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Conserved domains on  [gi|313103001|ref|NP_963291|]
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diacylglycerol kinase zeta isoform 3 [Homo sapiens]

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 ...
 451-608 5.14e-78

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: 250.72  E-value: 5.14e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313103001   451 VFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGTAFSDFLMGSSKDLAKHIRVVCDGMDLTPKIqdlKPQCV 530
Cdd:smart00045   1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLPN---SLEGI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313103001   531 VFLNIPRYCAGTMPWGHPGEH-HDFEPQRHDDGYLEVIGFTMTSLAA--LQVGGHGERLTQCREVVLT--TSKAIPVQVD 605
Cdd:smart00045  78 AVLNIPSYGGGTNLWGTTDKEdLNFSKQSHDDGLLEVVGLTGAMHMAqiRQVGLAGRRIAQCSEVRITikTSKTIPMQVD 157


                   ...
gi 313103001   606 GEP 608
Cdd:smart00045 158 GEP 160
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 302-423 1.15e-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: 179.80  E-value: 1.15e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313103001   302 LVFVNPKSGGNQGAKIIQSFLWYLNPRQVFDLSQGGPKEALEMYRKVHN-LRILACGGDGTVGWILSTLDQLRLKPP-PP 379
Cdd:smart00046   1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVPDfNRVLVCGGDGTVGWVLNALDKRELPLPePP 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 313103001   380 VAILPLGTGNDLARTLNWGGGYTDEPVSKILSHVEEGNVVQLDR 423
Cdd:smart00046  81 VAVLPLGTGNDLARSLGWGGGYDGEKLLKTLRDALESDTVKLDR 124
C1_DGKzeta_rpt2 cd20895
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta ...
 175-249 2.29e-51

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: 174.12  E-value: 2.29e-51
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 313103001 175 VRHHWVHRRRQDGKCRHCGKGFQQKFTFHSKEIVAISCSWCKQAYHSKVSCFMLQQIEEPCSLGVHAAVVIPPTW 249
Cdd:cd20895    1 VRHHWVHRRRQEGKCRQCGKGFQQKFAFHSKEIVAISCSWCKQAYHSKVSCFMLQQIEEPCSLGAHAAVIVPPTW 75
C1_DGKzeta_rpt1 cd20849
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta (DAG ...
 93-165 3.29e-48

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: 165.11  E-value: 3.29e-48
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 313103001  93 DWS-SATYGEHIWFETNVSGDFCYVGEQYCVARMLQKSVSRRKCAACKIVVHTPCIEQLEKINFRCKPSFRESG 165
Cdd:cd20849    1 DWSeSAVYGEHIWFETNVSGDFCYVGEQNCVAKQLQKSVSRKKCAACKIVVHTPCIEQLEKINFRCKPSFRESG 74
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
799-915 1.21e-17

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 84.62  E-value: 1.21e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313103001 799 LIEAAKRNDFCKLQELHRAGGDLMHRDEQSRTLLHHAVSTGSKDVVRYLLDH-APPEILDAveeNGETCLHQAAALGQRT 877
Cdd:COG0666   91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAgADVNAQDN---DGNTPLHLAAANGNLE 167

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 313103001 878 ICHYIVEAGASLMKTDQQGDTPRQRAEKAQDTELAAYL 915
Cdd:COG0666  168 IVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
 
Name Accession Description Interval E-value
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 451-608 5.14e-78

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: 250.72  E-value: 5.14e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313103001   451 VFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGTAFSDFLMGSSKDLAKHIRVVCDGMDLTPKIqdlKPQCV 530
Cdd:smart00045   1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLPN---SLEGI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313103001   531 VFLNIPRYCAGTMPWGHPGEH-HDFEPQRHDDGYLEVIGFTMTSLAA--LQVGGHGERLTQCREVVLT--TSKAIPVQVD 605
Cdd:smart00045  78 AVLNIPSYGGGTNLWGTTDKEdLNFSKQSHDDGLLEVVGLTGAMHMAqiRQVGLAGRRIAQCSEVRITikTSKTIPMQVD 157


                   ...
gi 313103001   606 GEP 608
Cdd:smart00045 158 GEP 160
DAGK_acc pfam00609
Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts ...
 451-608 3.95e-69

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: 226.71  E-value: 3.95e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313103001  451 VFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGTAFSDFLMGSSKDLAKHIRVVCDGMDLTPKiqdLKPQCV 530
Cdd:pfam00609   1 VMNNYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDMFQRSCKNLIEKVELEVDGKDLPLP---KSLEGI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313103001  531 VFLNIPRYCAGTMPWGHPGEHHD-FEPQRHDDGYLEVIGFT-MTSLAALQVGGHGE-RLTQCREVVLTTSKAIPVQVDGE 607
Cdd:pfam00609  78 VVLNIPSYAGGTDLWGNSKEDGLgFAPQSVDDGLLEVVGLTgALHLGQVQVGLGSAkRIAQGGPIRITTKKKIPMQVDGE 157


