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Conserved domains on  [gi|262205333|ref|NP_001160069|]
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diacylglycerol kinase zeta isoform 1 [Mus musculus]

Protein Classification

diacylglycerol kinase zeta( domain architecture ID 15336656)

diacylglycerol kinase zeta converts diacylglycerol/DAG into phosphatidic acid/phosphatidate/PA and regulates the respective levels of these two bioactive lipids

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 641-798 1.96e-76

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


:

Pssm-ID: 214486  Cd Length: 160  Bit Score: 248.40  E-value: 1.96e-76
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205333    641 VFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGTAFSDFLMGSSKDLAKHIRVVCDGMDLTPKIqdlKPQCI 720
Cdd:smart00045    1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLPN---SLEGI 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205333    721 VFLNIPRYCAGTMPWGHPGEH-HDFEPQRHDDGYLEVIGFTMTSLAA--LQVGGHGERLTQCREVLLT--TAKAIPVQVD 795
Cdd:smart00045   78 AVLNIPSYGGGTNLWGTTDKEdLNFSKQSHDDGLLEVVGLTGAMHMAqiRQVGLAGRRIAQCSEVRITikTSKTIPMQVD 157


                    ...
gi 262205333    796 GEP 798
Cdd:smart00045  158 GEP 160
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 492-613 2.69e-52

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


:

Pssm-ID: 214487 [Multi-domain]  Cd Length: 124  Bit Score: 179.03  E-value: 2.69e-52
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205333    492 LVFVNPKSGGNQGAKIIQSFLWYLNPRQVFDLSQGGPREALEMYRKVHN-LRILACGGDGTVGWILSTLDQLRLKPP-PP 569
Cdd:smart00046    1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVPDfNRVLVCGGDGTVGWVLNALDKRELPLPePP 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 262205333    570 VAILPLGTGNDLARTLNWGGGYTDEPVSKILSHVEEGNVVQLDR 613
Cdd:smart00046   81 VAVLPLGTGNDLARSLGWGGGYDGEKLLKTLRDALESDTVKLDR 124
C1_DGKzeta_rpt2 cd20895
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta ...
 365-439 2.07e-50

second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta (DAG kinase zeta) and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase zeta, also called diglyceride kinase zeta (DGK-zeta), displays a strong preference for 1,2-diacylglycerols over 1,3-diacylglycerols, but lacks substrate specificity among molecular species of long chain diacylglycerols. It is classified as a type IV DAG kinase (DGK), containing myristoylated alanine-rich protein kinase C substrate (MARCKS), PDZ-binding, and ankyrin domains, in addition to C1 and catalytic domains that are present in all DGKs. The MARCKS domain regulates the nuclear localizations of type IV DGKs while the PDZ-binding and ankyrin domains regulate interactions with several proteins. DAG kinase zeta contains two copies of the C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


:

Pssm-ID: 410445  Cd Length: 75  Bit Score: 171.80  E-value: 2.07e-50
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 262205333  365 VRHHWVHRRRQDGKCRHCGKGFQQKFTFHSKEIVAISCSWCKQAYHSKVSCFMMQQIEEPCSLGVHAAVVIPPTW 439
Cdd:cd20895     1 VRHHWVHRRRQEGKCRQCGKGFQQKFAFHSKEIVAISCSWCKQAYHSKVSCFMLQQIEEPCSLGAHAAVIVPPTW 75
C1_DGKzeta_rpt1 cd20849
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta (DAG ...
 282-355 1.70e-47

first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta (DAG kinase zeta) and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase zeta, also called diglyceride kinase zeta (DGK-zeta), displays a strong preference for 1,2-diacylglycerols over 1,3-diacylglycerols, but lacks substrate specificity among molecular species of long chain diacylglycerols. It is classified as a type IV DAG kinase (DGK), containing myristoylated alanine-rich protein kinase C substrate (MARCKS), PDZ-binding, and ankyrin domains, in addition to C1 and catalytic domains that are present in all DGKs. The MARCKS domain regulates the nuclear localizations of type IV DGKs while the PDZ-binding and ankyrin domains regulate interactions with several proteins. DAG kinase zeta contains two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


:

Pssm-ID: 410399  Cd Length: 74  Bit Score: 163.57  E-value: 1.70e-47
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 262205333  282 DWSESAVYGEHIWFETNVSGDFCYVGEQHCVAKMLPKSAPRKKCAACKIVVHTQCIKQLEKINFRCKPSFRESG 355
Cdd:cd20849     1 DWSESAVYGEHIWFETNVSGDFCYVGEQNCVAKQLQKSVSRKKCAACKIVVHTPCIEQLEKINFRCKPSFRESG 74
Ank_2 pfam12796
Ankyrin repeats (3 copies);
989-1083 6.12e-18

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.77  E-value: 6.12e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205333   989 LIEAAKRNDCCKLQELHRAGGDLMHRDQKSRTLLHHAVSTGSKEVVRYLLDHAPPEILDaveeNGETCLHQAAALGQRTI 1068
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD----NGRTALHYAARSGHLEI 76

                           90
                   ....*....|....*
gi 262205333  1069 CHYIVEAGASLMKTD 1083
Cdd:pfam12796   77 VKLLLEKGADINVKD 91
 
Name Accession Description Interval E-value
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 641-798 1.96e-76

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


Pssm-ID: 214486  Cd Length: 160  Bit Score: 248.40  E-value: 1.96e-76
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205333    641 VFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGTAFSDFLMGSSKDLAKHIRVVCDGMDLTPKIqdlKPQCI 720
Cdd:smart00045    1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLPN---SLEGI 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205333    721 VFLNIPRYCAGTMPWGHPGEH-HDFEPQRHDDGYLEVIGFTMTSLAA--LQVGGHGERLTQCREVLLT--TAKAIPVQVD 795
Cdd:smart00045   78 AVLNIPSYGGGTNLWGTTDKEdLNFSKQSHDDGLLEVVGLTGAMHMAqiRQVGLAGRRIAQCSEVRITikTSKTIPMQVD 157


                    ...
gi 262205333    796 GEP 798
Cdd:smart00045  158 GEP 160
DAGK_acc pfam00609
Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts ...
 641-798 2.96e-68

Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. This domain is assumed to be an accessory domain: its function is unknown.


