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Conserved domains on  [gi|161077650|ref|NP_001096916|]
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retinal degeneration A, isoform B [Drosophila melanogaster]

Protein Classification

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 ...
 516-670 6.34e-77

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: 249.17  E-value: 6.34e-77
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650    516 VINNYFSFGVDAHIALEFHEAREAHPERFNSRLRNKMYYGQMGGKDLILRQYRNLSQWVTLECDGQDFTGKLrdaGCHAV 595
Cdd:smart00045    1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLPN---SLEGI 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650    596 LFLNIPSYGGGTHPWNDS----FGASKPSIDDGLMEVVGLTTYQLP--MLQAGMHGTCICQCRKAR--IITKRTIPMQVD 667
Cdd:smart00045   78 AVLNIPSYGGGTNLWGTTdkedLNFSKQSHDDGLLEVVGLTGAMHMaqIRQVGLAGRRIAQCSEVRitIKTSKTIPMQVD 157


                    ...
gi 161077650    668 GEA 670
Cdd:smart00045  158 GEP 160
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 366-489 2.70e-55

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: 187.50  E-value: 2.70e-55
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650    366 IVFINPKSGGNQGHKLLGKFQHLLNPRQVFDLTQGGPKMGLDMFRKAPN-LRVLACGGDGTVGWVLSVLDQIQPPLqPAP 444
Cdd:smart00046    1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVPDfNRVLVCGGDGTVGWVLNALDKRELPL-PEP 79

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*
gi 161077650    445 AVGVLPLGTGNDLARALGWGGGYTDEPIGKILREIGMSQCVLMDR 489
Cdd:smart00046   80 PVAVLPLGTGNDLARSLGWGGGYDGEKLLKTLRDALESDTVKLDR 124
C1_DGK_typeIV_rpt2 cd20855
second protein kinase C conserved region 1 (C1 domain) found in type IV diacylglycerol kinases; ...
 213-279 1.45e-30

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: 114.75  E-value: 1.45e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 161077650  213 HHWVHRKLEKGKCKQCGKFFpmkqavQSKL-FGSKEIVALACAWCHEIYHNKEACFNQAKIGEECRLG 279
Cdd:cd20855     1 HHWVHRRKQEGKCKQCGKSF------QQKLsFSSKEIVAISCSWCKEAYHNKDSCFNMKKIEEPCNLG 62
C1_DGK_typeIV_rpt1 cd20802
first protein kinase C conserved region 1 (C1 domain) found in type IV diacylglycerol kinases; ...
 138-199 5.31e-29

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: 110.08  E-value: 5.31e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161077650  138 AVQGEHYWKPTSASGDLCCLNE-ECIKSGQRMKCSACQLVAHHNCIPFVNEKStLACKPTYRD 199
Cdd:cd20802     1 AVNGEHLWTDTSASGDLCYVGEqDCLKSGSRKKCSACKIVVHTGCIPQLEKIN-FKCKPTFRE 62
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
894-1015 1.06e-23

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 102.34  E-value: 1.06e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650  894 AILLAAQSGDLNMLRALHEQGYSLQSVNKNGQTALHFACKYNHRDIVKYIIAS-ATrrlINMADKElGQTALHIAAEQNR 972
Cdd:COG0666   123 PLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAgAD---VNARDND-GETPLHLAAENGH 198

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 161077650  973 RDICVMLVAAGAHLDTLDSGGNTPMMVAFNKNANEIATYLESQ 1015
Cdd:COG0666   199 LEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
 
Name Accession Description Interval E-value
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 516-670 6.34e-77

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: 249.17  E-value: 6.34e-77
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650    516 VINNYFSFGVDAHIALEFHEAREAHPERFNSRLRNKMYYGQMGGKDLILRQYRNLSQWVTLECDGQDFTGKLrdaGCHAV 595
Cdd:smart00045    1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLPN---SLEGI 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650    596 LFLNIPSYGGGTHPWNDS----FGASKPSIDDGLMEVVGLTTYQLP--MLQAGMHGTCICQCRKAR--IITKRTIPMQVD 667
Cdd:smart00045   78 AVLNIPSYGGGTNLWGTTdkedLNFSKQSHDDGLLEVVGLTGAMHMaqIRQVGLAGRRIAQCSEVRitIKTSKTIPMQVD 157


                    ...
gi 161077650    668 GEA 670
Cdd:smart00045  158 GEP 160
DAGK_acc pfam00609
Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts ...
 516-670 1.46e-67

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: 223.25  E-value: 1.46e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650   516 VINNYFSFGVDAHIALEFHEAREAHPERFNSRLRNKMYYGQMGGKDLILRQYRNLSQWVTLECDGQDFtgKLRdAGCHAV 595
Cdd:pfam00609    1 VMNNYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDMFQRSCKNLIEKVELEVDGKDL--PLP-KSLEGI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650   596 LFLNIPSYGGGTHPWNDSF----GASKPSIDDGLMEVVGLT-TYQLPMLQAGMH-GTCICQCRKARIITKRTIPMQVDGE 669
Cdd:pfam00609   78 VVLNIPSYAGGTDLWGNSKedglGFAPQSVDDGLLEVVGLTgALHLGQVQVGLGsAKRIAQGGPIRITTKKKIPMQVDGE 157


                   .
gi 161077650   670 A 670
Cdd:pfam00609  158 P 158
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 366-489 2.70e-55

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: 187.50  E-value: 2.70e-55
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650    366 IVFINPKSGGNQGHKLLGKFQHLLNPRQVFDLTQGGPKMGLDMFRKAPN-LRVLACGGDGTVGWVLSVLDQIQPPLqPAP 444
Cdd:smart00046    1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVPDfNRVLVCGGDGTVGWVLNALDKRELPL-PEP 79

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*
gi 161077650    445 AVGVLPLGTGNDLARALGWGGGYTDEPIGKILREIGMSQCVLMDR 489
Cdd:smart00046   80 PVAVLPLGTGNDLARSLGWGGGYDGEKLLKTLRDALESDTVKLDR 124
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 364-465 7.37e-36