                  .
gi 313103001  608 P 608
Cdd:pfam00609 158 P 158
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 302-423 1.15e-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: 179.80  E-value: 1.15e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313103001   302 LVFVNPKSGGNQGAKIIQSFLWYLNPRQVFDLSQGGPKEALEMYRKVHN-LRILACGGDGTVGWILSTLDQLRLKPP-PP 379
Cdd:smart00046   1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVPDfNRVLVCGGDGTVGWVLNALDKRELPLPePP 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 313103001   380 VAILPLGTGNDLARTLNWGGGYTDEPVSKILSHVEEGNVVQLDR 423
Cdd:smart00046  81 VAVLPLGTGNDLARSLGWGGGYDGEKLLKTLRDALESDTVKLDR 124
C1_DGKzeta_rpt2 cd20895
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta ...
 175-249 2.29e-51

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: 174.12  E-value: 2.29e-51
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 313103001 175 VRHHWVHRRRQDGKCRHCGKGFQQKFTFHSKEIVAISCSWCKQAYHSKVSCFMLQQIEEPCSLGVHAAVVIPPTW 249
Cdd:cd20895    1 VRHHWVHRRRQEGKCRQCGKGFQQKFAFHSKEIVAISCSWCKQAYHSKVSCFMLQQIEEPCSLGAHAAVIVPPTW 75
C1_DGKzeta_rpt1 cd20849
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta (DAG ...
 93-165 3.29e-48

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: 165.11  E-value: 3.29e-48
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 313103001  93 DWS-SATYGEHIWFETNVSGDFCYVGEQYCVARMLQKSVSRRKCAACKIVVHTPCIEQLEKINFRCKPSFRESG 165
Cdd:cd20849    1 DWSeSAVYGEHIWFETNVSGDFCYVGEQNCVAKQLQKSVSRKKCAACKIVVHTPCIEQLEKINFRCKPSFRESG 74
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 300-422 1.79e-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: 130.78  E-value: 1.79e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313103001  300 PLLVFVNPKSGGNQGAKIIQSFLWYLNPRQV-FDLSQ-GGPKEALEMYRKV---HNLRILACGGDGTVGWILSTLDqlRL 374
Cdd:pfam00781   1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVeVELVLtEGPGDALELAREAaedGYDRIVVAGGDGTVNEVLNGLA--GL 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 313103001  375 KPPPPVAILPLGTGNDLARTLNWGGgytdePVSKILSHVEEGNVVQLD 422
Cdd:pfam00781  79 ATRPPLGIIPLGTGNDFARALGIPG-----DPEEALEAILKGQTRPVD 121
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 298-621 5.74e-28

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


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 114.95  E-value: 5.74e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313103001 298 MKPLLVFVNPKSGGNQGAKIIQSFLWYLNpRQVFDLSQ---GGPKEALEMYRKVHNL---RILACGGDGTVGWILSTLdq 371
Cdd:COG1597    2 MMRALLIVNPASGRGRAARLLERLVAALR-AAGLEVEVletESPGDATELAREAAAEgadLVVAAGGDGTVNEVANGL-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313103001 372 lrLKPPPPVAILPLGTGNDLARTLNwgggyTDEPVSKILSHVEEGNVVQLD--RwdlhaepnpeagpedrdegATDRLpl 449
Cdd:COG1597   79 --AGTGPPLGILPLGTGNDFARALG-----IPLDPEAALEALLTGRTRRIDlgR-------------------VNGRY-- 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313103001 450 dvFNNYFSLGFDAHVTLEFHESReanpekfnSRFRNKMFYAGTAFSdfLMGSSKdlAKHIRVVCDGmdltpKIQDLKPQC 529
Cdd:COG1597  131 --FLNVAGIGFDAEVVERANRAL--------KRRLGKLAYVLAALR--ALLRYR--PFRLRIELDG-----EEIEGEALL 191

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313103001 530 VVFLNIPRYcagtmpwghpGEHHDFEPQ-RHDDGYLEVIGFT-------MTSLAALQVGGHGE----RLTQCREVVLTTS 597
Cdd:COG1597  192 VAVGNGPYY----------GGGLRLAPDaSLDDGLLDVVVVRplsrlrlLRLLPRLLRGRHLRhpgvRYFRAREVEIESD 261

