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Conserved domains on  [gi|320541875|ref|NP_001036264|]
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retinal degeneration A, isoform E [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 ...
 498-652 4.04e-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: 4.04e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541875   498 VINNYFSFGVDAHIALEFHEAREAHPERFNSRLRNKMYYGQMGGKDLILRQYRNLSQWVTLECDGQDFTGKLrdaGCHAV 577
Cdd:smart00045   1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLPN---SLEGI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541875   578 LFLNIPSYGGGTHPWNDS----FGASKPSIDDGLMEVVGLTTYQLP--MLQAGMHGTCICQCRKAR--IITKRTIPMQVD 649
Cdd:smart00045  78 AVLNIPSYGGGTNLWGTTdkedLNFSKQSHDDGLLEVVGLTGAMHMaqIRQVGLAGRRIAQCSEVRitIKTSKTIPMQVD 157


                   ...
gi 320541875   650 GEA 652
Cdd:smart00045 158 GEP 160
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 348-471 2.43e-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: 2.43e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541875   348 IVFINPKSGGNQGHKLLGKFQHLLNPRQVFDLTQGGPKMGLDMFRKAPN-LRVLACGGDGTVGWVLSVLDQIQPPLqPAP 426
Cdd:smart00046   1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVPDfNRVLVCGGDGTVGWVLNALDKRELPL-PEP 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 320541875   427 AVGVLPLGTGNDLARALGWGGGYTDEPIGKILREIGMSQCVLMDR 471
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; ...
 195-261 1.02e-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: 115.14  E-value: 1.02e-30
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 320541875 195 HHWVHRKLEKGKCKQCGKFFpmkqavQSKL-FGSKEIVALACAWCHEIYHNKEACFNQAKIGEECRLG 261
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; ...
 120-181 5.64e-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: 5.64e-29
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 320541875 120 AVQGEHYWKPTSASGDLCCLNE-ECIKSGQRMKCSACQLVAHHNCIPFVNEKStLACKPTYRD 181
Cdd:cd20802    1 AVNGEHLWTDTSASGDLCYVGEqDCLKSGSRKKCSACKIVVHTGCIPQLEKIN-FKCKPTFRE 62
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
858-979 1.01e-23

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 102.34  E-value: 1.01e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541875 858 AILLAAQSGDLNMLRALHEQGYSLQSVNKNGQTALHFACKYNHRDIVKYIIAS-ATrrlINMADKElGQTALHIAAEQNR 936
Cdd:COG0666  123 PLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAgAD---VNARDND-GETPLHLAAENGH 198

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 320541875 937 RDICVMLVAAGAHLDTLDSGGNTPMMVAFNKNANEIATYLESQ 979
Cdd:COG0666  199 LEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
 
Name Accession Description Interval E-value
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 498-652 4.04e-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: 4.04e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541875   498 VINNYFSFGVDAHIALEFHEAREAHPERFNSRLRNKMYYGQMGGKDLILRQYRNLSQWVTLECDGQDFTGKLrdaGCHAV 577
Cdd:smart00045   1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLPN---SLEGI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541875   578 LFLNIPSYGGGTHPWNDS----FGASKPSIDDGLMEVVGLTTYQLP--MLQAGMHGTCICQCRKAR--IITKRTIPMQVD 649
Cdd:smart00045  78 AVLNIPSYGGGTNLWGTTdkedLNFSKQSHDDGLLEVVGLTGAMHMaqIRQVGLAGRRIAQCSEVRitIKTSKTIPMQVD 157


                   ...
gi 320541875   650 GEA 652
Cdd:smart00045 158 GEP 160
DAGK_acc pfam00609
Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts ...
 498-652 6.75e-68

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


Pssm-ID: 459866  Cd Length: 158  Bit Score: 223.63  E-value: 6.75e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541875  498 VINNYFSFGVDAHIALEFHEAREAHPERFNSRLRNKMYYGQMGGKDLILRQYRNLSQWVTLECDGQDFtgKLRdAGCHAV 577
Cdd:pfam00609   1 VMNNYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDMFQRSCKNLIEKVELEVDGKDL--PLP-KSLEGI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541875  578 LFLNIPSYGGGTHPWNDSF----GASKPSIDDGLMEVVGLT-TYQLPMLQAGMH-GTCICQCRKARIITKRTIPMQVDGE 651
Cdd:pfam00609  78 VVLNIPSYAGGTDLWGNSKedglGFAPQSVDDGLLEVVGLTgALHLGQVQVGLGsAKRIAQGGPIRITTKKKIPMQVDGE 157


                  .
gi 320541875  652 A 652
Cdd:pfam00609 158 P 158
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 348-471 2.43e-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: 2.43e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541875   348 IVFINPKSGGNQGHKLLGKFQHLLNPRQVFDLTQGGPKMGLDMFRKAPN-LRVLACGGDGTVGWVLSVLDQIQPPLqPAP 426
Cdd:smart00046   1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVPDfNRVLVCGGDGTVGWVLNALDKRELPL-PEP 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 320541875   427 AVGVLPLGTGNDLARALGWGGGYTDEPIGKILREIGMSQCVLMDR 471
Cdd:smart00046  80 PVAVLPLGTGNDLARSLGWGGGYDGEKLLKTLRDALESDTVKLDR 124
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 346-447 7.09e-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: 7.09e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541875  346 PVIVFINPKSGGNQGHKLLGKFQHLLNPRQV-FDLTQ-GGPKMGLDMFRKAPNL---RVLACGGDGTVGWVLSVLDQIQP 420
Cdd:pfam00781   1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVeVELVLtEGPGDALELAREAAEDgydRIVVAGGDGTVNEVLNGLAGLAT 80

