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Conserved domains on  [gi|1958771504|ref|XP_038964298|]
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diacylglycerol kinase iota isoform X7 [Rattus norvegicus]

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 ...
 458-615 2.22e-74

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: 2.22e-74
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771504   458 VFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGAAFSDFLQRSSRDLSKHVKVVCDGTDLTPKIqdlKFQCI 537
Cdd:smart00045    1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLPN---SLEGI 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771504   538 VFLNIPRYCAGTMPWGNPGDH-HDFEPQRHDDGYIEVIGFTMASLAA--LQVGGHGERLHQCREV--MLLTYKSIPMQVD 612
Cdd:smart00045   78 AVLNIPSYGGGTNLWGTTDKEdLNFSKQSHDDGLLEVVGLTGAMHMAqiRQVGLAGRRIAQCSEVriTIKTSKTIPMQVD 157


                    ...
gi 1958771504   613 GEP 615
Cdd:smart00045  158 GEP 160
C1_DGKiota_rpt1 cd20850
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase iota (DAG ...
 163-235 1.93e-51

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: 174.44  E-value: 1.93e-51
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958771504  163 DWSENAVNGEHLWLETNVSGDLCYLGEENCQVRFAKSALRRKCAVCKIVVHTACIEQLEKINFRCKPTFREGG 235
Cdd:cd20850      1 DWSENAVNGEHLWLETNVSGDLCYLGEENCQVKFAKSALRRKCAACKIVVHTACIEQLEKINFRCKPTFREGG 73
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 310-431 1.19e-46

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: 162.85  E-value: 1.19e-46
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771504   310 LVFVNPKSGGNQGTKVLQMFMWYLNPRQVFDLSQEGPKDALELYRKVPN-LRILACGGDGTVGWILSILDELQL-SPQPP 387
Cdd:smart00046    1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVPDfNRVLVCGGDGTVGWVLNALDKRELpLPEPP 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 1958771504   388 VGVLPLGTGNDLARTLNWGGGYTDEPVSKILCQVEDGTIVQLDR 431
Cdd:smart00046   81 VAVLPLGTGNDLARSLGWGGGYDGEKLLKTLRDALESDTVKLDR 124
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
890-1007 1.30e-16

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 81.54  E-value: 1.30e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771504  890 KNGGSLLIQGPGHCSLLHYAAKTGNGEIVKYILDHGPAelLDMADSEtGETALHKAACQRNRAVCQLLVDAGASLRQTDS 969
Cdd:COG0666    141 EAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGAD--VNARDND-GETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1958771504  970 KGKTPQERAQQAGDPDLAAYLESRQNYKIIGHEDLETA 1007
Cdd:COG0666    218 DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTA 255
C1 super family cl00040
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ...
 246-264 1.07e-09

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 cd20855:

Pssm-ID: 412127  Cd Length: 62  Bit Score: 55.04  E-value: 1.07e-09
                           10
                   ....*....|....*....
gi 1958771504  246 HHWVHRRRQEGKCKQCGKN 264
Cdd:cd20855      1 HHWVHRRKQEGKCKQCGKS 19
 
Name Accession Description Interval E-value
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 458-615 2.22e-74

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: 2.22e-74
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771504   458 VFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGAAFSDFLQRSSRDLSKHVKVVCDGTDLTPKIqdlKFQCI 537
Cdd:smart00045    1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLPN---SLEGI 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771504   538 VFLNIPRYCAGTMPWGNPGDH-HDFEPQRHDDGYIEVIGFTMASLAA--LQVGGHGERLHQCREV--MLLTYKSIPMQVD 612
Cdd:smart00045   78 AVLNIPSYGGGTNLWGTTDKEdLNFSKQSHDDGLLEVVGLTGAMHMAqiRQVGLAGRRIAQCSEVriTIKTSKTIPMQVD 157