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: 131.94  E-value: 7.37e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650   364 PVIVFINPKSGGNQGHKLLGKFQHLLNPRQV-FDLTQ-GGPKMGLDMFRKAPNL---RVLACGGDGTVGWVLSVLDQIQP 438
Cdd:pfam00781    1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVeVELVLtEGPGDALELAREAAEDgydRIVVAGGDGTVNEVLNGLAGLAT 80

                           90       100
                   ....*....|....*....|....*..
gi 161077650   439 PlqpaPAVGVLPLGTGNDLARALGWGG 465
Cdd:pfam00781   81 R----PPLGIIPLGTGNDFARALGIPG 103
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 365-687 7.88e-33

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


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 129.20  E-value: 7.88e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650  365 VIVFINPKSGGNQGHKLLGKFQHLLNPR----QVFDLTQGGPkmGLDMFRKAPNL---RVLACGGDGTVGWVLSVLDQIQ 437
Cdd:COG1597     5 ALLIVNPASGRGRAARLLERLVAALRAAglevEVLETESPGD--ATELAREAAAEgadLVVAAGGDGTVNEVANGLAGTG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650  438 PPLqpapavGVLPLGTGNDLARALGwgggyTDEPIGKILREIGMSQCVLMDRWRVkvtpnddvtDDHVdrskpnvplnVI 517
Cdd:COG1597    83 PPL------GILPLGTGNDFARALG-----IPLDPEAALEALLTGRTRRIDLGRV---------NGRY----------FL 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650  518 NNyFSFGVDAHIALEFHEAReahperfnSRLRNKMYYGQMGGKdlILRQYRNLSqwVTLECDGQDFTGKlrdagCHAVLF 597
Cdd:COG1597   133 NV-AGIGFDAEVVERANRAL--------KRRLGKLAYVLAALR--ALLRYRPFR--LRIELDGEEIEGE-----ALLVAV 194

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650  598 LNIPSYGGGTHPwndsfgASKPSIDDGLMEVVGLTT-------YQLPMLQAGMHGTC----ICQCRKARIITKRTIPMQV 666
Cdd:COG1597   195 GNGPYYGGGLRL------APDASLDDGLLDVVVVRPlsrlrllRLLPRLLRGRHLRHpgvrYFRAREVEIESDRPLPVQL 268

                         330       340
                  ....*....|....*....|.
gi 161077650  667 DGEACRVKPSViEIELLNKAL 687
Cdd:COG1597   269 DGEPLGLATPL-EFEVLPGAL 288
C1_DGK_typeIV_rpt2 cd20855
second protein kinase C conserved region 1 (C1 domain) found in type IV diacylglycerol kinases; ...
 213-279 1.45e-30

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: 114.75  E-value: 1.45e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 161077650  213 HHWVHRKLEKGKCKQCGKFFpmkqavQSKL-FGSKEIVALACAWCHEIYHNKEACFNQAKIGEECRLG 279
Cdd:cd20855     1 HHWVHRRKQEGKCKQCGKSF------QQKLsFSSKEIVAISCSWCKEAYHNKDSCFNMKKIEEPCNLG 62
C1_DGK_typeIV_rpt1 cd20802
first protein kinase C conserved region 1 (C1 domain) found in type IV diacylglycerol kinases; ...
 138-199 5.31e-29

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: 110.08  E-value: 5.31e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161077650  138 AVQGEHYWKPTSASGDLCCLNE-ECIKSGQRMKCSACQLVAHHNCIPFVNEKStLACKPTYRD 199
Cdd:cd20802     1 AVNGEHLWTDTSASGDLCYVGEqDCLKSGSRKKCSACKIVVHTGCIPQLEKIN-FKCKPTFRE 62
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
894-1015 1.06e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 102.34  E-value: 1.06e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650  894 AILLAAQSGDLNMLRALHEQGYSLQSVNKNGQTALHFACKYNHRDIVKYIIAS-ATrrlINMADKElGQTALHIAAEQNR 972
Cdd:COG0666   123 PLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAgAD---VNARDND-GETPLHLAAENGH 198

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 161077650  973 RDICVMLVAAGAHLDTLDSGGNTPMMVAFNKNANEIATYLESQ 1015
Cdd:COG0666   199 LEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
Ank_2 pfam12796
Ankyrin repeats (3 copies);
895-990 8.72e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.86  E-value: 8.72e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650   895 ILLAAQSGDLNMLRALHEQGYSLQSVNKNGQTALHFACKYNHRDIVKYIIASATRRLINMadkelGQTALHIAAEQNRRD 974
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN-----GRTALHYAARSGHLE 75

                           90
                   ....*....|....*.
gi 161077650   975 ICVMLVAAGAHLDTLD 990
Cdd:pfam12796   76 IVKLLLEKGADINVKD 91
TIGR00147 TIGR00147
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ...
 369-680 2.33e-11

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: 65.99  E-value: 2.33e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650   369 INPKSGGNQGHKLLGKFQHLLNPRQVFDLTQGGPKMGLDMF-----RKAPNLRVLACGGDGTVGWVLSVLDqiqpPLQPA 443
Cdd:TIGR00147    8 LNPTAGKSNDNKPLREVIMLLREEGMEIHVRVTWEKGDAARyveeaRKFGVDTVIAGGGDGTINEVVNALI----QLDDI 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650   444 PAVGVLPLGTGNDLARALGWgggytdePIgKILREIgmsqcvlmdrwrvKVTPNDDVTDdhVDRSKPNVPLNVInNYFSF 523
Cdd:TIGR00147   84 PALGILPLGTANDFARSLGI-------PE-DLDKAA-------------KLVIAGDARA--IDMGQVNKQYCFI-NMAGG 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650   524 GVDAHIALEFheareahPERFNSRLRNKMYYgqmggkdliLRQYRNLS--QWVTLECDGQDFTGKLrdagcHAVLFL--N 599
Cdd:TIGR00147  140 GFGTEITTET-------PEKLKAALGSLSYI---------LSGLMRMDtlQPFRCEIRGEGEHWQG-----EAVVFLvgN 198

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650   600 IPSYGGGTHPWNDSfgaskpSIDDGLMEVVGLTTYQL-------PMLQAGMH----GTCICQCRKARIITKRTIPMQVDG 668
Cdd:TIGR00147  199 GRQAGGGQKLAPDA------SINDGLLDLRIFTNDNLlpalvltLMSDEGKHtdnpNIIYGKASRIDIQTPHKITFNLDG 272