                          90       100
                  ....*....|....*....|....*..
gi 320541875  421 PlqpaPAVGVLPLGTGNDLARALGWGG 447
Cdd:pfam00781  81 R----PPLGIIPLGTGNDFARALGIPG 103
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 347-669 7.53e-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: 7.53e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541875 347 VIVFINPKSGGNQGHKLLGKFQHLLNPR----QVFDLTQGGPkmGLDMFRKAPNL---RVLACGGDGTVGWVLSVLDQIQ 419
Cdd:COG1597    5 ALLIVNPASGRGRAARLLERLVAALRAAglevEVLETESPGD--ATELAREAAAEgadLVVAAGGDGTVNEVANGLAGTG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541875 420 PPLqpapavGVLPLGTGNDLARALGwgggyTDEPIGKILREIGMSQCVLMDRWRVkvtpnddvtDDHVdrskpnvplnVI 499
Cdd:COG1597   83 PPL------GILPLGTGNDFARALG-----IPLDPEAALEALLTGRTRRIDLGRV---------NGRY----------FL 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541875 500 NNyFSFGVDAHIALEFHEAReahperfnSRLRNKMYYGQMGGKdlILRQYRNLSqwVTLECDGQDFTGKlrdagCHAVLF 579
Cdd:COG1597  133 NV-AGIGFDAEVVERANRAL--------KRRLGKLAYVLAALR--ALLRYRPFR--LRIELDGEEIEGE-----ALLVAV 194

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541875 580 LNIPSYGGGTHPwndsfgASKPSIDDGLMEVVGLTT-------YQLPMLQAGMHGTC----ICQCRKARIITKRTIPMQV 648
Cdd:COG1597  195 GNGPYYGGGLRL------APDASLDDGLLDVVVVRPlsrlrllRLLPRLLRGRHLRHpgvrYFRAREVEIESDRPLPVQL 268

                        330       340
                 ....*....|....*....|.
gi 320541875 649 DGEACRVKPSViEIELLNKAL 669
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; ...
 195-261 1.02e-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: 115.14  E-value: 1.02e-30
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 320541875 195 HHWVHRKLEKGKCKQCGKFFpmkqavQSKL-FGSKEIVALACAWCHEIYHNKEACFNQAKIGEECRLG 261
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; ...
 120-181 5.64e-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: 5.64e-29
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 320541875 120 AVQGEHYWKPTSASGDLCCLNE-ECIKSGQRMKCSACQLVAHHNCIPFVNEKStLACKPTYRD 181
Cdd:cd20802    1 AVNGEHLWTDTSASGDLCYVGEqDCLKSGSRKKCSACKIVVHTGCIPQLEKIN-FKCKPTFRE 62
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
858-979 1.01e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 102.34  E-value: 1.01e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541875 858 AILLAAQSGDLNMLRALHEQGYSLQSVNKNGQTALHFACKYNHRDIVKYIIAS-ATrrlINMADKElGQTALHIAAEQNR 936
Cdd:COG0666  123 PLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAgAD---VNARDND-GETPLHLAAENGH 198

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 320541875 937 RDICVMLVAAGAHLDTLDSGGNTPMMVAFNKNANEIATYLESQ 979
Cdd:COG0666  199 LEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
Ank_2 pfam12796
Ankyrin repeats (3 copies);
859-954 8.40e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.86  E-value: 8.40e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541875  859 ILLAAQSGDLNMLRALHEQGYSLQSVNKNGQTALHFACKYNHRDIVKYIIASATRRLINMadkelGQTALHIAAEQNRRD 938
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN-----GRTALHYAARSGHLE 75

                          90
                  ....*....|....*.
gi 320541875  939 ICVMLVAAGAHLDTLD 954
Cdd:pfam12796  76 IVKLLLEKGADINVKD 91
TIGR00147 TIGR00147
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ...
 351-662 2.23e-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: 2.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541875  351 INPKSGGNQGHKLLGKFQHLLNPRQVFDLTQGGPKMGLDMF-----RKAPNLRVLACGGDGTVGWVLSVLDqiqpPLQPA 425
Cdd:TIGR00147   8 LNPTAGKSNDNKPLREVIMLLREEGMEIHVRVTWEKGDAARyveeaRKFGVDTVIAGGGDGTINEVVNALI----QLDDI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541875  426 PAVGVLPLGTGNDLARALGWgggytdePIgKILREIgmsqcvlmdrwrvKVTPNDDVTDdhVDRSKPNVPLNVInNYFSF 505
Cdd:TIGR00147  84 PALGILPLGTANDFARSLGI-------PE-DLDKAA-------------KLVIAGDARA--IDMGQVNKQYCFI-NMAGG 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541875  506 GVDAHIALEFheareahPERFNSRLRNKMYYgqmggkdliLRQYRNLS--QWVTLECDGQDFTGKLrdagcHAVLFL--N 581
Cdd:TIGR00147 140 GFGTEITTET-------PEKLKAALGSLSYI---------LSGLMRMDtlQPFRCEIRGEGEHWQG-----EAVVFLvgN 198

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541875  582 IPSYGGGTHPWNDSfgaskpSIDDGLMEVVGLTTYQL-------PMLQAGMH----GTCICQCRKARIITKRTIPMQVDG 650
Cdd:TIGR00147 199 GRQAGGGQKLAPDA------SINDGLLDLRIFTNDNLlpalvltLMSDEGKHtdnpNIIYGKASRIDIQTPHKITFNLDG 272