                        330       340
                 ....*....|....*....|....*...
gi 313103001 598 KAIPVQVDGEPCKLAAS-RIRI---ALR 621
Cdd:COG1597  262 RPLPVQLDGEPLGLATPlEFEVlpgALR 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
799-915 1.21e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 84.62  E-value: 1.21e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313103001 799 LIEAAKRNDFCKLQELHRAGGDLMHRDEQSRTLLHHAVSTGSKDVVRYLLDH-APPEILDAveeNGETCLHQAAALGQRT 877
Cdd:COG0666   91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAgADVNAQDN---DGNTPLHLAAANGNLE 167

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 313103001 878 ICHYIVEAGASLMKTDQQGDTPRQRAEKAQDTELAAYL 915
Cdd:COG0666  168 IVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
Ank_2 pfam12796
Ankyrin repeats (3 copies);
799-893 3.00e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.46  E-value: 3.00e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313103001  799 LIEAAKRNDFCKLQELHRAGGDLMHRDEQSRTLLHHAVSTGSKDVVRYLLDHAPPEILDaveeNGETCLHQAAALGQRTI 878
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD----NGRTALHYAARSGHLEI 76

                          90
                  ....*....|....*
gi 313103001  879 CHYIVEAGASLMKTD 893
Cdd:pfam12796  77 VKLLLEKGADINVKD 91
PRK12361 PRK12361
hypothetical protein; Provisional
 299-422 2.12e-08

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 57.71  E-value: 2.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313103001 299 KPLLVFVNPKSGGNQGAKIIQSFLWYLNPRqvFDLS--QGGP--------KEALEmyRKVHnlRILACGGDGTVGWILST 368
Cdd:PRK12361 243 KRAWLIANPVSGGGKWQEYGEQIQRELKAY--FDLTvkLTTPeisaealaKQARK--AGAD--IVIACGGDGTVTEVASE 316

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 313103001 369 L--DQLRLkppppvAILPLGTGNDLARTLnWGGGYTDEPVSKILSHVEEGNVVQLD 422
Cdd:PRK12361 317 LvnTDITL------GIIPLGTANALSHAL-FGLGSKLIPVEQACDNIIQGHTQRID 365
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
 177-236 1.79e-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: 48.59  E-value: 1.79e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 313103001  177 HHWVHRR-RQDGKCRHCGKgfqqkfTFHSKEIVAISCSWCKQAYHSKvsCFMLQQIEEPCS 236
Cdd:pfam00130   1 HHFVHRNfKQPTFCDHCGE------FLWGLGKQGLKCSWCKLNVHKR--CHEKVPPECGCD 53
PRK13057 PRK13057
lipid kinase;
302-607 4.04e-06

lipid kinase;


Pssm-ID: 183857 [Multi-domain]  Cd Length: 287  Bit Score: 49.53  E-value: 4.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313103001 302 LVFVNPKS--GGNQGAKIIQSF------LWYLNPRQVFDLSqggpkEALEMYRKVHNLRILAcGGDGTVGWILSTLDQLR 373
Cdd:PRK13057   1 LLLVNRHArsGRAALAAARAALeaagleLVEPPAEDPDDLS-----EVIEAYADGVDLVIVG-GGDGTLNAAAPALVETG 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313103001 374 LkpppPVAILPLGTGNDLARTLnwggGYTDEPvskilshVEEGNVV---QLDRWDLhAEPNPEAgpedrdegatdrlpld 450
Cdd:PRK13057  75 L----PLGILPLGTANDLARTL----GIPLDL-------EAAARVIatgQVRRIDL-GWVNGHY---------------- 122

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313103001 451 vFNNYFSLGFDAHVTLEFHesreanpEKFNSRFrNKMFYAGTAFSdfLMGSSKDLakHIRVVCDGMDLTPK-IQdlkpqc 529
Cdd:PRK13057 123 -FFNVASLGLSAELARRLT-------KELKRRW-GTLGYAIAALR--VLRRSRPF--TAEIEHDGRTERVKtLQ------ 183

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313103001 530 VVFLNiPRYCAGTMPwghpgEHHDFEPqrhDDGYLEVIGFTMTSLA-------ALQVGGHGE----RLTQCREVVLTTSK 598
Cdd:PRK13057 184 VAVGN-GRYYGGGMT-----VAHDATI---DDGRLDLYSLEVAHWWrllallpALRRGRHGEwpdvRAFRTTELELRTRK 254


                 ....*....
gi 313103001 599 AIPVQVDGE 607
Cdd:PRK13057 255 PRPINTDGE 263
PHA03095 PHA03095
ankyrin-like protein; Provisional
 805-899 1.07e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.79  E-value: 1.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313103001 805 RNDFCKLQELHRAGGDLMHRDEQSRTLLHHAVSTGSK---DVVRYLLDHAppeILDAVEENGETCLHQAAALGQRTICHY 881
Cdd:PHA03095 199 KPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCkrsLVLPLLIAGI---SINARNRYGQTPLHYAAVFNNPRACRR 275