                          330
                   ....*....|..
gi 161077650   669 EACRVKPSVIEI 680
Cdd:TIGR00147  273 EPLGGTPFHIEI 284
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
 143-192 5.97e-08

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: 50.13  E-value: 5.97e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 161077650   143 HYWKPTS-ASGDLCCLNEECI--KSGQRMKCSACQLVAHHNCIPFVNEKSTLA 192
Cdd:pfam00130    1 HHFVHRNfKQPTFCDHCGEFLwgLGKQGLKCSWCKLNVHKRCHEKVPPECGCD 53
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
 213-277 8.92e-08

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: 49.36  E-value: 8.92e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 161077650   213 HHWVHRKLEK-GKCKQCGKFFPMKqavqsklfgskEIVALACAWCHEIYHNKeaCFNQAKIGEECR 277
Cdd:pfam00130    1 HHFVHRNFKQpTFCDHCGEFLWGL-----------GKQGLKCSWCKLNVHKR--CHEKVPPECGCD 53
PRK13054 PRK13054
lipid kinase; Reviewed
 416-462 6.18e-07

lipid kinase; Reviewed


Pssm-ID: 237281 [Multi-domain]  Cd Length: 300  Bit Score: 52.57  E-value: 6.18e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 161077650  416 RVLACGGDGTVGWVLSVLDQIQPPLQpaPAVGVLPLGTGNDLARALG 462
Cdd:PRK13054   59 TVIAGGGDGTINEVATALAQLEGDAR--PALGILPLGTANDFATAAG 103
PHA03095 PHA03095
ankyrin-like protein; Provisional
 907-1015 7.10e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 53.10  E-value: 7.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650  907 LRALHEQGYSLQSVNKNGQTALHFACKYN---HRDIVKYIIASATrrlINMADKeLGQTALHIAAEQNRRDICVMLVAAG 983
Cdd:PHA03095  205 VRELIRAGCDPAATDMLGNTPLHSMATGSsckRSLVLPLLIAGIS---INARNR-YGQTPLHYAAVFNNPRACRRLIALG 280

                          90       100       110
                  ....*....|....*....|....*....|...
gi 161077650  984 AHLDTLDSGGNTPMMVAF-NKNANEIATYLESQ 1015
Cdd:PHA03095  281 ADINAVSSDGNTPLSLMVrNNNGRAVRAALAKN 313
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
 142-187 1.65e-06

Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.


Pssm-ID: 197519  Cd Length: 50  Bit Score: 45.92  E-value: 1.65e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 161077650    142 EHYWKPTSASGDLCCLNEECIKSG--QRMKCSACQLVAHHNCIPFVNE 187
Cdd:smart00109    1 HKHVFRTFTKPTFCCVCRKSIWGSfkQGLRCSECKVKCHKKCADKVPK 48
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 865-984 1.91e-06

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: 51.94  E-value: 1.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650  865 WKSNKDRLFsfnedvfgcgfspILEQ---TSDAILLAAQSGDLNMLRAL--------HEQGySLqsvnknGQTALHFACK 933
Cdd:cd22192     1 WAQMLDELH-------------LLQQkriSESPLLLAAKENDVQAIKKLlkcpscdlFQRG-AL------GETALHVAAL 60

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 161077650  934 YNHRDIVKyIIASATRRLINMA---DKELGQTALHIAAEQNRRDICVMLVAAGA 984
Cdd:cd22192    61 YDNLEAAV-VLMEAAPELVNEPmtsDLYQGETALHIAVVNQNLNLVRELIARGA 113
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 923-944 1.06e-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: 37.18  E-value: 1.06e-03
                            10        20
                    ....*....|....*....|..
gi 161077650    923 NGQTALHFACKYNHRDIVKYII 944
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLL 22
 
Name Accession Description Interval E-value
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 516-670 6.34e-77

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: 249.17  E-value: 6.34e-77
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650    516 VINNYFSFGVDAHIALEFHEAREAHPERFNSRLRNKMYYGQMGGKDLILRQYRNLSQWVTLECDGQDFTGKLrdaGCHAV 595
Cdd:smart00045    1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLPN---SLEGI 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650    596 LFLNIPSYGGGTHPWNDS----FGASKPSIDDGLMEVVGLTTYQLP--MLQAGMHGTCICQCRKAR--IITKRTIPMQVD 667
Cdd:smart00045   78 AVLNIPSYGGGTNLWGTTdkedLNFSKQSHDDGLLEVVGLTGAMHMaqIRQVGLAGRRIAQCSEVRitIKTSKTIPMQVD 157


                    ...
gi 161077650    668 GEA 670
Cdd:smart00045  158 GEP 160
DAGK_acc pfam00609
Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts ...
 516-670 1.46e-67

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: 223.25  E-value: 1.46e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650   516 VINNYFSFGVDAHIALEFHEAREAHPERFNSRLRNKMYYGQMGGKDLILRQYRNLSQWVTLECDGQDFtgKLRdAGCHAV 595
Cdd:pfam00609    1 VMNNYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDMFQRSCKNLIEKVELEVDGKDL--PLP-KSLEGI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650   596 LFLNIPSYGGGTHPWNDSF----GASKPSIDDGLMEVVGLT-TYQLPMLQAGMH-GTCICQCRKARIITKRTIPMQVDGE 669
Cdd:pfam00609   78 VVLNIPSYAGGTDLWGNSKedglGFAPQSVDDGLLEVVGLTgALHLGQVQVGLGsAKRIAQGGPIRITTKKKIPMQVDGE 157


                   .
gi 161077650   670 A 670
Cdd:pfam00609  158 P 158
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 366-489 2.70e-55

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: 187.50  E-value: 2.70e-55
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650    366 IVFINPKSGGNQGHKLLGKFQHLLNPRQVFDLTQGGPKMGLDMFRKAPN-LRVLACGGDGTVGWVLSVLDQIQPPLqPAP 444
Cdd:smart00046    1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVPDfNRVLVCGGDGTVGWVLNALDKRELPL-PEP 79

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*
gi 161077650    445 AVGVLPLGTGNDLARALGWGGGYTDEPIGKILREIGMSQCVLMDR 489
Cdd:smart00046   80 PVAVLPLGTGNDLARSLGWGGGYDGEKLLKTLRDALESDTVKLDR 124
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 364-465 7.37e-36

