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Conserved domains on  [gi|1012282641|ref|NP_001308639|]
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diacylglycerol kinase iota isoform 4 [Homo sapiens]

Protein Classification

diacylglycerol kinase( domain architecture ID 11618468)

diacylglycerol kinase catalyzes the conversion of diacylglycerol (DAG) to phosphatidic acid (PA), utilizing ATP as a source of the phosphate

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 ...
 226-383 4.82e-76

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


:

Pssm-ID: 214486  Cd Length: 160  Bit Score: 241.86  E-value: 4.82e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012282641  226 VFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGAAFSDFLQRSSRDLSKHVKVVCDGTDLTPKIqelKFQCI 305
Cdd:smart00045   1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLPN---SLEGI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012282641  306 VFLNIPRYCAGTMPWGNPGDH-HDFEPQRHDDGYIEVIGFTMASLAA--LQVGGHGERLHQCREV--MLLTYKSIPMQVD 380
Cdd:smart00045  78 AVLNIPSYGGGTNLWGTTDKEdLNFSKQSHDDGLLEVVGLTGAMHMAqiRQVGLAGRRIAQCSEVriTIKTSKTIPMQVD 157


                   ...
gi 1012282641  381 GEP 383
Cdd:smart00045 158 GEP 160
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 78-199 3.39e-47

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: 163.24  E-value: 3.39e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012282641   78 LVFVNPKSGGNQGTKVLQMFMWYLNPRQVFDLSQEGPKDALELYRKVPN-LRILACGGDGTVGWILSILDELQL-SPQPP 155
Cdd:smart00046   1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVPDfNRVLVCGGDGTVGWVLNALDKRELpLPEPP 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1012282641  156 VGVLPLGTGNDLARTLNWGGGYTDEPVSKILCQVEDGTVVQLDR 199
Cdd:smart00046  81 VAVLPLGTGNDLARSLGWGGGYDGEKLLKTLRDALESDTVKLDR 124
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
598-733 1.10e-17

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 84.24  E-value: 1.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012282641 598 AILQAVIAGDL--MK-LIEsykNGGSLLIQGPDHCSLLHYAAKTGNGEIVKYILDHGPSelLDMADSEtGETALHKAACQ 674
Cdd:COG0666   123 PLHLAAYNGNLeiVKlLLE---AGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGAD--VNARDND-GETPLHLAAEN 196

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1012282641 675 RNRAVCQLLVDAGASLRKTDSKGKTPQERAQQAGDPDLAAYLESRQNYKVIGHEDLETA 733
Cdd:COG0666   197 GHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTA 255
C1 super family cl00040
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ...
 1-23 1.33e-10

protein kinase C conserved region 1 (C1 domain) superfamily; 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 the motif HX12CX2CXnCX2CX4HX2CX7C, where C and H are cysteine and histidine, respectively; X represents other residues; and n is either 13 or 14. C1 has a globular fold with two separate Zn(2+)-binding sites. It was originally discovered as lipid-binding modules in protein kinase C (PKC) isoforms. C1 domains that bind and respond to phorbol esters (PE) and diacylglycerol (DAG) are referred to as typical, and those that do not respond to PE and DAG are deemed atypical. A C1 domain may also be referred to as PKC or non-PKC C1, based on the parent protein's activity. Most C1 domain-containing non-PKC proteins act as lipid kinases and scaffolds, except PKD which acts as a protein kinase. PKC C1 domains play roles in membrane translocation and activation of the enzyme.