                         90
                 ....*....|....*...
gi 313103001 882 IVEAGASLMKTDQQGDTP 899
Cdd:PHA03095 276 LIALGADINAVSSDGNTP 293
TIGR00147 TIGR00147
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ...
 352-395 1.80e-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: 1.80e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 313103001  352 RILACGGDGTVGWILSTLDQLRLKPPppVAILPLGTGNDLARTL 395
Cdd:TIGR00147  60 TVIAGGGDGTINEVVNALIQLDDIPA--LGILPLGTANDFARSL 101
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 829-850 2.24e-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: 2.24e-03
                           10        20
                   ....*....|....*....|..
gi 313103001   829 RTLLHHAVSTGSKDVVRYLLDH 850
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDK 24
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 799-891 4.79e-03

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: 40.77  E-value: 4.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313103001 799 LIEAAKRNDFCKLQELHR-AGGDLMHRDEQSRTLLHHAVSTGSKDVVRYLLDHAPPEILDAVEEN---GETCLHQAAALG 874
Cdd:cd22192   21 LLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMTSDlyqGETALHIAVVNQ 100

                         90
                 ....*....|....*..
gi 313103001 875 QRTICHYIVEAGASLMK 891
Cdd:cd22192  101 NLNLVRELIARGADVVS 117
 
Name Accession Description Interval E-value
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 451-608 5.14e-78

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: 250.72  E-value: 5.14e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313103001   451 VFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGTAFSDFLMGSSKDLAKHIRVVCDGMDLTPKIqdlKPQCV 530
Cdd:smart00045   1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLPN---SLEGI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313103001   531 VFLNIPRYCAGTMPWGHPGEH-HDFEPQRHDDGYLEVIGFTMTSLAA--LQVGGHGERLTQCREVVLT--TSKAIPVQVD 605
Cdd:smart00045  78 AVLNIPSYGGGTNLWGTTDKEdLNFSKQSHDDGLLEVVGLTGAMHMAqiRQVGLAGRRIAQCSEVRITikTSKTIPMQVD 157


                   ...
gi 313103001   606 GEP 608
Cdd:smart00045 158 GEP 160
DAGK_acc pfam00609
Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts ...
 451-608 3.95e-69

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: 226.71  E-value: 3.95e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313103001  451 VFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGTAFSDFLMGSSKDLAKHIRVVCDGMDLTPKiqdLKPQCV 530
Cdd:pfam00609   1 VMNNYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDMFQRSCKNLIEKVELEVDGKDLPLP---KSLEGI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313103001  531 VFLNIPRYCAGTMPWGHPGEHHD-FEPQRHDDGYLEVIGFT-MTSLAALQVGGHGE-RLTQCREVVLTTSKAIPVQVDGE 607
Cdd:pfam00609  78 VVLNIPSYAGGTDLWGNSKEDGLgFAPQSVDDGLLEVVGLTgALHLGQVQVGLGSAkRIAQGGPIRITTKKKIPMQVDGE 157


                  .
gi 313103001  608 P 608
Cdd:pfam00609 158 P 158
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 302-423 1.15e-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: 179.80  E-value: 1.15e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313103001   302 LVFVNPKSGGNQGAKIIQSFLWYLNPRQVFDLSQGGPKEALEMYRKVHN-LRILACGGDGTVGWILSTLDQLRLKPP-PP 379
Cdd:smart00046   1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVPDfNRVLVCGGDGTVGWVLNALDKRELPLPePP 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 313103001   380 VAILPLGTGNDLARTLNWGGGYTDEPVSKILSHVEEGNVVQLDR 423
Cdd:smart00046  81 VAVLPLGTGNDLARSLGWGGGYDGEKLLKTLRDALESDTVKLDR 124
C1_DGKzeta_rpt2 cd20895
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta ...
 175-249 2.29e-51

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: 174.12  E-value: 2.29e-51
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 313103001 175 VRHHWVHRRRQDGKCRHCGKGFQQKFTFHSKEIVAISCSWCKQAYHSKVSCFMLQQIEEPCSLGVHAAVVIPPTW 249
Cdd:cd20895    1 VRHHWVHRRRQEGKCRQCGKGFQQKFAFHSKEIVAISCSWCKQAYHSKVSCFMLQQIEEPCSLGAHAAVIVPPTW 75
C1_DGKzeta_rpt1 cd20849
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta (DAG ...
 93-165 3.29e-48

