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Conserved domains on  [gi|1907172876|ref|XP_036022114|]
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diacylglycerol kinase iota isoform X14 [Mus musculus]

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 ...
 196-353 5.01e-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: 242.24  E-value: 5.01e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172876  196 VFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGAAFSDFLQRSSRDLSKHVKVVCDGTDLTPKIqdlKFQCI 275
Cdd:smart00045   1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLPN---SLEGI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172876  276 VFLNIPRYCAGTMPWGNPGDH-HDFEPQRHDDGYIEVIGFTMASLAA--LQVGGHGERLHQCREV--MLLTYKSIPMQVD 350
Cdd:smart00045  78 AVLNIPSYGGGTNLWGTTDKEdLNFSKQSHDDGLLEVVGLTGAMHMAqiRQVGLAGRRIAQCSEVriTIKTSKTIPMQVD 157


                   ...
gi 1907172876  351 GEP 353
Cdd:smart00045 158 GEP 160
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 48-169 2.01e-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: 164.01  E-value: 2.01e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172876   48 LVFVNPKSGGNQGTKVLQMFMWYLNPRQVFDLSQEGPKDALEMYRKVPN-LRILACGGDGTVGWILSILDELQL-SPQPP 125
Cdd:smart00046   1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVPDfNRVLVCGGDGTVGWVLNALDKRELpLPEPP 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1907172876  126 VGVLPLGTGNDLARTLNWGGGYTDEPVSKILCQVEDGTIVQLDR 169
Cdd:smart00046  81 VAVLPLGTGNDLARSLGWGGGYDGEKLLKTLRDALESDTVKLDR 124
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
628-745 1.12e-16

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 81.15  E-value: 1.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172876 628 KNGGSLLIQGPGHCSLLHYAAKTGNGDIVKYILDHGPAelLDMADSEtGETALHKAACQRNRAVCQLLVDAGASLRQTDS 707
Cdd:COG0666   141 EAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGAD--VNARDND-GETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1907172876 708 KGKTPQERAQQAGDPDLAAYLESRQNYKIIGHEDLETA 745
Cdd:COG0666   218 DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTA 255
 
Name Accession Description Interval E-value
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 196-353 5.01e-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: 242.24  E-value: 5.01e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172876  196 VFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGAAFSDFLQRSSRDLSKHVKVVCDGTDLTPKIqdlKFQCI 275
Cdd:smart00045   1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLPN---SLEGI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172876  276 VFLNIPRYCAGTMPWGNPGDH-HDFEPQRHDDGYIEVIGFTMASLAA--LQVGGHGERLHQCREV--MLLTYKSIPMQVD 350
Cdd:smart00045  78 AVLNIPSYGGGTNLWGTTDKEdLNFSKQSHDDGLLEVVGLTGAMHMAqiRQVGLAGRRIAQCSEVriTIKTSKTIPMQVD 157


                   ...
gi 1907172876  351 GEP 353
Cdd:smart00045 158 GEP 160
DAGK_acc pfam00609
Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts ...
 196-353 3.75e-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: 3.75e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172876 196 VFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGAAFSDFLQRSSRDLSKHVKVVCDGTDLTPKiqdLKFQCI 275
Cdd:pfam00609   1 VMNNYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDMFQRSCKNLIEKVELEVDGKDLPLP---KSLEGI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172876 276 VFLNIPRYCAGTMPWGNPGDHHD-FEPQRHDDGYIEVIGFT-MASLAALQVGGHGE-RLHQCREVMLLTYKSIPMQVDGE 352
Cdd:pfam00609  78 VVLNIPSYAGGTDLWGNSKEDGLgFAPQSVDDGLLEVVGLTgALHLGQVQVGLGSAkRIAQGGPIRITTKKKIPMQVDGE 157