Pssm-ID: 459866  Cd Length: 158  Bit Score: 225.56  E-value: 2.96e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205333   641 VFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGTAFSDFLMGSSKDLAKHIRVVCDGMDLTPKiqdLKPQCI 720
Cdd:pfam00609    1 VMNNYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDMFQRSCKNLIEKVELEVDGKDLPLP---KSLEGI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205333   721 VFLNIPRYCAGTMPWGHPGEHHD-FEPQRHDDGYLEVIGFT-MTSLAALQVGGHGE-RLTQCREVLLTTAKAIPVQVDGE 797
Cdd:pfam00609   78 VVLNIPSYAGGTDLWGNSKEDGLgFAPQSVDDGLLEVVGLTgALHLGQVQVGLGSAkRIAQGGPIRITTKKKIPMQVDGE 157


                   .
gi 262205333   798 P 798
Cdd:pfam00609  158 P 158
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 492-613 2.69e-52

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


Pssm-ID: 214487 [Multi-domain]  Cd Length: 124  Bit Score: 179.03  E-value: 2.69e-52
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205333    492 LVFVNPKSGGNQGAKIIQSFLWYLNPRQVFDLSQGGPREALEMYRKVHN-LRILACGGDGTVGWILSTLDQLRLKPP-PP 569
Cdd:smart00046    1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVPDfNRVLVCGGDGTVGWVLNALDKRELPLPePP 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 262205333    570 VAILPLGTGNDLARTLNWGGGYTDEPVSKILSHVEEGNVVQLDR 613
Cdd:smart00046   81 VAVLPLGTGNDLARSLGWGGGYDGEKLLKTLRDALESDTVKLDR 124
C1_DGKzeta_rpt2 cd20895
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta ...
 365-439 2.07e-50

second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta (DAG kinase zeta) and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase zeta, also called diglyceride kinase zeta (DGK-zeta), displays a strong preference for 1,2-diacylglycerols over 1,3-diacylglycerols, but lacks substrate specificity among molecular species of long chain diacylglycerols. It is classified as a type IV DAG kinase (DGK), containing myristoylated alanine-rich protein kinase C substrate (MARCKS), PDZ-binding, and ankyrin domains, in addition to C1 and catalytic domains that are present in all DGKs. The MARCKS domain regulates the nuclear localizations of type IV DGKs while the PDZ-binding and ankyrin domains regulate interactions with several proteins. DAG kinase zeta contains two copies of the C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410445  Cd Length: 75  Bit Score: 171.80  E-value: 2.07e-50
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 262205333  365 VRHHWVHRRRQDGKCRHCGKGFQQKFTFHSKEIVAISCSWCKQAYHSKVSCFMMQQIEEPCSLGVHAAVVIPPTW 439
Cdd:cd20895     1 VRHHWVHRRRQEGKCRQCGKGFQQKFAFHSKEIVAISCSWCKQAYHSKVSCFMLQQIEEPCSLGAHAAVIVPPTW 75
C1_DGKzeta_rpt1 cd20849
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta (DAG ...
 282-355 1.70e-47

first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta (DAG kinase zeta) and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase zeta, also called diglyceride kinase zeta (DGK-zeta), displays a strong preference for 1,2-diacylglycerols over 1,3-diacylglycerols, but lacks substrate specificity among molecular species of long chain diacylglycerols. It is classified as a type IV DAG kinase (DGK), containing myristoylated alanine-rich protein kinase C substrate (MARCKS), PDZ-binding, and ankyrin domains, in addition to C1 and catalytic domains that are present in all DGKs. The MARCKS domain regulates the nuclear localizations of type IV DGKs while the PDZ-binding and ankyrin domains regulate interactions with several proteins. DAG kinase zeta contains two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410399  Cd Length: 74  Bit Score: 163.57  E-value: 1.70e-47
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 262205333  282 DWSESAVYGEHIWFETNVSGDFCYVGEQHCVAKMLPKSAPRKKCAACKIVVHTQCIKQLEKINFRCKPSFRESG 355
Cdd:cd20849     1 DWSESAVYGEHIWFETNVSGDFCYVGEQNCVAKQLQKSVSRKKCAACKIVVHTPCIEQLEKINFRCKPSFRESG 74
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 490-612 8.47e-35

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


Pssm-ID: 425868 [Multi-domain]  Cd Length: 125  Bit Score: 129.24  E-value: 8.47e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205333   490 PLLVFVNPKSGGNQGAKIIQSFLWYLNPRQV-FDLSQGGPRE-ALEMYRKV---HNLRILACGGDGTVGWILSTLDqlRL 564
Cdd:pfam00781    1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVeVELVLTEGPGdALELAREAaedGYDRIVVAGGDGTVNEVLNGLA--GL 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 262205333   565 KPPPPVAILPLGTGNDLARTLNWGGgytdePVSKILSHVEEGNVVQLD 612
Cdd:pfam00781   79 ATRPPLGIIPLGTGNDFARALGIPG-----DPEEALEAILKGQTRPVD 121
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 488-811 4.94e-27