The actual alignment was detected with superfamily member cd20896:

Pssm-ID: 412127  Cd Length: 75  Bit Score: 57.79  E-value: 1.33e-10
                          10        20
                  ....*....|....*....|...
gi 1012282641   1 MLHHIEEPCSLGAHAAVIVPPTW 23
Cdd:cd20896    53 MLHHIEEPCSLGAHAAVIVPPTW 75
 
Name Accession Description Interval E-value
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 226-383 4.82e-76

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


Pssm-ID: 214486  Cd Length: 160  Bit Score: 241.86  E-value: 4.82e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012282641  226 VFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGAAFSDFLQRSSRDLSKHVKVVCDGTDLTPKIqelKFQCI 305
Cdd:smart00045   1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLPN---SLEGI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012282641  306 VFLNIPRYCAGTMPWGNPGDH-HDFEPQRHDDGYIEVIGFTMASLAA--LQVGGHGERLHQCREV--MLLTYKSIPMQVD 380
Cdd:smart00045  78 AVLNIPSYGGGTNLWGTTDKEdLNFSKQSHDDGLLEVVGLTGAMHMAqiRQVGLAGRRIAQCSEVriTIKTSKTIPMQVD 157


                   ...
gi 1012282641  381 GEP 383
Cdd:smart00045 158 GEP 160
DAGK_acc pfam00609
Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts ...
 226-383 3.09e-69

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


Pssm-ID: 459866  Cd Length: 158  Bit Score: 224.02  E-value: 3.09e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012282641 226 VFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGAAFSDFLQRSSRDLSKHVKVVCDGTDLTPKiqeLKFQCI 305
Cdd:pfam00609   1 VMNNYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDMFQRSCKNLIEKVELEVDGKDLPLP---KSLEGI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012282641 306 VFLNIPRYCAGTMPWGNPGDHHD-FEPQRHDDGYIEVIGFT-MASLAALQVGGHGE-RLHQCREVMLLTYKSIPMQVDGE 382
Cdd:pfam00609  78 VVLNIPSYAGGTDLWGNSKEDGLgFAPQSVDDGLLEVVGLTgALHLGQVQVGLGSAkRIAQGGPIRITTKKKIPMQVDGE 157


                  .
gi 1012282641 383 P 383
Cdd:pfam00609 158 P 158
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 78-199 3.39e-47

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: 163.24  E-value: 3.39e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012282641   78 LVFVNPKSGGNQGTKVLQMFMWYLNPRQVFDLSQEGPKDALELYRKVPN-LRILACGGDGTVGWILSILDELQL-SPQPP 155
Cdd:smart00046   1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVPDfNRVLVCGGDGTVGWVLNALDKRELpLPEPP 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1012282641  156 VGVLPLGTGNDLARTLNWGGGYTDEPVSKILCQVEDGTVVQLDR 199
Cdd:smart00046  81 VAVLPLGTGNDLARSLGWGGGYDGEKLLKTLRDALESDTVKLDR 124
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 76-175 1.78e-34

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: 127.70  E-value: 1.78e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012282641  76 PLLVFVNPKSGGNQGTKVLQMFMWYLNPRQV-FDLSQ-EGPKDALELYRKVPNL---RILACGGDGTVGWILSILDELql 150
Cdd:pfam00781   1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVeVELVLtEGPGDALELAREAAEDgydRIVVAGGDGTVNEVLNGLAGL-- 78

                          90       100
                  ....*....|....*....|....*
gi 1012282641 151 SPQPPVGVLPLGTGNDLARTLNWGG 175
Cdd:pfam00781  79 ATRPPLGIIPLGTGNDFARALGIPG 103
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 74-393 1.86e-27

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


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 113.02  E-value: 1.86e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012282641  74 MKPLLVFVNPKSGGNQGTKVLQMFMWYLNpRQVFDLSQ---EGPKDALELYRKVPNL---RILACGGDGTVGWILSILde 147
Cdd:COG1597     2 MMRALLIVNPASGRGRAARLLERLVAALR-AAGLEVEVletESPGDATELAREAAAEgadLVVAAGGDGTVNEVANGL-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012282641 148 lqLSPQPPVGVLPLGTGNDLARTLNwgggyTDEPVSKILCQVEDGTVVQLDrwnlhvernpdlppeeledgVCKLPLNVF 227
Cdd:COG1597    79 --AGTGPPLGILPLGTGNDFARALG-----IPLDPEAALEALLTGRTRRID--------------------LGRVNGRYF 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012282641 228 NNYFSLGFDAHVTLEFHESReanpekfnSRFRNKMFYAGAAFSDFLQRSSRdlskHVKVVCDGTDLtpkiqELKFQCIVF 307
Cdd:COG1597   132 LNVAGIGFDAEVVERANRAL--------KRRLGKLAYVLAALRALLRYRPF----RLRIELDGEEI-----EGEALLVAV 194