                  .
gi 1907172876 353 P 353
Cdd:pfam00609 158 P 158
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 48-169 2.01e-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: 164.01  E-value: 2.01e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172876   48 LVFVNPKSGGNQGTKVLQMFMWYLNPRQVFDLSQEGPKDALEMYRKVPN-LRILACGGDGTVGWILSILDELQL-SPQPP 125
Cdd:smart00046   1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVPDfNRVLVCGGDGTVGWVLNALDKRELpLPEPP 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1907172876  126 VGVLPLGTGNDLARTLNWGGGYTDEPVSKILCQVEDGTIVQLDR 169
Cdd:smart00046  81 VAVLPLGTGNDLARSLGWGGGYDGEKLLKTLRDALESDTVKLDR 124
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 46-145 2.64e-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: 126.93  E-value: 2.64e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172876  46 PLLVFVNPKSGGNQGTKVLQMFMWYLNPRQV-FDLSQ-EGPKDALEMYRKVPNL---RILACGGDGTVGWILSILDELql 120
Cdd:pfam00781   1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVeVELVLtEGPGDALELAREAAEDgydRIVVAGGDGTVNEVLNGLAGL-- 78

                          90       100
                  ....*....|....*....|....*
gi 1907172876 121 SPQPPVGVLPLGTGNDLARTLNWGG 145
Cdd:pfam00781  79 ATRPPLGIIPLGTGNDFARALGIPG 103
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 44-363 1.35e-26

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


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 110.33  E-value: 1.35e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172876  44 MKPLLVFVNPKSGGNQGTKVLQMFMWYLNpRQVFDLSQ---EGPKDALEMYRKVPNL---RILACGGDGTVGWILSILde 117
Cdd:COG1597     2 MMRALLIVNPASGRGRAARLLERLVAALR-AAGLEVEVletESPGDATELAREAAAEgadLVVAAGGDGTVNEVANGL-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172876 118 lqLSPQPPVGVLPLGTGNDLARTLNwgggyTDEPVSKILCQVEDGTIVQLDrwnlhvernpdlppeeledgVCKLPLNVF 197
Cdd:COG1597    79 --AGTGPPLGILPLGTGNDFARALG-----IPLDPEAALEALLTGRTRRID--------------------LGRVNGRYF 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172876 198 NNYFSLGFDAHVTLEFHESReanpekfnSRFRNKMFYAGAAFSDFLQRSSRdlskHVKVVCDGTDLTpkiqdLKFQCIVF 277
Cdd:COG1597   132 LNVAGIGFDAEVVERANRAL--------KRRLGKLAYVLAALRALLRYRPF----RLRIELDGEEIE-----GEALLVAV 194

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172876 278 LNIPRYcaGTMPWGNPGDhhdfepqRHDDGYIEVIGFT-------MASLAALQVGGHGE----RLHQCREVMLLTYKSIP 346
Cdd:COG1597   195 GNGPYY--GGGLRLAPDA-------SLDDGLLDVVVVRplsrlrlLRLLPRLLRGRHLRhpgvRYFRAREVEIESDRPLP 265

                         330
                  ....*....|....*...
gi 1907172876 347 MQVDGEPCRLA-PAMIRI 363
Cdd:COG1597   266 VQLDGEPLGLAtPLEFEV 283
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
628-745 1.12e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 81.15  E-value: 1.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172876 628 KNGGSLLIQGPGHCSLLHYAAKTGNGDIVKYILDHGPAelLDMADSEtGETALHKAACQRNRAVCQLLVDAGASLRQTDS 707
Cdd:COG0666   141 EAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGAD--VNARDND-GETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1907172876 708 KGKTPQERAQQAGDPDLAAYLESRQNYKIIGHEDLETA 745
Cdd:COG0666   218 DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTA 255
Ank_2 pfam12796
Ankyrin repeats (3 copies);
611-706 9.67e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 64.37  E-value: 9.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172876 611 ILQAVLTGDLMKLMESYKNGGSLLIQGPGHCSLLHYAAKTGNGDIVKYILDHGPAELLDMadsetGETALHKAACQRNRA 690
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN-----GRTALHYAARSGHLE 75

                          90
                  ....*....|....*.
gi 1907172876 691 VCQLLVDAGASLRQTD 706
Cdd:pfam12796  76 IVKLLLEKGADINVKD 91
PRK13057 PRK13057
lipid kinase;
48-142 3.11e-08

lipid kinase;


