQSFKTDH 82
Cdd:pfam14513   1 EWVSLSPEEFAQLQKYAEYSSKKLKDVLEEFnEDGVLAKYNPEEPIDYEGFKLFMKTYLEVD-LPEDLCQHLFLSFQTKP 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622845385  83 CLNEANVTK----------------------------DVVCLNDVSCYFSLLEGGR 110
Cdd:pfam14513  80 SQESPDSPKegasssvkagfdknpsslppapsspsasPVVYLKDVSCYLSLLEGGR 135

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 1622845385 247 KDDGQHMWRPKRFPRPVYCNLCESSI-GLGKQGLSCNLCKYTVHDQCAMKALPCEVSTYAKS 307
Cdd:cd20799     1 KDDGQHVWRLKHFNKPAYCNVCENMLvGLRKQGLCCTFCKYTVHERCVSRAPASCIRTYVKS 62

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 1622845385  566 IINNYFSIGVDASIAHRFHIMREKYPEKFNSRMKNKLWYFEFATSESIFSTCKKLEESLTVEICGKPLDLSNlSLEGIAV 645
Cdd:smart00045   1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLPN-SLEGIAV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845385  646 LNIPSMHGGSNLWGDtrkphgdiyginqalgatakviTDPDILKTCVPDLSDKRLEVVGLEGAIEMGQIYtKLKNAGRRL 725
Cdd:smart00045  80 LNIPSYGGGTNLWGT----------------------TDKEDLNFSKQSHDDGLLEVVGLTGAMHMAQIR-QVGLAGRRI 136

                          170       180
                   ....*....|....*....|....
gi 1622845385  726 AKCSE--ITFHTTKTLPMQIDGEP 747
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 1622845385  424 LVFVNPKSGGKQGQRVLWKFQYILNPRQVFNLLKDGPEIGLRLFKDVP-DGRILVCGGDGTVGWILETIDKANLPVL-PP 501
Cdd:smart00046   1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVPdFNRVLVCGGDGTVGWVLNALDKRELPLPePP 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1622845385  502 VAVLPLGTGNDLARCLRWGGGYEGQNLAKILKDLETSKVVHMDR 545
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 1622845385 316 HVWVRGGCESGRCDRCQKKIRIYHSLTGLHCVWCHLEIHDDCLQAVGHECDCGLLRDHILPP 377
Cdd:cd20890     1 HVWVSGGCESSKCDKCQKKIKSFQSLTGLHCVWCHLKRHDECLSSVPSTCDCGPLRDHILPP 62

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 1622845385 247 KDDGQHMWRPKRFPRPVYCNLCESSI-GLGKQGLSCNLCKYTVHDQCAMKALPCEVSTYAKS 307
Cdd:cd20799     1 KDDGQHVWRLKHFNKPAYCNVCENMLvGLRKQGLCCTFCKYTVHERCVSRAPASCIRTYVKS 62

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 1622845385 252 HMWRPKRFPRPVYCNLCESSI-GLGKQGLSCNLCKYTVHDQCAMKALPCE 300
Cdd:pfam00130   1 HHFVHRNFKQPTFCDHCGEFLwGLGKQGLKCSWCKLNVHKRCHEKVPPEC 50

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
                   ....*....|....*....|....*....|....*....|....*...
gi 1622845385  252 HMWRPKRFPRPVYCNLCESSI-GLGKQGLSCNLCKYTVHDQCAMKALP 298
Cdd:smart00109   1 HKHVFRTFTKPTFCCVCRKSIwGSFKQGLRCSECKVKCHKKCADKVPK 48

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 1622845385 114 KLEFTFKLYDTDRNGILDssvswgpcmlgkgicvhlsapscpyfsrvlrnrrgwgerlspvglnLKEvdkiilqMMRVAE 193
Cdd:cd00051     1 ELREAFRLFDKDGDGTIS----------------------------------------------ADE-------LKAALK 27

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1622845385 194 YLDWDVSElrPILQEMMKEIDYDGSGSVSQAEWVRA 229
Cdd:cd00051    28 SLGEGLSE--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 1622845385  206 LQEMMKEIDYDGSGSVSQAEWVRA 229
Cdd:smart00054   2 LKEAFRLFDKDGDGKIDFEEFKDL 25

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 1622845385  566 IINNYFSIGVDASIAHRFHIMREKYPEKFNSRMKNKLWYFEFATSESIFSTCKKLEESLTVEICGKPLDLSNlSLEGIAV 645
Cdd:smart00045   1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLPN-SLEGIAV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845385  646 LNIPSMHGGSNLWGDtrkphgdiyginqalgatakviTDPDILKTCVPDLSDKRLEVVGLEGAIEMGQIYtKLKNAGRRL 725
Cdd:smart00045  80 LNIPSYGGGTNLWGT----------------------TDKEDLNFSKQSHDDGLLEVVGLTGAMHMAQIR-QVGLAGRRI 136