                         330
                  ....*....|..
gi 320541875  651 EACRVKPSVIEI 662
Cdd:TIGR00147 273 EPLGGTPFHIEI 284
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
 125-174 5.76e-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: 5.76e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 320541875  125 HYWKPTS-ASGDLCCLNEECI--KSGQRMKCSACQLVAHHNCIPFVNEKSTLA 174
Cdd:pfam00130   1 HHFVHRNfKQPTFCDHCGEFLwgLGKQGLKCSWCKLNVHKRCHEKVPPECGCD 53
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
 195-259 8.61e-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: 8.61e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 320541875  195 HHWVHRKLEK-GKCKQCGKFFPMKqavqsklfgskEIVALACAWCHEIYHNKeaCFNQAKIGEECR 259
Cdd:pfam00130   1 HHFVHRNFKQpTFCDHCGEFLWGL-----------GKQGLKCSWCKLNVHKR--CHEKVPPECGCD 53
PRK13054 PRK13054
lipid kinase; Reviewed
 398-444 5.92e-07

lipid kinase; Reviewed


Pssm-ID: 237281 [Multi-domain]  Cd Length: 300  Bit Score: 52.57  E-value: 5.92e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 320541875 398 RVLACGGDGTVGWVLSVLDQIQPPLQpaPAVGVLPLGTGNDLARALG 444
Cdd:PRK13054  59 TVIAGGGDGTINEVATALAQLEGDAR--PALGILPLGTANDFATAAG 103
PHA03095 PHA03095
ankyrin-like protein; Provisional
 871-979 6.80e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 53.10  E-value: 6.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541875 871 LRALHEQGYSLQSVNKNGQTALHFACKYN---HRDIVKYIIASATrrlINMADKeLGQTALHIAAEQNRRDICVMLVAAG 947
Cdd:PHA03095 205 VRELIRAGCDPAATDMLGNTPLHSMATGSsckRSLVLPLLIAGIS---INARNR-YGQTPLHYAAVFNNPRACRRLIALG 280

                         90       100       110
                 ....*....|....*....|....*....|...
gi 320541875 948 AHLDTLDSGGNTPMMVAF-NKNANEIATYLESQ 979
Cdd:PHA03095 281 ADINAVSSDGNTPLSLMVrNNNGRAVRAALAKN 313
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
 124-169 1.77e-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: 45.54  E-value: 1.77e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 320541875   124 EHYWKPTSASGDLCCLNEECIKSG--QRMKCSACQLVAHHNCIPFVNE 169
Cdd:smart00109   1 HKHVFRTFTKPTFCCVCRKSIWGSfkQGLRCSECKVKCHKKCADKVPK 48
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 859-948 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 320541875 859 ILLAAQSGDLNMLRAL--------HEQGySLqsvnknGQTALHFACKYNHRDIVKyIIASATRRLINMA---DKELGQTA 927
Cdd:cd22192   21 LLLAAKENDVQAIKKLlkcpscdlFQRG-AL------GETALHVAALYDNLEAAV-VLMEAAPELVNEPmtsDLYQGETA 92

                         90       100
                 ....*....|....*....|.
gi 320541875 928 LHIAAEQNRRDICVMLVAAGA 948
Cdd:cd22192   93 LHIAVVNQNLNLVRELIARGA 113
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 887-908 1.22e-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: 1.22e-03
                           10        20
                   ....*....|....*....|..
gi 320541875   887 NGQTALHFACKYNHRDIVKYII 908
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLL 22
 
Name Accession Description Interval E-value
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 498-652 4.04e-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: 4.04e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541875   498 VINNYFSFGVDAHIALEFHEAREAHPERFNSRLRNKMYYGQMGGKDLILRQYRNLSQWVTLECDGQDFTGKLrdaGCHAV 577
Cdd:smart00045   1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLPN---SLEGI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541875   578 LFLNIPSYGGGTHPWNDS----FGASKPSIDDGLMEVVGLTTYQLP--MLQAGMHGTCICQCRKAR--IITKRTIPMQVD 649
Cdd:smart00045  78 AVLNIPSYGGGTNLWGTTdkedLNFSKQSHDDGLLEVVGLTGAMHMaqIRQVGLAGRRIAQCSEVRitIKTSKTIPMQVD 157


                   ...
gi 320541875   650 GEA 652
Cdd:smart00045 158 GEP 160
DAGK_acc pfam00609
Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts ...
 498-652 6.75e-68

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


Pssm-ID: 459866  Cd Length: 158  Bit Score: 223.63  E-value: 6.75e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541875  498 VINNYFSFGVDAHIALEFHEAREAHPERFNSRLRNKMYYGQMGGKDLILRQYRNLSQWVTLECDGQDFtgKLRdAGCHAV 577
Cdd:pfam00609   1 VMNNYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDMFQRSCKNLIEKVELEVDGKDL--PLP-KSLEGI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541875  578 LFLNIPSYGGGTHPWNDSF----GASKPSIDDGLMEVVGLT-TYQLPMLQAGMH-GTCICQCRKARIITKRTIPMQVDGE 651
Cdd:pfam00609  78 VVLNIPSYAGGTDLWGNSKedglGFAPQSVDDGLLEVVGLTgALHLGQVQVGLGsAKRIAQGGPIRITTKKKIPMQVDGE 157


                  .
gi 320541875  652 A 652
Cdd:pfam00609 158 P 158
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 348-471 2.43e-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: 2.43e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541875   348 IVFINPKSGGNQGHKLLGKFQHLLNPRQVFDLTQGGPKMGLDMFRKAPN-LRVLACGGDGTVGWVLSVLDQIQPPLqPAP 426
Cdd:smart00046   1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVPDfNRVLVCGGDGTVGWVLNALDKRELPL-PEP 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 320541875   427 AVGVLPLGTGNDLARALGWGGGYTDEPIGKILREIGMSQCVLMDR 471
Cdd:smart00046  80 PVAVLPLGTGNDLARSLGWGGGYDGEKLLKTLRDALESDTVKLDR 124
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 346-447 7.09e-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: 7.09e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541875  346 PVIVFINPKSGGNQGHKLLGKFQHLLNPRQV-FDLTQ-GGPKMGLDMFRKAPNL---RVLACGGDGTVGWVLSVLDQIQP 420
Cdd:pfam00781   1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVeVELVLtEGPGDALELAREAAEDgydRIVVAGGDGTVNEVLNGLAGLAT 80