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


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 112.64  E-value: 4.94e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205333  488 MKPLLVFVNPKSGGNQGAKIIQSFLWYLNPR----QVFDLSQGGP-----REALEmyRKVHnlRILACGGDGTVGWILST 558
Cdd:COG1597     2 MMRALLIVNPASGRGRAARLLERLVAALRAAglevEVLETESPGDatelaREAAA--EGAD--LVVAAGGDGTVNEVANG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205333  559 LdqlrLKPPPPVAILPLGTGNDLARTLNwgggyTDEPVSKILSHVEEGNVVQLD--RwdlraepnpeagpeerddgATDR 636
Cdd:COG1597    78 L----AGTGPPLGILPLGTGNDFARALG-----IPLDPEAALEALLTGRTRRIDlgR-------------------VNGR 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205333  637 LpldvFNNYFSLGFDAHVTLEFHESReanpekfnSRFRNKMFYAGTAFSdfLMGSSKdlAKHIRVVCDGmdltpKIQDLK 716
Cdd:COG1597   130 Y----FLNVAGIGFDAEVVERANRAL--------KRRLGKLAYVLAALR--ALLRYR--PFRLRIELDG-----EEIEGE 188

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205333  717 PQCIVFLNIPRYcagtmpwghpGEHHDFEPQ-RHDDGYLEVIGFT-------MTSLAALQVGGHGE----RLTQCREVLL 784
Cdd:COG1597   189 ALLVAVGNGPYY----------GGGLRLAPDaSLDDGLLDVVVVRplsrlrlLRLLPRLLRGRHLRhpgvRYFRAREVEI 258

                         330       340       350
                  ....*....|....*....|....*....|.
gi 262205333  785 TTAKAIPVQVDGEPCKLSAS-RIRI---ALR 811
Cdd:COG1597   259 ESDRPLPVQLDGEPLGLATPlEFEVlpgALR 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
989-1083 6.12e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.77  E-value: 6.12e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205333   989 LIEAAKRNDCCKLQELHRAGGDLMHRDQKSRTLLHHAVSTGSKEVVRYLLDHAPPEILDaveeNGETCLHQAAALGQRTI 1068
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD----NGRTALHYAARSGHLEI 76

                           90
                   ....*....|....*
gi 262205333  1069 CHYIVEAGASLMKTD 1083
Cdd:pfam12796   77 VKLLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
989-1122 4.02e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 83.08  E-value: 4.02e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205333  989 LIEAAKRNDCCKLQELHRAGGDLMHRDQKSRTLLHHAVSTGSKEVVRYLLDH-APPEILDaveENGETCLHQAAALGQRT 1067
Cdd:COG0666   124 LHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAgADVNARD---NDGETPLHLAAENGHLE 200

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 262205333 1068 ICHYIVEAGASLMKTDLQGDTPRQRAEKAQDTELAAYLENRQHYQMIQREDQETA 1122
Cdd:COG0666   201 IVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTA 255
PRK12361 PRK12361
hypothetical protein; Provisional
 489-612 5.73e-08

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 56.94  E-value: 5.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205333  489 KPLLVFVNPKSGGNQGAKIIQSFLWYLNPRqvFDLS-------QGGPREALEMYRKVHNLrILACGGDGTVGWILSTL-- 559
Cdd:PRK12361  243 KRAWLIANPVSGGGKWQEYGEQIQRELKAY--FDLTvklttpeISAEALAKQARKAGADI-VIACGGDGTVTEVASELvn 319

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 262205333  560 DQLRLkppppvAILPLGTGNDLARTLnWGGGYTDEPVSKILSHVEEGNVVQLD 612
Cdd:PRK12361  320 TDITL------GIIPLGTANALSHAL-FGLGSKLIPVEQACDNIIQGHTQRID 365
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
 367-426 7.43e-07

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


Pssm-ID: 395079  Cd Length: 53  Bit Score: 47.05  E-value: 7.43e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 262205333   367 HHWVHRR-RQDGKCRHCGKgfqqkfTFHSKEIVAISCSWCKQAYHSKvsCFMMQQIEEPCS 426
Cdd:pfam00130    1 HHFVHRNfKQPTFCDHCGE------FLWGLGKQGLKCSWCKLNVHKR--CHEKVPPECGCD 53
PHA03095 PHA03095
ankyrin-like protein; Provisional
 995-1089 1.17e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.17  E-value: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205333  995 RNDCCKLQELHRAGGDLMHRDQKSRTLLHHAVSTGSKE---VVRYLLDHAppeILDAVEENGETCLHQAAALGQRTICHY 1071
Cdd:PHA03095  199 KPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrslVLPLLIAGI---SINARNRYGQTPLHYAAVFNNPRACRR 275

                          90
                  ....*....|....*...
gi 262205333 1072 IVEAGASLMKTDLQGDTP 1089
Cdd:PHA03095  276 LIALGADINAVSSDGNTP 293
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 989-1081 5.14e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 44.23  E-value: 5.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205333  989 LIEAAKRNDCCKLQELHR-AGGDLMHRDQKSRTLLHHAVSTGSKEVVRYLLDHAPPEILDAVEEN---GETCLHQAAALG 1064
Cdd:cd22192    21 LLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMTSDlyqGETALHIAVVNQ 100

                          90
                  ....*....|....*..
gi 262205333 1065 QRTICHYIVEAGASLMK 1081
Cdd:cd22192   101 NLNLVRELIARGADVVS 117
TIGR00147 TIGR00147
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ...
 542-585 2.22e-03

lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been purified and shown to have phosphatidylglycerol kinase activity. The member from M. tuberculosis, Rv2252, has diacylglycerol kinase activity. BmrU from B. subtilis is in an operon with multidrug efflux transporter Bmr, but is uncharacterized. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 161732 [Multi-domain]  Cd Length: 293  Bit Score: 41.34  E-value: 2.22e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 262205333   542 RILACGGDGTVGWILSTLDQLRLKPPppVAILPLGTGNDLARTL 585
Cdd:TIGR00147   60 TVIAGGGDGTINEVVNALIQLDDIPA--LGILPLGTANDFARSL 101
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 1019-1040 2.81e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.41  E-value: 2.81e-03
                            10        20
                    ....*....|....*....|..
gi 262205333   1019 RTLLHHAVSTGSKEVVRYLLDH 1040
Cdd:smart00248    3 RTPLHLAAENGNLEVVKLLLDK 24
 
Name Accession Description Interval E-value
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 641-798 1.96e-76

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


Pssm-ID: 214486  Cd Length: 160  Bit Score: 248.40  E-value: 1.96e-76
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205333    641 VFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGTAFSDFLMGSSKDLAKHIRVVCDGMDLTPKIqdlKPQCI 720
Cdd:smart00045    1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLPN---SLEGI 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205333    721 VFLNIPRYCAGTMPWGHPGEH-HDFEPQRHDDGYLEVIGFTMTSLAA--LQVGGHGERLTQCREVLLT--TAKAIPVQVD 795
Cdd:smart00045   78 AVLNIPSYGGGTNLWGTTDKEdLNFSKQSHDDGLLEVVGLTGAMHMAqiRQVGLAGRRIAQCSEVRITikTSKTIPMQVD 157


                    ...
gi 262205333    796 GEP 798
Cdd:smart00045  158 GEP 160
DAGK_acc pfam00609
Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts ...
 641-798 2.96e-68

Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. This domain is assumed to be an accessory domain: its function is unknown.


Pssm-ID: 459866  Cd Length: 158  Bit Score: 225.56  E-value: 2.96e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205333   641 VFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGTAFSDFLMGSSKDLAKHIRVVCDGMDLTPKiqdLKPQCI 720
Cdd:pfam00609    1 VMNNYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDMFQRSCKNLIEKVELEVDGKDLPLP---KSLEGI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205333   721 VFLNIPRYCAGTMPWGHPGEHHD-FEPQRHDDGYLEVIGFT-MTSLAALQVGGHGE-RLTQCREVLLTTAKAIPVQVDGE 797
Cdd:pfam00609   78 VVLNIPSYAGGTDLWGNSKEDGLgFAPQSVDDGLLEVVGLTgALHLGQVQVGLGSAkRIAQGGPIRITTKKKIPMQVDGE 157


                   .
gi 262205333   798 P 798
Cdd:pfam00609  158 P 158
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 492-613 2.69e-52

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


Pssm-ID: 214487 [Multi-domain]  Cd Length: 124  Bit Score: 179.03  E-value: 2.69e-52
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205333    492 LVFVNPKSGGNQGAKIIQSFLWYLNPRQVFDLSQGGPREALEMYRKVHN-LRILACGGDGTVGWILSTLDQLRLKPP-PP 569
Cdd:smart00046    1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVPDfNRVLVCGGDGTVGWVLNALDKRELPLPePP 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 262205333    570 VAILPLGTGNDLARTLNWGGGYTDEPVSKILSHVEEGNVVQLDR 613
Cdd:smart00046   81 VAVLPLGTGNDLARSLGWGGGYDGEKLLKTLRDALESDTVKLDR 124
C1_DGKzeta_rpt2 cd20895
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta ...
 365-439 2.07e-50

second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta (DAG kinase zeta) and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase zeta, also called diglyceride kinase zeta (DGK-zeta), displays a strong preference for 1,2-diacylglycerols over 1,3-diacylglycerols, but lacks substrate specificity among molecular species of long chain diacylglycerols. It is classified as a type IV DAG kinase (DGK), containing myristoylated alanine-rich protein kinase C substrate (MARCKS), PDZ-binding, and ankyrin domains, in addition to C1 and catalytic domains that are present in all DGKs. The MARCKS domain regulates the nuclear localizations of type IV DGKs while the PDZ-binding and ankyrin domains regulate interactions with several proteins. DAG kinase zeta contains two copies of the C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410445  Cd Length: 75  Bit Score: 171.80  E-value: 2.07e-50
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 262205333  365 VRHHWVHRRRQDGKCRHCGKGFQQKFTFHSKEIVAISCSWCKQAYHSKVSCFMMQQIEEPCSLGVHAAVVIPPTW 439
Cdd:cd20895     1 VRHHWVHRRRQEGKCRQCGKGFQQKFAFHSKEIVAISCSWCKQAYHSKVSCFMLQQIEEPCSLGAHAAVIVPPTW 75
C1_DGKzeta_rpt1 cd20849
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta (DAG ...
 282-355 1.70e-47