                          170       180
                   ....*....|....*....|....
gi 1622845385  726 AKCSE--ITFHTTKTLPMQIDGEP 747
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 1622845385  424 LVFVNPKSGGKQGQRVLWKFQYILNPRQVFNLLKDGPEIGLRLFKDVP-DGRILVCGGDGTVGWILETIDKANLPVL-PP 501
Cdd:smart00046   1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVPdFNRVLVCGGDGTVGWVLNALDKRELPLPePP 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1622845385  502 VAVLPLGTGNDLARCLRWGGGYEGQNLAKILKDLETSKVVHMDR 545
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 1622845385 316 HVWVRGGCESGRCDRCQKKIRIYHSLTGLHCVWCHLEIHDDCLQAVGHECDCGLLRDHILPP 377
Cdd:cd20890     1 HVWVSGGCESSKCDKCQKKIKSFQSLTGLHCVWCHLKRHDECLSSVPSTCDCGPLRDHILPP 62

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 1622845385 247 KDDGQHMWRPKRFPRPVYCNLCESSI-GLGKQGLSCNLCKYTVHDQCAMKALPCEVSTYAKS 307
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 1622845385 236 LLVLLGLEMTLKDDGQHMWRPKRFPRPVYCNLCESSI-GLGKQGLSCNLCKYTVHDQCAMKALPCEVSTYAKS 307
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 1622845385 316 HVWVRGGcESGRCDRCQKKIRIYHSLTGLHCVWCHLEIHDDCLQAVGHECDCGLLRDHILPP 377
Cdd:cd20892     1 HVWVEGN-SPVKCDRCHKSIKCYQGLTGLHCVWCQITLHNKCASHVSPECDGGQLKDHILLP 61

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845385 423 LLVFVNPKSGGKQGQRVLWKFQYILNpRQVFNLL-------KDGPEIGLRLFKDVPDgRILVCGGDGTVGWILETIDKAN 495
Cdd:COG1597     5 ALLIVNPASGRGRAARLLERLVAALR-AAGLEVEvletespGDATELAREAAAEGAD-LVVAAGGDGTVNEVANGLAGTG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845385 496 lpvlPPVAVLPLGTGNDLARCLRWgggyeGQNLAKILKDLETSKVVHMDrwsveVIpqqteeKSDPVPFqiINNyFSIGV 575
Cdd:COG1597    83 ----PPLGILPLGTGNDFARALGI-----PLDPEAALEALLTGRTRRID-----LG------RVNGRYF--LNV-AGIGF 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845385 576 DASIAHRfhimrekypekFNSRMKNKL-W--YFeFATSESIFSTcKKLEesLTVEICGKPLDLSNLSlegIAVLNIPSMH 652
Cdd:COG1597   140 DAEVVER-----------ANRALKRRLgKlaYV-LAALRALLRY-RPFR--LRIELDGEEIEGEALL---VAVGNGPYYG 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845385 653 GGSNLWGDtrkphgdiyginqalgatakvitdpdilktcvPDLSDKRLEVVGLE--GAIEMGQIYTKLKNaGR------- 723
Cdd:COG1597   202 GGLRLAPD--------------------------------ASLDDGLLDVVVVRplSRLRLLRLLPRLLR-GRhlrhpgv 248

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1622845385 724 RLAKCSEITFHTTKTLPMQIDGEP-WMQTPCTIKITHK 760
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 1622845385 252 HMWRPKRFPRPVYCNLCESSI-GLGKQGLSCNLCKYTVHDQCAMKALPCE 300
Cdd:pfam00130   1 HHFVHRNFKQPTFCDHCGEFLwGLGKQGLKCSWCKLNVHKRCHEKVPPEC 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 1622845385 316 HVWVRGG-CESGRCDRCQKKIRiYHSLTGLHCVWCHLEIHDDCLQAVGHECDCG 368
Cdd:pfam00130   1 HHFVHRNfKQPTFCDHCGEFLW-GLGKQGLKCSWCKLNVHKRCHEKVPPECGCD 53

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
                   ....*....|....*....|....*....|....*....|....*...
gi 1622845385  252 HMWRPKRFPRPVYCNLCESSI-GLGKQGLSCNLCKYTVHDQCAMKALP 298
Cdd:smart00109   1 HKHVFRTFTKPTFCCVCRKSIwGSFKQGLRCSECKVKCHKKCADKVPK 48

first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase delta (DAG kinase delta) and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase delta, also called 130 kDa diacylglycerol 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. 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. DAG kinase delta 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        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622845385 250 GQHMWRPKRFPRPVYCNLCESSI-GLGKQGLSCNLCKYTVHDQCAMKAL-PCEVSTYAKSRKD 310
Cdd:cd20847    23 GMHNWYACSHARPTYCNVCREALsGVTSHGLSCEVCKFKAHKRCAVRATnNCKWTTLASIGKD 85

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

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                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622845385 316 HVWVRGGCE-SGRCDRCQKKIRIYHSLTGLHCVWCHLEIHDDCLQAVGHECDCGLLRDHILPP 377
Cdd:cd20853     1 HHWVRGNLPlCSVCCVCNEQCGNQPGLCDYRCCWCQRTVHDDCLAKLPKECDLGAFRNFIVPP 63

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.