                          90       100
                  ....*....|....*....|....*..
gi 320541875  421 PlqpaPAVGVLPLGTGNDLARALGWGG 447
Cdd:pfam00781  81 R----PPLGIIPLGTGNDFARALGIPG 103
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 347-669 7.53e-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: 7.53e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541875 347 VIVFINPKSGGNQGHKLLGKFQHLLNPR----QVFDLTQGGPkmGLDMFRKAPNL---RVLACGGDGTVGWVLSVLDQIQ 419
Cdd:COG1597    5 ALLIVNPASGRGRAARLLERLVAALRAAglevEVLETESPGD--ATELAREAAAEgadLVVAAGGDGTVNEVANGLAGTG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541875 420 PPLqpapavGVLPLGTGNDLARALGwgggyTDEPIGKILREIGMSQCVLMDRWRVkvtpnddvtDDHVdrskpnvplnVI 499
Cdd:COG1597   83 PPL------GILPLGTGNDFARALG-----IPLDPEAALEALLTGRTRRIDLGRV---------NGRY----------FL 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541875 500 NNyFSFGVDAHIALEFHEAReahperfnSRLRNKMYYGQMGGKdlILRQYRNLSqwVTLECDGQDFTGKlrdagCHAVLF 579
Cdd:COG1597  133 NV-AGIGFDAEVVERANRAL--------KRRLGKLAYVLAALR--ALLRYRPFR--LRIELDGEEIEGE-----ALLVAV 194

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541875 580 LNIPSYGGGTHPwndsfgASKPSIDDGLMEVVGLTT-------YQLPMLQAGMHGTC----ICQCRKARIITKRTIPMQV 648
Cdd:COG1597  195 GNGPYYGGGLRL------APDASLDDGLLDVVVVRPlsrlrllRLLPRLLRGRHLRHpgvrYFRAREVEIESDRPLPVQL 268

                        330       340
                 ....*....|....*....|.
gi 320541875 649 DGEACRVKPSViEIELLNKAL 669
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; ...
 195-261 1.02e-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: 115.14  E-value: 1.02e-30
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 320541875 195 HHWVHRKLEKGKCKQCGKFFpmkqavQSKL-FGSKEIVALACAWCHEIYHNKEACFNQAKIGEECRLG 261
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; ...
 120-181 5.64e-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: 5.64e-29
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 320541875 120 AVQGEHYWKPTSASGDLCCLNE-ECIKSGQRMKCSACQLVAHHNCIPFVNEKStLACKPTYRD 181
Cdd:cd20802    1 AVNGEHLWTDTSASGDLCYVGEqDCLKSGSRKKCSACKIVVHTGCIPQLEKIN-FKCKPTFRE 62
C1_DGKiota_rpt2 cd20896
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase iota ...
 195-272 2.10e-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: 103.25  E-value: 2.10e-26
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 320541875 195 HHWVHRKLEKGKCKQCGKFFPMKQAvqsklFGSKEIVALACAWCHEIYHNKEACFNQAKIGEECRLGNYAPIIVPPSW 272
Cdd:cd20896    3 HHWVHRRRQEGKCKQCGKGFQQKFS-----FHSKEIVAISCSWCKQAFHNKVTCFMLHHIEEPCSLGAHAAVIVPPTW 75
C1_DGKzeta_rpt2 cd20895
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta ...
 195-272 4.82e-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: 102.08  E-value: 4.82e-26
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 320541875 195 HHWVHRKLEKGKCKQCGKFFPMKQAvqsklFGSKEIVALACAWCHEIYHNKEACFNQAKIGEECRLGNYAPIIVPPSW 272
Cdd:cd20895    3 HHWVHRRRQEGKCRQCGKGFQQKFA-----FHSKEIVAISCSWCKQAYHSKVSCFMLQQIEEPCSLGAHAAVIVPPTW 75
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
858-979 1.01e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 102.34  E-value: 1.01e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541875 858 AILLAAQSGDLNMLRALHEQGYSLQSVNKNGQTALHFACKYNHRDIVKYIIAS-ATrrlINMADKElGQTALHIAAEQNR 936
Cdd:COG0666  123 PLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAgAD---VNARDND-GETPLHLAAENGH 198

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 320541875 937 RDICVMLVAAGAHLDTLDSGGNTPMMVAFNKNANEIATYLESQ 979
Cdd:COG0666  199 LEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
856-976 1.74e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 101.95  E-value: 1.74e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541875 856 SDAILLAAQSGDLNMLRALHEQGYSLQSVNKNGQTALHFACKYNHRDIVKYIIASATRrlINMADKElGQTALHIAAEQN 935
Cdd:COG0666   88 NTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGAD--VNAQDND-GNTPLHLAAANG 164

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 320541875 936 RRDICVMLVAAGAHLDTLDSGGNTPMMVAFNKNANEIATYL 976
Cdd:COG0666  165 NLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
Ank_2 pfam12796
Ankyrin repeats (3 copies);
859-954 8.40e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.86  E-value: 8.40e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541875  859 ILLAAQSGDLNMLRALHEQGYSLQSVNKNGQTALHFACKYNHRDIVKYIIASATRRLINMadkelGQTALHIAAEQNRRD 938
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN-----GRTALHYAARSGHLE 75