first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta (DAG kinase zeta) and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase zeta, also called diglyceride kinase zeta (DGK-zeta), displays a strong preference for 1,2-diacylglycerols over 1,3-diacylglycerols, but lacks substrate specificity among molecular species of long chain diacylglycerols. It is classified as a type IV DAG kinase (DGK), containing myristoylated alanine-rich protein kinase C substrate (MARCKS), PDZ-binding, and ankyrin domains, in addition to C1 and catalytic domains that are present in all DGKs. The MARCKS domain regulates the nuclear localizations of type IV DGKs while the PDZ-binding and ankyrin domains regulate interactions with several proteins. DAG kinase zeta contains two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410399  Cd Length: 74  Bit Score: 163.57  E-value: 1.70e-47
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 262205333  282 DWSESAVYGEHIWFETNVSGDFCYVGEQHCVAKMLPKSAPRKKCAACKIVVHTQCIKQLEKINFRCKPSFRESG 355
Cdd:cd20849     1 DWSESAVYGEHIWFETNVSGDFCYVGEQNCVAKQLQKSVSRKKCAACKIVVHTPCIEQLEKINFRCKPSFRESG 74
C1_DGKiota_rpt2 cd20896
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase iota ...
 365-439 2.68e-45

second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase iota (DAG kinase iota) and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase iota, also called diglyceride kinase iota (DGK-iota), or DGKI, is a homolog of Drosophila DGK2, RdgA. It may have important cellular functions in the retina and brain. It is classified as a type IV DAG kinase (DGK), containing myristoylated alanine-rich protein kinase C substrate (MARCKS), PDZ-binding, and ankyrin domains, in addition to C1 and catalytic domains that are present in all DGKs. The MARCKS domain regulates the nuclear localizations of type IV DGKs while the PDZ-binding and ankyrin domains regulate interactions with several proteins. DAG kinase iota contains two copies of the C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410446  Cd Length: 75  Bit Score: 157.17  E-value: 2.68e-45
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 262205333  365 VRHHWVHRRRQDGKCRHCGKGFQQKFTFHSKEIVAISCSWCKQAYHSKVSCFMMQQIEEPCSLGVHAAVVIPPTW 439
Cdd:cd20896     1 VRHHWVHRRRQEGKCKQCGKGFQQKFSFHSKEIVAISCSWCKQAFHNKVTCFMLHHIEEPCSLGAHAAVIVPPTW 75
C1_DGK_typeIV_rpt2 cd20855
second protein kinase C conserved region 1 (C1 domain) found in type IV diacylglycerol kinases; ...
 367-428 2.58e-41

second protein kinase C conserved region 1 (C1 domain) found in type IV diacylglycerol kinases; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. Type IV DAG kinases (DGKs) contain myristoylated alanine-rich protein kinase C substrate (MARCKS), PDZ-binding, and ankyrin domains, in addition to C1 and catalytic domains that are present in all DGKs. The MARCKS domain regulates the nuclear localizations of type IV DGKs while the PDZ-binding and ankyrin domains regulate interactions with several proteins. Two DGK isozymes (zeta and iota) are classified as type IV. DAG kinase zeta, also called diglyceride kinase zeta (DGK-zeta), displays a strong preference for 1,2-diacylglycerols over 1,3-diacylglycerols, but lacks substrate specificity among molecular species of long chain diacylglycerols. DAG kinase iota, also called diglyceride kinase iota (DGK-iota), or DGKI, is a homolog of Drosophila DGK2, RdgA. It may have important cellular functions in the retina and brain. Members of this family contain two copies of the C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410405  Cd Length: 62  Bit Score: 145.57  E-value: 2.58e-41
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 262205333  367 HHWVHRRRQDGKCRHCGKGFQQKFTFHSKEIVAISCSWCKQAYHSKVSCFMMQQIEEPCSLG 428
Cdd:cd20855     1 HHWVHRRKQEGKCKQCGKSFQQKLSFSSKEIVAISCSWCKEAYHNKDSCFNMKKIEEPCNLG 62
C1_DGKiota_rpt1 cd20850
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase iota (DAG ...
 282-355 1.02e-38

first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase iota (DAG kinase iota) and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase iota, also called diglyceride kinase iota (DGK-iota), or DGKI, is a homolog of Drosophila DGK2, RdgA. It may have important cellular functions in the retina and brain. It is classified as a type IV DAG kinase (DGK), containing myristoylated alanine-rich protein kinase C substrate (MARCKS), PDZ-binding, and ankyrin domains, in addition to C1 and catalytic domains that are present in all DGKs. The MARCKS domain regulates the nuclear localizations of type IV DGKs while the PDZ-binding and ankyrin domains regulate interactions with several proteins. DAG kinase iota contains two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410400  Cd Length: 73  Bit Score: 138.23  E-value: 1.02e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 262205333  282 DWSESAVYGEHIWFETNVSGDFCYVGEQHCVAKmLPKSAPRKKCAACKIVVHTQCIKQLEKINFRCKPSFRESG 355
Cdd:cd20850     1 DWSENAVNGEHLWLETNVSGDLCYLGEENCQVK-FAKSALRRKCAACKIVVHTACIEQLEKINFRCKPTFREGG 73
C1_DGK_typeIV_rpt1 cd20802
first protein kinase C conserved region 1 (C1 domain) found in type IV diacylglycerol kinases; ...
 287-353 3.02e-35