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012282641 308 LNIPRYcaGTMPWGNPGDhhdfepqRHDDGYIEVIGFT-------MASLAALQVGGHGE----RLHQCREVMLLTYKSIP 376
Cdd:COG1597   195 GNGPYY--GGGLRLAPDA-------SLDDGLLDVVVVRplsrlrlLRLLPRLLRGRHLRhpgvRYFRAREVEIESDRPLP 265

                         330
                  ....*....|....*...
gi 1012282641 377 MQVDGEPCRLA-PAMIRI 393
Cdd:COG1597   266 VQLDGEPLGLAtPLEFEV 283
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
598-733 1.10e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 84.24  E-value: 1.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012282641 598 AILQAVIAGDL--MK-LIEsykNGGSLLIQGPDHCSLLHYAAKTGNGEIVKYILDHGPSelLDMADSEtGETALHKAACQ 674
Cdd:COG0666   123 PLHLAAYNGNLeiVKlLLE---AGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGAD--VNARDND-GETPLHLAAEN 196

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1012282641 675 RNRAVCQLLVDAGASLRKTDSKGKTPQERAQQAGDPDLAAYLESRQNYKVIGHEDLETA 733
Cdd:COG0666   197 GHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTA 255
Ank_2 pfam12796
Ankyrin repeats (3 copies);
599-694 1.63e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 66.68  E-value: 1.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012282641 599 ILQAVIAGDLMKLIESYKNGGSLLIQGPDHCSLLHYAAKTGNGEIVKYILDHGPSELLDMadsetGETALHKAACQRNRA 678
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN-----GRTALHYAARSGHLE 75

                          90
                  ....*....|....*.
gi 1012282641 679 VCQLLVDAGASLRKTD 694
Cdd:pfam12796  76 IVKLLLEKGADINVKD 91
C1_DGKiota_rpt2 cd20896
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase iota ...
 1-23 1.33e-10

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: 57.79  E-value: 1.33e-10
                          10        20
                  ....*....|....*....|...
gi 1012282641   1 MLHHIEEPCSLGAHAAVIVPPTW 23
Cdd:cd20896    53 MLHHIEEPCSLGAHAAVIVPPTW 75
PRK13057 PRK13057
lipid kinase;
78-172 2.22e-08

lipid kinase;


Pssm-ID: 183857 [Multi-domain]  Cd Length: 287  Bit Score: 56.08  E-value: 2.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012282641  78 LVFVNPKSggNQGTKVLQMFMWYLNPRQvFDLSQEGPKDALEL------YRKVPNLRILAcGGDGTVGWILSILDELQLs 151
Cdd:PRK13057    1 LLLVNRHA--RSGRAALAAARAALEAAG-LELVEPPAEDPDDLsevieaYADGVDLVIVG-GGDGTLNAAAPALVETGL- 75

                          90       100
                  ....*....|....*....|.
gi 1012282641 152 pqpPVGVLPLGTGNDLARTLN 172
Cdd:PRK13057   76 ---PLGILPLGTANDLARTLG 93
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 607-706 3.14e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.88  E-value: 3.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012282641 607 DLMKLIesYKNGGSLLIQGPDHCSLLHYAAKTGNGEIVKYILDHGPSellDMADSETGETALHKAACQrNRAVCQLLVDa 686
Cdd:PHA02874  171 DIIKLL--LEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNH---IMNKCKNGFTPLHNAIIH-NRSAIELLIN- 243

                          90       100
                  ....*....|....*....|
gi 1012282641 687 GASLRKTDSKGKTPQERAQQ 706
Cdd:PHA02874  244 NASINDQDIDGSTPLHHAIN 263
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 627-653 5.77e-04