                          90
                  ....*....|....*.
gi 320541875  939 ICVMLVAAGAHLDTLD 954
Cdd:pfam12796  76 IVKLLLEKGADINVKD 91
C1_DGKiota_rpt1 cd20850
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase iota (DAG ...
 115-183 4.31e-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: 85.08  E-value: 4.31e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 320541875 115 DWTENAVQGEHYWKPTSASGDLCCLNEE-CI----KSGQRMKCSACQLVAHHNCIPFVnEKSTLACKPTYRDVG 183
Cdd:cd20850    1 DWSENAVNGEHLWLETNVSGDLCYLGEEnCQvkfaKSALRRKCAACKIVVHTACIEQL-EKINFRCKPTFREGG 73
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
853-976 2.22e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 83.85  E-value: 2.22e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541875 853 EQTSDAILLAAQSGDLNMLRALHEQGYSLQSVNKNGQTALHFACKYNHRDIVKYIIASATRrlINMADKElGQTALHIAA 932
Cdd:COG0666   52 ALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGAD--VNARDKD-GETPLHLAA 128

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 320541875 933 EQNRRDICVMLVAAGAHLDTLDSGGNTPMMVAFNKNANEIATYL 976
Cdd:COG0666  129 YNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
858-976 2.94e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 83.46  E-value: 2.94e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541875 858 AILLAAQSGDLNMLRALHEQGYSLQSVNKNGQTALHFACKYNHRDIVKYIIAS-ATrrlINMADKElGQTALHIAAEQNR 936
Cdd:COG0666  156 PLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAgAD---VNAKDND-GKTALDLAAENGN 231

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 320541875 937 RDICVMLVAAGAHLDTLDSGGNTPMMVAFNKNANEIATYL 976
Cdd:COG0666  232 LEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLL 271
C1_DGKzeta_rpt1 cd20849
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta (DAG ...
 115-183 6.81e-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: 6.81e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 320541875 115 DWTENAVQGEHYWKPTSASGDLCCLNEE-CI-----KSGQRMKCSACQLVAHHNCIPFVnEKSTLACKPTYRDVG 183
Cdd:cd20849    1 DWSESAVYGEHIWFETNVSGDFCYVGEQnCVakqlqKSVSRKKCAACKIVVHTPCIEQL-EKINFRCKPSFRESG 74
TIGR00147 TIGR00147
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ...
 351-662 2.23e-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: 2.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541875  351 INPKSGGNQGHKLLGKFQHLLNPRQVFDLTQGGPKMGLDMF-----RKAPNLRVLACGGDGTVGWVLSVLDqiqpPLQPA 425
Cdd:TIGR00147   8 LNPTAGKSNDNKPLREVIMLLREEGMEIHVRVTWEKGDAARyveeaRKFGVDTVIAGGGDGTINEVVNALI----QLDDI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541875  426 PAVGVLPLGTGNDLARALGWgggytdePIgKILREIgmsqcvlmdrwrvKVTPNDDVTDdhVDRSKPNVPLNVInNYFSF 505
Cdd:TIGR00147  84 PALGILPLGTANDFARSLGI-------PE-DLDKAA-------------KLVIAGDARA--IDMGQVNKQYCFI-NMAGG 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541875  506 GVDAHIALEFheareahPERFNSRLRNKMYYgqmggkdliLRQYRNLS--QWVTLECDGQDFTGKLrdagcHAVLFL--N 581
Cdd:TIGR00147 140 GFGTEITTET-------PEKLKAALGSLSYI---------LSGLMRMDtlQPFRCEIRGEGEHWQG-----EAVVFLvgN 198

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541875  582 IPSYGGGTHPWNDSfgaskpSIDDGLMEVVGLTTYQL-------PMLQAGMH----GTCICQCRKARIITKRTIPMQVDG 650
Cdd:TIGR00147 199 GRQAGGGQKLAPDA------SINDGLLDLRIFTNDNLlpalvltLMSDEGKHtdnpNIIYGKASRIDIQTPHKITFNLDG 272

                         330
                  ....*....|..
gi 320541875  651 EACRVKPSVIEI 662
Cdd:TIGR00147 273 EPLGGTPFHIEI 284
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
858-976 1.03e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 63.82  E-value: 1.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541875 858 AILLAAQSGDLNMLRALHEQGYSLQSVNKNGQTALHFACKYNHRDIVKYIIASAtrrLINMADKELGQTALHIAAEQNRR 937
Cdd:COG0666   24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAG---ADINAKDDGGNTLLHAAARNGDL 100

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 320541875 938 DICVMLVAAGAHLDTLDSGGNTPMMVAFNKNANEIATYL 976
Cdd:COG0666  101 EIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLL 139
Ank_4 pfam13637
Ankyrin repeats (many copies);
855-908 4.58e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.05  E-value: 4.58e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 320541875  855 TSDAILLAAQSGDLNMLRALHEQGYSLQSVNKNGQTALHFACKYNHRDIVKYII 908
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
858-910 4.93e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 51.27  E-value: 4.93e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 320541875  858 AILLAAQSGDLNMLRALHEqgYSLQSVNKNGQTALHFACKYNHRDIVKYIIAS 910
Cdd:pfam12796  33 ALHLAAKNGHLEIVKLLLE--HADVNLKDNGRTALHYAARSGHLEIVKLLLEK 83
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
 125-174 5.76e-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: 5.76e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 320541875  125 HYWKPTS-ASGDLCCLNEECI--KSGQRMKCSACQLVAHHNCIPFVNEKSTLA 174
Cdd:pfam00130   1 HHFVHRNfKQPTFCDHCGEFLwgLGKQGLKCSWCKLNVHKRCHEKVPPECGCD 53
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
 195-259 8.61e-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: 8.61e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 320541875  195 HHWVHRKLEK-GKCKQCGKFFPMKqavqsklfgskEIVALACAWCHEIYHNKeaCFNQAKIGEECR 259
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 ...
 195-261 3.07e-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: 48.21  E-value: 3.07e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 320541875 195 HHWVHRKLEKG-KCKQCGKffpmkqavqsKLFGSKEIVALACAWCHEIYHNKeaCFNQAKIgEECRLG 261
Cdd:cd20805    1 HHWVEGNLPSGaKCSVCGK----------KCGSSFGLAGYRCSWCKRTVHSE--CIDKLGP-EECDLG 55
Ank_5 pfam13857
Ankyrin repeats (many copies);
874-931 5.00e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.34  E-value: 5.00e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 320541875  874 LHEQGY-SLQSVNKNGQTALHFACKYNHRDIVKYIIASatRRLINMADKElGQTALHIA 931
Cdd:pfam13857   1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAY--GVDLNLKDEE-GLTALDLA 56
PRK13054 PRK13054
lipid kinase; Reviewed
 398-444 5.92e-07