first protein kinase C conserved region 1 (C1 domain) found in type IV diacylglycerol kinases; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. Type IV DAG kinases (DGKs) contain myristoylated alanine-rich protein kinase C substrate (MARCKS), PDZ-binding, and ankyrin domains, in addition to C1 and catalytic domains that are present in all DGKs. The MARCKS domain regulates the nuclear localizations of type IV DGKs while the PDZ-binding and ankyrin domains regulate interactions with several proteins. Two DGK isozymes (zeta and iota) are classified as type IV. DAG kinase zeta, also called diglyceride kinase zeta (DGK-zeta), displays a strong preference for 1,2-diacylglycerols over 1,3-diacylglycerols, but lacks substrate specificity among molecular species of long chain diacylglycerols. DAG kinase iota, also called diglyceride kinase iota (DGK-iota), or DGKI, is a homolog of Drosophila DGK2, RdgA. It may have important cellular functions in the retina and brain. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410352  Cd Length: 62  Bit Score: 128.18  E-value: 3.02e-35
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 262205333  287 AVYGEHIWFETNVSGDFCYVGEQHCVakmlpKSAPRKKCAACKIVVHTQCIKQLEKINFRCKPSFRE 353
Cdd:cd20802     1 AVNGEHLWTDTSASGDLCYVGEQDCL-----KSGSRKKCSACKIVVHTGCIPQLEKINFKCKPTFRE 62
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 490-612 8.47e-35

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


Pssm-ID: 425868 [Multi-domain]  Cd Length: 125  Bit Score: 129.24  E-value: 8.47e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205333   490 PLLVFVNPKSGGNQGAKIIQSFLWYLNPRQV-FDLSQGGPRE-ALEMYRKV---HNLRILACGGDGTVGWILSTLDqlRL 564
Cdd:pfam00781    1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVeVELVLTEGPGdALELAREAaedGYDRIVVAGGDGTVNEVLNGLA--GL 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 262205333   565 KPPPPVAILPLGTGNDLARTLNWGGgytdePVSKILSHVEEGNVVQLD 612
Cdd:pfam00781   79 ATRPPLGIIPLGTGNDFARALGIPG-----DPEEALEAILKGQTRPVD 121
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 488-811 4.94e-27

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


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 112.64  E-value: 4.94e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205333  488 MKPLLVFVNPKSGGNQGAKIIQSFLWYLNPR----QVFDLSQGGP-----REALEmyRKVHnlRILACGGDGTVGWILST 558
Cdd:COG1597     2 MMRALLIVNPASGRGRAARLLERLVAALRAAglevEVLETESPGDatelaREAAA--EGAD--LVVAAGGDGTVNEVANG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205333  559 LdqlrLKPPPPVAILPLGTGNDLARTLNwgggyTDEPVSKILSHVEEGNVVQLD--RwdlraepnpeagpeerddgATDR 636
Cdd:COG1597    78 L----AGTGPPLGILPLGTGNDFARALG-----IPLDPEAALEALLTGRTRRIDlgR-------------------VNGR 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205333  637 LpldvFNNYFSLGFDAHVTLEFHESReanpekfnSRFRNKMFYAGTAFSdfLMGSSKdlAKHIRVVCDGmdltpKIQDLK 716
Cdd:COG1597   130 Y----FLNVAGIGFDAEVVERANRAL--------KRRLGKLAYVLAALR--ALLRYR--PFRLRIELDG-----EEIEGE 188

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205333  717 PQCIVFLNIPRYcagtmpwghpGEHHDFEPQ-RHDDGYLEVIGFT-------MTSLAALQVGGHGE----RLTQCREVLL 784
Cdd:COG1597   189 ALLVAVGNGPYY----------GGGLRLAPDaSLDDGLLDVVVVRplsrlrlLRLLPRLLRGRHLRhpgvRYFRAREVEI 258

                         330       340       350
                  ....*....|....*....|....*....|.
gi 262205333  785 TTAKAIPVQVDGEPCKLSAS-RIRI---ALR 811
Cdd:COG1597   259 ESDRPLPVQLDGEPLGLATPlEFEVlpgALR 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
989-1083 6.12e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.77  E-value: 6.12e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205333   989 LIEAAKRNDCCKLQELHRAGGDLMHRDQKSRTLLHHAVSTGSKEVVRYLLDHAPPEILDaveeNGETCLHQAAALGQRTI 1068
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD----NGRTALHYAARSGHLEI 76

                           90
                   ....*....|....*
gi 262205333  1069 CHYIVEAGASLMKTD 1083
Cdd:pfam12796   77 VKLLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
989-1122 4.02e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 83.08  E-value: 4.02e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205333  989 LIEAAKRNDCCKLQELHRAGGDLMHRDQKSRTLLHHAVSTGSKEVVRYLLDH-APPEILDaveENGETCLHQAAALGQRT 1067
Cdd:COG0666   124 LHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAgADVNARD---NDGETPLHLAAENGHLE 200

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 262205333 1068 ICHYIVEAGASLMKTDLQGDTPRQRAEKAQDTELAAYLENRQHYQMIQREDQETA 1122
Cdd:COG0666   201 IVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTA 255
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
989-1105 9.67e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 81.92  E-value: 9.67e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205333  989 LIEAAKRNDCCKLQELHRAGGDLMHRDQKSRTLLHHAVSTGSKEVVRYLLDH-APPEILDAveeNGETCLHQAAALGQRT 1067
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAgADVNAQDN---DGNTPLHLAAANGNLE 167