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: 131.94  E-value: 7.37e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650   364 PVIVFINPKSGGNQGHKLLGKFQHLLNPRQV-FDLTQ-GGPKMGLDMFRKAPNL---RVLACGGDGTVGWVLSVLDQIQP 438
Cdd:pfam00781    1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVeVELVLtEGPGDALELAREAAEDgydRIVVAGGDGTVNEVLNGLAGLAT 80

                           90       100
                   ....*....|....*....|....*..
gi 161077650   439 PlqpaPAVGVLPLGTGNDLARALGWGG 465
Cdd:pfam00781   81 R----PPLGIIPLGTGNDFARALGIPG 103
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 365-687 7.88e-33

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


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 129.20  E-value: 7.88e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650  365 VIVFINPKSGGNQGHKLLGKFQHLLNPR----QVFDLTQGGPkmGLDMFRKAPNL---RVLACGGDGTVGWVLSVLDQIQ 437
Cdd:COG1597     5 ALLIVNPASGRGRAARLLERLVAALRAAglevEVLETESPGD--ATELAREAAAEgadLVVAAGGDGTVNEVANGLAGTG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650  438 PPLqpapavGVLPLGTGNDLARALGwgggyTDEPIGKILREIGMSQCVLMDRWRVkvtpnddvtDDHVdrskpnvplnVI 517
Cdd:COG1597    83 PPL------GILPLGTGNDFARALG-----IPLDPEAALEALLTGRTRRIDLGRV---------NGRY----------FL 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650  518 NNyFSFGVDAHIALEFHEAReahperfnSRLRNKMYYGQMGGKdlILRQYRNLSqwVTLECDGQDFTGKlrdagCHAVLF 597
Cdd:COG1597   133 NV-AGIGFDAEVVERANRAL--------KRRLGKLAYVLAALR--ALLRYRPFR--LRIELDGEEIEGE-----ALLVAV 194

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650  598 LNIPSYGGGTHPwndsfgASKPSIDDGLMEVVGLTT-------YQLPMLQAGMHGTC----ICQCRKARIITKRTIPMQV 666
Cdd:COG1597   195 GNGPYYGGGLRL------APDASLDDGLLDVVVVRPlsrlrllRLLPRLLRGRHLRHpgvrYFRAREVEIESDRPLPVQL 268

                         330       340
                  ....*....|....*....|.
gi 161077650  667 DGEACRVKPSViEIELLNKAL 687
Cdd:COG1597   269 DGEPLGLATPL-EFEVLPGAL 288
C1_DGK_typeIV_rpt2 cd20855
second protein kinase C conserved region 1 (C1 domain) found in type IV diacylglycerol kinases; ...
 213-279 1.45e-30

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: 114.75  E-value: 1.45e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 161077650  213 HHWVHRKLEKGKCKQCGKFFpmkqavQSKL-FGSKEIVALACAWCHEIYHNKEACFNQAKIGEECRLG 279
Cdd:cd20855     1 HHWVHRRKQEGKCKQCGKSF------QQKLsFSSKEIVAISCSWCKEAYHNKDSCFNMKKIEEPCNLG 62
C1_DGK_typeIV_rpt1 cd20802
first protein kinase C conserved region 1 (C1 domain) found in type IV diacylglycerol kinases; ...
 138-199 5.31e-29

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: 110.08  E-value: 5.31e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161077650  138 AVQGEHYWKPTSASGDLCCLNE-ECIKSGQRMKCSACQLVAHHNCIPFVNEKStLACKPTYRD 199
Cdd:cd20802     1 AVNGEHLWTDTSASGDLCYVGEqDCLKSGSRKKCSACKIVVHTGCIPQLEKIN-FKCKPTFRE 62
C1_DGKiota_rpt2 cd20896
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase iota ...
 213-290 1.55e-26

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: 103.63  E-value: 1.55e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 161077650  213 HHWVHRKLEKGKCKQCGKFFPMKQAvqsklFGSKEIVALACAWCHEIYHNKEACFNQAKIGEECRLGNYAPIIVPPSW 290
Cdd:cd20896     3 HHWVHRRRQEGKCKQCGKGFQQKFS-----FHSKEIVAISCSWCKQAFHNKVTCFMLHHIEEPCSLGAHAAVIVPPTW 75
C1_DGKzeta_rpt2 cd20895
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta ...
 213-290 4.04e-26

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: 102.47  E-value: 4.04e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 161077650  213 HHWVHRKLEKGKCKQCGKFFPMKQAvqsklFGSKEIVALACAWCHEIYHNKEACFNQAKIGEECRLGNYAPIIVPPSW 290
Cdd:cd20895     3 HHWVHRRRQEGKCRQCGKGFQQKFA-----FHSKEIVAISCSWCKQAYHSKVSCFMLQQIEEPCSLGAHAAVIVPPTW 75
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
894-1015 1.06e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 102.34  E-value: 1.06e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650  894 AILLAAQSGDLNMLRALHEQGYSLQSVNKNGQTALHFACKYNHRDIVKYIIAS-ATrrlINMADKElGQTALHIAAEQNR 972
Cdd:COG0666   123 PLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAgAD---VNARDND-GETPLHLAAENGH 198

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 161077650  973 RDICVMLVAAGAHLDTLDSGGNTPMMVAFNKNANEIATYLESQ 1015
Cdd:COG0666   199 LEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
892-1012 1.82e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 101.95  E-value: 1.82e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650  892 SDAILLAAQSGDLNMLRALHEQGYSLQSVNKNGQTALHFACKYNHRDIVKYIIASATRrlINMADKElGQTALHIAAEQN 971
Cdd:COG0666    88 NTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGAD--VNAQDND-GNTPLHLAAANG 164

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 161077650  972 RRDICVMLVAAGAHLDTLDSGGNTPMMVAFNKNANEIATYL 1012
Cdd:COG0666   165 NLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
Ank_2 pfam12796
Ankyrin repeats (3 copies);
895-990 8.72e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.86  E-value: 8.72e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650   895 ILLAAQSGDLNMLRALHEQGYSLQSVNKNGQTALHFACKYNHRDIVKYIIASATRRLINMadkelGQTALHIAAEQNRRD 974
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN-----GRTALHYAARSGHLE 75