lipid kinase; Reviewed


Pssm-ID: 237281 [Multi-domain]  Cd Length: 300  Bit Score: 52.57  E-value: 5.92e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 320541875 398 RVLACGGDGTVGWVLSVLDQIQPPLQpaPAVGVLPLGTGNDLARALG 444
Cdd:PRK13054  59 TVIAGGGDGTINEVATALAQLEGDAR--PALGILPLGTANDFATAAG 103
PHA03095 PHA03095
ankyrin-like protein; Provisional
 871-979 6.80e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 53.10  E-value: 6.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541875 871 LRALHEQGYSLQSVNKNGQTALHFACKYN---HRDIVKYIIASATrrlINMADKeLGQTALHIAAEQNRRDICVMLVAAG 947
Cdd:PHA03095 205 VRELIRAGCDPAATDMLGNTPLHSMATGSsckRSLVLPLLIAGIS---INARNR-YGQTPLHYAAVFNNPRACRRLIALG 280

                         90       100       110
                 ....*....|....*....|....*....|...
gi 320541875 948 AHLDTLDSGGNTPMMVAF-NKNANEIATYLESQ 979
Cdd:PHA03095 281 ADINAVSSDGNTPLSLMVrNNNGRAVRAALAKN 313
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
 124-169 1.77e-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: 45.54  E-value: 1.77e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 320541875   124 EHYWKPTSASGDLCCLNEECIKSG--QRMKCSACQLVAHHNCIPFVNE 169
Cdd:smart00109   1 HKHVFRTFTKPTFCCVCRKSIWGSfkQGLRCSECKVKCHKKCADKVPK 48
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 859-948 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 320541875 859 ILLAAQSGDLNMLRAL--------HEQGySLqsvnknGQTALHFACKYNHRDIVKyIIASATRRLINMA---DKELGQTA 927
Cdd:cd22192   21 LLLAAKENDVQAIKKLlkcpscdlFQRG-AL------GETALHVAALYDNLEAAV-VLMEAAPELVNEPmtsDLYQGETA 92

                         90       100
                 ....*....|....*....|.
gi 320541875 928 LHIAAEQNRRDICVMLVAAGA 948
Cdd:cd22192   93 LHIAVVNQNLNLVRELIARGA 113
PRK12361 PRK12361
hypothetical protein; Provisional
 349-446 2.55e-06

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 51.16  E-value: 2.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541875 349 VFINPKSGGNQGHKLLGKFQHLLNPRqvFDLT--QGGPKMGLDMFRKAPNLR----VLACGGDGTVGWVLSVLDQIQPPL 422
Cdd:PRK12361 247 LIANPVSGGGKWQEYGEQIQRELKAY--FDLTvkLTTPEISAEALAKQARKAgadiVIACGGDGTVTEVASELVNTDITL 324

                         90       100
                 ....*....|....*....|....*
gi 320541875 423 qpapavGVLPLGTGNDLARAL-GWG 446
Cdd:PRK12361 325 ------GIIPLGTANALSHALfGLG 343
PRK13057 PRK13057
lipid kinase;
398-444 3.50e-06

lipid kinase;


Pssm-ID: 183857 [Multi-domain]  Cd Length: 287  Bit Score: 49.92  E-value: 3.50e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 320541875 398 RVLACGGDGTVGWVLSVLDQIQPPLqpapavGVLPLGTGNDLARALG 444
Cdd:PRK13057  53 LVIVGGGDGTLNAAAPALVETGLPL------GILPLGTANDLARTLG 93
Ank_4 pfam13637
Ankyrin repeats (many copies);
890-944 5.75e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.19  E-value: 5.75e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 320541875  890 TALHFACKYNHRDIVKYIIASATRrlINMADKElGQTALHIAAEQNRRDICVMLV 944
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGAD--INAVDGN-GETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
908-964 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 320541875  908 IASATRRLINMADKElGQTALHIAAEQNRRDICVMLVAAGAHLDTLDSGGNTPMMVA 964
Cdd:pfam13857   1 LLEHGPIDLNRLDGE-GYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_2 pfam12796
Ankyrin repeats (3 copies);
928-976 6.71e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 42.41  E-value: 6.71e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 320541875  928 LHIAAEQNRRDICVMLVAAGAHLDTLDSGGNTPMMVAFNKNANEIATYL 976
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL 49
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 853-964 8.48e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 46.41  E-value: 8.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541875 853 EQTSDAILLAAQSGD----LNMLRALHEQGYSLQSVNKN-GQTALHFACKYNHRDIVKYIIASATRrlINMADKeLGQTA 927
Cdd:PHA02878 128 IQTIDLVYIDKKSKDdiieAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGAN--VNIPDK-TNNSP 204