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: 165.11  E-value: 3.29e-48
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 313103001  93 DWS-SATYGEHIWFETNVSGDFCYVGEQYCVARMLQKSVSRRKCAACKIVVHTPCIEQLEKINFRCKPSFRESG 165
Cdd:cd20849    1 DWSeSAVYGEHIWFETNVSGDFCYVGEQNCVAKQLQKSVSRKKCAACKIVVHTPCIEQLEKINFRCKPSFRESG 74
C1_DGKiota_rpt2 cd20896
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase iota ...
 175-249 3.45e-46

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: 159.48  E-value: 3.45e-46
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 313103001 175 VRHHWVHRRRQDGKCRHCGKGFQQKFTFHSKEIVAISCSWCKQAYHSKVSCFMLQQIEEPCSLGVHAAVVIPPTW 249
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; ...
 177-238 3.19e-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: 144.80  E-value: 3.19e-41
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 313103001 177 HHWVHRRRQDGKCRHCGKGFQQKFTFHSKEIVAISCSWCKQAYHSKVSCFMLQQIEEPCSLG 238
Cdd:cd20855    1 HHWVHRRKQEGKCKQCGKSFQQKLSFSSKEIVAISCSWCKEAYHNKDSCFNMKKIEEPCNLG 62
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 300-422 1.79e-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: 130.78  E-value: 1.79e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313103001  300 PLLVFVNPKSGGNQGAKIIQSFLWYLNPRQV-FDLSQ-GGPKEALEMYRKV---HNLRILACGGDGTVGWILSTLDqlRL 374
Cdd:pfam00781   1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVeVELVLtEGPGDALELAREAaedGYDRIVVAGGDGTVNEVLNGLA--GL 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 313103001  375 KPPPPVAILPLGTGNDLARTLNWGGgytdePVSKILSHVEEGNVVQLD 422
Cdd:pfam00781  79 ATRPPLGIIPLGTGNDFARALGIPG-----DPEEALEAILKGQTRPVD 121
C1_DGKiota_rpt1 cd20850
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase iota (DAG ...
 93-165 2.59e-35

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: 128.60  E-value: 2.59e-35
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 313103001  93 DWS-SATYGEHIWFETNVSGDFCYVGEQYCVARmLQKSVSRRKCAACKIVVHTPCIEQLEKINFRCKPSFRESG 165
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; ...
 97-163 8.11e-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: 126.64  E-value: 8.11e-35
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 313103001  97 ATYGEHIWFETNVSGDFCYVGEQYCvarmlQKSVSRRKCAACKIVVHTPCIEQLEKINFRCKPSFRE 163
Cdd:cd20802    1 AVNGEHLWTDTSASGDLCYVGEQDC-----LKSGSRKKCSACKIVVHTGCIPQLEKINFKCKPTFRE 62
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 298-621 5.74e-28

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


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 114.95  E-value: 5.74e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313103001 298 MKPLLVFVNPKSGGNQGAKIIQSFLWYLNpRQVFDLSQ---GGPKEALEMYRKVHNL---RILACGGDGTVGWILSTLdq 371
Cdd:COG1597    2 MMRALLIVNPASGRGRAARLLERLVAALR-AAGLEVEVletESPGDATELAREAAAEgadLVVAAGGDGTVNEVANGL-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313103001 372 lrLKPPPPVAILPLGTGNDLARTLNwgggyTDEPVSKILSHVEEGNVVQLD--RwdlhaepnpeagpedrdegATDRLpl 449
Cdd:COG1597   79 --AGTGPPLGILPLGTGNDFARALG-----IPLDPEAALEALLTGRTRRIDlgR-------------------VNGRY-- 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313103001 450 dvFNNYFSLGFDAHVTLEFHESReanpekfnSRFRNKMFYAGTAFSdfLMGSSKdlAKHIRVVCDGmdltpKIQDLKPQC 529
Cdd:COG1597  131 --FLNVAGIGFDAEVVERANRAL--------KRRLGKLAYVLAALR--ALLRYR--PFRLRIELDG-----EEIEGEALL 191

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313103001 530 VVFLNIPRYcagtmpwghpGEHHDFEPQ-RHDDGYLEVIGFT-------MTSLAALQVGGHGE----RLTQCREVVLTTS 597
Cdd:COG1597  192 VAVGNGPYY----------GGGLRLAPDaSLDDGLLDVVVVRplsrlrlLRLLPRLLRGRHLRhpgvRYFRAREVEIESD 261

                        330       340
                 ....*....|....*....|....*...
gi 313103001 598 KAIPVQVDGEPCKLAAS-RIRI---ALR 621
Cdd:COG1597  262 RPLPVQLDGEPLGLATPlEFEVlpgALR 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
799-915 1.21e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 84.62  E-value: 1.21e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313103001 799 LIEAAKRNDFCKLQELHRAGGDLMHRDEQSRTLLHHAVSTGSKDVVRYLLDH-APPEILDAveeNGETCLHQAAALGQRT 877
Cdd:COG0666   91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAgADVNAQDN---DGNTPLHLAAANGNLE 167