                           90
                   ....*....|....*.
gi 161077650   975 ICVMLVAAGAHLDTLD 990
Cdd:pfam12796   76 IVKLLLEKGADINVKD 91
C1_DGKiota_rpt1 cd20850
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase iota (DAG ...
 133-201 6.54e-20

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: 84.69  E-value: 6.54e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161077650  133 DWTENAVQGEHYWKPTSASGDLCCLNEE-CI----KSGQRMKCSACQLVAHHNCIPFVnEKSTLACKPTYRDVG 201
Cdd:cd20850     1 DWSENAVNGEHLWLETNVSGDLCYLGEEnCQvkfaKSALRRKCAACKIVVHTACIEQL-EKINFRCKPTFREGG 73
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
889-1012 2.32e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 83.85  E-value: 2.32e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650  889 EQTSDAILLAAQSGDLNMLRALHEQGYSLQSVNKNGQTALHFACKYNHRDIVKYIIASATRrlINMADKElGQTALHIAA 968
Cdd:COG0666    52 ALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGAD--VNARDKD-GETPLHLAA 128

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 161077650  969 EQNRRDICVMLVAAGAHLDTLDSGGNTPMMVAFNKNANEIATYL 1012
Cdd:COG0666   129 YNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
894-1012 3.07e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 83.46  E-value: 3.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650  894 AILLAAQSGDLNMLRALHEQGYSLQSVNKNGQTALHFACKYNHRDIVKYIIAS-ATrrlINMADKElGQTALHIAAEQNR 972
Cdd:COG0666   156 PLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAgAD---VNAKDND-GKTALDLAAENGN 231

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 161077650  973 RDICVMLVAAGAHLDTLDSGGNTPMMVAFNKNANEIATYL 1012
Cdd:COG0666   232 LEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLL 271
C1_DGKzeta_rpt1 cd20849
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta (DAG ...
 133-201 8.01e-16

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: 73.05  E-value: 8.01e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 161077650  133 DWTENAVQGEHYWKPTSASGDLCCLNEE-CI-----KSGQRMKCSACQLVAHHNCIPFVnEKSTLACKPTYRDVG 201
Cdd:cd20849     1 DWSESAVYGEHIWFETNVSGDFCYVGEQnCVakqlqKSVSRKKCAACKIVVHTPCIEQL-EKINFRCKPSFRESG 74
TIGR00147 TIGR00147
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ...
 369-680 2.33e-11

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: 65.99  E-value: 2.33e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650   369 INPKSGGNQGHKLLGKFQHLLNPRQVFDLTQGGPKMGLDMF-----RKAPNLRVLACGGDGTVGWVLSVLDqiqpPLQPA 443
Cdd:TIGR00147    8 LNPTAGKSNDNKPLREVIMLLREEGMEIHVRVTWEKGDAARyveeaRKFGVDTVIAGGGDGTINEVVNALI----QLDDI 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650   444 PAVGVLPLGTGNDLARALGWgggytdePIgKILREIgmsqcvlmdrwrvKVTPNDDVTDdhVDRSKPNVPLNVInNYFSF 523
Cdd:TIGR00147   84 PALGILPLGTANDFARSLGI-------PE-DLDKAA-------------KLVIAGDARA--IDMGQVNKQYCFI-NMAGG 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650   524 GVDAHIALEFheareahPERFNSRLRNKMYYgqmggkdliLRQYRNLS--QWVTLECDGQDFTGKLrdagcHAVLFL--N 599
Cdd:TIGR00147  140 GFGTEITTET-------PEKLKAALGSLSYI---------LSGLMRMDtlQPFRCEIRGEGEHWQG-----EAVVFLvgN 198

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650   600 IPSYGGGTHPWNDSfgaskpSIDDGLMEVVGLTTYQL-------PMLQAGMH----GTCICQCRKARIITKRTIPMQVDG 668
Cdd:TIGR00147  199 GRQAGGGQKLAPDA------SINDGLLDLRIFTNDNLlpalvltLMSDEGKHtdnpNIIYGKASRIDIQTPHKITFNLDG 272

                          330
                   ....*....|..
gi 161077650   669 EACRVKPSVIEI 680
Cdd:TIGR00147  273 EPLGGTPFHIEI 284
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
894-1012 1.08e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 63.82  E-value: 1.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650  894 AILLAAQSGDLNMLRALHEQGYSLQSVNKNGQTALHFACKYNHRDIVKYIIASAtrrLINMADKELGQTALHIAAEQNRR 973
Cdd:COG0666    24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAG---ADINAKDDGGNTLLHAAARNGDL 100

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 161077650  974 DICVMLVAAGAHLDTLDSGGNTPMMVAFNKNANEIATYL 1012
Cdd:COG0666   101 EIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLL 139
Ank_4 pfam13637
Ankyrin repeats (many copies);
891-944 4.14e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.43  E-value: 4.14e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 161077650   891 TSDAILLAAQSGDLNMLRALHEQGYSLQSVNKNGQTALHFACKYNHRDIVKYII 944
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
894-946 5.12e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 51.27  E-value: 5.12e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 161077650   894 AILLAAQSGDLNMLRALHEqgYSLQSVNKNGQTALHFACKYNHRDIVKYIIAS 946
Cdd:pfam12796   33 ALHLAAKNGHLEIVKLLLE--HADVNLKDNGRTALHYAARSGHLEIVKLLLEK 83
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
 143-192 5.97e-08

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: 50.13  E-value: 5.97e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 161077650   143 HYWKPTS-ASGDLCCLNEECI--KSGQRMKCSACQLVAHHNCIPFVNEKSTLA 192
Cdd:pfam00130    1 HHFVHRNfKQPTFCDHCGEFLwgLGKQGLKCSWCKLNVHKRCHEKVPPECGCD 53
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
 213-277 8.92e-08

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: 49.36  E-value: 8.92e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 161077650   213 HHWVHRKLEK-GKCKQCGKFFPMKqavqsklfgskEIVALACAWCHEIYHNKeaCFNQAKIGEECR 277
Cdd:pfam00130    1 HHFVHRNFKQpTFCDHCGEFLWGL-----------GKQGLKCSWCKLNVHKR--CHEKVPPECGCD 53
C1_DGK_rpt2 cd20805
second protein kinase C conserved region 1 (C1 domain) found in the diacylglycerol kinase ...
 213-279 3.31e-07