Pssm-ID: 183857 [Multi-domain]  Cd Length: 287  Bit Score: 55.69  E-value: 3.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172876  48 LVFVNPKSggNQGTKVLQMFMWYLNPRQvFDLSQEGPKDA------LEMYRKVPNLRILAcGGDGTVGWILSILDELQLs 121
Cdd:PRK13057    1 LLLVNRHA--RSGRAALAAARAALEAAG-LELVEPPAEDPddlsevIEAYADGVDLVIVG-GGDGTLNAAAPALVETGL- 75

                          90       100
                  ....*....|....*....|.
gi 1907172876 122 pqpPVGVLPLGTGNDLARTLN 142
Cdd:PRK13057   76 ---PLGILPLGTANDLARTLG 93
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 619-718 8.91e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 45.72  E-value: 8.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172876 619 DLMKLMesYKNGGSLLIQGPGHCSLLHYAAKTGNGDIVKYILDHGPAellDMADSETGETALHKAACQrNRAVCQLLVDa 698
Cdd:PHA02874  171 DIIKLL--LEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNH---IMNKCKNGFTPLHNAIIH-NRSAIELLIN- 243

                          90       100
                  ....*....|....*....|
gi 1907172876 699 GASLRQTDSKGKTPQERAQQ 718
Cdd:PHA02874  244 NASINDQDIDGSTPLHHAIN 263
TIGR00147 TIGR00147
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ...
 98-141 7.95e-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: 7.95e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1907172876  98 RILACGGDGTVGWILSILdeLQLSPQPPVGVLPLGTGNDLARTL 141
Cdd:TIGR00147  60 TVIAGGGDGTINEVVNAL--IQLDDIPALGILPLGTANDFARSL 101
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 641-664 2.77e-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: 35.64  E-value: 2.77e-03
                           10        20
                   ....*....|....*....|....
gi 1907172876  641 CSLLHYAAKTGNGDIVKYILDHGP 664
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGA 26
 
Name Accession Description Interval E-value
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 196-353 5.01e-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: 242.24  E-value: 5.01e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172876  196 VFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGAAFSDFLQRSSRDLSKHVKVVCDGTDLTPKIqdlKFQCI 275
Cdd:smart00045   1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLPN---SLEGI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172876  276 VFLNIPRYCAGTMPWGNPGDH-HDFEPQRHDDGYIEVIGFTMASLAA--LQVGGHGERLHQCREV--MLLTYKSIPMQVD 350
Cdd:smart00045  78 AVLNIPSYGGGTNLWGTTDKEdLNFSKQSHDDGLLEVVGLTGAMHMAqiRQVGLAGRRIAQCSEVriTIKTSKTIPMQVD 157


                   ...
gi 1907172876  351 GEP 353
Cdd:smart00045 158 GEP 160
DAGK_acc pfam00609
Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts ...
 196-353 3.75e-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: 3.75e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172876 196 VFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGAAFSDFLQRSSRDLSKHVKVVCDGTDLTPKiqdLKFQCI 275
Cdd:pfam00609   1 VMNNYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDMFQRSCKNLIEKVELEVDGKDLPLP---KSLEGI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172876 276 VFLNIPRYCAGTMPWGNPGDHHD-FEPQRHDDGYIEVIGFT-MASLAALQVGGHGE-RLHQCREVMLLTYKSIPMQVDGE 352
Cdd:pfam00609  78 VVLNIPSYAGGTDLWGNSKEDGLgFAPQSVDDGLLEVVGLTgALHLGQVQVGLGSAkRIAQGGPIRITTKKKIPMQVDGE 157