                    ...
gi 1958771504   613 GEP 615
Cdd:smart00045  158 GEP 160
DAGK_acc pfam00609
Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts ...
 458-615 7.11e-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: 224.02  E-value: 7.11e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771504  458 VFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGAAFSDFLQRSSRDLSKHVKVVCDGTDLTPKiqdLKFQCI 537
Cdd:pfam00609    1 VMNNYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDMFQRSCKNLIEKVELEVDGKDLPLP---KSLEGI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771504  538 VFLNIPRYCAGTMPWGNPGDHHD-FEPQRHDDGYIEVIGFT-MASLAALQVGGHGE-RLHQCREVMLLTYKSIPMQVDGE 614
Cdd:pfam00609   78 VVLNIPSYAGGTDLWGNSKEDGLgFAPQSVDDGLLEVVGLTgALHLGQVQVGLGSAkRIAQGGPIRITTKKKIPMQVDGE 157


                   .
gi 1958771504  615 P 615
Cdd:pfam00609  158 P 158
C1_DGKiota_rpt1 cd20850
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase iota (DAG ...
 163-235 1.93e-51

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: 174.44  E-value: 1.93e-51
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958771504  163 DWSENAVNGEHLWLETNVSGDLCYLGEENCQVRFAKSALRRKCAVCKIVVHTACIEQLEKINFRCKPTFREGG 235
Cdd:cd20850      1 DWSENAVNGEHLWLETNVSGDLCYLGEENCQVKFAKSALRRKCAACKIVVHTACIEQLEKINFRCKPTFREGG 73
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 310-431 1.19e-46

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: 162.85  E-value: 1.19e-46
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771504   310 LVFVNPKSGGNQGTKVLQMFMWYLNPRQVFDLSQEGPKDALELYRKVPN-LRILACGGDGTVGWILSILDELQL-SPQPP 387
Cdd:smart00046    1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVPDfNRVLVCGGDGTVGWVLNALDKRELpLPEPP 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 1958771504   388 VGVLPLGTGNDLARTLNWGGGYTDEPVSKILCQVEDGTIVQLDR 431
Cdd:smart00046   81 VAVLPLGTGNDLARSLGWGGGYDGEKLLKTLRDALESDTVKLDR 124
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 308-407 2.69e-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: 2.69e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771504  308 PLLVFVNPKSGGNQGTKVLQMFMWYLNPRQV-FDLSQ-EGPKDALELYRKVPNL---RILACGGDGTVGWILSILDELql 382
Cdd:pfam00781    1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVeVELVLtEGPGDALELAREAAEDgydRIVVAGGDGTVNEVLNGLAGL-- 78

                           90       100
                   ....*....|....*....|....*
gi 1958771504  383 SPQPPVGVLPLGTGNDLARTLNWGG 407
Cdd:pfam00781   79 ATRPPLGIIPLGTGNDFARALGIPG 103
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 306-625 8.45e-27

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


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 111.48  E-value: 8.45e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771504  306 MKPLLVFVNPKSGGNQGTKVLQMFMWYLNpRQVFDLSQ---EGPKDALELYRKVPNL---RILACGGDGTVGWILSILde 379
Cdd:COG1597      2 MMRALLIVNPASGRGRAARLLERLVAALR-AAGLEVEVletESPGDATELAREAAAEgadLVVAAGGDGTVNEVANGL-- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771504  380 lqLSPQPPVGVLPLGTGNDLARTLNwgggyTDEPVSKILCQVEDGTIVQLDrwnlhvernpdlppeeledgVCKLPLNVF 459
Cdd:COG1597     79 --AGTGPPLGILPLGTGNDFARALG-----IPLDPEAALEALLTGRTRRID--------------------LGRVNGRYF 131

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771504  460 NNYFSLGFDAHVTLEFHESReanpekfnSRFRNKMFYAGAAFSDFLQRSSRdlskHVKVVCDGTDLTpkiqdLKFQCIVF 539
Cdd:COG1597    132 LNVAGIGFDAEVVERANRAL--------KRRLGKLAYVLAALRALLRYRPF----RLRIELDGEEIE-----GEALLVAV 194

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771504  540 LNIPRYcaGTMPWGNPGDhhdfepqRHDDGYIEVIGFT-------MASLAALQVGGHGE----RLHQCREVMLLTYKSIP 608
Cdd:COG1597    195 GNGPYY--GGGLRLAPDA-------SLDDGLLDVVVVRplsrlrlLRLLPRLLRGRHLRhpgvRYFRAREVEIESDRPLP 265