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 320541875 928 LHIAAEQNRRDICVMLVAAGAHLDTLDSGGNTPMMVA 964
Cdd:PHA02878 205 LHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS 241
PRK13055 PRK13055
putative lipid kinase; Reviewed
 399-470 1.01e-04

putative lipid kinase; Reviewed


Pssm-ID: 237282 [Multi-domain]  Cd Length: 334  Bit Score: 45.75  E-value: 1.01e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 320541875 399 VLACGGDGTVGWVLSVLdqiqPPLQPAPAVGVLPLGTGNDLARALGWGggyTDEPIgKILREIGMSQCVLMD 470
Cdd:PRK13055  63 IIAAGGDGTINEVVNGI----APLEKRPKMAIIPAGTTNDYARALKIP---RDNPV-EAAKVILKNQTIKMD 126
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 869-961 1.50e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 45.34  E-value: 1.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541875 869 NMLRALHEQGYSLQSVNKNGQTALHFACKYNHRDIVKYIIAsaTRRLINMADKElGQTALHIAAEQNRRDICVMLVAAGA 948
Cdd:PHA02874 105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFE--YGADVNIEDDN-GCYPIHIAIKHNFFDIIKLLLEKGA 181

                         90
                 ....*....|...
gi 320541875 949 HLDTLDSGGNTPM 961
Cdd:PHA02874 182 YANVKDNNGESPL 194
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 878-955 1.65e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 45.04  E-value: 1.65e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 320541875 878 GYSLQSVNKNGQTALHFACKYNHRDIVKYII-ASATRRLINMadkeLGQTALHIAAEQNRRDICVMLVAAGAHLDTLDS 955
Cdd:PHA03100 182 GVPINIKDVYGFTPLHYAVYNNNPEFVKYLLdLGANPNLVNK----YGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 859-966 1.67e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 45.34  E-value: 1.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541875 859 ILLAAQSGDLNMLRALHEQGYSLQSVNKNGQTALHFACKYNHRDIVKYIIASaTRRLINMADKelGQTALHIAAEQNRRd 938
Cdd:PHA02874 161 IHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDH-GNHIMNKCKN--GFTPLHNAIIHNRS- 236

                         90       100
                 ....*....|....*....|....*...
gi 320541875 939 iCVMLVAAGAHLDTLDSGGNTPMMVAFN 966
Cdd:PHA02874 237 -AIELLINNASINDQDIDGSTPLHHAIN 263
C1_DGKepsilon_typeIII_rpt2 cd20853
second protein kinase C conserved region 1 (C1 domain) found in type III diacylglycerol kinase, ...
 195-270 1.78e-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: 40.34  E-value: 1.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541875 195 HHWVHRKLEKG-KC----KQCGkffpmkqaVQSKLfgskeiVALACAWCHEIYHNKeaCFnqAKIGEECRLGNYAPIIVP 269
Cdd:cd20853    1 HHWVRGNLPLCsVCcvcnEQCG--------NQPGL------CDYRCCWCQRTVHDD--CL--AKLPKECDLGAFRNFIVP 62


                 .
gi 320541875 270 P 270
Cdd:cd20853   63 P 63
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 857-960 3.04e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 44.86  E-value: 3.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541875 857 DAILLAAQSGDLNMLRALHEQGYSLQSVNKNGQTALHFACKYNHRDIVKYIIASATRRLINMADKELGQTALH--IAAEQ 934
Cdd:PLN03192 624 DLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDDFSPTELRelLQKRE 703

                         90       100
                 ....*....|....*....|....*.
gi 320541875 935 NRRDICVMLVAAGAHLDTLDSGGNTP 960
Cdd:PLN03192 704 LGHSITIVDSVPADEPDLGRDGGSRP 729
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 887-908 3.31e-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: 3.31e-04
                          10        20
                  ....*....|....*....|..
gi 320541875  887 NGQTALHFACKYNHRDIVKYII 908
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLL 22
Ank_4 pfam13637
Ankyrin repeats (many copies);
926-976 4.99e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.79  E-value: 4.99e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 320541875  926 TALHIAAEQNRRDICVMLVAAGAHLDTLDSGGNTPM-MVAFNKNAnEIATYL 976
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALhFAASNGNV-EVLKLL 53
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 886-976 6.86e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 43.33  E-value: 6.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541875 886 KNGQTA-LHFACKYNHRDIVKYIIasaTRRL------INMADKELGQTALHIAAEQNRRDICVMLVAAGAHLDTLDSGGN 958
Cdd:PHA02878 126 KNIQTIdLVYIDKKSKDDIIEAEI---TKLLlsygadINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNN 202

                         90
                 ....*....|....*...
gi 320541875 959 TPMMVAFNKNANEIATYL 976
Cdd:PHA02878 203 SPLHHAVKHYNKPIVHIL 220
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 855-976 7.68e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 43.12  E-value: 7.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541875 855 TSDAILLAAQSGDLNMLRALHEQGYSLQSVNKNGQTALHFACKYNHRDI------------------VKYIIASATrrLI 916
Cdd:PHA03100 108 TPLLYAISKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkilkllidkgvdinaknrVNYLLSYGV--PI 185

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541875 917 NMADkELGQTALHIAAEQNRRDICVMLVAAGAHLDTLDSGGNTPMMVAFNKNANEIATYL 976
Cdd:PHA03100 186 NIKD-VYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 863-943 7.76e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.35  E-value: 7.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541875 863 AQSGDLNMLRALHEQGYSLQSVNKNGQTALHFACKYNHRDIVKYII---ASATrrlinMADKElGQTALHIAAEQNRRDI 939
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLefgADPT-----LLDKD-GKTPLELAEENGFREV 163