                  .
gi 1907172876 353 P 353
Cdd:pfam00609 158 P 158
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 48-169 2.01e-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: 164.01  E-value: 2.01e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172876   48 LVFVNPKSGGNQGTKVLQMFMWYLNPRQVFDLSQEGPKDALEMYRKVPN-LRILACGGDGTVGWILSILDELQL-SPQPP 125
Cdd:smart00046   1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVPDfNRVLVCGGDGTVGWVLNALDKRELpLPEPP 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1907172876  126 VGVLPLGTGNDLARTLNWGGGYTDEPVSKILCQVEDGTIVQLDR 169
Cdd:smart00046  81 VAVLPLGTGNDLARSLGWGGGYDGEKLLKTLRDALESDTVKLDR 124
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 46-145 2.64e-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: 126.93  E-value: 2.64e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172876  46 PLLVFVNPKSGGNQGTKVLQMFMWYLNPRQV-FDLSQ-EGPKDALEMYRKVPNL---RILACGGDGTVGWILSILDELql 120
Cdd:pfam00781   1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVeVELVLtEGPGDALELAREAAEDgydRIVVAGGDGTVNEVLNGLAGL-- 78

                          90       100
                  ....*....|....*....|....*
gi 1907172876 121 SPQPPVGVLPLGTGNDLARTLNWGG 145
Cdd:pfam00781  79 ATRPPLGIIPLGTGNDFARALGIPG 103
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 44-363 1.35e-26

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


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 110.33  E-value: 1.35e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172876  44 MKPLLVFVNPKSGGNQGTKVLQMFMWYLNpRQVFDLSQ---EGPKDALEMYRKVPNL---RILACGGDGTVGWILSILde 117
Cdd:COG1597     2 MMRALLIVNPASGRGRAARLLERLVAALR-AAGLEVEVletESPGDATELAREAAAEgadLVVAAGGDGTVNEVANGL-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172876 118 lqLSPQPPVGVLPLGTGNDLARTLNwgggyTDEPVSKILCQVEDGTIVQLDrwnlhvernpdlppeeledgVCKLPLNVF 197
Cdd:COG1597    79 --AGTGPPLGILPLGTGNDFARALG-----IPLDPEAALEALLTGRTRRID--------------------LGRVNGRYF 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172876 198 NNYFSLGFDAHVTLEFHESReanpekfnSRFRNKMFYAGAAFSDFLQRSSRdlskHVKVVCDGTDLTpkiqdLKFQCIVF 277
Cdd:COG1597   132 LNVAGIGFDAEVVERANRAL--------KRRLGKLAYVLAALRALLRYRPF----RLRIELDGEEIE-----GEALLVAV 194

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172876 278 LNIPRYcaGTMPWGNPGDhhdfepqRHDDGYIEVIGFT-------MASLAALQVGGHGE----RLHQCREVMLLTYKSIP 346
Cdd:COG1597   195 GNGPYY--GGGLRLAPDA-------SLDDGLLDVVVVRplsrlrlLRLLPRLLRGRHLRhpgvRYFRAREVEIESDRPLP 265

                         330
                  ....*....|....*...
gi 1907172876 347 MQVDGEPCRLA-PAMIRI 363
Cdd:COG1597   266 VQLDGEPLGLAtPLEFEV 283
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
628-745 1.12e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 81.15  E-value: 1.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172876 628 KNGGSLLIQGPGHCSLLHYAAKTGNGDIVKYILDHGPAelLDMADSEtGETALHKAACQRNRAVCQLLVDAGASLRQTDS 707
Cdd:COG0666   141 EAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGAD--VNARDND-GETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1907172876 708 KGKTPQERAQQAGDPDLAAYLESRQNYKIIGHEDLETA 745
Cdd:COG0666   218 DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTA 255
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
608-728 6.38e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 69.98  E-value: 6.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172876 608 DHAILQAVLTGDLMKLMESYKNGGSLLIQGPGHCSLLHYAAKTGNGDIVKYILDHGpAELLdmADSETGETALHKAACQR 687
Cdd:COG0666    55 ALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAG-ADVN--ARDKDGETPLHLAAYNG 131

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1907172876 688 NRAVCQLLVDAGASLRQTDSKGKTPQERAQQAGDPDLAAYL 728
Cdd:COG0666   132 NLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
611-706 9.67e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 64.37  E-value: 9.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172876 611 ILQAVLTGDLMKLMESYKNGGSLLIQGPGHCSLLHYAAKTGNGDIVKYILDHGPAELLDMadsetGETALHKAACQRNRA 690
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN-----GRTALHYAARSGHLE 75