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: 37.57  E-value: 5.77e-04
                           10        20
                   ....*....|....*....|....*..
gi 1012282641  627 DHCSLLHYAAKTGNGEIVKYILDHGPS 653
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
TIGR00147 TIGR00147
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ...
 128-171 7.80e-04

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: 42.11  E-value: 7.80e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1012282641 128 RILACGGDGTVGWILSILdeLQLSPQPPVGVLPLGTGNDLARTL 171
Cdd:TIGR00147  60 TVIAGGGDGTINEVVNAL--IQLDDIPALGILPLGTANDFARSL 101
 
Name Accession Description Interval E-value
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 226-383 4.82e-76

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


Pssm-ID: 214486  Cd Length: 160  Bit Score: 241.86  E-value: 4.82e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012282641  226 VFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGAAFSDFLQRSSRDLSKHVKVVCDGTDLTPKIqelKFQCI 305
Cdd:smart00045   1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLPN---SLEGI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012282641  306 VFLNIPRYCAGTMPWGNPGDH-HDFEPQRHDDGYIEVIGFTMASLAA--LQVGGHGERLHQCREV--MLLTYKSIPMQVD 380
Cdd:smart00045  78 AVLNIPSYGGGTNLWGTTDKEdLNFSKQSHDDGLLEVVGLTGAMHMAqiRQVGLAGRRIAQCSEVriTIKTSKTIPMQVD 157


                   ...
gi 1012282641  381 GEP 383
Cdd:smart00045 158 GEP 160
DAGK_acc pfam00609
Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts ...
 226-383 3.09e-69

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


Pssm-ID: 459866  Cd Length: 158  Bit Score: 224.02  E-value: 3.09e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012282641 226 VFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGAAFSDFLQRSSRDLSKHVKVVCDGTDLTPKiqeLKFQCI 305
Cdd:pfam00609   1 VMNNYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDMFQRSCKNLIEKVELEVDGKDLPLP---KSLEGI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012282641 306 VFLNIPRYCAGTMPWGNPGDHHD-FEPQRHDDGYIEVIGFT-MASLAALQVGGHGE-RLHQCREVMLLTYKSIPMQVDGE 382
Cdd:pfam00609  78 VVLNIPSYAGGTDLWGNSKEDGLgFAPQSVDDGLLEVVGLTgALHLGQVQVGLGSAkRIAQGGPIRITTKKKIPMQVDGE 157


                  .
gi 1012282641 383 P 383
Cdd:pfam00609 158 P 158
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 78-199 3.39e-47

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: 163.24  E-value: 3.39e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012282641   78 LVFVNPKSGGNQGTKVLQMFMWYLNPRQVFDLSQEGPKDALELYRKVPN-LRILACGGDGTVGWILSILDELQL-SPQPP 155
Cdd:smart00046   1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVPDfNRVLVCGGDGTVGWVLNALDKRELpLPEPP 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1012282641  156 VGVLPLGTGNDLARTLNWGGGYTDEPVSKILCQVEDGTVVQLDR 199
Cdd:smart00046  81 VAVLPLGTGNDLARSLGWGGGYDGEKLLKTLRDALESDTVKLDR 124
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 76-175 1.78e-34

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: 127.70  E-value: 1.78e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012282641  76 PLLVFVNPKSGGNQGTKVLQMFMWYLNPRQV-FDLSQ-EGPKDALELYRKVPNL---RILACGGDGTVGWILSILDELql 150
Cdd:pfam00781   1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVeVELVLtEGPGDALELAREAAEDgydRIVVAGGDGTVNEVLNGLAGL-- 78

                          90       100
                  ....*....|....*....|....*
gi 1012282641 151 SPQPPVGVLPLGTGNDLARTLNWGG 175
Cdd:pfam00781  79 ATRPPLGIIPLGTGNDFARALGIPG 103
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 74-393 1.86e-27