                          330
                   ....*....|....*...
gi 1958771504  609 MQVDGEPCRLA-PAMIRI 625
Cdd:COG1597    266 VQLDGEPLGLAtPLEFEV 283
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
890-1007 1.30e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 81.54  E-value: 1.30e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771504  890 KNGGSLLIQGPGHCSLLHYAAKTGNGEIVKYILDHGPAelLDMADSEtGETALHKAACQRNRAVCQLLVDAGASLRQTDS 969
Cdd:COG0666    141 EAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGAD--VNARDND-GETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1958771504  970 KGKTPQERAQQAGDPDLAAYLESRQNYKIIGHEDLETA 1007
Cdd:COG0666    218 DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTA 255
Ank_2 pfam12796
Ankyrin repeats (3 copies);
873-968 1.16e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 64.75  E-value: 1.16e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771504  873 ILQAVITGDLMKLMESYKNGGSLLIQGPGHCSLLHYAAKTGNGEIVKYILDHGPAELLDMadsetGETALHKAACQRNRA 952
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN-----GRTALHYAARSGHLE 75

                           90
                   ....*....|....*.
gi 1958771504  953 VCQLLVDAGASLRQTD 968
Cdd:pfam12796   76 IVKLLLEKGADINVKD 91
C1_DGK_typeIV_rpt2 cd20855
second protein kinase C conserved region 1 (C1 domain) found in type IV diacylglycerol kinases; ...
 246-264 1.07e-09

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: 55.04  E-value: 1.07e-09
                           10
                   ....*....|....*....
gi 1958771504  246 HHWVHRRRQEGKCKQCGKN 264
Cdd:cd20855      1 HHWVHRRKQEGKCKQCGKS 19
PRK13057 PRK13057
lipid kinase;
310-404 3.91e-08

lipid kinase;


Pssm-ID: 183857 [Multi-domain]  Cd Length: 287  Bit Score: 56.08  E-value: 3.91e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771504  310 LVFVNPKSggNQGTKVLQMFMWYLNPRQvFDLSQEGPKDALEL------YRKVPNLRILAcGGDGTVGWILSILDELQLs 383
Cdd:PRK13057     1 LLLVNRHA--RSGRAALAAARAALEAAG-LELVEPPAEDPDDLsevieaYADGVDLVIVG-GGDGTLNAAAPALVETGL- 75

                           90       100
                   ....*....|....*....|.
gi 1958771504  384 pqpPVGVLPLGTGNDLARTLN 404
Cdd:PRK13057    76 ---PLGILPLGTANDLARTLG 93
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 881-980 8.83e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.11  E-value: 8.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771504  881 DLMKLMesYKNGGSLLIQGPGHCSLLHYAAKTGNGEIVKYILDHGPAellDMADSETGETALHKAACQrNRAVCQLLVDa 960
Cdd:PHA02874   171 DIIKLL--LEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNH---IMNKCKNGFTPLHNAIIH-NRSAIELLIN- 243

                           90       100
                   ....*....|....*....|
gi 1958771504  961 GASLRQTDSKGKTPQERAQQ 980
Cdd:PHA02874   244 NASINDQDIDGSTPLHHAIN 263
TIGR00147 TIGR00147
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ...
 360-403 1.14e-03

lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been purified and shown to have phosphatidylglycerol kinase activity. The member from M. tuberculosis, Rv2252, has diacylglycerol kinase activity. BmrU from B. subtilis is in an operon with multidrug efflux transporter Bmr, but is uncharacterized. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 161732 [Multi-domain]  Cd Length: 293  Bit Score: 42.11  E-value: 1.14e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1958771504  360 RILACGGDGTVGWILSILdeLQLSPQPPVGVLPLGTGNDLARTL 403
Cdd:TIGR00147   60 TVIAGGGDGTINEVVNAL--IQLDDIPALGILPLGTANDFARSL 101
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 903-926 3.88e-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: 3.88e-03
                            10        20
                    ....*....|....*....|....
gi 1958771504   903 CSLLHYAAKTGNGEIVKYILDHGP 926
Cdd:smart00248    3 RTPLHLAAENGNLEVVKLLLDKGA 26
 
Name Accession Description Interval E-value
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 458-615 2.22e-74