                          90
                  ....*....|....*.
gi 1907172876 691 VCQLLVDAGASLRQTD 706
Cdd:pfam12796  76 IVKLLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
610-745 7.43e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 57.66  E-value: 7.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172876 610 AILQAVLTG--DLMKLMEsyKNGGSLLIQGPGHCSLLHYAAKTGNGDIVKYILDHGPAelLDMADSEtGETALHKAACQR 687
Cdd:COG0666   156 PLHLAAANGnlEIVKLLL--EAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGAD--VNAKDND-GKTALDLAAENG 230

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907172876 688 NRAVCQLLVDAGASLRQTDSKGKTPQERAQQAGDPDLAAYLESRQNYKIIGHEDLETA 745
Cdd:COG0666   231 NLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
608-728 1.45e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 56.89  E-value: 1.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172876 608 DHAILQAVLTGDLMKLMESYKNGGSLLIQGPGHCSLLHYAAKTGNGDIVKYILDHGpaeLLDMADSETGETALHKAACQR 687
Cdd:COG0666    22 ALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAG---ADINAKDDGGNTLLHAAARNG 98

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1907172876 688 NRAVCQLLVDAGASLRQTDSKGKTPQERAQQAGDPDLAAYL 728
Cdd:COG0666    99 DLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLL 139
PRK13057 PRK13057
lipid kinase;
48-142 3.11e-08

lipid kinase;


Pssm-ID: 183857 [Multi-domain]  Cd Length: 287  Bit Score: 55.69  E-value: 3.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172876  48 LVFVNPKSggNQGTKVLQMFMWYLNPRQvFDLSQEGPKDA------LEMYRKVPNLRILAcGGDGTVGWILSILDELQLs 121
Cdd:PRK13057    1 LLLVNRHA--RSGRAALAAARAALEAAG-LELVEPPAEDPddlsevIEAYADGVDLVIVG-GGDGTLNAAAPALVETGL- 75

                          90       100
                  ....*....|....*....|.
gi 1907172876 122 pqpPVGVLPLGTGNDLARTLN 142
Cdd:PRK13057   76 ---PLGILPLGTANDLARTLG 93
PRK12361 PRK12361
hypothetical protein; Provisional
 45-162 1.72e-07

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 54.63  E-value: 1.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172876  45 KPLLVFVNPKSGGNQGTKVLQMFMWYLNPRqvFDLS-QEGPKD------ALEMYRKVPNLrILACGGDGTVGWILSIL-- 115
Cdd:PRK12361  243 KRAWLIANPVSGGGKWQEYGEQIQRELKAY--FDLTvKLTTPEisaealAKQARKAGADI-VIACGGDGTVTEVASELvn 319

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1907172876 116 DELQLspqppvGVLPLGTGNDLARTLnWGGGYTDEPVSKILCQVEDG 162
Cdd:PRK12361  320 TDITL------GIIPLGTANALSHAL-FGLGSKLIPVEQACDNIIQG 359
PRK13054 PRK13054
lipid kinase; Reviewed
 98-139 8.94e-06

lipid kinase; Reviewed


Pssm-ID: 237281 [Multi-domain]  Cd Length: 300  Bit Score: 48.33  E-value: 8.94e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1907172876  98 RILACGGDGTVGWILSILDELQLSPQPPVGVLPLGTGNDLAR 139
Cdd:PRK13054   59 TVIAGGGDGTINEVATALAQLEGDARPALGILPLGTANDFAT 100
Ank_4 pfam13637
Ankyrin repeats (many copies);
642-696 9.19e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.42  E-value: 9.19e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907172876 642 SLLHYAAKTGNGDIVKYILDHGPAelLDMADSEtGETALHKAACQRNRAVCQLLV 696
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGAD--INAVDGN-GETALHFAASNGNVEVLKLLL 54
PRK13059 PRK13059
putative lipid kinase; Reviewed
 44-142 1.31e-05

putative lipid kinase; Reviewed


Pssm-ID: 183858  Cd Length: 295  Bit Score: 47.72  E-value: 1.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172876  44 MKPLLVFVNPKSGGN----QGTKVLQMFMWYLNPRQVFDLSQEGP-KDALEMYRKVPNLrILACGGDGTVGWILSILDEL 118
Cdd:PRK13059    1 MKKVKFIYNPYSGENaiisELDKVIRIHQEKGYLVVPYRISLEYDlKNAFKDIDESYKY-ILIAGGDGTVDNVVNAMKKL 79