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 313103001 878 ICHYIVEAGASLMKTDQQGDTPRQRAEKAQDTELAAYL 915
Cdd:COG0666  168 IVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
Ank_2 pfam12796
Ankyrin repeats (3 copies);
799-893 3.00e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.46  E-value: 3.00e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313103001  799 LIEAAKRNDFCKLQELHRAGGDLMHRDEQSRTLLHHAVSTGSKDVVRYLLDHAPPEILDaveeNGETCLHQAAALGQRTI 878
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD----NGRTALHYAARSGHLEI 76

                          90
                  ....*....|....*
gi 313103001  879 CHYIVEAGASLMKTD 893
Cdd:pfam12796  77 VKLLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
799-932 2.24e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 68.83  E-value: 2.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313103001 799 LIEAAKRNDFCKLQELHRAGGDLMHRDEQSRTLLHHAVSTGSKDVVRYLLDH-APPEILDAveeNGETCLHQAAALGQRT 877
Cdd:COG0666  157 LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAgADVNAKDN---DGKTALDLAAENGNLE 233

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 313103001 878 ICHYIVEAGASLMKTDQQGDTPRQRAEKAQDTELAAYLENRQHYQMIQREDQETA 932
Cdd:COG0666  234 IVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
C1_DGK_rpt2 cd20805
second protein kinase C conserved region 1 (C1 domain) found in the diacylglycerol kinase ...
 177-238 9.95e-12

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: 60.54  E-value: 9.95e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 313103001 177 HHWVHRRRQ-DGKCRHCGKGFQQKFTFHSKeivaiSCSWCKQAYHSkvSCFMLQQIEEpCSLG 238
Cdd:cd20805    1 HHWVEGNLPsGAKCSVCGKKCGSSFGLAGY-----RCSWCKRTVHS--ECIDKLGPEE-CDLG 55
PRK12361 PRK12361
hypothetical protein; Provisional
 299-422 2.12e-08

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 57.71  E-value: 2.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313103001 299 KPLLVFVNPKSGGNQGAKIIQSFLWYLNPRqvFDLS--QGGP--------KEALEmyRKVHnlRILACGGDGTVGWILST 368
Cdd:PRK12361 243 KRAWLIANPVSGGGKWQEYGEQIQRELKAY--FDLTvkLTTPeisaealaKQARK--AGAD--IVIACGGDGTVTEVASE 316

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 313103001 369 L--DQLRLkppppvAILPLGTGNDLARTLnWGGGYTDEPVSKILSHVEEGNVVQLD 422
Cdd:PRK12361 317 LvnTDITL------GIIPLGTANALSHAL-FGLGSKLIPVEQACDNIIQGHTQRID 365
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
 177-236 1.79e-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: 48.59  E-value: 1.79e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 313103001  177 HHWVHRR-RQDGKCRHCGKgfqqkfTFHSKEIVAISCSWCKQAYHSKvsCFMLQQIEEPCS 236
Cdd:pfam00130   1 HHFVHRNfKQPTFCDHCGE------FLWGLGKQGLKCSWCKLNVHKR--CHEKVPPECGCD 53
Ank_4 pfam13637
Ankyrin repeats (many copies);
829-883 7.53e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.88  E-value: 7.53e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 313103001  829 RTLLHHAVSTGSKDVVRYLLDHAPPeiLDAVEENGETCLHQAAALGQRTICHYIV 883
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGAD--INAVDGNGETALHFAASNGNVEVLKLLL 54
PRK13054 PRK13054
lipid kinase; Reviewed
 352-393 8.46e-07

lipid kinase; Reviewed


Pssm-ID: 237281 [Multi-domain]  Cd Length: 300  Bit Score: 51.80  E-value: 8.46e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 313103001 352 RILACGGDGTVGWILSTLDQLRLKPPPPVAILPLGTGNDLAR 393
Cdd:PRK13054  59 TVIAGGGDGTINEVATALAQLEGDARPALGILPLGTANDFAT 100
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
799-915 1.42e-06

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 51.11  E-value: 1.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313103001 799 LIEAAKRNDFCKLQELHRAGGDLMHRDEQSRTLLHHAVSTGSKDVVRYLLDHAPPeiLDAVEENGETCLHQAAALGQRTI 878
Cdd:COG0666   25 LLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGAD--INAKDDGGNTLLHAAARNGDLEI 102

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 313103001 879 CHYIVEAGASLMKTDQQGDTPRQRAEKAQDTELAAYL 915
Cdd:COG0666  103 VKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLL 139
PRK13057 PRK13057
lipid kinase;
302-607 4.04e-06

lipid kinase;