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: 2.22e-74
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771504   458 VFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGAAFSDFLQRSSRDLSKHVKVVCDGTDLTPKIqdlKFQCI 537
Cdd:smart00045    1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLPN---SLEGI 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771504   538 VFLNIPRYCAGTMPWGNPGDH-HDFEPQRHDDGYIEVIGFTMASLAA--LQVGGHGERLHQCREV--MLLTYKSIPMQVD 612
Cdd:smart00045   78 AVLNIPSYGGGTNLWGTTDKEdLNFSKQSHDDGLLEVVGLTGAMHMAqiRQVGLAGRRIAQCSEVriTIKTSKTIPMQVD 157


                    ...
gi 1958771504   613 GEP 615
Cdd:smart00045  158 GEP 160
DAGK_acc pfam00609
Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts ...
 458-615 7.11e-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: 224.02  E-value: 7.11e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771504  458 VFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGAAFSDFLQRSSRDLSKHVKVVCDGTDLTPKiqdLKFQCI 537
Cdd:pfam00609    1 VMNNYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDMFQRSCKNLIEKVELEVDGKDLPLP---KSLEGI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771504  538 VFLNIPRYCAGTMPWGNPGDHHD-FEPQRHDDGYIEVIGFT-MASLAALQVGGHGE-RLHQCREVMLLTYKSIPMQVDGE 614
Cdd:pfam00609   78 VVLNIPSYAGGTDLWGNSKEDGLgFAPQSVDDGLLEVVGLTgALHLGQVQVGLGSAkRIAQGGPIRITTKKKIPMQVDGE 157


                   .
gi 1958771504  615 P 615
Cdd:pfam00609  158 P 158
C1_DGKiota_rpt1 cd20850
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase iota (DAG ...
 163-235 1.93e-51

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: 174.44  E-value: 1.93e-51
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958771504  163 DWSENAVNGEHLWLETNVSGDLCYLGEENCQVRFAKSALRRKCAVCKIVVHTACIEQLEKINFRCKPTFREGG 235
Cdd:cd20850      1 DWSENAVNGEHLWLETNVSGDLCYLGEENCQVKFAKSALRRKCAACKIVVHTACIEQLEKINFRCKPTFREGG 73
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 310-431 1.19e-46

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: 162.85  E-value: 1.19e-46
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771504   310 LVFVNPKSGGNQGTKVLQMFMWYLNPRQVFDLSQEGPKDALELYRKVPN-LRILACGGDGTVGWILSILDELQL-SPQPP 387
Cdd:smart00046    1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVPDfNRVLVCGGDGTVGWVLNALDKRELpLPEPP 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 1958771504   388 VGVLPLGTGNDLARTLNWGGGYTDEPVSKILCQVEDGTIVQLDR 431
Cdd:smart00046   81 VAVLPLGTGNDLARSLGWGGGYDGEKLLKTLRDALESDTVKLDR 124
C1_DGKzeta_rpt1 cd20849
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta (DAG ...
 163-235 2.96e-39

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: 139.69  E-value: 2.96e-39
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958771504  163 DWSENAVNGEHLWLETNVSGDLCYLGEENCQVR-FAKSALRRKCAVCKIVVHTACIEQLEKINFRCKPTFREGG 235
Cdd:cd20849      1 DWSESAVYGEHIWFETNVSGDFCYVGEQNCVAKqLQKSVSRKKCAACKIVVHTPCIEQLEKINFRCKPSFRESG 74
C1_DGK_typeIV_rpt1 cd20802
first protein kinase C conserved region 1 (C1 domain) found in type IV diacylglycerol kinases; ...
 168-233 5.95e-36

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: 130.11  E-value: 5.95e-36
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958771504  168 AVNGEHLWLETNVSGDLCYLGEENCQvrfaKSALRRKCAVCKIVVHTACIEQLEKINFRCKPTFRE 233
Cdd:cd20802      1 AVNGEHLWTDTSASGDLCYVGEQDCL----KSGSRKKCSACKIVVHTGCIPQLEKINFKCKPTFRE 62
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 308-407 2.69e-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: 2.69e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771504  308 PLLVFVNPKSGGNQGTKVLQMFMWYLNPRQV-FDLSQ-EGPKDALELYRKVPNL---RILACGGDGTVGWILSILDELql 382
Cdd:pfam00781    1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVeVELVLtEGPGDALELAREAAEDgydRIVVAGGDGTVNEVLNGLAGL-- 78