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                  ....*....|....*....|....*....|....*....|....*..
gi 1622845385 252 HMWRPKRFPRPVYCNLCESSI-GLGKQGLSCNLCKYTVHDQCAMKAL 297
Cdd:cd20834     8 HEFIAKFFRQPTFCSVCKEFLwGFNKQGYQCRQCNAAVHKKCHDKIL 54

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.

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                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622845385 316 HVWVRGGCESG-RCDRCQKKIRIYHSLTGLHCVWCHLEIHDDCLQAVGHECDCGLLRDHILPP 377
Cdd:cd20854     1 HHWREGNLPSNsKCEVCKKSCGSSECLAGMRCEWCGITAHASCYKSLPKECNFGRLRNIILPP 63

protein kinase C conserved region 1 (C1 domain) found in the Myotonic dystrophy kinase-related Cdc42-binding kinase (MRCK) family; MRCK is thought to be a coincidence detector of signaling by the small GTPase Cdc42 and phosphoinositides. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. MRCK has been shown to promote cytoskeletal reorganization, which affects many biological processes. Three isoforms of MRCK are known, named alpha, beta and gamma. MRCKgamma is expressed in heart and skeletal muscles, unlike MRCKalpha and MRCKbeta, which are expressed ubiquitously. MRCK consists of a serine/threonine kinase domain, a cysteine rich (C1) region, a PH domain and a p21 binding motif. 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.

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                  ....*....|....*....|....*....|....*....|....*...
gi 1622845385 252 HMWRPKRFPRPVYCNLCES-SIGLGKQGLSCNLCKYTVHDQCAMKALP 298
Cdd:cd20809     1 HKFIVRTFSTPTKCNHCTSlMVGLVRQGLVCEVCGYACHVSCADKAPQ 48

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.

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                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622845385 252 HMWRPKRFPRPVYCNLCESSIG--LGKQGLSCNLCKYTVHDQCAMKA-LPC 299
Cdd:cd20831     6 HTFVATHFKGGPSCAVCNKLIPgrFGKQGYQCRDCGLICHKRCHVKVeTHC 56

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 1622845385 252 HMWRPKRFPRPVYCNLCESSI-GLGKQGLSCNLCKYTVHDQCA 293
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 1622845385 252 HMWRPKRFPRPVYCNLCES-SIGLGKQGLSCNLCKYTVHDQCAMKA 296
Cdd:cd20864     3 HQFVVKSFTTPTKCNQCTSlMVGLIRQGCTCEVCGFSCHVTCADKA 48

protein kinase C conserved region 1 (C1 domain) found in the atypical protein kinase C (aPKC) iota 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-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 C1 domain found in aPKC isoform iota. 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 1622845385 252 HMWRPKRFPRPVYCNLCESSI-GLGKQGLSCNLCKYTVHDQC 292
Cdd:cd21094     3 HTFQAKRFNRRAHCAICTDRIwGLGRQGYKCINCKLLVHKKC 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.

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                  ....*....|....*....|....*....|....*....|....*....|..
gi 1622845385 252 HMWRPKRFPRPVYCNLCESSIGlgKQGLSCNLCKYTVHDQC-AMKALPCEVS 302
Cdd:cd20826     3 HSFKEKSFRKPRTCDVCKQIIW--NEGSSCRVCKYACHRKCePKVTAACSPS 52

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 1622845385 259 FPRPVYCNLCESSI-GLGKQGLSCNLCKYTVHDQCAMKALPC 299
Cdd:cd20817     8 FKKPTFCDVCKELLvGLSKQGLRCKNCKMNVHHKCQEGVPDC 49

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.

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                  ....*....|....*....|....*....|....*....|..
gi 1622845385 252 HMWRPKRFPRPVYCNLCESSI-GLGKQGLSCNLCKYTVHDQC 292
Cdd:cd20793     1 HKFKVHTYYSPTFCDHCGSLLyGLVRQGLKCKDCGMNVHHRC 42

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.

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                  ....*....|....*....|....*....|....*....|....*....|
gi 1622845385 252 HMWRPKRFPRPVYCNLCESSI-GLGKQGLSCNLCKYTVHDQCAMKAL-PC 299
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 1622845385 251 QHMWRPKRFPRPVYCNLCESSI-GLGKQGLSCNLCKYTVHDQCA 293
Cdd:cd20828     5 PHNFEPHSFVTPTNCDYCLQILwGIVKKGMKCSECGYNCHEKCQ 48

lipid kinase; Reviewed

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gi 1622845385 474 RILVCGGDGTVGWILETIDKANLPVLPPVAVLPLGTGNDLAR 515
Cdd:PRK13054   59 TVIAGGGDGTINEVATALAQLEGDARPALGILPLGTANDFAT 100