Pssm-ID: 183857 [Multi-domain]  Cd Length: 287  Bit Score: 49.53  E-value: 4.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313103001 302 LVFVNPKS--GGNQGAKIIQSF------LWYLNPRQVFDLSqggpkEALEMYRKVHNLRILAcGGDGTVGWILSTLDQLR 373
Cdd:PRK13057   1 LLLVNRHArsGRAALAAARAALeaagleLVEPPAEDPDDLS-----EVIEAYADGVDLVIVG-GGDGTLNAAAPALVETG 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313103001 374 LkpppPVAILPLGTGNDLARTLnwggGYTDEPvskilshVEEGNVV---QLDRWDLhAEPNPEAgpedrdegatdrlpld 450
Cdd:PRK13057  75 L----PLGILPLGTANDLARTL----GIPLDL-------EAAARVIatgQVRRIDL-GWVNGHY---------------- 122

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313103001 451 vFNNYFSLGFDAHVTLEFHesreanpEKFNSRFrNKMFYAGTAFSdfLMGSSKDLakHIRVVCDGMDLTPK-IQdlkpqc 529
Cdd:PRK13057 123 -FFNVASLGLSAELARRLT-------KELKRRW-GTLGYAIAALR--VLRRSRPF--TAEIEHDGRTERVKtLQ------ 183

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313103001 530 VVFLNiPRYCAGTMPwghpgEHHDFEPqrhDDGYLEVIGFTMTSLA-------ALQVGGHGE----RLTQCREVVLTTSK 598
Cdd:PRK13057 184 VAVGN-GRYYGGGMT-----VAHDATI---DDGRLDLYSLEVAHWWrllallpALRRGRHGEwpdvRAFRTTELELRTRK 254


                 ....*....
gi 313103001 599 AIPVQVDGE 607
Cdd:PRK13057 255 PRPINTDGE 263
PRK13059 PRK13059
putative lipid kinase; Reviewed
 298-396 4.93e-06

putative lipid kinase; Reviewed


Pssm-ID: 183858  Cd Length: 295  Bit Score: 49.26  E-value: 4.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313103001 298 MKPLLVFVNPKSGGNQGA----KIIQSFLWYLNPRQVFDLSQGGP-KEALEMYRKVHNLrILACGGDGTVGWILSTLDQL 372
Cdd:PRK13059   1 MKKVKFIYNPYSGENAIIseldKVIRIHQEKGYLVVPYRISLEYDlKNAFKDIDESYKY-ILIAGGDGTVDNVVNAMKKL 79

                         90       100
                 ....*....|....*....|....
gi 313103001 373 RLKPPppVAILPLGTGNDLARTLN 396
Cdd:PRK13059  80 NIDLP--IGILPVGTANDFAKFLG 101
Ank_2 pfam12796
Ankyrin repeats (3 copies);
832-915 7.95e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 45.11  E-value: 7.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313103001  832 LHHAVSTGSKDVVRYLLDHapPEILDAVEENGETCLHQAAALGQRTICHYIVEAGASLMKTDqqGDTPRQRAEKAQDTEL 911
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLEN--GADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN--GRTALHYAARSGHLEI 76


                  ....
gi 313103001  912 AAYL 915
Cdd:pfam12796  77 VKLL 80
PRK13055 PRK13055
putative lipid kinase; Reviewed
 353-396 2.71e-05

putative lipid kinase; Reviewed


Pssm-ID: 237282 [Multi-domain]  Cd Length: 334  Bit Score: 47.29  E-value: 2.71e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 313103001 353 ILACGGDGTVGWILSTLDQlrLKPPPPVAILPLGTGNDLARTLN 396
Cdd:PRK13055  63 IIAAGGDGTINEVVNGIAP--LEKRPKMAIIPAGTTNDYARALK 104
Ank_4 pfam13637
Ankyrin repeats (many copies);
799-848 5.72e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.49  E-value: 5.72e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 313103001  799 LIEAAKRNDFCKLQELHRAGGDLMHRDEQSRTLLHHAVSTGSKDVVRYLL 848
Cdd:pfam13637   5 LHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 805-899 1.07e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.79  E-value: 1.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313103001 805 RNDFCKLQELHRAGGDLMHRDEQSRTLLHHAVSTGSK---DVVRYLLDHAppeILDAVEENGETCLHQAAALGQRTICHY 881
Cdd:PHA03095 199 KPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCkrsLVLPLLIAGI---SINARNRYGQTPLHYAAVFNNPRACRR 275