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: 47.83  E-value: 3.31e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 161077650  213 HHWVHRKLEKG-KCKQCGKffpmkqavqsKLFGSKEIVALACAWCHEIYHNKeaCFNQAKIgEECRLG 279
Cdd:cd20805     1 HHWVEGNLPSGaKCSVCGK----------KCGSSFGLAGYRCSWCKRTVHSE--CIDKLGP-EECDLG 55
Ank_5 pfam13857
Ankyrin repeats (many copies);
910-967 4.94e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.34  E-value: 4.94e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 161077650   910 LHEQGY-SLQSVNKNGQTALHFACKYNHRDIVKYIIASatRRLINMADKElGQTALHIA 967
Cdd:pfam13857    1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAY--GVDLNLKDEE-GLTALDLA 56
PRK13054 PRK13054
lipid kinase; Reviewed
 416-462 6.18e-07

lipid kinase; Reviewed


Pssm-ID: 237281 [Multi-domain]  Cd Length: 300  Bit Score: 52.57  E-value: 6.18e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 161077650  416 RVLACGGDGTVGWVLSVLDQIQPPLQpaPAVGVLPLGTGNDLARALG 462
Cdd:PRK13054   59 TVIAGGGDGTINEVATALAQLEGDAR--PALGILPLGTANDFATAAG 103
PHA03095 PHA03095
ankyrin-like protein; Provisional
 907-1015 7.10e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 53.10  E-value: 7.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650  907 LRALHEQGYSLQSVNKNGQTALHFACKYN---HRDIVKYIIASATrrlINMADKeLGQTALHIAAEQNRRDICVMLVAAG 983
Cdd:PHA03095  205 VRELIRAGCDPAATDMLGNTPLHSMATGSsckRSLVLPLLIAGIS---INARNR-YGQTPLHYAAVFNNPRACRRLIALG 280

                          90       100       110
                  ....*....|....*....|....*....|...
gi 161077650  984 AHLDTLDSGGNTPMMVAF-NKNANEIATYLESQ 1015
Cdd:PHA03095  281 ADINAVSSDGNTPLSLMVrNNNGRAVRAALAKN 313
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
 142-187 1.65e-06

Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.


Pssm-ID: 197519  Cd Length: 50  Bit Score: 45.92  E-value: 1.65e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 161077650    142 EHYWKPTSASGDLCCLNEECIKSG--QRMKCSACQLVAHHNCIPFVNE 187
Cdd:smart00109    1 HKHVFRTFTKPTFCCVCRKSIWGSfkQGLRCSECKVKCHKKCADKVPK 48
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 865-984 1.91e-06

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: 51.94  E-value: 1.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650  865 WKSNKDRLFsfnedvfgcgfspILEQ---TSDAILLAAQSGDLNMLRAL--------HEQGySLqsvnknGQTALHFACK 933
Cdd:cd22192     1 WAQMLDELH-------------LLQQkriSESPLLLAAKENDVQAIKKLlkcpscdlFQRG-AL------GETALHVAAL 60

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 161077650  934 YNHRDIVKyIIASATRRLINMA---DKELGQTALHIAAEQNRRDICVMLVAAGA 984
Cdd:cd22192    61 YDNLEAAV-VLMEAAPELVNEPmtsDLYQGETALHIAVVNQNLNLVRELIARGA 113
PRK12361 PRK12361
hypothetical protein; Provisional
 367-464 2.66e-06

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 51.16  E-value: 2.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650  367 VFINPKSGGNQGHKLLGKFQHLLNPRqvFDLT--QGGPKMGLDMFRKAPNLR----VLACGGDGTVGWVLSVLDQIQPPL 440
Cdd:PRK12361  247 LIANPVSGGGKWQEYGEQIQRELKAY--FDLTvkLTTPEISAEALAKQARKAgadiVIACGGDGTVTEVASELVNTDITL 324

                          90       100
                  ....*....|....*....|....*
gi 161077650  441 qpapavGVLPLGTGNDLARAL-GWG 464
Cdd:PRK12361  325 ------GIIPLGTANALSHALfGLG 343
PRK13057 PRK13057
lipid kinase;
416-462 3.66e-06

lipid kinase;


Pssm-ID: 183857 [Multi-domain]  Cd Length: 287  Bit Score: 49.92  E-value: 3.66e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 161077650  416 RVLACGGDGTVGWVLSVLDQIQPPLqpapavGVLPLGTGNDLARALG 462
Cdd:PRK13057   53 LVIVGGGDGTLNAAAPALVETGLPL------GILPLGTANDLARTLG 93
Ank_4 pfam13637
Ankyrin repeats (many copies);
926-980 5.20e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 5.20e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 161077650   926 TALHFACKYNHRDIVKYIIASATRrlINMADKElGQTALHIAAEQNRRDICVMLV 980
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGAD--INAVDGN-GETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
944-1000 1.76e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.10  E-value: 1.76e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 161077650   944 IASATRRLINMADKElGQTALHIAAEQNRRDICVMLVAAGAHLDTLDSGGNTPMMVA 1000
Cdd:pfam13857    1 LLEHGPIDLNRLDGE-GYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 889-1000 6.89e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 46.80  E-value: 6.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650  889 EQTSDAILLAAQSGD----LNMLRALHEQGYSLQSVNKN-GQTALHFACKYNHRDIVKYIIASATRrlINMADKeLGQTA 963
Cdd:PHA02878  128 IQTIDLVYIDKKSKDdiieAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGAN--VNIPDK-TNNSP 204