                           90       100
                   ....*....|....*....|....*
gi 1958771504  383 SPQPPVGVLPLGTGNDLARTLNWGG 407
Cdd:pfam00781   79 ATRPPLGIIPLGTGNDFARALGIPG 103
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 306-625 8.45e-27

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


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 111.48  E-value: 8.45e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771504  306 MKPLLVFVNPKSGGNQGTKVLQMFMWYLNpRQVFDLSQ---EGPKDALELYRKVPNL---RILACGGDGTVGWILSILde 379
Cdd:COG1597      2 MMRALLIVNPASGRGRAARLLERLVAALR-AAGLEVEVletESPGDATELAREAAAEgadLVVAAGGDGTVNEVANGL-- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771504  380 lqLSPQPPVGVLPLGTGNDLARTLNwgggyTDEPVSKILCQVEDGTIVQLDrwnlhvernpdlppeeledgVCKLPLNVF 459
Cdd:COG1597     79 --AGTGPPLGILPLGTGNDFARALG-----IPLDPEAALEALLTGRTRRID--------------------LGRVNGRYF 131

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771504  460 NNYFSLGFDAHVTLEFHESReanpekfnSRFRNKMFYAGAAFSDFLQRSSRdlskHVKVVCDGTDLTpkiqdLKFQCIVF 539
Cdd:COG1597    132 LNVAGIGFDAEVVERANRAL--------KRRLGKLAYVLAALRALLRYRPF----RLRIELDGEEIE-----GEALLVAV 194

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771504  540 LNIPRYcaGTMPWGNPGDhhdfepqRHDDGYIEVIGFT-------MASLAALQVGGHGE----RLHQCREVMLLTYKSIP 608
Cdd:COG1597    195 GNGPYY--GGGLRLAPDA-------SLDDGLLDVVVVRplsrlrlLRLLPRLLRGRHLRhpgvRYFRAREVEIESDRPLP 265

                          330
                   ....*....|....*...
gi 1958771504  609 MQVDGEPCRLA-PAMIRI 625
Cdd:COG1597    266 VQLDGEPLGLAtPLEFEV 283
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
890-1007 1.30e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 81.54  E-value: 1.30e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771504  890 KNGGSLLIQGPGHCSLLHYAAKTGNGEIVKYILDHGPAelLDMADSEtGETALHKAACQRNRAVCQLLVDAGASLRQTDS 969
Cdd:COG0666    141 EAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGAD--VNARDND-GETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1958771504  970 KGKTPQERAQQAGDPDLAAYLESRQNYKIIGHEDLETA 1007
Cdd:COG0666    218 DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTA 255
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
870-990 6.49e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 70.37  E-value: 6.49e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771504  870 DHAILQAVITGDLMKLMESYKNGGSLLIQGPGHCSLLHYAAKTGNGEIVKYILDHGpAELLdmADSETGETALHKAACQR 949
Cdd:COG0666     55 ALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAG-ADVN--ARDKDGETPLHLAAYNG 131

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1958771504  950 NRAVCQLLVDAGASLRQTDSKGKTPQERAQQAGDPDLAAYL 990
Cdd:COG0666    132 NLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
873-968 1.16e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 64.75  E-value: 1.16e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771504  873 ILQAVITGDLMKLMESYKNGGSLLIQGPGHCSLLHYAAKTGNGEIVKYILDHGPAELLDMadsetGETALHKAACQRNRA 952
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN-----GRTALHYAARSGHLE 75

                           90
                   ....*....|....*.
gi 1958771504  953 VCQLLVDAGASLRQTD 968
Cdd:pfam12796   76 IVKLLLEKGADINVKD 91
C1_DGK_typeIV_rpt2 cd20855
second protein kinase C conserved region 1 (C1 domain) found in type IV diacylglycerol kinases; ...
 246-264 1.07e-09

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: 55.04  E-value: 1.07e-09
                           10
                   ....*....|....*....
gi 1958771504  246 HHWVHRRRQEGKCKQCGKN 264
Cdd:cd20855      1 HHWVHRRKQEGKCKQCGKS 19
C1_DGKzeta_rpt2 cd20895
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta ...
 244-263 2.62e-09