                 ....
gi 320541875 940 CVML 943
Cdd:PTZ00322 164 VQLL 167
PRK00861 PRK00861
putative lipid kinase; Reviewed
 352-444 8.11e-04

putative lipid kinase; Reviewed


Pssm-ID: 234850 [Multi-domain]  Cd Length: 300  Bit Score: 42.69  E-value: 8.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541875 352 NPKSGGNQGHKLLGKFQHLLNPRQVFDLTQGGPKMGLDMFRKAPNLR----VLACGGDGTVGWVLSVLDQIQPPLqpapa 427
Cdd:PRK00861  10 NPVAGQGNPEVDLALIRAILEPEMDLDIYLTTPEIGADQLAQEAIERgaelIIASGGDGTLSAVAGALIGTDIPL----- 84

                         90
                 ....*....|....*..
gi 320541875 428 vGVLPLGTGNDLARALG 444
Cdd:PRK00861  85 -GIIPRGTANAFAAALG 100
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 887-908 1.22e-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: 1.22e-03
                           10        20
                   ....*....|....*....|..
gi 320541875   887 NGQTALHFACKYNHRDIVKYII 908
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLL 22
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 885-979 2.99e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 39.47  E-value: 2.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541875 885 NKNGQTALHFACKynHRDIV-----KYIIASATRRLINMADKElGQTALHIAAEQNR---RDICVMLVAAGAHLDTLDS- 955
Cdd:PHA02736  14 DIEGENILHYLCR--NGGVTdllafKNAISDENRYLVLEYNRH-GKQCVHIVSNPDKadpQEKLKLLMEWGADINGKERv 90

                         90       100
                 ....*....|....*....|....
gi 320541875 956 GGNTPMMVAFNKNANEIATYLESQ 979
Cdd:PHA02736  91 FGNTPLHIAVYTQNYELATWLCNQ 114
C1_DGK_typeI_like_rpt2 cd20851
second protein kinase C conserved region 1 (C1 domain) found in type I diacylglycerol kinases; ...
 195-261 3.04e-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: 3.04e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 320541875 195 HHWVHRKLEkGKCKQCGKFFPMKQAVQsklfgskeivALACAWCHEIYHNKeaCFNQakIGEECRLG 261
Cdd:cd20851    1 HHWVEGNCP-GKCDKCHKSIKSYQGLT----------GLHCVWCHITLHNK--CASH--VKPECDLG 52
PHA03095 PHA03095
ankyrin-like protein; Provisional
 859-964 4.65e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 40.78  E-value: 4.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541875 859 ILLAAQSGDLNMLRALHEQGYSLQSVNKNGQTALHFACKyNHR---DIVKYIIASATrrliNMADKEL-GQTALHIAAEQ 934
Cdd:PHA03095 123 VYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLK-SRNanvELLRLLIDAGA----DVYAVDDrFRSLLHHHLQS 197

                         90       100       110
                 ....*....|....*....|....*....|..
gi 320541875 935 NRRDICVM--LVAAGAHLDTLDSGGNTPMMVA 964
Cdd:PHA03095 198 FKPRARIVreLIRAGCDPAATDMLGNTPLHSM 229
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 887-981 5.72e-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: 5.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541875 887 NGQTALHFAC---KYNHRDIVKYIIASAT-----RRLINMADKE---LGQTALHIAAEQNRRDICVMLVAAGAHLDTLDS 955
Cdd:cd22194   93 TGKTCLMKALlniNENTKEIVRILLAFAEengilDRFINAEYTEeayEGQTALNIAIERRQGDIVKLLIAKGADVNAHAK 172

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 320541875 956 G--------------GNTPMMVAFNKNANEIATYLESQER 981
Cdd:cd22194  173 GvffnpkykhegfyfGETPLALAACTNQPEIVQLLMEKES 212
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 924-952 5.96e-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: 5.96e-03
                          10        20
                  ....*....|....*....|....*....
gi 320541875  924 GQTALHIAAEQNRRDICVMLVAAGAHLDT 952
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PRK13059 PRK13059
putative lipid kinase; Reviewed
 399-444 8.50e-03

putative lipid kinase; Reviewed


Pssm-ID: 183858  Cd Length: 295  Bit Score: 39.25  E-value: 8.50e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 320541875 399 VLACGGDGTVGWVLSVLDQ--IQPPLqpapavGVLPLGTGNDLARALG 444
Cdd:PRK13059  60 ILIAGGDGTVDNVVNAMKKlnIDLPI------GILPVGTANDFAKFLG 101
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 924-978 8.82e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 39.88  E-value: 8.82e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 320541875 924 GQTALHIAAEQNRRDICVMLVAAGAHLDTLDSGGNTPMMVAFNKNANEIATYLES 978
Cdd:PTZ00322 115 GRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 862-972 8.89e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 39.56  E-value: 8.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541875 862 AAQSGDLNMLRALHEQGYSLQSVNKNGQTALHFACKYNHRDIVKYIIASATrrLINMADKElGQTALHIAAEQNRRDICV 941
Cdd:PHA02874 131 AIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGA--YANVKDNN-GESPLHNAAEYGDYACIK 207

                         90       100       110
                 ....*....|....*....|....*....|...
gi 320541875 942 MLVAAGAHLDTLDSGGNTPMMVA--FNKNANEI 972
Cdd:PHA02874 208 LLIDHGNHIMNKCKNGFTPLHNAiiHNRSAIEL 240
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 924-954 9.14e-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: 9.14e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 320541875  924 GQTALHIAAEQ-NRRDICVMLVAAGAHLDTLD 954
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
 
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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