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 161077650  964 LHIAAEQNRRDICVMLVAAGAHLDTLDSGGNTPMMVA 1000
Cdd:PHA02878  205 LHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS 241
Ank_2 pfam12796
Ankyrin repeats (3 copies);
964-1012 6.96e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 42.41  E-value: 6.96e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 161077650   964 LHIAAEQNRRDICVMLVAAGAHLDTLDSGGNTPMMVAFNKNANEIATYL 1012
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL 49
PRK13055 PRK13055
putative lipid kinase; Reviewed
 417-488 1.05e-04

putative lipid kinase; Reviewed


Pssm-ID: 237282 [Multi-domain]  Cd Length: 334  Bit Score: 45.75  E-value: 1.05e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161077650  417 VLACGGDGTVGWVLSVLdqiqPPLQPAPAVGVLPLGTGNDLARALGWGggyTDEPIgKILREIGMSQCVLMD 488
Cdd:PRK13055   63 IIAAGGDGTINEVVNGI----APLEKRPKMAIIPAGTTNDYARALKIP---RDNPV-EAAKVILKNQTIKMD 126
C1_DGKepsilon_typeIII_rpt2 cd20853
second protein kinase C conserved region 1 (C1 domain) found in type III diacylglycerol kinase, ...
 213-288 1.40e-04

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


Pssm-ID: 410403  Cd Length: 63  Bit Score: 40.72  E-value: 1.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650  213 HHWVHRKLEKG-KC----KQCGkffpmkqaVQSKLfgskeiVALACAWCHEIYHNKeaCFnqAKIGEECRLGNYAPIIVP 287
Cdd:cd20853     1 HHWVRGNLPLCsVCcvcnEQCG--------NQPGL------CDYRCCWCQRTVHDD--CL--AKLPKECDLGAFRNFIVP 62


                  .
gi 161077650  288 P 288
Cdd:cd20853    63 P 63
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 905-997 1.57e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 45.34  E-value: 1.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650  905 NMLRALHEQGYSLQSVNKNGQTALHFACKYNHRDIVKYIIAsaTRRLINMADKElGQTALHIAAEQNRRDICVMLVAAGA 984
Cdd:PHA02874  105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFE--YGADVNIEDDN-GCYPIHIAIKHNFFDIIKLLLEKGA 181

                          90
                  ....*....|...
gi 161077650  985 HLDTLDSGGNTPM 997
Cdd:PHA02874  182 YANVKDNNGESPL 194
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 914-991 1.69e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 45.43  E-value: 1.69e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 161077650  914 GYSLQSVNKNGQTALHFACKYNHRDIVKYII-ASATRRLINMadkeLGQTALHIAAEQNRRDICVMLVAAGAHLDTLDS 991
Cdd:PHA03100  182 GVPINIKDVYGFTPLHYAVYNNNPEFVKYLLdLGANPNLVNK----YGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 895-1002 1.74e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 45.34  E-value: 1.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650  895 ILLAAQSGDLNMLRALHEQGYSLQSVNKNGQTALHFACKYNHRDIVKYIIASaTRRLINMADKelGQTALHIAAEQNRRd 974
Cdd:PHA02874  161 IHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDH-GNHIMNKCKN--GFTPLHNAIIHNRS- 236

                          90       100
                  ....*....|....*....|....*...
gi 161077650  975 iCVMLVAAGAHLDTLDSGGNTPMMVAFN 1002
Cdd:PHA02874  237 -AIELLINNASINDQDIDGSTPLHHAIN 263
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 923-944 2.87e-04

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: 38.78  E-value: 2.87e-04
                           10        20
                   ....*....|....*....|..
gi 161077650   923 NGQTALHFACKYNHRDIVKYII 944
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLL 22
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 893-996 3.17e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 44.86  E-value: 3.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650  893 DAILLAAQSGDLNMLRALHEQGYSLQSVNKNGQTALHFACKYNHRDIVKYIIASATRRLINMADKELGQTALH--IAAEQ 970
Cdd:PLN03192  624 DLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDDFSPTELRelLQKRE 703

                          90       100
                  ....*....|....*....|....*.
gi 161077650  971 NRRDICVMLVAAGAHLDTLDSGGNTP 996
Cdd:PLN03192  704 LGHSITIVDSVPADEPDLGRDGGSRP 729
Ank_4 pfam13637
Ankyrin repeats (many copies);
962-1012 4.60e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.18  E-value: 4.60e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 161077650   962 TALHIAAEQNRRDICVMLVAAGAHLDTLDSGGNTPM-MVAFNKNAnEIATYL 1012
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALhFAASNGNV-EVLKLL 53
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 922-1012 5.97e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 43.72  E-value: 5.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650  922 KNGQTA-LHFACKYNHRDIVKYIIasaTRRL------INMADKELGQTALHIAAEQNRRDICVMLVAAGAHLDTLDSGGN 994
Cdd:PHA02878  126 KNIQTIdLVYIDKKSKDDIIEAEI---TKLLlsygadINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNN 202

                          90
                  ....*....|....*...
gi 161077650  995 TPMMVAFNKNANEIATYL 1012
Cdd:PHA02878  203 SPLHHAVKHYNKPIVHIL 220
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 899-979 7.50e-04

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.35  E-value: 7.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650  899 AQSGDLNMLRALHEQGYSLQSVNKNGQTALHFACKYNHRDIVKYII---ASATrrlinMADKElGQTALHIAAEQNRRDI 975
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLefgADPT-----LLDKD-GKTPLELAEENGFREV 163


                  ....
gi 161077650  976 CVML 979
Cdd:PTZ00322  164 VQLL 167
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 891-1012 8.08e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 43.12  E-value: 8.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650  891 TSDAILLAAQSGDLNMLRALHEQGYSLQSVNKNGQTALHFACKYNHRDI------------------VKYIIASATrrLI 952
Cdd:PHA03100  108 TPLLYAISKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkilkllidkgvdinaknrVNYLLSYGV--PI 185

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650  953 NMADkELGQTALHIAAEQNRRDICVMLVAAGAHLDTLDSGGNTPMMVAFNKNANEIATYL 1012
Cdd:PHA03100  186 NIKD-VYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244
PRK00861 PRK00861
putative lipid kinase; Reviewed
 370-462 8.46e-04

putative lipid kinase; Reviewed


Pssm-ID: 234850 [Multi-domain]  Cd Length: 300  Bit Score: 42.69  E-value: 8.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650  370 NPKSGGNQGHKLLGKFQHLLNPRQVFDLTQGGPKMGLDMFRKAPNLR----VLACGGDGTVGWVLSVLDQIQPPLqpapa 445
Cdd:PRK00861   10 NPVAGQGNPEVDLALIRAILEPEMDLDIYLTTPEIGADQLAQEAIERgaelIIASGGDGTLSAVAGALIGTDIPL----- 84