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 262205333 1068 ICHYIVEAGASLMKTDLQGDTPRQRAEKAQDTELAAYL 1105
Cdd:COG0666   168 IVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
C1_DGK_rpt2 cd20805
second protein kinase C conserved region 1 (C1 domain) found in the diacylglycerol kinase ...
 367-428 1.98e-11

second protein kinase C conserved region 1 (C1 domain) found in the diacylglycerol kinase family; The diacylglycerol kinase (DGK, EC 2.7.1.107) family of enzymes plays critical roles in lipid signaling pathways by converting diacylglycerol to phosphatidic acid, thereby downregulating signaling by the former and upregulating signaling by the latter second messenger. Ten DGK family isozymes have been identified to date, which possess different interaction motifs imparting distinct temporal and spatial control of DGK activity to each isozyme. They have been classified into five types (I-V), according to domain architecture and some common features. All DGK isozymes, except for DGKtheta, contain two copies of the C1 domain. This model corresponds to the second one. DGKtheta harbors three C1 domains. Its third C1 domain is included here. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410355  Cd Length: 55  Bit Score: 60.15  E-value: 1.98e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 262205333  367 HHWVHRRRQ-DGKCRHCGKGFQQKFTFHSKeivaiSCSWCKQAYHSkvSCFMMQQIEEpCSLG 428
Cdd:cd20805     1 HHWVEGNLPsGAKCSVCGKKCGSSFGLAGY-----RCSWCKRTVHS--ECIDKLGPEE-CDLG 55
PRK12361 PRK12361
hypothetical protein; Provisional
 489-612 5.73e-08

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 56.94  E-value: 5.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205333  489 KPLLVFVNPKSGGNQGAKIIQSFLWYLNPRqvFDLS-------QGGPREALEMYRKVHNLrILACGGDGTVGWILSTL-- 559
Cdd:PRK12361  243 KRAWLIANPVSGGGKWQEYGEQIQRELKAY--FDLTvklttpeISAEALAKQARKAGADI-VIACGGDGTVTEVASELvn 319

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 262205333  560 DQLRLkppppvAILPLGTGNDLARTLnWGGGYTDEPVSKILSHVEEGNVVQLD 612
Cdd:PRK12361  320 TDITL------GIIPLGTANALSHAL-FGLGSKLIPVEQACDNIIQGHTQRID 365
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
 367-426 7.43e-07

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


Pssm-ID: 395079  Cd Length: 53  Bit Score: 47.05  E-value: 7.43e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 262205333   367 HHWVHRR-RQDGKCRHCGKgfqqkfTFHSKEIVAISCSWCKQAYHSKvsCFMMQQIEEPCS 426
Cdd:pfam00130    1 HHFVHRNfKQPTFCDHCGE------FLWGLGKQGLKCSWCKLNVHKR--CHEKVPPECGCD 53
Ank_4 pfam13637
Ankyrin repeats (many copies);
1019-1073 9.44e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.88  E-value: 9.44e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 262205333  1019 RTLLHHAVSTGSKEVVRYLLDHAPPeiLDAVEENGETCLHQAAALGQRTICHYIV 1073
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGAD--INAVDGNGETALHFAASNGNVEVLKLLL 54
PRK13054 PRK13054
lipid kinase; Reviewed
 542-583 1.19e-06

lipid kinase; Reviewed


Pssm-ID: 237281 [Multi-domain]  Cd Length: 300  Bit Score: 51.80  E-value: 1.19e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 262205333  542 RILACGGDGTVGWILSTLDQLRLKPPPPVAILPLGTGNDLAR 583
Cdd:PRK13054   59 TVIAGGGDGTINEVATALAQLEGDARPALGILPLGTANDFAT 100
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
989-1105 3.58e-06

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 49.95  E-value: 3.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205333  989 LIEAAKRNDCCKLQELHRAGGDLMHRDQKSRTLLHHAVSTGSKEVVRYLLDHAPPeiLDAVEENGETCLHQAAALGQRTI 1068
Cdd:COG0666    25 LLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGAD--INAKDDGGNTLLHAAARNGDLEI 102

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 262205333 1069 CHYIVEAGASLMKTDLQGDTPRQRAEKAQDTELAAYL 1105
Cdd:COG0666   103 VKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLL 139
PRK13057 PRK13057
lipid kinase;
529-586 1.08e-05

lipid kinase;


Pssm-ID: 183857 [Multi-domain]  Cd Length: 287  Bit Score: 48.76  E-value: 1.08e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 262205333  529 REALEMYRKVHNLRILAcGGDGTVGWILSTLDQLRLkpppPVAILPLGTGNDLARTLN 586
Cdd:PRK13057   41 SEVIEAYADGVDLVIVG-GGDGTLNAAAPALVETGL----PLGILPLGTANDLARTLG 93
PRK13059 PRK13059
putative lipid kinase; Reviewed
 488-586 1.95e-05

putative lipid kinase; Reviewed


Pssm-ID: 183858  Cd Length: 295  Bit Score: 47.72  E-value: 1.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205333  488 MKPLLVFVNPKSGGNQGA----KIIQSFLWYLNPRQVFDLSQGGP-REALEMYRKVHNLrILACGGDGTVGWILSTLDQL 562
Cdd:PRK13059    1 MKKVKFIYNPYSGENAIIseldKVIRIHQEKGYLVVPYRISLEYDlKNAFKDIDESYKY-ILIAGGDGTVDNVVNAMKKL 79

                          90       100
                  ....*....|....*....|....
gi 262205333  563 RLKPPppVAILPLGTGNDLARTLN 586
Cdd:PRK13059   80 NIDLP--IGILPVGTANDFAKFLG 101
PRK13055 PRK13055
putative lipid kinase; Reviewed
 543-586 3.38e-05

putative lipid kinase; Reviewed


Pssm-ID: 237282 [Multi-domain]  Cd Length: 334  Bit Score: 47.29  E-value: 3.38e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 262205333  543 ILACGGDGTVGWILSTLDQlrLKPPPPVAILPLGTGNDLARTLN 586
Cdd:PRK13055   63 IIAAGGDGTINEVVNGIAP--LEKRPKMAIIPAGTTNDYARALK 104
PHA03095 PHA03095
ankyrin-like protein; Provisional
 995-1089 1.17e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.17  E-value: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205333  995 RNDCCKLQELHRAGGDLMHRDQKSRTLLHHAVSTGSKE---VVRYLLDHAppeILDAVEENGETCLHQAAALGQRTICHY 1071
Cdd:PHA03095  199 KPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrslVLPLLIAGI---SINARNRYGQTPLHYAAVFNNPRACRR 275