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


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 113.02  E-value: 1.86e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012282641  74 MKPLLVFVNPKSGGNQGTKVLQMFMWYLNpRQVFDLSQ---EGPKDALELYRKVPNL---RILACGGDGTVGWILSILde 147
Cdd:COG1597     2 MMRALLIVNPASGRGRAARLLERLVAALR-AAGLEVEVletESPGDATELAREAAAEgadLVVAAGGDGTVNEVANGL-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012282641 148 lqLSPQPPVGVLPLGTGNDLARTLNwgggyTDEPVSKILCQVEDGTVVQLDrwnlhvernpdlppeeledgVCKLPLNVF 227
Cdd:COG1597    79 --AGTGPPLGILPLGTGNDFARALG-----IPLDPEAALEALLTGRTRRID--------------------LGRVNGRYF 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012282641 228 NNYFSLGFDAHVTLEFHESReanpekfnSRFRNKMFYAGAAFSDFLQRSSRdlskHVKVVCDGTDLtpkiqELKFQCIVF 307
Cdd:COG1597   132 LNVAGIGFDAEVVERANRAL--------KRRLGKLAYVLAALRALLRYRPF----RLRIELDGEEI-----EGEALLVAV 194

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012282641 308 LNIPRYcaGTMPWGNPGDhhdfepqRHDDGYIEVIGFT-------MASLAALQVGGHGE----RLHQCREVMLLTYKSIP 376
Cdd:COG1597   195 GNGPYY--GGGLRLAPDA-------SLDDGLLDVVVVRplsrlrlLRLLPRLLRGRHLRhpgvRYFRAREVEIESDRPLP 265

                         330
                  ....*....|....*...
gi 1012282641 377 MQVDGEPCRLA-PAMIRI 393
Cdd:COG1597   266 VQLDGEPLGLAtPLEFEV 283
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
598-733 1.10e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 84.24  E-value: 1.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012282641 598 AILQAVIAGDL--MK-LIEsykNGGSLLIQGPDHCSLLHYAAKTGNGEIVKYILDHGPSelLDMADSEtGETALHKAACQ 674
Cdd:COG0666   123 PLHLAAYNGNLeiVKlLLE---AGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGAD--VNARDND-GETPLHLAAEN 196

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1012282641 675 RNRAVCQLLVDAGASLRKTDSKGKTPQERAQQAGDPDLAAYLESRQNYKVIGHEDLETA 733
Cdd:COG0666   197 GHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTA 255
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
596-716 1.08e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 72.29  E-value: 1.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012282641 596 DHAILQAVIAGDLMKLIESYKNGGSLLIQGPDHCSLLHYAAKTGNGEIVKYILDHGPSelLDMADSEtGETALHKAACQR 675
Cdd:COG0666    55 ALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGAD--VNARDKD-GETPLHLAAYNG 131

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1012282641 676 NRAVCQLLVDAGASLRKTDSKGKTPQERAQQAGDPDLAAYL 716
Cdd:COG0666   132 NLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
599-694 1.63e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 66.68  E-value: 1.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012282641 599 ILQAVIAGDLMKLIESYKNGGSLLIQGPDHCSLLHYAAKTGNGEIVKYILDHGPSELLDMadsetGETALHKAACQRNRA 678
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN-----GRTALHYAARSGHLE 75

                          90
                  ....*....|....*.
gi 1012282641 679 VCQLLVDAGASLRKTD 694
Cdd:pfam12796  76 IVKLLLEKGADINVKD 91
C1_DGKiota_rpt2 cd20896
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase iota ...
 1-23 1.33e-10

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: 57.79  E-value: 1.33e-10
                          10        20
                  ....*....|....*....|...
gi 1012282641   1 MLHHIEEPCSLGAHAAVIVPPTW 23
Cdd:cd20896    53 MLHHIEEPCSLGAHAAVIVPPTW 75
C1_DGKzeta_rpt2 cd20895
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta ...
 1-23 2.05e-10

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: 57.40  E-value: 2.05e-10
                          10        20
                  ....*....|....*....|...
gi 1012282641   1 MLHHIEEPCSLGAHAAVIVPPTW 23
Cdd:cd20895    53 MLQQIEEPCSLGAHAAVIVPPTW 75
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
598-733 3.88e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 61.51  E-value: 3.88e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012282641 598 AILQAVIAG--DLMK-LIEsykNGGSLLIQGPDHCSLLHYAAKTGNGEIVKYILDHGPSelLDMADSEtGETALHKAACQ 674
Cdd:COG0666   156 PLHLAAANGnlEIVKlLLE---AGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGAD--VNAKDND-GKTALDLAAEN 229