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: 54.70  E-value: 2.62e-09
                           10        20
                   ....*....|....*....|
gi 1958771504  244 VRHHWVHRRRQEGKCKQCGK 263
Cdd:cd20895      1 VRHHWVHRRRQEGKCRQCGK 20
C1_DGKiota_rpt2 cd20896
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase iota ...
 244-263 2.74e-09

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: 54.71  E-value: 2.74e-09
                           10        20
                   ....*....|....*....|
gi 1958771504  244 VRHHWVHRRRQEGKCKQCGK 263
Cdd:cd20896      1 VRHHWVHRRRQEGKCKQCGK 20
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
872-1007 6.34e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 58.43  E-value: 6.34e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771504  872 AILQAVITG--DLMKLMEsyKNGGSLLIQGPGHCSLLHYAAKTGNGEIVKYILDHGPAelLDMADSEtGETALHKAACQR 949
Cdd:COG0666    156 PLHLAAANGnlEIVKLLL--EAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGAD--VNAKDND-GKTALDLAAENG 230

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958771504  950 NRAVCQLLVDAGASLRQTDSKGKTPQERAQQAGDPDLAAYLESRQNYKIIGHEDLETA 1007
Cdd:COG0666    231 NLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
870-990 2.13e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 56.89  E-value: 2.13e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771504  870 DHAILQAVITGDLMKLMESYKNGGSLLIQGPGHCSLLHYAAKTGNGEIVKYILDHGpaeLLDMADSETGETALHKAACQR 949
Cdd:COG0666     22 ALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAG---ADINAKDDGGNTLLHAAARNG 98

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1958771504  950 NRAVCQLLVDAGASLRQTDSKGKTPQERAQQAGDPDLAAYL 990
Cdd:COG0666     99 DLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLL 139
PRK13057 PRK13057
lipid kinase;
310-404 3.91e-08

lipid kinase;


Pssm-ID: 183857 [Multi-domain]  Cd Length: 287  Bit Score: 56.08  E-value: 3.91e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771504  310 LVFVNPKSggNQGTKVLQMFMWYLNPRQvFDLSQEGPKDALEL------YRKVPNLRILAcGGDGTVGWILSILDELQLs 383
Cdd:PRK13057     1 LLLVNRHA--RSGRAALAAARAALEAAG-LELVEPPAEDPDDLsevieaYADGVDLVIVG-GGDGTLNAAAPALVETGL- 75

                           90       100
                   ....*....|....*....|.
gi 1958771504  384 pqpPVGVLPLGTGNDLARTLN 404
Cdd:PRK13057    76 ---PLGILPLGTANDLARTLG 93
PRK12361 PRK12361
hypothetical protein; Provisional
 307-424 3.01e-07

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 54.24  E-value: 3.01e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771504  307 KPLLVFVNPKSGGNQGTKVLQMFMWYLNPRqvFDLS-QEGPKD------ALELYRKVPNLrILACGGDGTVGWILSIL-- 377
Cdd:PRK12361   243 KRAWLIANPVSGGGKWQEYGEQIQRELKAY--FDLTvKLTTPEisaealAKQARKAGADI-VIACGGDGTVTEVASELvn 319

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1958771504  378 DELQLspqppvGVLPLGTGNDLARTLnWGGGYTDEPVSKILCQVEDG 424
Cdd:PRK12361   320 TDITL------GIIPLGTANALSHAL-FGLGSKLIPVEQACDNIIQG 359
PRK13059 PRK13059
putative lipid kinase; Reviewed
 306-404 7.38e-06

putative lipid kinase; Reviewed


Pssm-ID: 183858  Cd Length: 295  Bit Score: 48.88  E-value: 7.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771504  306 MKPLLVFVNPKSGGN----QGTKVLQMFMWYLNPRQVFDLSQEGP-KDALELYRKVPNLrILACGGDGTVGWILSILDEL 380
Cdd:PRK13059     1 MKKVKFIYNPYSGENaiisELDKVIRIHQEKGYLVVPYRISLEYDlKNAFKDIDESYKY-ILIAGGDGTVDNVVNAMKKL 79