                          90
                  ....*....|....*...
gi 262205333 1072 IVEAGASLMKTDLQGDTP 1089
Cdd:PHA03095  276 LIALGADINAVSSDGNTP 293
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 989-1081 5.14e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 44.23  E-value: 5.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205333  989 LIEAAKRNDCCKLQELHR-AGGDLMHRDQKSRTLLHHAVSTGSKEVVRYLLDHAPPEILDAVEEN---GETCLHQAAALG 1064
Cdd:cd22192    21 LLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMTSDlyqGETALHIAVVNQ 100

                          90
                  ....*....|....*..
gi 262205333 1065 QRTICHYIVEAGASLMK 1081
Cdd:cd22192   101 NLNLVRELIARGADVVS 117
Ank_5 pfam13857
Ankyrin repeats (many copies);
1004-1060 6.25e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 6.25e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 262205333  1004 LHRAGG-DLMHRDQKSRTLLHHAVSTGSKEVVRYLLDHapPEILDAVEENGETCLHQA 1060
Cdd:pfam13857    1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAY--GVDLNLKDEEGLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 1007-1105 9.05e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.03  E-value: 9.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205333 1007 AGGDLMHRDQKSRTLLHHAVSTGSKEVVRYLLDH-APPEILDaveENGETCLHQAAALGQRTICHYIVEAGASLMKTDLQ 1085
Cdd:PHA02874  113 CGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYgADVNIED---DNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNN 189

                          90       100
                  ....*....|....*....|
gi 262205333 1086 GDTPRQRAEKAQDTELAAYL 1105
Cdd:PHA02874  190 GESPLHNAAEYGDYACIKLL 209
TIGR00147 TIGR00147
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ...
 542-585 2.22e-03

lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been purified and shown to have phosphatidylglycerol kinase activity. The member from M. tuberculosis, Rv2252, has diacylglycerol kinase activity. BmrU from B. subtilis is in an operon with multidrug efflux transporter Bmr, but is uncharacterized. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 161732 [Multi-domain]  Cd Length: 293  Bit Score: 41.34  E-value: 2.22e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 262205333   542 RILACGGDGTVGWILSTLDQLRLKPPppVAILPLGTGNDLARTL 585
Cdd:TIGR00147   60 TVIAGGGDGTINEVVNALIQLDDIPA--LGILPLGTANDFARSL 101
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 1019-1040 2.81e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.41  E-value: 2.81e-03
                            10        20
                    ....*....|....*....|..
gi 262205333   1019 RTLLHHAVSTGSKEVVRYLLDH 1040
Cdd:smart00248    3 RTPLHLAAENGNLEVVKLLLDK 24
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 979-1068 4.82e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.01  E-value: 4.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205333  979 GDTALPQGEE---------LIEAAKRNDCCKLQELHRAGGDLMHRDQKSRTLLHHAVSTGSKEVVRYLLDHA-PPEILDA 1048
Cdd:PLN03192  510 GDLLGDNGGEhddpnmasnLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHAcNVHIRDA 589

                          90       100
                  ....*....|....*....|
gi 262205333 1049 veeNGETCLHQAAALGQRTI 1068
Cdd:PLN03192  590 ---NGNTALWNAISAKHHKI 606
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 996-1062 6.92e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 40.03  E-value: 6.92e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 262205333  996 NDCCKLQELHRAGGDLMHRDQKSRTLLHHAVSTGSKEVVRYLLDH-APPEILDaveENGETCLHQAAA 1062
Cdd:PHA03100  170 NAKNRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLgANPNLVN---KYGDTPLHIAIL 234
Ank_4 pfam13637
Ankyrin repeats (many copies);
989-1038 7.40e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 35.71  E-value: 7.40e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 262205333   989 LIEAAKRN--DCCKLqeLHRAGGDLMHRDQKSRTLLHHAVSTGSKEVVRYLL 1038
Cdd:pfam13637    5 LHAAAASGhlELLRL--LLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
1055-1105 8.50e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 35.71  E-value: 8.50e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 262205333  1055 TCLHQAAALGQRTICHYIVEAGASLMKTDLQGDTPRQRAEKAQDTELAAYL 1105
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
C1_DGKepsilon_typeIII_rpt1 cd20801
first protein kinase C conserved region 1 (C1 domain) found in type III diacylglycerol kinase, ...
 292-348 8.84e-03

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


Pssm-ID: 410351  Cd Length: 54  Bit Score: 35.37  E-value: 8.84e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 262205333  292 HIWFETNVSGD--FCYVGEQHCVAKMlpksaprkKCAACKIVVHTQCIKQLEKInFRCK 348
Cdd:cd20801     4 HHWVSTDLFSKptYCSVCETLILSGA--------FCDCCGLCVDEGCLRKADKR-FPCK 53
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1019-1040 9.06e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.93  E-value: 9.06e-03
                           10        20
                   ....*....|....*....|..
gi 262205333  1019 RTLLHHAVSTGSKEVVRYLLDH 1040
Cdd:pfam13606    3 NTPLHLAARNGRLEIVKLLLEN 24
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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