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1012282641 675 RNRAVCQLLVDAGASLRKTDSKGKTPQERAQQAGDPDLAAYLESRQNYKVIGHEDLETA 733
Cdd:COG0666   230 GNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
596-716 9.13e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 57.27  E-value: 9.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012282641 596 DHAILQAVIAGDLMKLIESYKNGGSLLIQGPDHCSLLHYAAKTGNGEIVKYILDHGpseLLDMADSETGETALHKAACQR 675
Cdd:COG0666    22 ALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAG---ADINAKDDGGNTLLHAAARNG 98

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1012282641 676 NRAVCQLLVDAGASLRKTDSKGKTPQERAQQAGDPDLAAYL 716
Cdd:COG0666    99 DLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLL 139
PRK13057 PRK13057
lipid kinase;
78-172 2.22e-08

lipid kinase;


Pssm-ID: 183857 [Multi-domain]  Cd Length: 287  Bit Score: 56.08  E-value: 2.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012282641  78 LVFVNPKSggNQGTKVLQMFMWYLNPRQvFDLSQEGPKDALEL------YRKVPNLRILAcGGDGTVGWILSILDELQLs 151
Cdd:PRK13057    1 LLLVNRHA--RSGRAALAAARAALEAAG-LELVEPPAEDPDDLsevieaYADGVDLVIVG-GGDGTLNAAAPALVETGL- 75

                          90       100
                  ....*....|....*....|.
gi 1012282641 152 pqpPVGVLPLGTGNDLARTLN 172
Cdd:PRK13057   76 ---PLGILPLGTANDLARTLG 93
PRK12361 PRK12361
hypothetical protein; Provisional
 75-192 1.98e-07

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 54.24  E-value: 1.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012282641  75 KPLLVFVNPKSGGNQGTKVLQMFMWYLNPRqvFDLS-QEGPKD------ALELYRKVPNLrILACGGDGTVGWILSIL-- 145
Cdd:PRK12361  243 KRAWLIANPVSGGGKWQEYGEQIQRELKAY--FDLTvKLTTPEisaealAKQARKAGADI-VIACGGDGTVTEVASELvn 319

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1012282641 146 DELQLspqppvGVLPLGTGNDLARTLnWGGGYTDEPVSKILCQVEDG 192
Cdd:PRK12361  320 TDITL------GIIPLGTANALSHAL-FGLGSKLIPVEQACDNIIQG 359
Ank_4 pfam13637
Ankyrin repeats (many copies);
630-684 2.57e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.96  E-value: 2.57e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1012282641 630 SLLHYAAKTGNGEIVKYILDHGPSelLDMADSEtGETALHKAACQRNRAVCQLLV 684
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGAD--INAVDGN-GETALHFAASNGNVEVLKLLL 54
PRK13059 PRK13059
putative lipid kinase; Reviewed
 74-172 5.01e-06

putative lipid kinase; Reviewed


Pssm-ID: 183858  Cd Length: 295  Bit Score: 48.88  E-value: 5.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012282641  74 MKPLLVFVNPKSGGN----QGTKVLQMFMWYLNPRQVFDLSQEGP-KDALELYRKVPNLrILACGGDGTVGWILSILDEL 148
Cdd:PRK13059    1 MKKVKFIYNPYSGENaiisELDKVIRIHQEKGYLVVPYRISLEYDlKNAFKDIDESYKY-ILIAGGDGTVDNVVNAMKKL 79