                          90
                  ....*....|....*..
gi 161077650  446 vGVLPLGTGNDLARALG 462
Cdd:PRK00861   85 -GIIPRGTANAFAAALG 100
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 923-944 1.06e-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: 37.18  E-value: 1.06e-03
                            10        20
                    ....*....|....*....|..
gi 161077650    923 NGQTALHFACKYNHRDIVKYII 944
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLL 22
PHA03095 PHA03095
ankyrin-like protein; Provisional
 881-1000 2.61e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.55  E-value: 2.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650  881 GCGFSPIleqtsdAILLAAQSGDLNMLRALHEQGYSLQSVNKNGQTALHFACKyNHR---DIVKYIIASATrrliNMADK 957
Cdd:PHA03095  115 KVGRTPL------HVYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLK-SRNanvELLRLLIDAGA----DVYAV 183

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 161077650  958 EL-GQTALHIAAEQNRRDICVM--LVAAGAHLDTLDSGGNTPMMVA 1000
Cdd:PHA03095  184 DDrFRSLLHHHLQSFKPRARIVreLIRAGCDPAATDMLGNTPLHSM 229
C1_DGK_typeI_like_rpt2 cd20851
second protein kinase C conserved region 1 (C1 domain) found in type I diacylglycerol kinases; ...
 213-279 3.12e-03

second protein kinase C conserved region 1 (C1 domain) found in type I diacylglycerol kinases; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. Type I DAG kinases (DGKs) contain EF-hand structures that bind Ca(2+) and recoverin homology domains, in addition to C1 and catalytic domains that are present in all DGKs. Type I DGKs, regulated by calcium binding, include three DGK isozymes (alpha, beta and gamma). DAG kinase alpha, also called 80 kDa DAG kinase, or diglyceride kinase alpha (DGK-alpha), is active upon cell stimulation, initiating the resynthesis of phosphatidylinositols and attenuating protein kinase C activity. DAG kinase beta, also called 90 kDa DAG kinase, or diglyceride kinase beta (DGK-beta), exhibits high phosphorylation activity for long-chain diacylglycerols. DAG kinase gamma, also called diglyceride kinase gamma (DGK-gamma), reverses the normal flow of glycerolipid biosynthesis by phosphorylating diacylglycerol back to phosphatidic acid. Members of this family contain two copies of the C1 domain. This model corresponds to the second one. DGK-alpha contains atypical C1 domains, while DGK-beta and DGK-gamma contain typical C1 domains that bind DAG and phorbol esters. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410401  Cd Length: 52  Bit Score: 36.56  E-value: 3.12e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 161077650  213 HHWVHRKLEkGKCKQCGKFFPMKQAVQsklfgskeivALACAWCHEIYHNKeaCFNQakIGEECRLG 279
Cdd:cd20851     1 HHWVEGNCP-GKCDKCHKSIKSYQGLT----------GLHCVWCHITLHNK--CASH--VKPECDLG 52
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 921-1015 3.38e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 39.09  E-value: 3.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650  921 NKNGQTALHFACKynHRDIV-----KYIIASATRRLINMADKElGQTALHIAAEQNR---RDICVMLVAAGAHLDTLDS- 991
Cdd:PHA02736   14 DIEGENILHYLCR--NGGVTdllafKNAISDENRYLVLEYNRH-GKQCVHIVSNPDKadpQEKLKLLMEWGADINGKERv 90

                          90       100
                  ....*....|....*....|....
gi 161077650  992 GGNTPMMVAFNKNANEIATYLESQ 1015
Cdd:PHA02736   91 FGNTPLHIAVYTQNYELATWLCNQ 114
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 960-988 5.17e-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: 35.31  E-value: 5.17e-03
                           10        20
                   ....*....|....*....|....*....
gi 161077650   960 GQTALHIAAEQNRRDICVMLVAAGAHLDT 988
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 923-1017 5.62e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 40.51  E-value: 5.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650  923 NGQTALHFAC---KYNHRDIVKYIIASAT-----RRLINMADKE---LGQTALHIAAEQNRRDICVMLVAAGAHLDTLDS 991
Cdd:cd22194    93 TGKTCLMKALlniNENTKEIVRILLAFAEengilDRFINAEYTEeayEGQTALNIAIERRQGDIVKLLIAKGADVNAHAK 172

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 161077650  992 G--------------GNTPMMVAFNKNANEIATYLESQER 1017
Cdd:cd22194   173 GvffnpkykhegfyfGETPLALAACTNQPEIVQLLMEKES 212
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 960-1014 8.66e-03

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 39.88  E-value: 8.66e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 161077650  960 GQTALHIAAEQNRRDICVMLVAAGAHLDTLDSGGNTPMMVAFNKNANEIATYLES 1014
Cdd:PTZ00322  115 GRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 960-990 8.75e-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. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.96  E-value: 8.75e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 161077650   960 GQTALHIAAEQ-NRRDICVMLVAAGAHLDTLD 990
Cdd:pfam00023    2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
PRK13059 PRK13059
putative lipid kinase; Reviewed
 417-462 8.85e-03

putative lipid kinase; Reviewed


Pssm-ID: 183858  Cd Length: 295  Bit Score: 39.25  E-value: 8.85e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 161077650  417 VLACGGDGTVGWVLSVLDQ--IQPPLqpapavGVLPLGTGNDLARALG 462
Cdd:PRK13059   60 ILIAGGDGTVDNVVNAMKKlnIDLPI------GILPVGTANDFAKFLG 101
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 898-1008 9.26e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 39.56  E-value: 9.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077650  898 AAQSGDLNMLRALHEQGYSLQSVNKNGQTALHFACKYNHRDIVKYIIASATrrLINMADKElGQTALHIAAEQNRRDICV 977
Cdd:PHA02874  131 AIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGA--YANVKDNN-GESPLHNAAEYGDYACIK 207

                          90       100       110
                  ....*....|....*....|....*....|...
gi 161077650  978 MLVAAGAHLDTLDSGGNTPMMVA--FNKNANEI 1008
Cdd:PHA02874  208 LLIDHGNHIMNKCKNGFTPLHNAiiHNRSAIEL 240
 
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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