                          90       100
                  ....*....|....*....|....
gi 1907172876 119 QLSPqpPVGVLPLGTGNDLARTLN 142
Cdd:PRK13059   80 NIDL--PIGILPVGTANDFAKFLG 101
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 619-718 8.91e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 45.72  E-value: 8.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172876 619 DLMKLMesYKNGGSLLIQGPGHCSLLHYAAKTGNGDIVKYILDHGPAellDMADSETGETALHKAACQrNRAVCQLLVDa 698
Cdd:PHA02874  171 DIIKLL--LEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNH---IMNKCKNGFTPLHNAIIH-NRSAIELLIN- 243

                          90       100
                  ....*....|....*....|
gi 1907172876 699 GASLRQTDSKGKTPQERAQQ 718
Cdd:PHA02874  244 NASINDQDIDGSTPLHHAIN 263
Ank_5 pfam13857
Ankyrin repeats (many copies);
659-716 3.39e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 3.39e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907172876 659 ILDHGPAELLDmaDSETGETALHKAACQRNRAVCQLLVDAGASLRQTDSKGKTPQERA 716
Cdd:pfam13857   1 LLEHGPIDLNR--LDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PRK13055 PRK13055
putative lipid kinase; Reviewed
 99-142 7.55e-04

putative lipid kinase; Reviewed


Pssm-ID: 237282 [Multi-domain]  Cd Length: 334  Bit Score: 42.28  E-value: 7.55e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1907172876  99 ILACGGDGTVGWILSILdeLQLSPQPPVGVLPLGTGNDLARTLN 142
Cdd:PRK13055   63 IIAAGGDGTINEVVNGI--APLEKRPKMAIIPAGTTNDYARALK 104
TIGR00147 TIGR00147
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ...
 98-141 7.95e-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: 7.95e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1907172876  98 RILACGGDGTVGWILSILdeLQLSPQPPVGVLPLGTGNDLARTL 141
Cdd:TIGR00147  60 TVIAGGGDGTINEVVNAL--IQLDDIPALGILPLGTANDFARSL 101
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 676-706 2.48e-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: 36.11  E-value: 2.48e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1907172876 676 GETALHKAACQRNRA-VCQLLVDAGASLRQTD 706
Cdd:pfam00023   2 GNTPLHLAAGRRGNLeIVKLLLSKGADVNARD 33
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 641-664 2.77e-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: 35.64  E-value: 2.77e-03
                           10        20
                   ....*....|....*....|....
gi 1907172876  641 CSLLHYAAKTGNGDIVKYILDHGP 664
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGA 26
Ank_5 pfam13857
Ankyrin repeats (many copies);
644-683 3.17e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.56  E-value: 3.17e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1907172876 644 LHYAAKTGNGDIVKYILDHGpaELLDMADSEtGETALHKA 683
Cdd:pfam13857  20 LHVAAKYGALEIVRVLLAYG--VDLNLKDEE-GLTALDLA 56
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 642-712 8.47e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 39.48  E-value: 8.47e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907172876 642 SLLHYAAKTGNGDIVKYILDHGP-AELLDMADSetgeTALHKAACQRNRAVCQLLVDAGASLRQTDSKGKTP 712
Cdd:PHA02878  170 TALHYATENKDQRLTELLLSYGAnVNIPDKTNN----SPLHHAVKHYNKPIVHILLENGASTDARDKCGNTP 237
Ank_2 pfam12796
Ankyrin repeats (3 copies);
680-728 9.19e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 36.25  E-value: 9.19e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1907172876 680 LHKAACQRNRAVCQLLVDAGASLRQTDSKGKTPQERAQQAGDPDLAAYL 728
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL 49
 
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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