                          90       100
                  ....*....|....*....|....
gi 1012282641 149 QLSPqpPVGVLPLGTGNDLARTLN 172
Cdd:PRK13059   80 NIDL--PIGILPVGTANDFAKFLG 101
PRK13054 PRK13054
lipid kinase; Reviewed
 128-169 9.33e-06

lipid kinase; Reviewed


Pssm-ID: 237281 [Multi-domain]  Cd Length: 300  Bit Score: 48.33  E-value: 9.33e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1012282641 128 RILACGGDGTVGWILSILDELQLSPQPPVGVLPLGTGNDLAR 169
Cdd:PRK13054   59 TVIAGGGDGTINEVATALAQLEGDARPALGILPLGTANDFAT 100
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 607-706 3.14e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.88  E-value: 3.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012282641 607 DLMKLIesYKNGGSLLIQGPDHCSLLHYAAKTGNGEIVKYILDHGPSellDMADSETGETALHKAACQrNRAVCQLLVDa 686
Cdd:PHA02874  171 DIIKLL--LEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNH---IMNKCKNGFTPLHNAIIH-NRSAIELLIN- 243

                          90       100
                  ....*....|....*....|
gi 1012282641 687 GASLRKTDSKGKTPQERAQQ 706
Cdd:PHA02874  244 NASINDQDIDGSTPLHHAIN 263
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 627-653 5.77e-04

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: 37.57  E-value: 5.77e-04
                           10        20
                   ....*....|....*....|....*..
gi 1012282641  627 DHCSLLHYAAKTGNGEIVKYILDHGPS 653
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
PRK13055 PRK13055
putative lipid kinase; Reviewed
 129-172 7.40e-04

putative lipid kinase; Reviewed


Pssm-ID: 237282 [Multi-domain]  Cd Length: 334  Bit Score: 42.28  E-value: 7.40e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1012282641 129 ILACGGDGTVGWILSILdeLQLSPQPPVGVLPLGTGNDLARTLN 172
Cdd:PRK13055   63 IIAAGGDGTINEVVNGI--APLEKRPKMAIIPAGTTNDYARALK 104
TIGR00147 TIGR00147
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ...
 128-171 7.80e-04

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: 42.11  E-value: 7.80e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1012282641 128 RILACGGDGTVGWILSILdeLQLSPQPPVGVLPLGTGNDLARTL 171
Cdd:TIGR00147  60 TVIAGGGDGTINEVVNAL--IQLDDIPALGILPLGTANDFARSL 101
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 607-719 1.30e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.90  E-value: 1.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012282641 607 DLMKLIESYKNGGSllIQGPDHCSLLHYAAKTGNGEIVKYILDHGPSelLDMADSeTGETALHKAACQRNRAVCQLLVDA 686
Cdd:PHA02875  116 DIMKLLIARGADPD--IPNTDKFSPLHLAVMMGDIKGIELLIDHKAC--LDIEDC-CGCTPLIIAMAKGDIAICKMLLDS 190

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1012282641 687 GASLRKTDSKGK-TPQERAQQAGDPDLAAYLESR 719
Cdd:PHA02875  191 GANIDYFGKNGCvAALCYAIENNKIDIVRLFIKR 224
Ank_5 pfam13857
Ankyrin repeats (many copies);
632-671 3.06e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.56  E-value: 3.06e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1012282641 632 LHYAAKTGNGEIVKYILDHGpsELLDMADSEtGETALHKA 671
Cdd:pfam13857  20 LHVAAKYGALEIVRVLLAYG--VDLNLKDEE-GLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
647-704 3.62e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 3.62e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1012282641 647 ILDHGPSELLDmaDSETGETALHKAACQRNRAVCQLLVDAGASLRKTDSKGKTPQERA 704
Cdd:pfam13857   1 LLEHGPIDLNR--LDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 664-694 3.76e-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: 35.34  E-value: 3.76e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1012282641 664 GETALHKAACQRNRA-VCQLLVDAGASLRKTD 694
Cdd:pfam00023   2 GNTPLHLAAGRRGNLeIVKLLLSKGADVNARD 33
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 627-653 5.49e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.93  E-value: 5.49e-03
                          10        20
                  ....*....|....*....|....*..
gi 1012282641 627 DHCSLLHYAAKTGNGEIVKYILDHGPS 653
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGAD 27
 
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.
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