                         90
                 ....*....|....*...
gi 313103001 882 IVEAGASLMKTDQQGDTP 899
Cdd:PHA03095 276 LIALGADINAVSSDGNTP 293
Ank_5 pfam13857
Ankyrin repeats (many copies);
814-870 1.06e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 1.06e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 313103001  814 LHRAGG-DLMHRDEQSRTLLHHAVSTGSKDVVRYLLDHapPEILDAVEENGETCLHQA 870
Cdd:pfam13857   1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAY--GVDLNLKDEEGLTALDLA 56
TIGR00147 TIGR00147
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ...
 352-395 1.80e-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: 1.80e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 313103001  352 RILACGGDGTVGWILSTLDQLRLKPPppVAILPLGTGNDLARTL 395
Cdd:TIGR00147  60 TVIAGGGDGTINEVVNALIQLDDIPA--LGILPLGTANDFARSL 101
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 829-850 2.24e-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: 2.24e-03
                           10        20
                   ....*....|....*....|..
gi 313103001   829 RTLLHHAVSTGSKDVVRYLLDH 850
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDK 24
PHA03095 PHA03095
ankyrin-like protein; Provisional
 800-899 3.65e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 40.78  E-value: 3.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313103001 800 IEAAKRNDFCKLQELHRAGGDLMHRDEQSRTLLHHAVSTGS---KDVVRYLLDHAPpeILDAVEENGETCLHQAAALGQR 876
Cdd:PHA03095  19 LLNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGA--DVNAPERCGFTPLHLYLYNATT 96

                         90       100
                 ....*....|....*....|....
gi 313103001 877 -TICHYIVEAGASLMKTDQQGDTP 899
Cdd:PHA03095  97 lDVIKLLIKAGADVNAKDKVGRTP 120
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 802-903 3.85e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 40.72  E-value: 3.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313103001 802 AAKRNDFCKLQELHRAGGDLMHRDEQSRTLLHHAVSTGSKDVVRYLLDHAPpeILDAVEENGETCLHQAAALGQRTICHY 881
Cdd:PHA02874 131 AIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGA--YANVKDNNGESPLHNAAEYGDYACIKL 208

                         90       100
                 ....*....|....*....|..
gi 313103001 882 IVEAGASLMKTDQQGDTPRQRA 903
Cdd:PHA02874 209 LIDHGNHIMNKCKNGFTPLHNA 230
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 817-915 4.26e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 40.72  E-value: 4.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313103001 817 AGGDLMHRDEQSRTLLHHAVSTGSKDVVRYLLDH-APPEILDaveENGETCLHQAAALGQRTICHYIVEAGASLMKTDQQ 895
Cdd:PHA02874 113 CGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYgADVNIED---DNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNN 189

                         90       100
                 ....*....|....*....|
gi 313103001 896 GDTPRQRAEKAQDTELAAYL 915
Cdd:PHA02874 190 GESPLHNAAEYGDYACIKLL 209
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 799-891 4.79e-03

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: 40.77  E-value: 4.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313103001 799 LIEAAKRNDFCKLQELHR-AGGDLMHRDEQSRTLLHHAVSTGSKDVVRYLLDHAPPEILDAVEEN---GETCLHQAAALG 874
Cdd:cd22192   21 LLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMTSDlyqGETALHIAVVNQ 100

                         90
                 ....*....|....*..
gi 313103001 875 QRTICHYIVEAGASLMK 891
Cdd:cd22192  101 NLNLVRELIARGADVVS 117
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 824-872 5.63e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 40.03  E-value: 5.63e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 313103001 824 RDEQSRTLLHHAVSTGSKDVVRYLLDH-APPEILDaveENGETCLHQAAA 872
Cdd:PHA03100 188 KDVYGFTPLHYAVYNNNPEFVKYLLDLgANPNLVN---KYGDTPLHIAIL 234
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 790-878 7.28e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 40.24  E-value: 7.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313103001 790 DAAPPQGEELIEAAKRNDFCKLQELHRAGGDLMHRDEQSRTLLHHAVSTGSKDVVRYLLDHA-PPEILDAveeNGETCLH 868
Cdd:PLN03192 520 HDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHAcNVHIRDA---NGNTALW 596

                         90
                 ....*....|
gi 313103001 869 QAAALGQRTI 878
Cdd:PLN03192 597 NAISAKHHKI 606
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 829-850 7.84e-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: 7.84e-03
                          10        20
                  ....*....|....*....|..
gi 313103001  829 RTLLHHAVSTGSKDVVRYLLDH 850
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLEN 24
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 796-848 8.77e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 39.85  E-value: 8.77e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 313103001 796 GEELIEAAKRNDFCKLQELHRAGGDLMHRDEQSRTLLHHAVSTGSKDVVRYLL 848
Cdd:PLN03192 623 GDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLI 675
 
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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