                           90       100
                   ....*....|....*....|....
gi 1958771504  381 QLSPqpPVGVLPLGTGNDLARTLN 404
Cdd:PRK13059    80 NIDL--PIGILPVGTANDFAKFLG 101
PRK13054 PRK13054
lipid kinase; Reviewed
 360-401 1.32e-05

lipid kinase; Reviewed


Pssm-ID: 237281 [Multi-domain]  Cd Length: 300  Bit Score: 48.33  E-value: 1.32e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1958771504  360 RILACGGDGTVGWILSILDELQLSPQPPVGVLPLGTGNDLAR 401
Cdd:PRK13054    59 TVIAGGGDGTINEVATALAQLEGDARPALGILPLGTANDFAT 100
Ank_4 pfam13637
Ankyrin repeats (many copies);
904-958 1.58e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.03  E-value: 1.58e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958771504  904 SLLHYAAKTGNGEIVKYILDHGPAelLDMADSEtGETALHKAACQRNRAVCQLLV 958
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGAD--INAVDGN-GETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 881-980 8.83e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.11  E-value: 8.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771504  881 DLMKLMesYKNGGSLLIQGPGHCSLLHYAAKTGNGEIVKYILDHGPAellDMADSETGETALHKAACQrNRAVCQLLVDa 960
Cdd:PHA02874   171 DIIKLL--LEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNH---IMNKCKNGFTPLHNAIIH-NRSAIELLIN- 243

                           90       100
                   ....*....|....*....|
gi 1958771504  961 GASLRQTDSKGKTPQERAQQ 980
Cdd:PHA02874   244 NASINDQDIDGSTPLHHAIN 263
Ank_5 pfam13857
Ankyrin repeats (many copies);
921-978 4.79e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 4.79e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958771504  921 ILDHGPAELLDmaDSETGETALHKAACQRNRAVCQLLVDAGASLRQTDSKGKTPQERA 978
Cdd:pfam13857    1 LLEHGPIDLNR--LDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PRK13055 PRK13055
putative lipid kinase; Reviewed
 361-404 1.08e-03

putative lipid kinase; Reviewed


Pssm-ID: 237282 [Multi-domain]  Cd Length: 334  Bit Score: 42.28  E-value: 1.08e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1958771504  361 ILACGGDGTVGWILSILdeLQLSPQPPVGVLPLGTGNDLARTLN 404
Cdd:PRK13055    63 IIAAGGDGTINEVVNGI--APLEKRPKMAIIPAGTTNDYARALK 104
TIGR00147 TIGR00147
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ...
 360-403 1.14e-03

lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been purified and shown to have phosphatidylglycerol kinase activity. The member from M. tuberculosis, Rv2252, has diacylglycerol kinase activity. BmrU from B. subtilis is in an operon with multidrug efflux transporter Bmr, but is uncharacterized. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 161732 [Multi-domain]  Cd Length: 293  Bit Score: 42.11  E-value: 1.14e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1958771504  360 RILACGGDGTVGWILSILdeLQLSPQPPVGVLPLGTGNDLARTL 403
Cdd:TIGR00147   60 TVIAGGGDGTINEVVNAL--IQLDDIPALGILPLGTANDFARSL 101
C1_DGK_rpt2 cd20805
second protein kinase C conserved region 1 (C1 domain) found in the diacylglycerol kinase ...
 173-220 2.39e-03

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: 37.04  E-value: 2.39e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1958771504  173 HLWLETNV-SGDLCYLGEENCQVRFAKSALRrkCAVCKIVVHTACIEQL 220
Cdd:cd20805      1 HHWVEGNLpSGAKCSVCGKKCGSSFGLAGYR--CSWCKRTVHSECIDKL 47
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 938-968 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: 35.73  E-value: 3.76e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1958771504  938 GETALHKAACQRNRA-VCQLLVDAGASLRQTD 968
Cdd:pfam00023    2 GNTPLHLAAGRRGNLeIVKLLLSKGADVNARD 33
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 903-926 3.88e-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: 3.88e-03
                            10        20
                    ....*....|....*....|....
gi 1958771504   903 CSLLHYAAKTGNGEIVKYILDHGP 926
Cdd:smart00248    3 RTPLHLAAENGNLEVVKLLLDKGA 26
Ank_5 pfam13857
Ankyrin repeats (many copies);
906-945 4.57e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 4.57e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1958771504  906 LHYAAKTGNGEIVKYILDHGpaELLDMADSEtGETALHKA 945
Cdd:pfam13857   20 LHVAAKYGALEIVRVLLAYG--VDLNLKDEE-GLTALDLA 56
 
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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